data_9CVZ
# 
_entry.id   9CVZ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9CVZ         pdb_00009cvz 10.2210/pdb9cvz/pdb 
WWPDB D_1000286252 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-30 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9CVZ 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-29 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              poulos@uci.edu 
_pdbx_contact_author.name_first         Thomas 
_pdbx_contact_author.name_last          Poulos 
_pdbx_contact_author.name_mi            L 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5648-3510 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Li, H.'       1 0000-0003-4867-367X 
'Poulos, T.L.' 2 0000-0002-5648-3510 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Bioorg.Med.Chem. 
_citation.journal_id_ASTM           BMECEP 
_citation.journal_id_CSD            1200 
_citation.journal_id_ISSN           1464-3391 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            124 
_citation.language                  ? 
_citation.page_first                118193 
_citation.page_last                 118193 
_citation.title                     
;Truncated pyridinylbenzylamines: Potent, selective, and highly membrane permeable inhibitors of human neuronal nitric oxide synthase.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.bmc.2025.118193 
_citation.pdbx_database_id_PubMed   40252563 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Vasu, D.'        1 ? 
primary 'Do, H.T.'        2 ? 
primary 'Li, H.'          3 ? 
primary 'Hardy, C.D.'     4 ? 
primary 'Poulos, T.L.'    5 ? 
primary 'Silverman, R.B.' 6 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Nitric oxide synthase, brain'                                                         48996.781 4   1.14.13.39 
'R354A, G357D' ? ? 
2 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE'                                                      616.487   4   ?          
?              ? ? 
3 non-polymer syn 5,6,7,8-TETRAHYDROBIOPTERIN                                                            241.247   4   ?          
?              ? ? 
4 non-polymer syn '(6M)-6-(2,3-difluoro-5-{[(2-fluoroethyl)amino]methyl}phenyl)-4-methylpyridin-2-amine' 295.303   4   ?          
?              ? ? 
5 non-polymer syn GLYCEROL                                                                               92.094    6   ?          
?              ? ? 
6 non-polymer syn 'ZINC ION'                                                                             65.409    2   ?          
?              ? ? 
7 water       nat water                                                                                  18.015    347 ?          
?              ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Constitutive NOS,NC-NOS,NOS type I,Neuronal NOS,nNOS,Peptidyl-cysteine S-nitrosylase NOS1,bNOS' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;CPRFLKVKNWETEVVLTDTLHLKSTLETGCTEYICMGSIMHPSQHARRPEDVATKDQLFPLAKEFIDQYYSSIKRFGSKA
HMERLEEVNKEIDTTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLR
SAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKPPRGRFDVLPLLLQANGNDPELFQI
PPELVLEVPIRHPKFEWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEEVAKKMNL
DMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEML
NYRLTPSFEYQPDPWNTHVWKLV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;CPRFLKVKNWETEVVLTDTLHLKSTLETGCTEYICMGSIMHPSQHARRPEDVATKDQLFPLAKEFIDQYYSSIKRFGSKA
HMERLEEVNKEIDTTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLR
SAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKPPRGRFDVLPLLLQANGNDPELFQI
PPELVLEVPIRHPKFEWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEEVAKKMNL
DMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEML
NYRLTPSFEYQPDPWNTHVWKLV
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'PROTOPORPHYRIN IX CONTAINING FE'                                                      HEM   
3 5,6,7,8-TETRAHYDROBIOPTERIN                                                            H4B   
4 '(6M)-6-(2,3-difluoro-5-{[(2-fluoroethyl)amino]methyl}phenyl)-4-methylpyridin-2-amine' A1AZ9 
5 GLYCEROL                                                                               GOL   
6 'ZINC ION'                                                                             ZN    
7 water                                                                                  HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   CYS n 
1 2   PRO n 
1 3   ARG n 
1 4   PHE n 
1 5   LEU n 
1 6   LYS n 
1 7   VAL n 
1 8   LYS n 
1 9   ASN n 
1 10  TRP n 
1 11  GLU n 
1 12  THR n 
1 13  GLU n 
1 14  VAL n 
1 15  VAL n 
1 16  LEU n 
1 17  THR n 
1 18  ASP n 
1 19  THR n 
1 20  LEU n 
1 21  HIS n 
1 22  LEU n 
1 23  LYS n 
1 24  SER n 
1 25  THR n 
1 26  LEU n 
1 27  GLU n 
1 28  THR n 
1 29  GLY n 
1 30  CYS n 
1 31  THR n 
1 32  GLU n 
1 33  TYR n 
1 34  ILE n 
1 35  CYS n 
1 36  MET n 
1 37  GLY n 
1 38  SER n 
1 39  ILE n 
1 40  MET n 
1 41  HIS n 
1 42  PRO n 
1 43  SER n 
1 44  GLN n 
1 45  HIS n 
1 46  ALA n 
1 47  ARG n 
1 48  ARG n 
1 49  PRO n 
1 50  GLU n 
1 51  ASP n 
1 52  VAL n 
1 53  ALA n 
1 54  THR n 
1 55  LYS n 
1 56  ASP n 
1 57  GLN n 
1 58  LEU n 
1 59  PHE n 
1 60  PRO n 
1 61  LEU n 
1 62  ALA n 
1 63  LYS n 
1 64  GLU n 
1 65  PHE n 
1 66  ILE n 
1 67  ASP n 
1 68  GLN n 
1 69  TYR n 
1 70  TYR n 
1 71  SER n 
1 72  SER n 
1 73  ILE n 
1 74  LYS n 
1 75  ARG n 
1 76  PHE n 
1 77  GLY n 
1 78  SER n 
1 79  LYS n 
1 80  ALA n 
1 81  HIS n 
1 82  MET n 
1 83  GLU n 
1 84  ARG n 
1 85  LEU n 
1 86  GLU n 
1 87  GLU n 
1 88  VAL n 
1 89  ASN n 
1 90  LYS n 
1 91  GLU n 
1 92  ILE n 
1 93  ASP n 
1 94  THR n 
1 95  THR n 
1 96  SER n 
1 97  THR n 
1 98  TYR n 
1 99  GLN n 
1 100 LEU n 
1 101 LYS n 
1 102 ASP n 
1 103 THR n 
1 104 GLU n 
1 105 LEU n 
1 106 ILE n 
1 107 TYR n 
1 108 GLY n 
1 109 ALA n 
1 110 LYS n 
1 111 HIS n 
1 112 ALA n 
1 113 TRP n 
1 114 ARG n 
1 115 ASN n 
1 116 ALA n 
1 117 SER n 
1 118 ARG n 
1 119 CYS n 
1 120 VAL n 
1 121 GLY n 
1 122 ARG n 
1 123 ILE n 
1 124 GLN n 
1 125 TRP n 
1 126 SER n 
1 127 LYS n 
1 128 LEU n 
1 129 GLN n 
1 130 VAL n 
1 131 PHE n 
1 132 ASP n 
1 133 ALA n 
1 134 ARG n 
1 135 ASP n 
1 136 CYS n 
1 137 THR n 
1 138 THR n 
1 139 ALA n 
1 140 HIS n 
1 141 GLY n 
1 142 MET n 
1 143 PHE n 
1 144 ASN n 
1 145 TYR n 
1 146 ILE n 
1 147 CYS n 
1 148 ASN n 
1 149 HIS n 
1 150 VAL n 
1 151 LYS n 
1 152 TYR n 
1 153 ALA n 
1 154 THR n 
1 155 ASN n 
1 156 LYS n 
1 157 GLY n 
1 158 ASN n 
1 159 LEU n 
1 160 ARG n 
1 161 SER n 
1 162 ALA n 
1 163 ILE n 
1 164 THR n 
1 165 ILE n 
1 166 PHE n 
1 167 PRO n 
1 168 GLN n 
1 169 ARG n 
1 170 THR n 
1 171 ASP n 
1 172 GLY n 
1 173 LYS n 
1 174 HIS n 
1 175 ASP n 
1 176 PHE n 
1 177 ARG n 
1 178 VAL n 
1 179 TRP n 
1 180 ASN n 
1 181 SER n 
1 182 GLN n 
1 183 LEU n 
1 184 ILE n 
1 185 ARG n 
1 186 TYR n 
1 187 ALA n 
1 188 GLY n 
1 189 TYR n 
1 190 LYS n 
1 191 GLN n 
1 192 PRO n 
1 193 ASP n 
1 194 GLY n 
1 195 SER n 
1 196 THR n 
1 197 LEU n 
1 198 GLY n 
1 199 ASP n 
1 200 PRO n 
1 201 ALA n 
1 202 ASN n 
1 203 VAL n 
1 204 GLN n 
1 205 PHE n 
1 206 THR n 
1 207 GLU n 
1 208 ILE n 
1 209 CYS n 
1 210 ILE n 
1 211 GLN n 
1 212 GLN n 
1 213 GLY n 
1 214 TRP n 
1 215 LYS n 
1 216 PRO n 
1 217 PRO n 
1 218 ARG n 
1 219 GLY n 
1 220 ARG n 
1 221 PHE n 
1 222 ASP n 
1 223 VAL n 
1 224 LEU n 
1 225 PRO n 
1 226 LEU n 
1 227 LEU n 
1 228 LEU n 
1 229 GLN n 
1 230 ALA n 
1 231 ASN n 
1 232 GLY n 
1 233 ASN n 
1 234 ASP n 
1 235 PRO n 
1 236 GLU n 
1 237 LEU n 
1 238 PHE n 
1 239 GLN n 
1 240 ILE n 
1 241 PRO n 
1 242 PRO n 
1 243 GLU n 
1 244 LEU n 
1 245 VAL n 
1 246 LEU n 
1 247 GLU n 
1 248 VAL n 
1 249 PRO n 
1 250 ILE n 
1 251 ARG n 
1 252 HIS n 
1 253 PRO n 
1 254 LYS n 
1 255 PHE n 
1 256 GLU n 
1 257 TRP n 
1 258 PHE n 
1 259 LYS n 
1 260 ASP n 
1 261 LEU n 
1 262 GLY n 
1 263 LEU n 
1 264 LYS n 
1 265 TRP n 
1 266 TYR n 
1 267 GLY n 
1 268 LEU n 
1 269 PRO n 
1 270 ALA n 
1 271 VAL n 
1 272 SER n 
1 273 ASN n 
1 274 MET n 
1 275 LEU n 
1 276 LEU n 
1 277 GLU n 
1 278 ILE n 
1 279 GLY n 
1 280 GLY n 
1 281 LEU n 
1 282 GLU n 
1 283 PHE n 
1 284 SER n 
1 285 ALA n 
1 286 CYS n 
1 287 PRO n 
1 288 PHE n 
1 289 SER n 
1 290 GLY n 
1 291 TRP n 
1 292 TYR n 
1 293 MET n 
1 294 GLY n 
1 295 THR n 
1 296 GLU n 
1 297 ILE n 
1 298 GLY n 
1 299 VAL n 
1 300 ARG n 
1 301 ASP n 
1 302 TYR n 
1 303 CYS n 
1 304 ASP n 
1 305 ASN n 
1 306 SER n 
1 307 ARG n 
1 308 TYR n 
1 309 ASN n 
1 310 ILE n 
1 311 LEU n 
1 312 GLU n 
1 313 GLU n 
1 314 VAL n 
1 315 ALA n 
1 316 LYS n 
1 317 LYS n 
1 318 MET n 
1 319 ASN n 
1 320 LEU n 
1 321 ASP n 
1 322 MET n 
1 323 ARG n 
1 324 LYS n 
1 325 THR n 
1 326 SER n 
1 327 SER n 
1 328 LEU n 
1 329 TRP n 
1 330 LYS n 
1 331 ASP n 
1 332 GLN n 
1 333 ALA n 
1 334 LEU n 
1 335 VAL n 
1 336 GLU n 
1 337 ILE n 
1 338 ASN n 
1 339 ILE n 
1 340 ALA n 
1 341 VAL n 
1 342 LEU n 
1 343 TYR n 
1 344 SER n 
1 345 PHE n 
1 346 GLN n 
1 347 SER n 
1 348 ASP n 
1 349 LYS n 
1 350 VAL n 
1 351 THR n 
1 352 ILE n 
1 353 VAL n 
1 354 ASP n 
1 355 HIS n 
1 356 HIS n 
1 357 SER n 
1 358 ALA n 
1 359 THR n 
1 360 GLU n 
1 361 SER n 
1 362 PHE n 
1 363 ILE n 
1 364 LYS n 
1 365 HIS n 
1 366 MET n 
1 367 GLU n 
1 368 ASN n 
1 369 GLU n 
1 370 TYR n 
1 371 ARG n 
1 372 CYS n 
1 373 ARG n 
1 374 GLY n 
1 375 GLY n 
1 376 CYS n 
1 377 PRO n 
1 378 ALA n 
1 379 ASP n 
1 380 TRP n 
1 381 VAL n 
1 382 TRP n 
1 383 ILE n 
1 384 VAL n 
1 385 PRO n 
1 386 PRO n 
1 387 MET n 
1 388 SER n 
1 389 GLY n 
1 390 SER n 
1 391 ILE n 
1 392 THR n 
1 393 PRO n 
1 394 VAL n 
1 395 PHE n 
1 396 HIS n 
1 397 GLN n 
1 398 GLU n 
1 399 MET n 
1 400 LEU n 
1 401 ASN n 
1 402 TYR n 
1 403 ARG n 
1 404 LEU n 
1 405 THR n 
1 406 PRO n 
1 407 SER n 
1 408 PHE n 
1 409 GLU n 
1 410 TYR n 
1 411 GLN n 
1 412 PRO n 
1 413 ASP n 
1 414 PRO n 
1 415 TRP n 
1 416 ASN n 
1 417 THR n 
1 418 HIS n 
1 419 VAL n 
1 420 TRP n 
1 421 LYS n 
1 422 LEU n 
1 423 VAL n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   423 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 NOS1 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                brain 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET22b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1AZ9 non-polymer         . '(6M)-6-(2,3-difluoro-5-{[(2-fluoroethyl)amino]methyl}phenyl)-4-methylpyridin-2-amine' ? 
'C15 H16 F3 N3'    295.303 
ALA   'L-peptide linking' y ALANINE                                                                                ? 'C3 H7 N O2' 
89.093  
ARG   'L-peptide linking' y ARGININE                                                                               ? 
'C6 H15 N4 O2 1'   175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                             ? 'C4 H8 N2 O3' 
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                        ? 'C4 H7 N O4' 
133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                               ? 
'C3 H7 N O2 S'     121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                              ? 
'C5 H10 N2 O3'     146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                        ? 'C5 H9 N O4' 
147.129 
GLY   'peptide linking'   y GLYCINE                                                                                ? 'C2 H5 N O2' 
75.067  
GOL   non-polymer         . GLYCEROL                                                                               
'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'         92.094  
H4B   non-polymer         . 5,6,7,8-TETRAHYDROBIOPTERIN                                                            ? 
'C9 H15 N5 O3'     241.247 
HEM   non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE'                                                      HEME 
'C34 H32 Fe N4 O4' 616.487 
HIS   'L-peptide linking' y HISTIDINE                                                                              ? 
'C6 H10 N3 O2 1'   156.162 
HOH   non-polymer         . WATER                                                                                  ? 'H2 O' 18.015 
ILE   'L-peptide linking' y ISOLEUCINE                                                                             ? 'C6 H13 N O2' 
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                ? 'C6 H13 N O2' 
131.173 
LYS   'L-peptide linking' y LYSINE                                                                                 ? 
'C6 H15 N2 O2 1'   147.195 
MET   'L-peptide linking' y METHIONINE                                                                             ? 
'C5 H11 N O2 S'    149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                          ? 'C9 H11 N O2' 
165.189 
PRO   'L-peptide linking' y PROLINE                                                                                ? 'C5 H9 N O2' 
115.130 
SER   'L-peptide linking' y SERINE                                                                                 ? 'C3 H7 N O3' 
105.093 
THR   'L-peptide linking' y THREONINE                                                                              ? 'C4 H9 N O3' 
119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                             ? 
'C11 H12 N2 O2'    204.225 
TYR   'L-peptide linking' y TYROSINE                                                                               ? 'C9 H11 N O3' 
181.189 
VAL   'L-peptide linking' y VALINE                                                                                 ? 'C5 H11 N O2' 
117.146 
ZN    non-polymer         . 'ZINC ION'                                                                             ? 'Zn 2' 65.409 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   CYS 1   302 ?   ?   ?   A . n 
A 1 2   PRO 2   303 ?   ?   ?   A . n 
A 1 3   ARG 3   304 304 ARG ARG A . n 
A 1 4   PHE 4   305 305 PHE PHE A . n 
A 1 5   LEU 5   306 306 LEU LEU A . n 
A 1 6   LYS 6   307 307 LYS LYS A . n 
A 1 7   VAL 7   308 308 VAL VAL A . n 
A 1 8   LYS 8   309 309 LYS LYS A . n 
A 1 9   ASN 9   310 310 ASN ASN A . n 
A 1 10  TRP 10  311 311 TRP TRP A . n 
A 1 11  GLU 11  312 312 GLU GLU A . n 
A 1 12  THR 12  313 313 THR THR A . n 
A 1 13  GLU 13  314 314 GLU GLU A . n 
A 1 14  VAL 14  315 315 VAL VAL A . n 
A 1 15  VAL 15  316 316 VAL VAL A . n 
A 1 16  LEU 16  317 317 LEU LEU A . n 
A 1 17  THR 17  318 318 THR THR A . n 
A 1 18  ASP 18  319 319 ASP ASP A . n 
A 1 19  THR 19  320 320 THR THR A . n 
A 1 20  LEU 20  321 321 LEU LEU A . n 
A 1 21  HIS 21  322 322 HIS HIS A . n 
A 1 22  LEU 22  323 323 LEU LEU A . n 
A 1 23  LYS 23  324 324 LYS LYS A . n 
A 1 24  SER 24  325 325 SER SER A . n 
A 1 25  THR 25  326 326 THR THR A . n 
A 1 26  LEU 26  327 327 LEU LEU A . n 
A 1 27  GLU 27  328 328 GLU GLU A . n 
A 1 28  THR 28  329 329 THR THR A . n 
A 1 29  GLY 29  330 330 GLY GLY A . n 
A 1 30  CYS 30  331 331 CYS CYS A . n 
A 1 31  THR 31  332 332 THR THR A . n 
A 1 32  GLU 32  333 333 GLU GLU A . n 
A 1 33  TYR 33  334 334 TYR TYR A . n 
A 1 34  ILE 34  335 335 ILE ILE A . n 
A 1 35  CYS 35  336 336 CYS CYS A . n 
A 1 36  MET 36  337 337 MET MET A . n 
A 1 37  GLY 37  338 338 GLY GLY A . n 
A 1 38  SER 38  339 339 SER SER A . n 
A 1 39  ILE 39  340 340 ILE ILE A . n 
A 1 40  MET 40  341 341 MET MET A . n 
A 1 41  HIS 41  342 342 HIS HIS A . n 
A 1 42  PRO 42  343 343 PRO PRO A . n 
A 1 43  SER 43  344 ?   ?   ?   A . n 
A 1 44  GLN 44  345 ?   ?   ?   A . n 
A 1 45  HIS 45  346 ?   ?   ?   A . n 
A 1 46  ALA 46  347 ?   ?   ?   A . n 
A 1 47  ARG 47  348 ?   ?   ?   A . n 
A 1 48  ARG 48  349 349 ARG ARG A . n 
A 1 49  PRO 49  350 350 PRO PRO A . n 
A 1 50  GLU 50  351 351 GLU GLU A . n 
A 1 51  ASP 51  352 352 ASP ASP A . n 
A 1 52  VAL 52  353 353 VAL VAL A . n 
A 1 53  ALA 53  354 354 ALA ALA A . n 
A 1 54  THR 54  355 355 THR THR A . n 
A 1 55  LYS 55  356 356 LYS LYS A . n 
A 1 56  ASP 56  357 357 ASP ASP A . n 
A 1 57  GLN 57  358 358 GLN GLN A . n 
A 1 58  LEU 58  359 359 LEU LEU A . n 
A 1 59  PHE 59  360 360 PHE PHE A . n 
A 1 60  PRO 60  361 361 PRO PRO A . n 
A 1 61  LEU 61  362 362 LEU LEU A . n 
A 1 62  ALA 62  363 363 ALA ALA A . n 
A 1 63  LYS 63  364 364 LYS LYS A . n 
A 1 64  GLU 64  365 365 GLU GLU A . n 
A 1 65  PHE 65  366 366 PHE PHE A . n 
A 1 66  ILE 66  367 367 ILE ILE A . n 
A 1 67  ASP 67  368 368 ASP ASP A . n 
A 1 68  GLN 68  369 369 GLN GLN A . n 
A 1 69  TYR 69  370 370 TYR TYR A . n 
A 1 70  TYR 70  371 371 TYR TYR A . n 
A 1 71  SER 71  372 372 SER SER A . n 
A 1 72  SER 72  373 373 SER SER A . n 
A 1 73  ILE 73  374 374 ILE ILE A . n 
A 1 74  LYS 74  375 375 LYS LYS A . n 
A 1 75  ARG 75  376 376 ARG ARG A . n 
A 1 76  PHE 76  377 377 PHE PHE A . n 
A 1 77  GLY 77  378 378 GLY GLY A . n 
A 1 78  SER 78  379 379 SER SER A . n 
A 1 79  LYS 79  380 380 LYS LYS A . n 
A 1 80  ALA 80  381 381 ALA ALA A . n 
A 1 81  HIS 81  382 382 HIS HIS A . n 
A 1 82  MET 82  383 383 MET MET A . n 
A 1 83  GLU 83  384 384 GLU GLU A . n 
A 1 84  ARG 84  385 385 ARG ARG A . n 
A 1 85  LEU 85  386 386 LEU LEU A . n 
A 1 86  GLU 86  387 387 GLU GLU A . n 
A 1 87  GLU 87  388 388 GLU GLU A . n 
A 1 88  VAL 88  389 389 VAL VAL A . n 
A 1 89  ASN 89  390 390 ASN ASN A . n 
A 1 90  LYS 90  391 391 LYS LYS A . n 
A 1 91  GLU 91  392 392 GLU GLU A . n 
A 1 92  ILE 92  393 393 ILE ILE A . n 
A 1 93  ASP 93  394 394 ASP ASP A . n 
A 1 94  THR 94  395 395 THR THR A . n 
A 1 95  THR 95  396 396 THR THR A . n 
A 1 96  SER 96  397 397 SER SER A . n 
A 1 97  THR 97  398 398 THR THR A . n 
A 1 98  TYR 98  399 399 TYR TYR A . n 
A 1 99  GLN 99  400 400 GLN GLN A . n 
A 1 100 LEU 100 401 401 LEU LEU A . n 
A 1 101 LYS 101 402 402 LYS LYS A . n 
A 1 102 ASP 102 403 403 ASP ASP A . n 
A 1 103 THR 103 404 404 THR THR A . n 
A 1 104 GLU 104 405 405 GLU GLU A . n 
A 1 105 LEU 105 406 406 LEU LEU A . n 
A 1 106 ILE 106 407 407 ILE ILE A . n 
A 1 107 TYR 107 408 408 TYR TYR A . n 
A 1 108 GLY 108 409 409 GLY GLY A . n 
A 1 109 ALA 109 410 410 ALA ALA A . n 
A 1 110 LYS 110 411 411 LYS LYS A . n 
A 1 111 HIS 111 412 412 HIS HIS A . n 
A 1 112 ALA 112 413 413 ALA ALA A . n 
A 1 113 TRP 113 414 414 TRP TRP A . n 
A 1 114 ARG 114 415 415 ARG ARG A . n 
A 1 115 ASN 115 416 416 ASN ASN A . n 
A 1 116 ALA 116 417 417 ALA ALA A . n 
A 1 117 SER 117 418 418 SER SER A . n 
A 1 118 ARG 118 419 419 ARG ARG A . n 
A 1 119 CYS 119 420 420 CYS CYS A . n 
A 1 120 VAL 120 421 421 VAL VAL A . n 
A 1 121 GLY 121 422 422 GLY GLY A . n 
A 1 122 ARG 122 423 423 ARG ARG A . n 
A 1 123 ILE 123 424 424 ILE ILE A . n 
A 1 124 GLN 124 425 425 GLN GLN A . n 
A 1 125 TRP 125 426 426 TRP TRP A . n 
A 1 126 SER 126 427 427 SER SER A . n 
A 1 127 LYS 127 428 428 LYS LYS A . n 
A 1 128 LEU 128 429 429 LEU LEU A . n 
A 1 129 GLN 129 430 430 GLN GLN A . n 
A 1 130 VAL 130 431 431 VAL VAL A . n 
A 1 131 PHE 131 432 432 PHE PHE A . n 
A 1 132 ASP 132 433 433 ASP ASP A . n 
A 1 133 ALA 133 434 434 ALA ALA A . n 
A 1 134 ARG 134 435 435 ARG ARG A . n 
A 1 135 ASP 135 436 436 ASP ASP A . n 
A 1 136 CYS 136 437 437 CYS CYS A . n 
A 1 137 THR 137 438 438 THR THR A . n 
A 1 138 THR 138 439 439 THR THR A . n 
A 1 139 ALA 139 440 440 ALA ALA A . n 
A 1 140 HIS 140 441 441 HIS HIS A . n 
A 1 141 GLY 141 442 442 GLY GLY A . n 
A 1 142 MET 142 443 443 MET MET A . n 
A 1 143 PHE 143 444 444 PHE PHE A . n 
A 1 144 ASN 144 445 445 ASN ASN A . n 
A 1 145 TYR 145 446 446 TYR TYR A . n 
A 1 146 ILE 146 447 447 ILE ILE A . n 
A 1 147 CYS 147 448 448 CYS CYS A . n 
A 1 148 ASN 148 449 449 ASN ASN A . n 
A 1 149 HIS 149 450 450 HIS HIS A . n 
A 1 150 VAL 150 451 451 VAL VAL A . n 
A 1 151 LYS 151 452 452 LYS LYS A . n 
A 1 152 TYR 152 453 453 TYR TYR A . n 
A 1 153 ALA 153 454 454 ALA ALA A . n 
A 1 154 THR 154 455 455 THR THR A . n 
A 1 155 ASN 155 456 456 ASN ASN A . n 
A 1 156 LYS 156 457 457 LYS LYS A . n 
A 1 157 GLY 157 458 458 GLY GLY A . n 
A 1 158 ASN 158 459 459 ASN ASN A . n 
A 1 159 LEU 159 460 460 LEU LEU A . n 
A 1 160 ARG 160 461 461 ARG ARG A . n 
A 1 161 SER 161 462 462 SER SER A . n 
A 1 162 ALA 162 463 463 ALA ALA A . n 
A 1 163 ILE 163 464 464 ILE ILE A . n 
A 1 164 THR 164 465 465 THR THR A . n 
A 1 165 ILE 165 466 466 ILE ILE A . n 
A 1 166 PHE 166 467 467 PHE PHE A . n 
A 1 167 PRO 167 468 468 PRO PRO A . n 
A 1 168 GLN 168 469 469 GLN GLN A . n 
A 1 169 ARG 169 470 470 ARG ARG A . n 
A 1 170 THR 170 471 471 THR THR A . n 
A 1 171 ASP 171 472 472 ASP ASP A . n 
A 1 172 GLY 172 473 473 GLY GLY A . n 
A 1 173 LYS 173 474 474 LYS LYS A . n 
A 1 174 HIS 174 475 475 HIS HIS A . n 
A 1 175 ASP 175 476 476 ASP ASP A . n 
A 1 176 PHE 176 477 477 PHE PHE A . n 
A 1 177 ARG 177 478 478 ARG ARG A . n 
A 1 178 VAL 178 479 479 VAL VAL A . n 
A 1 179 TRP 179 480 480 TRP TRP A . n 
A 1 180 ASN 180 481 481 ASN ASN A . n 
A 1 181 SER 181 482 482 SER SER A . n 
A 1 182 GLN 182 483 483 GLN GLN A . n 
A 1 183 LEU 183 484 484 LEU LEU A . n 
A 1 184 ILE 184 485 485 ILE ILE A . n 
A 1 185 ARG 185 486 486 ARG ARG A . n 
A 1 186 TYR 186 487 487 TYR TYR A . n 
A 1 187 ALA 187 488 488 ALA ALA A . n 
A 1 188 GLY 188 489 489 GLY GLY A . n 
A 1 189 TYR 189 490 490 TYR TYR A . n 
A 1 190 LYS 190 491 491 LYS LYS A . n 
A 1 191 GLN 191 492 492 GLN GLN A . n 
A 1 192 PRO 192 493 493 PRO PRO A . n 
A 1 193 ASP 193 494 494 ASP ASP A . n 
A 1 194 GLY 194 495 495 GLY GLY A . n 
A 1 195 SER 195 496 496 SER SER A . n 
A 1 196 THR 196 497 497 THR THR A . n 
A 1 197 LEU 197 498 498 LEU LEU A . n 
A 1 198 GLY 198 499 499 GLY GLY A . n 
A 1 199 ASP 199 500 500 ASP ASP A . n 
A 1 200 PRO 200 501 501 PRO PRO A . n 
A 1 201 ALA 201 502 502 ALA ALA A . n 
A 1 202 ASN 202 503 503 ASN ASN A . n 
A 1 203 VAL 203 504 504 VAL VAL A . n 
A 1 204 GLN 204 505 505 GLN GLN A . n 
A 1 205 PHE 205 506 506 PHE PHE A . n 
A 1 206 THR 206 507 507 THR THR A . n 
A 1 207 GLU 207 508 508 GLU GLU A . n 
A 1 208 ILE 208 509 509 ILE ILE A . n 
A 1 209 CYS 209 510 510 CYS CYS A . n 
A 1 210 ILE 210 511 511 ILE ILE A . n 
A 1 211 GLN 211 512 512 GLN GLN A . n 
A 1 212 GLN 212 513 513 GLN GLN A . n 
A 1 213 GLY 213 514 514 GLY GLY A . n 
A 1 214 TRP 214 515 515 TRP TRP A . n 
A 1 215 LYS 215 516 516 LYS LYS A . n 
A 1 216 PRO 216 517 517 PRO PRO A . n 
A 1 217 PRO 217 518 518 PRO PRO A . n 
A 1 218 ARG 218 519 519 ARG ARG A . n 
A 1 219 GLY 219 520 520 GLY GLY A . n 
A 1 220 ARG 220 521 521 ARG ARG A . n 
A 1 221 PHE 221 522 522 PHE PHE A . n 
A 1 222 ASP 222 523 523 ASP ASP A . n 
A 1 223 VAL 223 524 524 VAL VAL A . n 
A 1 224 LEU 224 525 525 LEU LEU A . n 
A 1 225 PRO 225 526 526 PRO PRO A . n 
A 1 226 LEU 226 527 527 LEU LEU A . n 
A 1 227 LEU 227 528 528 LEU LEU A . n 
A 1 228 LEU 228 529 529 LEU LEU A . n 
A 1 229 GLN 229 530 530 GLN GLN A . n 
A 1 230 ALA 230 531 531 ALA ALA A . n 
A 1 231 ASN 231 532 532 ASN ASN A . n 
A 1 232 GLY 232 533 533 GLY GLY A . n 
A 1 233 ASN 233 534 534 ASN ASN A . n 
A 1 234 ASP 234 535 535 ASP ASP A . n 
A 1 235 PRO 235 536 536 PRO PRO A . n 
A 1 236 GLU 236 537 537 GLU GLU A . n 
A 1 237 LEU 237 538 538 LEU LEU A . n 
A 1 238 PHE 238 539 539 PHE PHE A . n 
A 1 239 GLN 239 540 540 GLN GLN A . n 
A 1 240 ILE 240 541 541 ILE ILE A . n 
A 1 241 PRO 241 542 542 PRO PRO A . n 
A 1 242 PRO 242 543 543 PRO PRO A . n 
A 1 243 GLU 243 544 544 GLU GLU A . n 
A 1 244 LEU 244 545 545 LEU LEU A . n 
A 1 245 VAL 245 546 546 VAL VAL A . n 
A 1 246 LEU 246 547 547 LEU LEU A . n 
A 1 247 GLU 247 548 548 GLU GLU A . n 
A 1 248 VAL 248 549 549 VAL VAL A . n 
A 1 249 PRO 249 550 550 PRO PRO A . n 
A 1 250 ILE 250 551 551 ILE ILE A . n 
A 1 251 ARG 251 552 552 ARG ARG A . n 
A 1 252 HIS 252 553 553 HIS HIS A . n 
A 1 253 PRO 253 554 554 PRO PRO A . n 
A 1 254 LYS 254 555 555 LYS LYS A . n 
A 1 255 PHE 255 556 556 PHE PHE A . n 
A 1 256 GLU 256 557 557 GLU GLU A . n 
A 1 257 TRP 257 558 558 TRP TRP A . n 
A 1 258 PHE 258 559 559 PHE PHE A . n 
A 1 259 LYS 259 560 560 LYS LYS A . n 
A 1 260 ASP 260 561 561 ASP ASP A . n 
A 1 261 LEU 261 562 562 LEU LEU A . n 
A 1 262 GLY 262 563 563 GLY GLY A . n 
A 1 263 LEU 263 564 564 LEU LEU A . n 
A 1 264 LYS 264 565 565 LYS LYS A . n 
A 1 265 TRP 265 566 566 TRP TRP A . n 
A 1 266 TYR 266 567 567 TYR TYR A . n 
A 1 267 GLY 267 568 568 GLY GLY A . n 
A 1 268 LEU 268 569 569 LEU LEU A . n 
A 1 269 PRO 269 570 570 PRO PRO A . n 
A 1 270 ALA 270 571 571 ALA ALA A . n 
A 1 271 VAL 271 572 572 VAL VAL A . n 
A 1 272 SER 272 573 573 SER SER A . n 
A 1 273 ASN 273 574 574 ASN ASN A . n 
A 1 274 MET 274 575 575 MET MET A . n 
A 1 275 LEU 275 576 576 LEU LEU A . n 
A 1 276 LEU 276 577 577 LEU LEU A . n 
A 1 277 GLU 277 578 578 GLU GLU A . n 
A 1 278 ILE 278 579 579 ILE ILE A . n 
A 1 279 GLY 279 580 580 GLY GLY A . n 
A 1 280 GLY 280 581 581 GLY GLY A . n 
A 1 281 LEU 281 582 582 LEU LEU A . n 
A 1 282 GLU 282 583 583 GLU GLU A . n 
A 1 283 PHE 283 584 584 PHE PHE A . n 
A 1 284 SER 284 585 585 SER SER A . n 
A 1 285 ALA 285 586 586 ALA ALA A . n 
A 1 286 CYS 286 587 587 CYS CYS A . n 
A 1 287 PRO 287 588 588 PRO PRO A . n 
A 1 288 PHE 288 589 589 PHE PHE A . n 
A 1 289 SER 289 590 590 SER SER A . n 
A 1 290 GLY 290 591 591 GLY GLY A . n 
A 1 291 TRP 291 592 592 TRP TRP A . n 
A 1 292 TYR 292 593 593 TYR TYR A . n 
A 1 293 MET 293 594 594 MET MET A . n 
A 1 294 GLY 294 595 595 GLY GLY A . n 
A 1 295 THR 295 596 596 THR THR A . n 
A 1 296 GLU 296 597 597 GLU GLU A . n 
A 1 297 ILE 297 598 598 ILE ILE A . n 
A 1 298 GLY 298 599 599 GLY GLY A . n 
A 1 299 VAL 299 600 600 VAL VAL A . n 
A 1 300 ARG 300 601 601 ARG ARG A . n 
A 1 301 ASP 301 602 602 ASP ASP A . n 
A 1 302 TYR 302 603 603 TYR TYR A . n 
A 1 303 CYS 303 604 604 CYS CYS A . n 
A 1 304 ASP 304 605 605 ASP ASP A . n 
A 1 305 ASN 305 606 606 ASN ASN A . n 
A 1 306 SER 306 607 607 SER SER A . n 
A 1 307 ARG 307 608 608 ARG ARG A . n 
A 1 308 TYR 308 609 609 TYR TYR A . n 
A 1 309 ASN 309 610 610 ASN ASN A . n 
A 1 310 ILE 310 611 611 ILE ILE A . n 
A 1 311 LEU 311 612 612 LEU LEU A . n 
A 1 312 GLU 312 613 613 GLU GLU A . n 
A 1 313 GLU 313 614 614 GLU GLU A . n 
A 1 314 VAL 314 615 615 VAL VAL A . n 
A 1 315 ALA 315 616 616 ALA ALA A . n 
A 1 316 LYS 316 617 617 LYS LYS A . n 
A 1 317 LYS 317 618 618 LYS LYS A . n 
A 1 318 MET 318 619 619 MET MET A . n 
A 1 319 ASN 319 620 620 ASN ASN A . n 
A 1 320 LEU 320 621 621 LEU LEU A . n 
A 1 321 ASP 321 622 622 ASP ASP A . n 
A 1 322 MET 322 623 623 MET MET A . n 
A 1 323 ARG 323 624 624 ARG ARG A . n 
A 1 324 LYS 324 625 625 LYS LYS A . n 
A 1 325 THR 325 626 626 THR THR A . n 
A 1 326 SER 326 627 627 SER SER A . n 
A 1 327 SER 327 628 628 SER SER A . n 
A 1 328 LEU 328 629 629 LEU LEU A . n 
A 1 329 TRP 329 630 630 TRP TRP A . n 
A 1 330 LYS 330 631 631 LYS LYS A . n 
A 1 331 ASP 331 632 632 ASP ASP A . n 
A 1 332 GLN 332 633 633 GLN GLN A . n 
A 1 333 ALA 333 634 634 ALA ALA A . n 
A 1 334 LEU 334 635 635 LEU LEU A . n 
A 1 335 VAL 335 636 636 VAL VAL A . n 
A 1 336 GLU 336 637 637 GLU GLU A . n 
A 1 337 ILE 337 638 638 ILE ILE A . n 
A 1 338 ASN 338 639 639 ASN ASN A . n 
A 1 339 ILE 339 640 640 ILE ILE A . n 
A 1 340 ALA 340 641 641 ALA ALA A . n 
A 1 341 VAL 341 642 642 VAL VAL A . n 
A 1 342 LEU 342 643 643 LEU LEU A . n 
A 1 343 TYR 343 644 644 TYR TYR A . n 
A 1 344 SER 344 645 645 SER SER A . n 
A 1 345 PHE 345 646 646 PHE PHE A . n 
A 1 346 GLN 346 647 647 GLN GLN A . n 
A 1 347 SER 347 648 648 SER SER A . n 
A 1 348 ASP 348 649 649 ASP ASP A . n 
A 1 349 LYS 349 650 650 LYS LYS A . n 
A 1 350 VAL 350 651 651 VAL VAL A . n 
A 1 351 THR 351 652 652 THR THR A . n 
A 1 352 ILE 352 653 653 ILE ILE A . n 
A 1 353 VAL 353 654 654 VAL VAL A . n 
A 1 354 ASP 354 655 655 ASP ASP A . n 
A 1 355 HIS 355 656 656 HIS HIS A . n 
A 1 356 HIS 356 657 657 HIS HIS A . n 
A 1 357 SER 357 658 658 SER SER A . n 
A 1 358 ALA 358 659 659 ALA ALA A . n 
A 1 359 THR 359 660 660 THR THR A . n 
A 1 360 GLU 360 661 661 GLU GLU A . n 
A 1 361 SER 361 662 662 SER SER A . n 
A 1 362 PHE 362 663 663 PHE PHE A . n 
A 1 363 ILE 363 664 664 ILE ILE A . n 
A 1 364 LYS 364 665 665 LYS LYS A . n 
A 1 365 HIS 365 666 666 HIS HIS A . n 
A 1 366 MET 366 667 667 MET MET A . n 
A 1 367 GLU 367 668 668 GLU GLU A . n 
A 1 368 ASN 368 669 669 ASN ASN A . n 
A 1 369 GLU 369 670 670 GLU GLU A . n 
A 1 370 TYR 370 671 671 TYR TYR A . n 
A 1 371 ARG 371 672 672 ARG ARG A . n 
A 1 372 CYS 372 673 673 CYS CYS A . n 
A 1 373 ARG 373 674 674 ARG ARG A . n 
A 1 374 GLY 374 675 675 GLY GLY A . n 
A 1 375 GLY 375 676 676 GLY GLY A . n 
A 1 376 CYS 376 677 677 CYS CYS A . n 
A 1 377 PRO 377 678 678 PRO PRO A . n 
A 1 378 ALA 378 679 679 ALA ALA A . n 
A 1 379 ASP 379 680 680 ASP ASP A . n 
A 1 380 TRP 380 681 681 TRP TRP A . n 
A 1 381 VAL 381 682 682 VAL VAL A . n 
A 1 382 TRP 382 683 683 TRP TRP A . n 
A 1 383 ILE 383 684 684 ILE ILE A . n 
A 1 384 VAL 384 685 685 VAL VAL A . n 
A 1 385 PRO 385 686 686 PRO PRO A . n 
A 1 386 PRO 386 687 687 PRO PRO A . n 
A 1 387 MET 387 688 688 MET MET A . n 
A 1 388 SER 388 689 689 SER SER A . n 
A 1 389 GLY 389 690 690 GLY GLY A . n 
A 1 390 SER 390 691 691 SER SER A . n 
A 1 391 ILE 391 692 692 ILE ILE A . n 
A 1 392 THR 392 693 693 THR THR A . n 
A 1 393 PRO 393 694 694 PRO PRO A . n 
A 1 394 VAL 394 695 695 VAL VAL A . n 
A 1 395 PHE 395 696 696 PHE PHE A . n 
A 1 396 HIS 396 697 697 HIS HIS A . n 
A 1 397 GLN 397 698 698 GLN GLN A . n 
A 1 398 GLU 398 699 699 GLU GLU A . n 
A 1 399 MET 399 700 700 MET MET A . n 
A 1 400 LEU 400 701 701 LEU LEU A . n 
A 1 401 ASN 401 702 702 ASN ASN A . n 
A 1 402 TYR 402 703 703 TYR TYR A . n 
A 1 403 ARG 403 704 704 ARG ARG A . n 
A 1 404 LEU 404 705 705 LEU LEU A . n 
A 1 405 THR 405 706 706 THR THR A . n 
A 1 406 PRO 406 707 707 PRO PRO A . n 
A 1 407 SER 407 708 708 SER SER A . n 
A 1 408 PHE 408 709 709 PHE PHE A . n 
A 1 409 GLU 409 710 710 GLU GLU A . n 
A 1 410 TYR 410 711 711 TYR TYR A . n 
A 1 411 GLN 411 712 712 GLN GLN A . n 
A 1 412 PRO 412 713 713 PRO PRO A . n 
A 1 413 ASP 413 714 714 ASP ASP A . n 
A 1 414 PRO 414 715 715 PRO PRO A . n 
A 1 415 TRP 415 716 716 TRP TRP A . n 
A 1 416 ASN 416 717 717 ASN ASN A . n 
A 1 417 THR 417 718 718 THR THR A . n 
A 1 418 HIS 418 719 719 HIS HIS A . n 
A 1 419 VAL 419 720 720 VAL VAL A . n 
A 1 420 TRP 420 721 721 TRP TRP A . n 
A 1 421 LYS 421 722 722 LYS LYS A . n 
A 1 422 LEU 422 723 ?   ?   ?   A . n 
A 1 423 VAL 423 724 ?   ?   ?   A . n 
B 1 1   CYS 1   302 ?   ?   ?   B . n 
B 1 2   PRO 2   303 ?   ?   ?   B . n 
B 1 3   ARG 3   304 304 ARG ARG B . n 
B 1 4   PHE 4   305 305 PHE PHE B . n 
B 1 5   LEU 5   306 306 LEU LEU B . n 
B 1 6   LYS 6   307 307 LYS LYS B . n 
B 1 7   VAL 7   308 308 VAL VAL B . n 
B 1 8   LYS 8   309 309 LYS LYS B . n 
B 1 9   ASN 9   310 310 ASN ASN B . n 
B 1 10  TRP 10  311 311 TRP TRP B . n 
B 1 11  GLU 11  312 312 GLU GLU B . n 
B 1 12  THR 12  313 313 THR THR B . n 
B 1 13  GLU 13  314 314 GLU GLU B . n 
B 1 14  VAL 14  315 315 VAL VAL B . n 
B 1 15  VAL 15  316 316 VAL VAL B . n 
B 1 16  LEU 16  317 317 LEU LEU B . n 
B 1 17  THR 17  318 318 THR THR B . n 
B 1 18  ASP 18  319 319 ASP ASP B . n 
B 1 19  THR 19  320 320 THR THR B . n 
B 1 20  LEU 20  321 321 LEU LEU B . n 
B 1 21  HIS 21  322 322 HIS HIS B . n 
B 1 22  LEU 22  323 323 LEU LEU B . n 
B 1 23  LYS 23  324 324 LYS LYS B . n 
B 1 24  SER 24  325 325 SER SER B . n 
B 1 25  THR 25  326 326 THR THR B . n 
B 1 26  LEU 26  327 327 LEU LEU B . n 
B 1 27  GLU 27  328 328 GLU GLU B . n 
B 1 28  THR 28  329 329 THR THR B . n 
B 1 29  GLY 29  330 330 GLY GLY B . n 
B 1 30  CYS 30  331 331 CYS CYS B . n 
B 1 31  THR 31  332 332 THR THR B . n 
B 1 32  GLU 32  333 333 GLU GLU B . n 
B 1 33  TYR 33  334 334 TYR TYR B . n 
B 1 34  ILE 34  335 335 ILE ILE B . n 
B 1 35  CYS 35  336 336 CYS CYS B . n 
B 1 36  MET 36  337 337 MET MET B . n 
B 1 37  GLY 37  338 338 GLY GLY B . n 
B 1 38  SER 38  339 339 SER SER B . n 
B 1 39  ILE 39  340 340 ILE ILE B . n 
B 1 40  MET 40  341 341 MET MET B . n 
B 1 41  HIS 41  342 342 HIS HIS B . n 
B 1 42  PRO 42  343 343 PRO PRO B . n 
B 1 43  SER 43  344 344 SER SER B . n 
B 1 44  GLN 44  345 345 GLN GLN B . n 
B 1 45  HIS 45  346 346 HIS HIS B . n 
B 1 46  ALA 46  347 347 ALA ALA B . n 
B 1 47  ARG 47  348 348 ARG ARG B . n 
B 1 48  ARG 48  349 349 ARG ARG B . n 
B 1 49  PRO 49  350 350 PRO PRO B . n 
B 1 50  GLU 50  351 351 GLU GLU B . n 
B 1 51  ASP 51  352 352 ASP ASP B . n 
B 1 52  VAL 52  353 353 VAL VAL B . n 
B 1 53  ALA 53  354 354 ALA ALA B . n 
B 1 54  THR 54  355 355 THR THR B . n 
B 1 55  LYS 55  356 356 LYS LYS B . n 
B 1 56  ASP 56  357 357 ASP ASP B . n 
B 1 57  GLN 57  358 358 GLN GLN B . n 
B 1 58  LEU 58  359 359 LEU LEU B . n 
B 1 59  PHE 59  360 360 PHE PHE B . n 
B 1 60  PRO 60  361 361 PRO PRO B . n 
B 1 61  LEU 61  362 362 LEU LEU B . n 
B 1 62  ALA 62  363 363 ALA ALA B . n 
B 1 63  LYS 63  364 364 LYS LYS B . n 
B 1 64  GLU 64  365 365 GLU GLU B . n 
B 1 65  PHE 65  366 366 PHE PHE B . n 
B 1 66  ILE 66  367 367 ILE ILE B . n 
B 1 67  ASP 67  368 368 ASP ASP B . n 
B 1 68  GLN 68  369 369 GLN GLN B . n 
B 1 69  TYR 69  370 370 TYR TYR B . n 
B 1 70  TYR 70  371 371 TYR TYR B . n 
B 1 71  SER 71  372 372 SER SER B . n 
B 1 72  SER 72  373 373 SER SER B . n 
B 1 73  ILE 73  374 374 ILE ILE B . n 
B 1 74  LYS 74  375 375 LYS LYS B . n 
B 1 75  ARG 75  376 376 ARG ARG B . n 
B 1 76  PHE 76  377 377 PHE PHE B . n 
B 1 77  GLY 77  378 378 GLY GLY B . n 
B 1 78  SER 78  379 379 SER SER B . n 
B 1 79  LYS 79  380 380 LYS LYS B . n 
B 1 80  ALA 80  381 381 ALA ALA B . n 
B 1 81  HIS 81  382 382 HIS HIS B . n 
B 1 82  MET 82  383 383 MET MET B . n 
B 1 83  GLU 83  384 384 GLU GLU B . n 
B 1 84  ARG 84  385 385 ARG ARG B . n 
B 1 85  LEU 85  386 386 LEU LEU B . n 
B 1 86  GLU 86  387 387 GLU GLU B . n 
B 1 87  GLU 87  388 388 GLU GLU B . n 
B 1 88  VAL 88  389 389 VAL VAL B . n 
B 1 89  ASN 89  390 390 ASN ASN B . n 
B 1 90  LYS 90  391 391 LYS LYS B . n 
B 1 91  GLU 91  392 392 GLU GLU B . n 
B 1 92  ILE 92  393 393 ILE ILE B . n 
B 1 93  ASP 93  394 394 ASP ASP B . n 
B 1 94  THR 94  395 395 THR THR B . n 
B 1 95  THR 95  396 396 THR THR B . n 
B 1 96  SER 96  397 397 SER SER B . n 
B 1 97  THR 97  398 398 THR THR B . n 
B 1 98  TYR 98  399 399 TYR TYR B . n 
B 1 99  GLN 99  400 400 GLN GLN B . n 
B 1 100 LEU 100 401 401 LEU LEU B . n 
B 1 101 LYS 101 402 402 LYS LYS B . n 
B 1 102 ASP 102 403 403 ASP ASP B . n 
B 1 103 THR 103 404 404 THR THR B . n 
B 1 104 GLU 104 405 405 GLU GLU B . n 
B 1 105 LEU 105 406 406 LEU LEU B . n 
B 1 106 ILE 106 407 407 ILE ILE B . n 
B 1 107 TYR 107 408 408 TYR TYR B . n 
B 1 108 GLY 108 409 409 GLY GLY B . n 
B 1 109 ALA 109 410 410 ALA ALA B . n 
B 1 110 LYS 110 411 411 LYS LYS B . n 
B 1 111 HIS 111 412 412 HIS HIS B . n 
B 1 112 ALA 112 413 413 ALA ALA B . n 
B 1 113 TRP 113 414 414 TRP TRP B . n 
B 1 114 ARG 114 415 415 ARG ARG B . n 
B 1 115 ASN 115 416 416 ASN ASN B . n 
B 1 116 ALA 116 417 417 ALA ALA B . n 
B 1 117 SER 117 418 418 SER SER B . n 
B 1 118 ARG 118 419 419 ARG ARG B . n 
B 1 119 CYS 119 420 420 CYS CYS B . n 
B 1 120 VAL 120 421 421 VAL VAL B . n 
B 1 121 GLY 121 422 422 GLY GLY B . n 
B 1 122 ARG 122 423 423 ARG ARG B . n 
B 1 123 ILE 123 424 424 ILE ILE B . n 
B 1 124 GLN 124 425 425 GLN GLN B . n 
B 1 125 TRP 125 426 426 TRP TRP B . n 
B 1 126 SER 126 427 427 SER SER B . n 
B 1 127 LYS 127 428 428 LYS LYS B . n 
B 1 128 LEU 128 429 429 LEU LEU B . n 
B 1 129 GLN 129 430 430 GLN GLN B . n 
B 1 130 VAL 130 431 431 VAL VAL B . n 
B 1 131 PHE 131 432 432 PHE PHE B . n 
B 1 132 ASP 132 433 433 ASP ASP B . n 
B 1 133 ALA 133 434 434 ALA ALA B . n 
B 1 134 ARG 134 435 435 ARG ARG B . n 
B 1 135 ASP 135 436 436 ASP ASP B . n 
B 1 136 CYS 136 437 437 CYS CYS B . n 
B 1 137 THR 137 438 438 THR THR B . n 
B 1 138 THR 138 439 439 THR THR B . n 
B 1 139 ALA 139 440 440 ALA ALA B . n 
B 1 140 HIS 140 441 441 HIS HIS B . n 
B 1 141 GLY 141 442 442 GLY GLY B . n 
B 1 142 MET 142 443 443 MET MET B . n 
B 1 143 PHE 143 444 444 PHE PHE B . n 
B 1 144 ASN 144 445 445 ASN ASN B . n 
B 1 145 TYR 145 446 446 TYR TYR B . n 
B 1 146 ILE 146 447 447 ILE ILE B . n 
B 1 147 CYS 147 448 448 CYS CYS B . n 
B 1 148 ASN 148 449 449 ASN ASN B . n 
B 1 149 HIS 149 450 450 HIS HIS B . n 
B 1 150 VAL 150 451 451 VAL VAL B . n 
B 1 151 LYS 151 452 452 LYS LYS B . n 
B 1 152 TYR 152 453 453 TYR TYR B . n 
B 1 153 ALA 153 454 454 ALA ALA B . n 
B 1 154 THR 154 455 455 THR THR B . n 
B 1 155 ASN 155 456 456 ASN ASN B . n 
B 1 156 LYS 156 457 457 LYS LYS B . n 
B 1 157 GLY 157 458 458 GLY GLY B . n 
B 1 158 ASN 158 459 459 ASN ASN B . n 
B 1 159 LEU 159 460 460 LEU LEU B . n 
B 1 160 ARG 160 461 461 ARG ARG B . n 
B 1 161 SER 161 462 462 SER SER B . n 
B 1 162 ALA 162 463 463 ALA ALA B . n 
B 1 163 ILE 163 464 464 ILE ILE B . n 
B 1 164 THR 164 465 465 THR THR B . n 
B 1 165 ILE 165 466 466 ILE ILE B . n 
B 1 166 PHE 166 467 467 PHE PHE B . n 
B 1 167 PRO 167 468 468 PRO PRO B . n 
B 1 168 GLN 168 469 469 GLN GLN B . n 
B 1 169 ARG 169 470 470 ARG ARG B . n 
B 1 170 THR 170 471 471 THR THR B . n 
B 1 171 ASP 171 472 472 ASP ASP B . n 
B 1 172 GLY 172 473 473 GLY GLY B . n 
B 1 173 LYS 173 474 474 LYS LYS B . n 
B 1 174 HIS 174 475 475 HIS HIS B . n 
B 1 175 ASP 175 476 476 ASP ASP B . n 
B 1 176 PHE 176 477 477 PHE PHE B . n 
B 1 177 ARG 177 478 478 ARG ARG B . n 
B 1 178 VAL 178 479 479 VAL VAL B . n 
B 1 179 TRP 179 480 480 TRP TRP B . n 
B 1 180 ASN 180 481 481 ASN ASN B . n 
B 1 181 SER 181 482 482 SER SER B . n 
B 1 182 GLN 182 483 483 GLN GLN B . n 
B 1 183 LEU 183 484 484 LEU LEU B . n 
B 1 184 ILE 184 485 485 ILE ILE B . n 
B 1 185 ARG 185 486 486 ARG ARG B . n 
B 1 186 TYR 186 487 487 TYR TYR B . n 
B 1 187 ALA 187 488 488 ALA ALA B . n 
B 1 188 GLY 188 489 489 GLY GLY B . n 
B 1 189 TYR 189 490 490 TYR TYR B . n 
B 1 190 LYS 190 491 491 LYS LYS B . n 
B 1 191 GLN 191 492 492 GLN GLN B . n 
B 1 192 PRO 192 493 493 PRO PRO B . n 
B 1 193 ASP 193 494 494 ASP ASP B . n 
B 1 194 GLY 194 495 495 GLY GLY B . n 
B 1 195 SER 195 496 496 SER SER B . n 
B 1 196 THR 196 497 497 THR THR B . n 
B 1 197 LEU 197 498 498 LEU LEU B . n 
B 1 198 GLY 198 499 499 GLY GLY B . n 
B 1 199 ASP 199 500 500 ASP ASP B . n 
B 1 200 PRO 200 501 501 PRO PRO B . n 
B 1 201 ALA 201 502 502 ALA ALA B . n 
B 1 202 ASN 202 503 503 ASN ASN B . n 
B 1 203 VAL 203 504 504 VAL VAL B . n 
B 1 204 GLN 204 505 505 GLN GLN B . n 
B 1 205 PHE 205 506 506 PHE PHE B . n 
B 1 206 THR 206 507 507 THR THR B . n 
B 1 207 GLU 207 508 508 GLU GLU B . n 
B 1 208 ILE 208 509 509 ILE ILE B . n 
B 1 209 CYS 209 510 510 CYS CYS B . n 
B 1 210 ILE 210 511 511 ILE ILE B . n 
B 1 211 GLN 211 512 512 GLN GLN B . n 
B 1 212 GLN 212 513 513 GLN GLN B . n 
B 1 213 GLY 213 514 514 GLY GLY B . n 
B 1 214 TRP 214 515 515 TRP TRP B . n 
B 1 215 LYS 215 516 516 LYS LYS B . n 
B 1 216 PRO 216 517 517 PRO PRO B . n 
B 1 217 PRO 217 518 518 PRO PRO B . n 
B 1 218 ARG 218 519 519 ARG ARG B . n 
B 1 219 GLY 219 520 520 GLY GLY B . n 
B 1 220 ARG 220 521 521 ARG ARG B . n 
B 1 221 PHE 221 522 522 PHE PHE B . n 
B 1 222 ASP 222 523 523 ASP ASP B . n 
B 1 223 VAL 223 524 524 VAL VAL B . n 
B 1 224 LEU 224 525 525 LEU LEU B . n 
B 1 225 PRO 225 526 526 PRO PRO B . n 
B 1 226 LEU 226 527 527 LEU LEU B . n 
B 1 227 LEU 227 528 528 LEU LEU B . n 
B 1 228 LEU 228 529 529 LEU LEU B . n 
B 1 229 GLN 229 530 530 GLN GLN B . n 
B 1 230 ALA 230 531 531 ALA ALA B . n 
B 1 231 ASN 231 532 532 ASN ASN B . n 
B 1 232 GLY 232 533 533 GLY GLY B . n 
B 1 233 ASN 233 534 534 ASN ASN B . n 
B 1 234 ASP 234 535 535 ASP ASP B . n 
B 1 235 PRO 235 536 536 PRO PRO B . n 
B 1 236 GLU 236 537 537 GLU GLU B . n 
B 1 237 LEU 237 538 538 LEU LEU B . n 
B 1 238 PHE 238 539 539 PHE PHE B . n 
B 1 239 GLN 239 540 540 GLN GLN B . n 
B 1 240 ILE 240 541 541 ILE ILE B . n 
B 1 241 PRO 241 542 542 PRO PRO B . n 
B 1 242 PRO 242 543 543 PRO PRO B . n 
B 1 243 GLU 243 544 544 GLU GLU B . n 
B 1 244 LEU 244 545 545 LEU LEU B . n 
B 1 245 VAL 245 546 546 VAL VAL B . n 
B 1 246 LEU 246 547 547 LEU LEU B . n 
B 1 247 GLU 247 548 548 GLU GLU B . n 
B 1 248 VAL 248 549 549 VAL VAL B . n 
B 1 249 PRO 249 550 550 PRO PRO B . n 
B 1 250 ILE 250 551 551 ILE ILE B . n 
B 1 251 ARG 251 552 552 ARG ARG B . n 
B 1 252 HIS 252 553 553 HIS HIS B . n 
B 1 253 PRO 253 554 554 PRO PRO B . n 
B 1 254 LYS 254 555 555 LYS LYS B . n 
B 1 255 PHE 255 556 556 PHE PHE B . n 
B 1 256 GLU 256 557 557 GLU GLU B . n 
B 1 257 TRP 257 558 558 TRP TRP B . n 
B 1 258 PHE 258 559 559 PHE PHE B . n 
B 1 259 LYS 259 560 560 LYS LYS B . n 
B 1 260 ASP 260 561 561 ASP ASP B . n 
B 1 261 LEU 261 562 562 LEU LEU B . n 
B 1 262 GLY 262 563 563 GLY GLY B . n 
B 1 263 LEU 263 564 564 LEU LEU B . n 
B 1 264 LYS 264 565 565 LYS LYS B . n 
B 1 265 TRP 265 566 566 TRP TRP B . n 
B 1 266 TYR 266 567 567 TYR TYR B . n 
B 1 267 GLY 267 568 568 GLY GLY B . n 
B 1 268 LEU 268 569 569 LEU LEU B . n 
B 1 269 PRO 269 570 570 PRO PRO B . n 
B 1 270 ALA 270 571 571 ALA ALA B . n 
B 1 271 VAL 271 572 572 VAL VAL B . n 
B 1 272 SER 272 573 573 SER SER B . n 
B 1 273 ASN 273 574 574 ASN ASN B . n 
B 1 274 MET 274 575 575 MET MET B . n 
B 1 275 LEU 275 576 576 LEU LEU B . n 
B 1 276 LEU 276 577 577 LEU LEU B . n 
B 1 277 GLU 277 578 578 GLU GLU B . n 
B 1 278 ILE 278 579 579 ILE ILE B . n 
B 1 279 GLY 279 580 580 GLY GLY B . n 
B 1 280 GLY 280 581 581 GLY GLY B . n 
B 1 281 LEU 281 582 582 LEU LEU B . n 
B 1 282 GLU 282 583 583 GLU GLU B . n 
B 1 283 PHE 283 584 584 PHE PHE B . n 
B 1 284 SER 284 585 585 SER SER B . n 
B 1 285 ALA 285 586 586 ALA ALA B . n 
B 1 286 CYS 286 587 587 CYS CYS B . n 
B 1 287 PRO 287 588 588 PRO PRO B . n 
B 1 288 PHE 288 589 589 PHE PHE B . n 
B 1 289 SER 289 590 590 SER SER B . n 
B 1 290 GLY 290 591 591 GLY GLY B . n 
B 1 291 TRP 291 592 592 TRP TRP B . n 
B 1 292 TYR 292 593 593 TYR TYR B . n 
B 1 293 MET 293 594 594 MET MET B . n 
B 1 294 GLY 294 595 595 GLY GLY B . n 
B 1 295 THR 295 596 596 THR THR B . n 
B 1 296 GLU 296 597 597 GLU GLU B . n 
B 1 297 ILE 297 598 598 ILE ILE B . n 
B 1 298 GLY 298 599 599 GLY GLY B . n 
B 1 299 VAL 299 600 600 VAL VAL B . n 
B 1 300 ARG 300 601 601 ARG ARG B . n 
B 1 301 ASP 301 602 602 ASP ASP B . n 
B 1 302 TYR 302 603 603 TYR TYR B . n 
B 1 303 CYS 303 604 604 CYS CYS B . n 
B 1 304 ASP 304 605 605 ASP ASP B . n 
B 1 305 ASN 305 606 606 ASN ASN B . n 
B 1 306 SER 306 607 607 SER SER B . n 
B 1 307 ARG 307 608 608 ARG ARG B . n 
B 1 308 TYR 308 609 609 TYR TYR B . n 
B 1 309 ASN 309 610 610 ASN ASN B . n 
B 1 310 ILE 310 611 611 ILE ILE B . n 
B 1 311 LEU 311 612 612 LEU LEU B . n 
B 1 312 GLU 312 613 613 GLU GLU B . n 
B 1 313 GLU 313 614 614 GLU GLU B . n 
B 1 314 VAL 314 615 615 VAL VAL B . n 
B 1 315 ALA 315 616 616 ALA ALA B . n 
B 1 316 LYS 316 617 617 LYS LYS B . n 
B 1 317 LYS 317 618 618 LYS LYS B . n 
B 1 318 MET 318 619 619 MET MET B . n 
B 1 319 ASN 319 620 620 ASN ASN B . n 
B 1 320 LEU 320 621 621 LEU LEU B . n 
B 1 321 ASP 321 622 622 ASP ASP B . n 
B 1 322 MET 322 623 623 MET MET B . n 
B 1 323 ARG 323 624 624 ARG ARG B . n 
B 1 324 LYS 324 625 625 LYS LYS B . n 
B 1 325 THR 325 626 626 THR THR B . n 
B 1 326 SER 326 627 627 SER SER B . n 
B 1 327 SER 327 628 628 SER SER B . n 
B 1 328 LEU 328 629 629 LEU LEU B . n 
B 1 329 TRP 329 630 630 TRP TRP B . n 
B 1 330 LYS 330 631 631 LYS LYS B . n 
B 1 331 ASP 331 632 632 ASP ASP B . n 
B 1 332 GLN 332 633 633 GLN GLN B . n 
B 1 333 ALA 333 634 634 ALA ALA B . n 
B 1 334 LEU 334 635 635 LEU LEU B . n 
B 1 335 VAL 335 636 636 VAL VAL B . n 
B 1 336 GLU 336 637 637 GLU GLU B . n 
B 1 337 ILE 337 638 638 ILE ILE B . n 
B 1 338 ASN 338 639 639 ASN ASN B . n 
B 1 339 ILE 339 640 640 ILE ILE B . n 
B 1 340 ALA 340 641 641 ALA ALA B . n 
B 1 341 VAL 341 642 642 VAL VAL B . n 
B 1 342 LEU 342 643 643 LEU LEU B . n 
B 1 343 TYR 343 644 644 TYR TYR B . n 
B 1 344 SER 344 645 645 SER SER B . n 
B 1 345 PHE 345 646 646 PHE PHE B . n 
B 1 346 GLN 346 647 647 GLN GLN B . n 
B 1 347 SER 347 648 648 SER SER B . n 
B 1 348 ASP 348 649 649 ASP ASP B . n 
B 1 349 LYS 349 650 650 LYS LYS B . n 
B 1 350 VAL 350 651 651 VAL VAL B . n 
B 1 351 THR 351 652 652 THR THR B . n 
B 1 352 ILE 352 653 653 ILE ILE B . n 
B 1 353 VAL 353 654 654 VAL VAL B . n 
B 1 354 ASP 354 655 655 ASP ASP B . n 
B 1 355 HIS 355 656 656 HIS HIS B . n 
B 1 356 HIS 356 657 657 HIS HIS B . n 
B 1 357 SER 357 658 658 SER SER B . n 
B 1 358 ALA 358 659 659 ALA ALA B . n 
B 1 359 THR 359 660 660 THR THR B . n 
B 1 360 GLU 360 661 661 GLU GLU B . n 
B 1 361 SER 361 662 662 SER SER B . n 
B 1 362 PHE 362 663 663 PHE PHE B . n 
B 1 363 ILE 363 664 664 ILE ILE B . n 
B 1 364 LYS 364 665 665 LYS LYS B . n 
B 1 365 HIS 365 666 666 HIS HIS B . n 
B 1 366 MET 366 667 667 MET MET B . n 
B 1 367 GLU 367 668 668 GLU GLU B . n 
B 1 368 ASN 368 669 669 ASN ASN B . n 
B 1 369 GLU 369 670 670 GLU GLU B . n 
B 1 370 TYR 370 671 671 TYR TYR B . n 
B 1 371 ARG 371 672 672 ARG ARG B . n 
B 1 372 CYS 372 673 673 CYS CYS B . n 
B 1 373 ARG 373 674 674 ARG ARG B . n 
B 1 374 GLY 374 675 675 GLY GLY B . n 
B 1 375 GLY 375 676 676 GLY GLY B . n 
B 1 376 CYS 376 677 677 CYS CYS B . n 
B 1 377 PRO 377 678 678 PRO PRO B . n 
B 1 378 ALA 378 679 679 ALA ALA B . n 
B 1 379 ASP 379 680 680 ASP ASP B . n 
B 1 380 TRP 380 681 681 TRP TRP B . n 
B 1 381 VAL 381 682 682 VAL VAL B . n 
B 1 382 TRP 382 683 683 TRP TRP B . n 
B 1 383 ILE 383 684 684 ILE ILE B . n 
B 1 384 VAL 384 685 685 VAL VAL B . n 
B 1 385 PRO 385 686 686 PRO PRO B . n 
B 1 386 PRO 386 687 687 PRO PRO B . n 
B 1 387 MET 387 688 688 MET MET B . n 
B 1 388 SER 388 689 689 SER SER B . n 
B 1 389 GLY 389 690 690 GLY GLY B . n 
B 1 390 SER 390 691 691 SER SER B . n 
B 1 391 ILE 391 692 692 ILE ILE B . n 
B 1 392 THR 392 693 693 THR THR B . n 
B 1 393 PRO 393 694 694 PRO PRO B . n 
B 1 394 VAL 394 695 695 VAL VAL B . n 
B 1 395 PHE 395 696 696 PHE PHE B . n 
B 1 396 HIS 396 697 697 HIS HIS B . n 
B 1 397 GLN 397 698 698 GLN GLN B . n 
B 1 398 GLU 398 699 699 GLU GLU B . n 
B 1 399 MET 399 700 700 MET MET B . n 
B 1 400 LEU 400 701 701 LEU LEU B . n 
B 1 401 ASN 401 702 702 ASN ASN B . n 
B 1 402 TYR 402 703 703 TYR TYR B . n 
B 1 403 ARG 403 704 704 ARG ARG B . n 
B 1 404 LEU 404 705 705 LEU LEU B . n 
B 1 405 THR 405 706 706 THR THR B . n 
B 1 406 PRO 406 707 707 PRO PRO B . n 
B 1 407 SER 407 708 708 SER SER B . n 
B 1 408 PHE 408 709 709 PHE PHE B . n 
B 1 409 GLU 409 710 710 GLU GLU B . n 
B 1 410 TYR 410 711 711 TYR TYR B . n 
B 1 411 GLN 411 712 712 GLN GLN B . n 
B 1 412 PRO 412 713 713 PRO PRO B . n 
B 1 413 ASP 413 714 714 ASP ASP B . n 
B 1 414 PRO 414 715 715 PRO PRO B . n 
B 1 415 TRP 415 716 716 TRP TRP B . n 
B 1 416 ASN 416 717 717 ASN ASN B . n 
B 1 417 THR 417 718 718 THR THR B . n 
B 1 418 HIS 418 719 719 HIS HIS B . n 
B 1 419 VAL 419 720 720 VAL VAL B . n 
B 1 420 TRP 420 721 721 TRP TRP B . n 
B 1 421 LYS 421 722 722 LYS LYS B . n 
B 1 422 LEU 422 723 ?   ?   ?   B . n 
B 1 423 VAL 423 724 ?   ?   ?   B . n 
C 1 1   CYS 1   302 ?   ?   ?   C . n 
C 1 2   PRO 2   303 303 PRO PRO C . n 
C 1 3   ARG 3   304 304 ARG ARG C . n 
C 1 4   PHE 4   305 305 PHE PHE C . n 
C 1 5   LEU 5   306 306 LEU LEU C . n 
C 1 6   LYS 6   307 307 LYS LYS C . n 
C 1 7   VAL 7   308 308 VAL VAL C . n 
C 1 8   LYS 8   309 309 LYS LYS C . n 
C 1 9   ASN 9   310 310 ASN ASN C . n 
C 1 10  TRP 10  311 311 TRP TRP C . n 
C 1 11  GLU 11  312 312 GLU GLU C . n 
C 1 12  THR 12  313 313 THR THR C . n 
C 1 13  GLU 13  314 314 GLU GLU C . n 
C 1 14  VAL 14  315 315 VAL VAL C . n 
C 1 15  VAL 15  316 316 VAL VAL C . n 
C 1 16  LEU 16  317 317 LEU LEU C . n 
C 1 17  THR 17  318 318 THR THR C . n 
C 1 18  ASP 18  319 319 ASP ASP C . n 
C 1 19  THR 19  320 320 THR THR C . n 
C 1 20  LEU 20  321 321 LEU LEU C . n 
C 1 21  HIS 21  322 322 HIS HIS C . n 
C 1 22  LEU 22  323 323 LEU LEU C . n 
C 1 23  LYS 23  324 324 LYS LYS C . n 
C 1 24  SER 24  325 325 SER SER C . n 
C 1 25  THR 25  326 326 THR THR C . n 
C 1 26  LEU 26  327 327 LEU LEU C . n 
C 1 27  GLU 27  328 328 GLU GLU C . n 
C 1 28  THR 28  329 329 THR THR C . n 
C 1 29  GLY 29  330 330 GLY GLY C . n 
C 1 30  CYS 30  331 331 CYS CYS C . n 
C 1 31  THR 31  332 332 THR THR C . n 
C 1 32  GLU 32  333 333 GLU GLU C . n 
C 1 33  TYR 33  334 334 TYR TYR C . n 
C 1 34  ILE 34  335 335 ILE ILE C . n 
C 1 35  CYS 35  336 336 CYS CYS C . n 
C 1 36  MET 36  337 337 MET MET C . n 
C 1 37  GLY 37  338 338 GLY GLY C . n 
C 1 38  SER 38  339 339 SER SER C . n 
C 1 39  ILE 39  340 340 ILE ILE C . n 
C 1 40  MET 40  341 341 MET MET C . n 
C 1 41  HIS 41  342 342 HIS HIS C . n 
C 1 42  PRO 42  343 343 PRO PRO C . n 
C 1 43  SER 43  344 344 SER SER C . n 
C 1 44  GLN 44  345 345 GLN GLN C . n 
C 1 45  HIS 45  346 346 HIS HIS C . n 
C 1 46  ALA 46  347 347 ALA ALA C . n 
C 1 47  ARG 47  348 348 ARG ARG C . n 
C 1 48  ARG 48  349 349 ARG ARG C . n 
C 1 49  PRO 49  350 350 PRO PRO C . n 
C 1 50  GLU 50  351 351 GLU GLU C . n 
C 1 51  ASP 51  352 352 ASP ASP C . n 
C 1 52  VAL 52  353 353 VAL VAL C . n 
C 1 53  ALA 53  354 354 ALA ALA C . n 
C 1 54  THR 54  355 355 THR THR C . n 
C 1 55  LYS 55  356 356 LYS LYS C . n 
C 1 56  ASP 56  357 357 ASP ASP C . n 
C 1 57  GLN 57  358 358 GLN GLN C . n 
C 1 58  LEU 58  359 359 LEU LEU C . n 
C 1 59  PHE 59  360 360 PHE PHE C . n 
C 1 60  PRO 60  361 361 PRO PRO C . n 
C 1 61  LEU 61  362 362 LEU LEU C . n 
C 1 62  ALA 62  363 363 ALA ALA C . n 
C 1 63  LYS 63  364 364 LYS LYS C . n 
C 1 64  GLU 64  365 365 GLU GLU C . n 
C 1 65  PHE 65  366 366 PHE PHE C . n 
C 1 66  ILE 66  367 367 ILE ILE C . n 
C 1 67  ASP 67  368 368 ASP ASP C . n 
C 1 68  GLN 68  369 369 GLN GLN C . n 
C 1 69  TYR 69  370 370 TYR TYR C . n 
C 1 70  TYR 70  371 371 TYR TYR C . n 
C 1 71  SER 71  372 372 SER SER C . n 
C 1 72  SER 72  373 373 SER SER C . n 
C 1 73  ILE 73  374 374 ILE ILE C . n 
C 1 74  LYS 74  375 375 LYS LYS C . n 
C 1 75  ARG 75  376 376 ARG ARG C . n 
C 1 76  PHE 76  377 377 PHE PHE C . n 
C 1 77  GLY 77  378 378 GLY GLY C . n 
C 1 78  SER 78  379 379 SER SER C . n 
C 1 79  LYS 79  380 380 LYS LYS C . n 
C 1 80  ALA 80  381 381 ALA ALA C . n 
C 1 81  HIS 81  382 382 HIS HIS C . n 
C 1 82  MET 82  383 383 MET MET C . n 
C 1 83  GLU 83  384 384 GLU GLU C . n 
C 1 84  ARG 84  385 385 ARG ARG C . n 
C 1 85  LEU 85  386 386 LEU LEU C . n 
C 1 86  GLU 86  387 387 GLU GLU C . n 
C 1 87  GLU 87  388 388 GLU GLU C . n 
C 1 88  VAL 88  389 389 VAL VAL C . n 
C 1 89  ASN 89  390 390 ASN ASN C . n 
C 1 90  LYS 90  391 391 LYS LYS C . n 
C 1 91  GLU 91  392 392 GLU GLU C . n 
C 1 92  ILE 92  393 393 ILE ILE C . n 
C 1 93  ASP 93  394 394 ASP ASP C . n 
C 1 94  THR 94  395 395 THR THR C . n 
C 1 95  THR 95  396 396 THR THR C . n 
C 1 96  SER 96  397 397 SER SER C . n 
C 1 97  THR 97  398 398 THR THR C . n 
C 1 98  TYR 98  399 399 TYR TYR C . n 
C 1 99  GLN 99  400 400 GLN GLN C . n 
C 1 100 LEU 100 401 401 LEU LEU C . n 
C 1 101 LYS 101 402 402 LYS LYS C . n 
C 1 102 ASP 102 403 403 ASP ASP C . n 
C 1 103 THR 103 404 404 THR THR C . n 
C 1 104 GLU 104 405 405 GLU GLU C . n 
C 1 105 LEU 105 406 406 LEU LEU C . n 
C 1 106 ILE 106 407 407 ILE ILE C . n 
C 1 107 TYR 107 408 408 TYR TYR C . n 
C 1 108 GLY 108 409 409 GLY GLY C . n 
C 1 109 ALA 109 410 410 ALA ALA C . n 
C 1 110 LYS 110 411 411 LYS LYS C . n 
C 1 111 HIS 111 412 412 HIS HIS C . n 
C 1 112 ALA 112 413 413 ALA ALA C . n 
C 1 113 TRP 113 414 414 TRP TRP C . n 
C 1 114 ARG 114 415 415 ARG ARG C . n 
C 1 115 ASN 115 416 416 ASN ASN C . n 
C 1 116 ALA 116 417 417 ALA ALA C . n 
C 1 117 SER 117 418 418 SER SER C . n 
C 1 118 ARG 118 419 419 ARG ARG C . n 
C 1 119 CYS 119 420 420 CYS CYS C . n 
C 1 120 VAL 120 421 421 VAL VAL C . n 
C 1 121 GLY 121 422 422 GLY GLY C . n 
C 1 122 ARG 122 423 423 ARG ARG C . n 
C 1 123 ILE 123 424 424 ILE ILE C . n 
C 1 124 GLN 124 425 425 GLN GLN C . n 
C 1 125 TRP 125 426 426 TRP TRP C . n 
C 1 126 SER 126 427 427 SER SER C . n 
C 1 127 LYS 127 428 428 LYS LYS C . n 
C 1 128 LEU 128 429 429 LEU LEU C . n 
C 1 129 GLN 129 430 430 GLN GLN C . n 
C 1 130 VAL 130 431 431 VAL VAL C . n 
C 1 131 PHE 131 432 432 PHE PHE C . n 
C 1 132 ASP 132 433 433 ASP ASP C . n 
C 1 133 ALA 133 434 434 ALA ALA C . n 
C 1 134 ARG 134 435 435 ARG ARG C . n 
C 1 135 ASP 135 436 436 ASP ASP C . n 
C 1 136 CYS 136 437 437 CYS CYS C . n 
C 1 137 THR 137 438 438 THR THR C . n 
C 1 138 THR 138 439 439 THR THR C . n 
C 1 139 ALA 139 440 440 ALA ALA C . n 
C 1 140 HIS 140 441 441 HIS HIS C . n 
C 1 141 GLY 141 442 442 GLY GLY C . n 
C 1 142 MET 142 443 443 MET MET C . n 
C 1 143 PHE 143 444 444 PHE PHE C . n 
C 1 144 ASN 144 445 445 ASN ASN C . n 
C 1 145 TYR 145 446 446 TYR TYR C . n 
C 1 146 ILE 146 447 447 ILE ILE C . n 
C 1 147 CYS 147 448 448 CYS CYS C . n 
C 1 148 ASN 148 449 449 ASN ASN C . n 
C 1 149 HIS 149 450 450 HIS HIS C . n 
C 1 150 VAL 150 451 451 VAL VAL C . n 
C 1 151 LYS 151 452 452 LYS LYS C . n 
C 1 152 TYR 152 453 453 TYR TYR C . n 
C 1 153 ALA 153 454 454 ALA ALA C . n 
C 1 154 THR 154 455 455 THR THR C . n 
C 1 155 ASN 155 456 456 ASN ASN C . n 
C 1 156 LYS 156 457 457 LYS LYS C . n 
C 1 157 GLY 157 458 458 GLY GLY C . n 
C 1 158 ASN 158 459 459 ASN ASN C . n 
C 1 159 LEU 159 460 460 LEU LEU C . n 
C 1 160 ARG 160 461 461 ARG ARG C . n 
C 1 161 SER 161 462 462 SER SER C . n 
C 1 162 ALA 162 463 463 ALA ALA C . n 
C 1 163 ILE 163 464 464 ILE ILE C . n 
C 1 164 THR 164 465 465 THR THR C . n 
C 1 165 ILE 165 466 466 ILE ILE C . n 
C 1 166 PHE 166 467 467 PHE PHE C . n 
C 1 167 PRO 167 468 468 PRO PRO C . n 
C 1 168 GLN 168 469 469 GLN GLN C . n 
C 1 169 ARG 169 470 470 ARG ARG C . n 
C 1 170 THR 170 471 471 THR THR C . n 
C 1 171 ASP 171 472 472 ASP ASP C . n 
C 1 172 GLY 172 473 473 GLY GLY C . n 
C 1 173 LYS 173 474 474 LYS LYS C . n 
C 1 174 HIS 174 475 475 HIS HIS C . n 
C 1 175 ASP 175 476 476 ASP ASP C . n 
C 1 176 PHE 176 477 477 PHE PHE C . n 
C 1 177 ARG 177 478 478 ARG ARG C . n 
C 1 178 VAL 178 479 479 VAL VAL C . n 
C 1 179 TRP 179 480 480 TRP TRP C . n 
C 1 180 ASN 180 481 481 ASN ASN C . n 
C 1 181 SER 181 482 482 SER SER C . n 
C 1 182 GLN 182 483 483 GLN GLN C . n 
C 1 183 LEU 183 484 484 LEU LEU C . n 
C 1 184 ILE 184 485 485 ILE ILE C . n 
C 1 185 ARG 185 486 486 ARG ARG C . n 
C 1 186 TYR 186 487 487 TYR TYR C . n 
C 1 187 ALA 187 488 488 ALA ALA C . n 
C 1 188 GLY 188 489 489 GLY GLY C . n 
C 1 189 TYR 189 490 490 TYR TYR C . n 
C 1 190 LYS 190 491 491 LYS LYS C . n 
C 1 191 GLN 191 492 492 GLN GLN C . n 
C 1 192 PRO 192 493 493 PRO PRO C . n 
C 1 193 ASP 193 494 494 ASP ASP C . n 
C 1 194 GLY 194 495 495 GLY GLY C . n 
C 1 195 SER 195 496 496 SER SER C . n 
C 1 196 THR 196 497 497 THR THR C . n 
C 1 197 LEU 197 498 498 LEU LEU C . n 
C 1 198 GLY 198 499 499 GLY GLY C . n 
C 1 199 ASP 199 500 500 ASP ASP C . n 
C 1 200 PRO 200 501 501 PRO PRO C . n 
C 1 201 ALA 201 502 502 ALA ALA C . n 
C 1 202 ASN 202 503 503 ASN ASN C . n 
C 1 203 VAL 203 504 504 VAL VAL C . n 
C 1 204 GLN 204 505 505 GLN GLN C . n 
C 1 205 PHE 205 506 506 PHE PHE C . n 
C 1 206 THR 206 507 507 THR THR C . n 
C 1 207 GLU 207 508 508 GLU GLU C . n 
C 1 208 ILE 208 509 509 ILE ILE C . n 
C 1 209 CYS 209 510 510 CYS CYS C . n 
C 1 210 ILE 210 511 511 ILE ILE C . n 
C 1 211 GLN 211 512 512 GLN GLN C . n 
C 1 212 GLN 212 513 513 GLN GLN C . n 
C 1 213 GLY 213 514 514 GLY GLY C . n 
C 1 214 TRP 214 515 515 TRP TRP C . n 
C 1 215 LYS 215 516 516 LYS LYS C . n 
C 1 216 PRO 216 517 517 PRO PRO C . n 
C 1 217 PRO 217 518 518 PRO PRO C . n 
C 1 218 ARG 218 519 519 ARG ARG C . n 
C 1 219 GLY 219 520 520 GLY GLY C . n 
C 1 220 ARG 220 521 521 ARG ARG C . n 
C 1 221 PHE 221 522 522 PHE PHE C . n 
C 1 222 ASP 222 523 523 ASP ASP C . n 
C 1 223 VAL 223 524 524 VAL VAL C . n 
C 1 224 LEU 224 525 525 LEU LEU C . n 
C 1 225 PRO 225 526 526 PRO PRO C . n 
C 1 226 LEU 226 527 527 LEU LEU C . n 
C 1 227 LEU 227 528 528 LEU LEU C . n 
C 1 228 LEU 228 529 529 LEU LEU C . n 
C 1 229 GLN 229 530 530 GLN GLN C . n 
C 1 230 ALA 230 531 531 ALA ALA C . n 
C 1 231 ASN 231 532 532 ASN ASN C . n 
C 1 232 GLY 232 533 533 GLY GLY C . n 
C 1 233 ASN 233 534 534 ASN ASN C . n 
C 1 234 ASP 234 535 535 ASP ASP C . n 
C 1 235 PRO 235 536 536 PRO PRO C . n 
C 1 236 GLU 236 537 537 GLU GLU C . n 
C 1 237 LEU 237 538 538 LEU LEU C . n 
C 1 238 PHE 238 539 539 PHE PHE C . n 
C 1 239 GLN 239 540 540 GLN GLN C . n 
C 1 240 ILE 240 541 541 ILE ILE C . n 
C 1 241 PRO 241 542 542 PRO PRO C . n 
C 1 242 PRO 242 543 543 PRO PRO C . n 
C 1 243 GLU 243 544 544 GLU GLU C . n 
C 1 244 LEU 244 545 545 LEU LEU C . n 
C 1 245 VAL 245 546 546 VAL VAL C . n 
C 1 246 LEU 246 547 547 LEU LEU C . n 
C 1 247 GLU 247 548 548 GLU GLU C . n 
C 1 248 VAL 248 549 549 VAL VAL C . n 
C 1 249 PRO 249 550 550 PRO PRO C . n 
C 1 250 ILE 250 551 551 ILE ILE C . n 
C 1 251 ARG 251 552 552 ARG ARG C . n 
C 1 252 HIS 252 553 553 HIS HIS C . n 
C 1 253 PRO 253 554 554 PRO PRO C . n 
C 1 254 LYS 254 555 555 LYS LYS C . n 
C 1 255 PHE 255 556 556 PHE PHE C . n 
C 1 256 GLU 256 557 557 GLU GLU C . n 
C 1 257 TRP 257 558 558 TRP TRP C . n 
C 1 258 PHE 258 559 559 PHE PHE C . n 
C 1 259 LYS 259 560 560 LYS LYS C . n 
C 1 260 ASP 260 561 561 ASP ASP C . n 
C 1 261 LEU 261 562 562 LEU LEU C . n 
C 1 262 GLY 262 563 563 GLY GLY C . n 
C 1 263 LEU 263 564 564 LEU LEU C . n 
C 1 264 LYS 264 565 565 LYS LYS C . n 
C 1 265 TRP 265 566 566 TRP TRP C . n 
C 1 266 TYR 266 567 567 TYR TYR C . n 
C 1 267 GLY 267 568 568 GLY GLY C . n 
C 1 268 LEU 268 569 569 LEU LEU C . n 
C 1 269 PRO 269 570 570 PRO PRO C . n 
C 1 270 ALA 270 571 571 ALA ALA C . n 
C 1 271 VAL 271 572 572 VAL VAL C . n 
C 1 272 SER 272 573 573 SER SER C . n 
C 1 273 ASN 273 574 574 ASN ASN C . n 
C 1 274 MET 274 575 575 MET MET C . n 
C 1 275 LEU 275 576 576 LEU LEU C . n 
C 1 276 LEU 276 577 577 LEU LEU C . n 
C 1 277 GLU 277 578 578 GLU GLU C . n 
C 1 278 ILE 278 579 579 ILE ILE C . n 
C 1 279 GLY 279 580 580 GLY GLY C . n 
C 1 280 GLY 280 581 581 GLY GLY C . n 
C 1 281 LEU 281 582 582 LEU LEU C . n 
C 1 282 GLU 282 583 583 GLU GLU C . n 
C 1 283 PHE 283 584 584 PHE PHE C . n 
C 1 284 SER 284 585 585 SER SER C . n 
C 1 285 ALA 285 586 586 ALA ALA C . n 
C 1 286 CYS 286 587 587 CYS CYS C . n 
C 1 287 PRO 287 588 588 PRO PRO C . n 
C 1 288 PHE 288 589 589 PHE PHE C . n 
C 1 289 SER 289 590 590 SER SER C . n 
C 1 290 GLY 290 591 591 GLY GLY C . n 
C 1 291 TRP 291 592 592 TRP TRP C . n 
C 1 292 TYR 292 593 593 TYR TYR C . n 
C 1 293 MET 293 594 594 MET MET C . n 
C 1 294 GLY 294 595 595 GLY GLY C . n 
C 1 295 THR 295 596 596 THR THR C . n 
C 1 296 GLU 296 597 597 GLU GLU C . n 
C 1 297 ILE 297 598 598 ILE ILE C . n 
C 1 298 GLY 298 599 599 GLY GLY C . n 
C 1 299 VAL 299 600 600 VAL VAL C . n 
C 1 300 ARG 300 601 601 ARG ARG C . n 
C 1 301 ASP 301 602 602 ASP ASP C . n 
C 1 302 TYR 302 603 603 TYR TYR C . n 
C 1 303 CYS 303 604 604 CYS CYS C . n 
C 1 304 ASP 304 605 605 ASP ASP C . n 
C 1 305 ASN 305 606 606 ASN ASN C . n 
C 1 306 SER 306 607 607 SER SER C . n 
C 1 307 ARG 307 608 608 ARG ARG C . n 
C 1 308 TYR 308 609 609 TYR TYR C . n 
C 1 309 ASN 309 610 610 ASN ASN C . n 
C 1 310 ILE 310 611 611 ILE ILE C . n 
C 1 311 LEU 311 612 612 LEU LEU C . n 
C 1 312 GLU 312 613 613 GLU GLU C . n 
C 1 313 GLU 313 614 614 GLU GLU C . n 
C 1 314 VAL 314 615 615 VAL VAL C . n 
C 1 315 ALA 315 616 616 ALA ALA C . n 
C 1 316 LYS 316 617 617 LYS LYS C . n 
C 1 317 LYS 317 618 618 LYS LYS C . n 
C 1 318 MET 318 619 619 MET MET C . n 
C 1 319 ASN 319 620 620 ASN ASN C . n 
C 1 320 LEU 320 621 621 LEU LEU C . n 
C 1 321 ASP 321 622 622 ASP ASP C . n 
C 1 322 MET 322 623 623 MET MET C . n 
C 1 323 ARG 323 624 624 ARG ARG C . n 
C 1 324 LYS 324 625 625 LYS LYS C . n 
C 1 325 THR 325 626 626 THR THR C . n 
C 1 326 SER 326 627 627 SER SER C . n 
C 1 327 SER 327 628 628 SER SER C . n 
C 1 328 LEU 328 629 629 LEU LEU C . n 
C 1 329 TRP 329 630 630 TRP TRP C . n 
C 1 330 LYS 330 631 631 LYS LYS C . n 
C 1 331 ASP 331 632 632 ASP ASP C . n 
C 1 332 GLN 332 633 633 GLN GLN C . n 
C 1 333 ALA 333 634 634 ALA ALA C . n 
C 1 334 LEU 334 635 635 LEU LEU C . n 
C 1 335 VAL 335 636 636 VAL VAL C . n 
C 1 336 GLU 336 637 637 GLU GLU C . n 
C 1 337 ILE 337 638 638 ILE ILE C . n 
C 1 338 ASN 338 639 639 ASN ASN C . n 
C 1 339 ILE 339 640 640 ILE ILE C . n 
C 1 340 ALA 340 641 641 ALA ALA C . n 
C 1 341 VAL 341 642 642 VAL VAL C . n 
C 1 342 LEU 342 643 643 LEU LEU C . n 
C 1 343 TYR 343 644 644 TYR TYR C . n 
C 1 344 SER 344 645 645 SER SER C . n 
C 1 345 PHE 345 646 646 PHE PHE C . n 
C 1 346 GLN 346 647 647 GLN GLN C . n 
C 1 347 SER 347 648 648 SER SER C . n 
C 1 348 ASP 348 649 649 ASP ASP C . n 
C 1 349 LYS 349 650 650 LYS LYS C . n 
C 1 350 VAL 350 651 651 VAL VAL C . n 
C 1 351 THR 351 652 652 THR THR C . n 
C 1 352 ILE 352 653 653 ILE ILE C . n 
C 1 353 VAL 353 654 654 VAL VAL C . n 
C 1 354 ASP 354 655 655 ASP ASP C . n 
C 1 355 HIS 355 656 656 HIS HIS C . n 
C 1 356 HIS 356 657 657 HIS HIS C . n 
C 1 357 SER 357 658 658 SER SER C . n 
C 1 358 ALA 358 659 659 ALA ALA C . n 
C 1 359 THR 359 660 660 THR THR C . n 
C 1 360 GLU 360 661 661 GLU GLU C . n 
C 1 361 SER 361 662 662 SER SER C . n 
C 1 362 PHE 362 663 663 PHE PHE C . n 
C 1 363 ILE 363 664 664 ILE ILE C . n 
C 1 364 LYS 364 665 665 LYS LYS C . n 
C 1 365 HIS 365 666 666 HIS HIS C . n 
C 1 366 MET 366 667 667 MET MET C . n 
C 1 367 GLU 367 668 668 GLU GLU C . n 
C 1 368 ASN 368 669 669 ASN ASN C . n 
C 1 369 GLU 369 670 670 GLU GLU C . n 
C 1 370 TYR 370 671 671 TYR TYR C . n 
C 1 371 ARG 371 672 672 ARG ARG C . n 
C 1 372 CYS 372 673 673 CYS CYS C . n 
C 1 373 ARG 373 674 674 ARG ARG C . n 
C 1 374 GLY 374 675 675 GLY GLY C . n 
C 1 375 GLY 375 676 676 GLY GLY C . n 
C 1 376 CYS 376 677 677 CYS CYS C . n 
C 1 377 PRO 377 678 678 PRO PRO C . n 
C 1 378 ALA 378 679 679 ALA ALA C . n 
C 1 379 ASP 379 680 680 ASP ASP C . n 
C 1 380 TRP 380 681 681 TRP TRP C . n 
C 1 381 VAL 381 682 682 VAL VAL C . n 
C 1 382 TRP 382 683 683 TRP TRP C . n 
C 1 383 ILE 383 684 684 ILE ILE C . n 
C 1 384 VAL 384 685 685 VAL VAL C . n 
C 1 385 PRO 385 686 686 PRO PRO C . n 
C 1 386 PRO 386 687 687 PRO PRO C . n 
C 1 387 MET 387 688 688 MET MET C . n 
C 1 388 SER 388 689 689 SER SER C . n 
C 1 389 GLY 389 690 690 GLY GLY C . n 
C 1 390 SER 390 691 691 SER SER C . n 
C 1 391 ILE 391 692 692 ILE ILE C . n 
C 1 392 THR 392 693 693 THR THR C . n 
C 1 393 PRO 393 694 694 PRO PRO C . n 
C 1 394 VAL 394 695 695 VAL VAL C . n 
C 1 395 PHE 395 696 696 PHE PHE C . n 
C 1 396 HIS 396 697 697 HIS HIS C . n 
C 1 397 GLN 397 698 698 GLN GLN C . n 
C 1 398 GLU 398 699 699 GLU GLU C . n 
C 1 399 MET 399 700 700 MET MET C . n 
C 1 400 LEU 400 701 701 LEU LEU C . n 
C 1 401 ASN 401 702 702 ASN ASN C . n 
C 1 402 TYR 402 703 703 TYR TYR C . n 
C 1 403 ARG 403 704 704 ARG ARG C . n 
C 1 404 LEU 404 705 705 LEU LEU C . n 
C 1 405 THR 405 706 706 THR THR C . n 
C 1 406 PRO 406 707 707 PRO PRO C . n 
C 1 407 SER 407 708 708 SER SER C . n 
C 1 408 PHE 408 709 709 PHE PHE C . n 
C 1 409 GLU 409 710 710 GLU GLU C . n 
C 1 410 TYR 410 711 711 TYR TYR C . n 
C 1 411 GLN 411 712 712 GLN GLN C . n 
C 1 412 PRO 412 713 713 PRO PRO C . n 
C 1 413 ASP 413 714 714 ASP ASP C . n 
C 1 414 PRO 414 715 715 PRO PRO C . n 
C 1 415 TRP 415 716 716 TRP TRP C . n 
C 1 416 ASN 416 717 717 ASN ASN C . n 
C 1 417 THR 417 718 718 THR THR C . n 
C 1 418 HIS 418 719 719 HIS HIS C . n 
C 1 419 VAL 419 720 720 VAL VAL C . n 
C 1 420 TRP 420 721 721 TRP TRP C . n 
C 1 421 LYS 421 722 722 LYS LYS C . n 
C 1 422 LEU 422 723 ?   ?   ?   C . n 
C 1 423 VAL 423 724 ?   ?   ?   C . n 
D 1 1   CYS 1   302 ?   ?   ?   D . n 
D 1 2   PRO 2   303 ?   ?   ?   D . n 
D 1 3   ARG 3   304 304 ARG ARG D . n 
D 1 4   PHE 4   305 305 PHE PHE D . n 
D 1 5   LEU 5   306 306 LEU LEU D . n 
D 1 6   LYS 6   307 307 LYS LYS D . n 
D 1 7   VAL 7   308 308 VAL VAL D . n 
D 1 8   LYS 8   309 309 LYS LYS D . n 
D 1 9   ASN 9   310 310 ASN ASN D . n 
D 1 10  TRP 10  311 311 TRP TRP D . n 
D 1 11  GLU 11  312 312 GLU GLU D . n 
D 1 12  THR 12  313 313 THR THR D . n 
D 1 13  GLU 13  314 314 GLU GLU D . n 
D 1 14  VAL 14  315 315 VAL VAL D . n 
D 1 15  VAL 15  316 316 VAL VAL D . n 
D 1 16  LEU 16  317 317 LEU LEU D . n 
D 1 17  THR 17  318 318 THR THR D . n 
D 1 18  ASP 18  319 319 ASP ASP D . n 
D 1 19  THR 19  320 320 THR THR D . n 
D 1 20  LEU 20  321 321 LEU LEU D . n 
D 1 21  HIS 21  322 322 HIS HIS D . n 
D 1 22  LEU 22  323 323 LEU LEU D . n 
D 1 23  LYS 23  324 324 LYS LYS D . n 
D 1 24  SER 24  325 325 SER SER D . n 
D 1 25  THR 25  326 326 THR THR D . n 
D 1 26  LEU 26  327 327 LEU LEU D . n 
D 1 27  GLU 27  328 328 GLU GLU D . n 
D 1 28  THR 28  329 329 THR THR D . n 
D 1 29  GLY 29  330 330 GLY GLY D . n 
D 1 30  CYS 30  331 331 CYS CYS D . n 
D 1 31  THR 31  332 332 THR THR D . n 
D 1 32  GLU 32  333 333 GLU GLU D . n 
D 1 33  TYR 33  334 334 TYR TYR D . n 
D 1 34  ILE 34  335 335 ILE ILE D . n 
D 1 35  CYS 35  336 336 CYS CYS D . n 
D 1 36  MET 36  337 337 MET MET D . n 
D 1 37  GLY 37  338 338 GLY GLY D . n 
D 1 38  SER 38  339 339 SER SER D . n 
D 1 39  ILE 39  340 340 ILE ILE D . n 
D 1 40  MET 40  341 341 MET MET D . n 
D 1 41  HIS 41  342 342 HIS HIS D . n 
D 1 42  PRO 42  343 343 PRO PRO D . n 
D 1 43  SER 43  344 344 SER SER D . n 
D 1 44  GLN 44  345 ?   ?   ?   D . n 
D 1 45  HIS 45  346 ?   ?   ?   D . n 
D 1 46  ALA 46  347 ?   ?   ?   D . n 
D 1 47  ARG 47  348 ?   ?   ?   D . n 
D 1 48  ARG 48  349 ?   ?   ?   D . n 
D 1 49  PRO 49  350 350 PRO PRO D . n 
D 1 50  GLU 50  351 351 GLU GLU D . n 
D 1 51  ASP 51  352 352 ASP ASP D . n 
D 1 52  VAL 52  353 353 VAL VAL D . n 
D 1 53  ALA 53  354 354 ALA ALA D . n 
D 1 54  THR 54  355 355 THR THR D . n 
D 1 55  LYS 55  356 356 LYS LYS D . n 
D 1 56  ASP 56  357 357 ASP ASP D . n 
D 1 57  GLN 57  358 358 GLN GLN D . n 
D 1 58  LEU 58  359 359 LEU LEU D . n 
D 1 59  PHE 59  360 360 PHE PHE D . n 
D 1 60  PRO 60  361 361 PRO PRO D . n 
D 1 61  LEU 61  362 362 LEU LEU D . n 
D 1 62  ALA 62  363 363 ALA ALA D . n 
D 1 63  LYS 63  364 364 LYS LYS D . n 
D 1 64  GLU 64  365 365 GLU GLU D . n 
D 1 65  PHE 65  366 366 PHE PHE D . n 
D 1 66  ILE 66  367 367 ILE ILE D . n 
D 1 67  ASP 67  368 368 ASP ASP D . n 
D 1 68  GLN 68  369 369 GLN GLN D . n 
D 1 69  TYR 69  370 370 TYR TYR D . n 
D 1 70  TYR 70  371 371 TYR TYR D . n 
D 1 71  SER 71  372 372 SER SER D . n 
D 1 72  SER 72  373 373 SER SER D . n 
D 1 73  ILE 73  374 374 ILE ILE D . n 
D 1 74  LYS 74  375 375 LYS LYS D . n 
D 1 75  ARG 75  376 376 ARG ARG D . n 
D 1 76  PHE 76  377 377 PHE PHE D . n 
D 1 77  GLY 77  378 378 GLY GLY D . n 
D 1 78  SER 78  379 379 SER SER D . n 
D 1 79  LYS 79  380 380 LYS LYS D . n 
D 1 80  ALA 80  381 381 ALA ALA D . n 
D 1 81  HIS 81  382 382 HIS HIS D . n 
D 1 82  MET 82  383 383 MET MET D . n 
D 1 83  GLU 83  384 384 GLU GLU D . n 
D 1 84  ARG 84  385 385 ARG ARG D . n 
D 1 85  LEU 85  386 386 LEU LEU D . n 
D 1 86  GLU 86  387 387 GLU GLU D . n 
D 1 87  GLU 87  388 388 GLU GLU D . n 
D 1 88  VAL 88  389 389 VAL VAL D . n 
D 1 89  ASN 89  390 390 ASN ASN D . n 
D 1 90  LYS 90  391 391 LYS LYS D . n 
D 1 91  GLU 91  392 392 GLU GLU D . n 
D 1 92  ILE 92  393 393 ILE ILE D . n 
D 1 93  ASP 93  394 394 ASP ASP D . n 
D 1 94  THR 94  395 395 THR THR D . n 
D 1 95  THR 95  396 396 THR THR D . n 
D 1 96  SER 96  397 397 SER SER D . n 
D 1 97  THR 97  398 398 THR THR D . n 
D 1 98  TYR 98  399 399 TYR TYR D . n 
D 1 99  GLN 99  400 400 GLN GLN D . n 
D 1 100 LEU 100 401 401 LEU LEU D . n 
D 1 101 LYS 101 402 402 LYS LYS D . n 
D 1 102 ASP 102 403 403 ASP ASP D . n 
D 1 103 THR 103 404 404 THR THR D . n 
D 1 104 GLU 104 405 405 GLU GLU D . n 
D 1 105 LEU 105 406 406 LEU LEU D . n 
D 1 106 ILE 106 407 407 ILE ILE D . n 
D 1 107 TYR 107 408 408 TYR TYR D . n 
D 1 108 GLY 108 409 409 GLY GLY D . n 
D 1 109 ALA 109 410 410 ALA ALA D . n 
D 1 110 LYS 110 411 411 LYS LYS D . n 
D 1 111 HIS 111 412 412 HIS HIS D . n 
D 1 112 ALA 112 413 413 ALA ALA D . n 
D 1 113 TRP 113 414 414 TRP TRP D . n 
D 1 114 ARG 114 415 415 ARG ARG D . n 
D 1 115 ASN 115 416 416 ASN ASN D . n 
D 1 116 ALA 116 417 417 ALA ALA D . n 
D 1 117 SER 117 418 418 SER SER D . n 
D 1 118 ARG 118 419 419 ARG ARG D . n 
D 1 119 CYS 119 420 420 CYS CYS D . n 
D 1 120 VAL 120 421 421 VAL VAL D . n 
D 1 121 GLY 121 422 422 GLY GLY D . n 
D 1 122 ARG 122 423 423 ARG ARG D . n 
D 1 123 ILE 123 424 424 ILE ILE D . n 
D 1 124 GLN 124 425 425 GLN GLN D . n 
D 1 125 TRP 125 426 426 TRP TRP D . n 
D 1 126 SER 126 427 427 SER SER D . n 
D 1 127 LYS 127 428 428 LYS LYS D . n 
D 1 128 LEU 128 429 429 LEU LEU D . n 
D 1 129 GLN 129 430 430 GLN GLN D . n 
D 1 130 VAL 130 431 431 VAL VAL D . n 
D 1 131 PHE 131 432 432 PHE PHE D . n 
D 1 132 ASP 132 433 433 ASP ASP D . n 
D 1 133 ALA 133 434 434 ALA ALA D . n 
D 1 134 ARG 134 435 435 ARG ARG D . n 
D 1 135 ASP 135 436 436 ASP ASP D . n 
D 1 136 CYS 136 437 437 CYS CYS D . n 
D 1 137 THR 137 438 438 THR THR D . n 
D 1 138 THR 138 439 439 THR THR D . n 
D 1 139 ALA 139 440 440 ALA ALA D . n 
D 1 140 HIS 140 441 441 HIS HIS D . n 
D 1 141 GLY 141 442 442 GLY GLY D . n 
D 1 142 MET 142 443 443 MET MET D . n 
D 1 143 PHE 143 444 444 PHE PHE D . n 
D 1 144 ASN 144 445 445 ASN ASN D . n 
D 1 145 TYR 145 446 446 TYR TYR D . n 
D 1 146 ILE 146 447 447 ILE ILE D . n 
D 1 147 CYS 147 448 448 CYS CYS D . n 
D 1 148 ASN 148 449 449 ASN ASN D . n 
D 1 149 HIS 149 450 450 HIS HIS D . n 
D 1 150 VAL 150 451 451 VAL VAL D . n 
D 1 151 LYS 151 452 452 LYS LYS D . n 
D 1 152 TYR 152 453 453 TYR TYR D . n 
D 1 153 ALA 153 454 454 ALA ALA D . n 
D 1 154 THR 154 455 455 THR THR D . n 
D 1 155 ASN 155 456 456 ASN ASN D . n 
D 1 156 LYS 156 457 457 LYS LYS D . n 
D 1 157 GLY 157 458 458 GLY GLY D . n 
D 1 158 ASN 158 459 459 ASN ASN D . n 
D 1 159 LEU 159 460 460 LEU LEU D . n 
D 1 160 ARG 160 461 461 ARG ARG D . n 
D 1 161 SER 161 462 462 SER SER D . n 
D 1 162 ALA 162 463 463 ALA ALA D . n 
D 1 163 ILE 163 464 464 ILE ILE D . n 
D 1 164 THR 164 465 465 THR THR D . n 
D 1 165 ILE 165 466 466 ILE ILE D . n 
D 1 166 PHE 166 467 467 PHE PHE D . n 
D 1 167 PRO 167 468 468 PRO PRO D . n 
D 1 168 GLN 168 469 469 GLN GLN D . n 
D 1 169 ARG 169 470 470 ARG ARG D . n 
D 1 170 THR 170 471 471 THR THR D . n 
D 1 171 ASP 171 472 472 ASP ASP D . n 
D 1 172 GLY 172 473 473 GLY GLY D . n 
D 1 173 LYS 173 474 474 LYS LYS D . n 
D 1 174 HIS 174 475 475 HIS HIS D . n 
D 1 175 ASP 175 476 476 ASP ASP D . n 
D 1 176 PHE 176 477 477 PHE PHE D . n 
D 1 177 ARG 177 478 478 ARG ARG D . n 
D 1 178 VAL 178 479 479 VAL VAL D . n 
D 1 179 TRP 179 480 480 TRP TRP D . n 
D 1 180 ASN 180 481 481 ASN ASN D . n 
D 1 181 SER 181 482 482 SER SER D . n 
D 1 182 GLN 182 483 483 GLN GLN D . n 
D 1 183 LEU 183 484 484 LEU LEU D . n 
D 1 184 ILE 184 485 485 ILE ILE D . n 
D 1 185 ARG 185 486 486 ARG ARG D . n 
D 1 186 TYR 186 487 487 TYR TYR D . n 
D 1 187 ALA 187 488 488 ALA ALA D . n 
D 1 188 GLY 188 489 489 GLY GLY D . n 
D 1 189 TYR 189 490 490 TYR TYR D . n 
D 1 190 LYS 190 491 491 LYS LYS D . n 
D 1 191 GLN 191 492 492 GLN GLN D . n 
D 1 192 PRO 192 493 493 PRO PRO D . n 
D 1 193 ASP 193 494 494 ASP ASP D . n 
D 1 194 GLY 194 495 495 GLY GLY D . n 
D 1 195 SER 195 496 496 SER SER D . n 
D 1 196 THR 196 497 497 THR THR D . n 
D 1 197 LEU 197 498 498 LEU LEU D . n 
D 1 198 GLY 198 499 499 GLY GLY D . n 
D 1 199 ASP 199 500 500 ASP ASP D . n 
D 1 200 PRO 200 501 501 PRO PRO D . n 
D 1 201 ALA 201 502 502 ALA ALA D . n 
D 1 202 ASN 202 503 503 ASN ASN D . n 
D 1 203 VAL 203 504 504 VAL VAL D . n 
D 1 204 GLN 204 505 505 GLN GLN D . n 
D 1 205 PHE 205 506 506 PHE PHE D . n 
D 1 206 THR 206 507 507 THR THR D . n 
D 1 207 GLU 207 508 508 GLU GLU D . n 
D 1 208 ILE 208 509 509 ILE ILE D . n 
D 1 209 CYS 209 510 510 CYS CYS D . n 
D 1 210 ILE 210 511 511 ILE ILE D . n 
D 1 211 GLN 211 512 512 GLN GLN D . n 
D 1 212 GLN 212 513 513 GLN GLN D . n 
D 1 213 GLY 213 514 514 GLY GLY D . n 
D 1 214 TRP 214 515 515 TRP TRP D . n 
D 1 215 LYS 215 516 516 LYS LYS D . n 
D 1 216 PRO 216 517 517 PRO PRO D . n 
D 1 217 PRO 217 518 518 PRO PRO D . n 
D 1 218 ARG 218 519 519 ARG ARG D . n 
D 1 219 GLY 219 520 520 GLY GLY D . n 
D 1 220 ARG 220 521 521 ARG ARG D . n 
D 1 221 PHE 221 522 522 PHE PHE D . n 
D 1 222 ASP 222 523 523 ASP ASP D . n 
D 1 223 VAL 223 524 524 VAL VAL D . n 
D 1 224 LEU 224 525 525 LEU LEU D . n 
D 1 225 PRO 225 526 526 PRO PRO D . n 
D 1 226 LEU 226 527 527 LEU LEU D . n 
D 1 227 LEU 227 528 528 LEU LEU D . n 
D 1 228 LEU 228 529 529 LEU LEU D . n 
D 1 229 GLN 229 530 530 GLN GLN D . n 
D 1 230 ALA 230 531 531 ALA ALA D . n 
D 1 231 ASN 231 532 532 ASN ASN D . n 
D 1 232 GLY 232 533 533 GLY GLY D . n 
D 1 233 ASN 233 534 534 ASN ASN D . n 
D 1 234 ASP 234 535 535 ASP ASP D . n 
D 1 235 PRO 235 536 536 PRO PRO D . n 
D 1 236 GLU 236 537 537 GLU GLU D . n 
D 1 237 LEU 237 538 538 LEU LEU D . n 
D 1 238 PHE 238 539 539 PHE PHE D . n 
D 1 239 GLN 239 540 540 GLN GLN D . n 
D 1 240 ILE 240 541 541 ILE ILE D . n 
D 1 241 PRO 241 542 542 PRO PRO D . n 
D 1 242 PRO 242 543 543 PRO PRO D . n 
D 1 243 GLU 243 544 544 GLU GLU D . n 
D 1 244 LEU 244 545 545 LEU LEU D . n 
D 1 245 VAL 245 546 546 VAL VAL D . n 
D 1 246 LEU 246 547 547 LEU LEU D . n 
D 1 247 GLU 247 548 548 GLU GLU D . n 
D 1 248 VAL 248 549 549 VAL VAL D . n 
D 1 249 PRO 249 550 550 PRO PRO D . n 
D 1 250 ILE 250 551 551 ILE ILE D . n 
D 1 251 ARG 251 552 552 ARG ARG D . n 
D 1 252 HIS 252 553 553 HIS HIS D . n 
D 1 253 PRO 253 554 554 PRO PRO D . n 
D 1 254 LYS 254 555 555 LYS LYS D . n 
D 1 255 PHE 255 556 556 PHE PHE D . n 
D 1 256 GLU 256 557 557 GLU GLU D . n 
D 1 257 TRP 257 558 558 TRP TRP D . n 
D 1 258 PHE 258 559 559 PHE PHE D . n 
D 1 259 LYS 259 560 560 LYS LYS D . n 
D 1 260 ASP 260 561 561 ASP ASP D . n 
D 1 261 LEU 261 562 562 LEU LEU D . n 
D 1 262 GLY 262 563 563 GLY GLY D . n 
D 1 263 LEU 263 564 564 LEU LEU D . n 
D 1 264 LYS 264 565 565 LYS LYS D . n 
D 1 265 TRP 265 566 566 TRP TRP D . n 
D 1 266 TYR 266 567 567 TYR TYR D . n 
D 1 267 GLY 267 568 568 GLY GLY D . n 
D 1 268 LEU 268 569 569 LEU LEU D . n 
D 1 269 PRO 269 570 570 PRO PRO D . n 
D 1 270 ALA 270 571 571 ALA ALA D . n 
D 1 271 VAL 271 572 572 VAL VAL D . n 
D 1 272 SER 272 573 573 SER SER D . n 
D 1 273 ASN 273 574 574 ASN ASN D . n 
D 1 274 MET 274 575 575 MET MET D . n 
D 1 275 LEU 275 576 576 LEU LEU D . n 
D 1 276 LEU 276 577 577 LEU LEU D . n 
D 1 277 GLU 277 578 578 GLU GLU D . n 
D 1 278 ILE 278 579 579 ILE ILE D . n 
D 1 279 GLY 279 580 580 GLY GLY D . n 
D 1 280 GLY 280 581 581 GLY GLY D . n 
D 1 281 LEU 281 582 582 LEU LEU D . n 
D 1 282 GLU 282 583 583 GLU GLU D . n 
D 1 283 PHE 283 584 584 PHE PHE D . n 
D 1 284 SER 284 585 585 SER SER D . n 
D 1 285 ALA 285 586 586 ALA ALA D . n 
D 1 286 CYS 286 587 587 CYS CYS D . n 
D 1 287 PRO 287 588 588 PRO PRO D . n 
D 1 288 PHE 288 589 589 PHE PHE D . n 
D 1 289 SER 289 590 590 SER SER D . n 
D 1 290 GLY 290 591 591 GLY GLY D . n 
D 1 291 TRP 291 592 592 TRP TRP D . n 
D 1 292 TYR 292 593 593 TYR TYR D . n 
D 1 293 MET 293 594 594 MET MET D . n 
D 1 294 GLY 294 595 595 GLY GLY D . n 
D 1 295 THR 295 596 596 THR THR D . n 
D 1 296 GLU 296 597 597 GLU GLU D . n 
D 1 297 ILE 297 598 598 ILE ILE D . n 
D 1 298 GLY 298 599 599 GLY GLY D . n 
D 1 299 VAL 299 600 600 VAL VAL D . n 
D 1 300 ARG 300 601 601 ARG ARG D . n 
D 1 301 ASP 301 602 602 ASP ASP D . n 
D 1 302 TYR 302 603 603 TYR TYR D . n 
D 1 303 CYS 303 604 604 CYS CYS D . n 
D 1 304 ASP 304 605 605 ASP ASP D . n 
D 1 305 ASN 305 606 606 ASN ASN D . n 
D 1 306 SER 306 607 607 SER SER D . n 
D 1 307 ARG 307 608 608 ARG ARG D . n 
D 1 308 TYR 308 609 609 TYR TYR D . n 
D 1 309 ASN 309 610 610 ASN ASN D . n 
D 1 310 ILE 310 611 611 ILE ILE D . n 
D 1 311 LEU 311 612 612 LEU LEU D . n 
D 1 312 GLU 312 613 613 GLU GLU D . n 
D 1 313 GLU 313 614 614 GLU GLU D . n 
D 1 314 VAL 314 615 615 VAL VAL D . n 
D 1 315 ALA 315 616 616 ALA ALA D . n 
D 1 316 LYS 316 617 617 LYS LYS D . n 
D 1 317 LYS 317 618 618 LYS LYS D . n 
D 1 318 MET 318 619 619 MET MET D . n 
D 1 319 ASN 319 620 620 ASN ASN D . n 
D 1 320 LEU 320 621 621 LEU LEU D . n 
D 1 321 ASP 321 622 622 ASP ASP D . n 
D 1 322 MET 322 623 623 MET MET D . n 
D 1 323 ARG 323 624 624 ARG ARG D . n 
D 1 324 LYS 324 625 625 LYS LYS D . n 
D 1 325 THR 325 626 626 THR THR D . n 
D 1 326 SER 326 627 627 SER SER D . n 
D 1 327 SER 327 628 628 SER SER D . n 
D 1 328 LEU 328 629 629 LEU LEU D . n 
D 1 329 TRP 329 630 630 TRP TRP D . n 
D 1 330 LYS 330 631 631 LYS LYS D . n 
D 1 331 ASP 331 632 632 ASP ASP D . n 
D 1 332 GLN 332 633 633 GLN GLN D . n 
D 1 333 ALA 333 634 634 ALA ALA D . n 
D 1 334 LEU 334 635 635 LEU LEU D . n 
D 1 335 VAL 335 636 636 VAL VAL D . n 
D 1 336 GLU 336 637 637 GLU GLU D . n 
D 1 337 ILE 337 638 638 ILE ILE D . n 
D 1 338 ASN 338 639 639 ASN ASN D . n 
D 1 339 ILE 339 640 640 ILE ILE D . n 
D 1 340 ALA 340 641 641 ALA ALA D . n 
D 1 341 VAL 341 642 642 VAL VAL D . n 
D 1 342 LEU 342 643 643 LEU LEU D . n 
D 1 343 TYR 343 644 644 TYR TYR D . n 
D 1 344 SER 344 645 645 SER SER D . n 
D 1 345 PHE 345 646 646 PHE PHE D . n 
D 1 346 GLN 346 647 647 GLN GLN D . n 
D 1 347 SER 347 648 648 SER SER D . n 
D 1 348 ASP 348 649 649 ASP ASP D . n 
D 1 349 LYS 349 650 650 LYS LYS D . n 
D 1 350 VAL 350 651 651 VAL VAL D . n 
D 1 351 THR 351 652 652 THR THR D . n 
D 1 352 ILE 352 653 653 ILE ILE D . n 
D 1 353 VAL 353 654 654 VAL VAL D . n 
D 1 354 ASP 354 655 655 ASP ASP D . n 
D 1 355 HIS 355 656 656 HIS HIS D . n 
D 1 356 HIS 356 657 657 HIS HIS D . n 
D 1 357 SER 357 658 658 SER SER D . n 
D 1 358 ALA 358 659 659 ALA ALA D . n 
D 1 359 THR 359 660 660 THR THR D . n 
D 1 360 GLU 360 661 661 GLU GLU D . n 
D 1 361 SER 361 662 662 SER SER D . n 
D 1 362 PHE 362 663 663 PHE PHE D . n 
D 1 363 ILE 363 664 664 ILE ILE D . n 
D 1 364 LYS 364 665 665 LYS LYS D . n 
D 1 365 HIS 365 666 666 HIS HIS D . n 
D 1 366 MET 366 667 667 MET MET D . n 
D 1 367 GLU 367 668 668 GLU GLU D . n 
D 1 368 ASN 368 669 669 ASN ASN D . n 
D 1 369 GLU 369 670 670 GLU GLU D . n 
D 1 370 TYR 370 671 671 TYR TYR D . n 
D 1 371 ARG 371 672 672 ARG ARG D . n 
D 1 372 CYS 372 673 673 CYS CYS D . n 
D 1 373 ARG 373 674 674 ARG ARG D . n 
D 1 374 GLY 374 675 675 GLY GLY D . n 
D 1 375 GLY 375 676 676 GLY GLY D . n 
D 1 376 CYS 376 677 677 CYS CYS D . n 
D 1 377 PRO 377 678 678 PRO PRO D . n 
D 1 378 ALA 378 679 679 ALA ALA D . n 
D 1 379 ASP 379 680 680 ASP ASP D . n 
D 1 380 TRP 380 681 681 TRP TRP D . n 
D 1 381 VAL 381 682 682 VAL VAL D . n 
D 1 382 TRP 382 683 683 TRP TRP D . n 
D 1 383 ILE 383 684 684 ILE ILE D . n 
D 1 384 VAL 384 685 685 VAL VAL D . n 
D 1 385 PRO 385 686 686 PRO PRO D . n 
D 1 386 PRO 386 687 687 PRO PRO D . n 
D 1 387 MET 387 688 688 MET MET D . n 
D 1 388 SER 388 689 689 SER SER D . n 
D 1 389 GLY 389 690 690 GLY GLY D . n 
D 1 390 SER 390 691 691 SER SER D . n 
D 1 391 ILE 391 692 692 ILE ILE D . n 
D 1 392 THR 392 693 693 THR THR D . n 
D 1 393 PRO 393 694 694 PRO PRO D . n 
D 1 394 VAL 394 695 695 VAL VAL D . n 
D 1 395 PHE 395 696 696 PHE PHE D . n 
D 1 396 HIS 396 697 697 HIS HIS D . n 
D 1 397 GLN 397 698 698 GLN GLN D . n 
D 1 398 GLU 398 699 699 GLU GLU D . n 
D 1 399 MET 399 700 700 MET MET D . n 
D 1 400 LEU 400 701 701 LEU LEU D . n 
D 1 401 ASN 401 702 702 ASN ASN D . n 
D 1 402 TYR 402 703 703 TYR TYR D . n 
D 1 403 ARG 403 704 704 ARG ARG D . n 
D 1 404 LEU 404 705 705 LEU LEU D . n 
D 1 405 THR 405 706 706 THR THR D . n 
D 1 406 PRO 406 707 707 PRO PRO D . n 
D 1 407 SER 407 708 708 SER SER D . n 
D 1 408 PHE 408 709 709 PHE PHE D . n 
D 1 409 GLU 409 710 710 GLU GLU D . n 
D 1 410 TYR 410 711 711 TYR TYR D . n 
D 1 411 GLN 411 712 712 GLN GLN D . n 
D 1 412 PRO 412 713 713 PRO PRO D . n 
D 1 413 ASP 413 714 714 ASP ASP D . n 
D 1 414 PRO 414 715 715 PRO PRO D . n 
D 1 415 TRP 415 716 716 TRP TRP D . n 
D 1 416 ASN 416 717 717 ASN ASN D . n 
D 1 417 THR 417 718 718 THR THR D . n 
D 1 418 HIS 418 719 719 HIS HIS D . n 
D 1 419 VAL 419 720 720 VAL VAL D . n 
D 1 420 TRP 420 721 721 TRP TRP D . n 
D 1 421 LYS 421 722 722 LYS LYS D . n 
D 1 422 LEU 422 723 ?   ?   ?   D . n 
D 1 423 VAL 423 724 ?   ?   ?   D . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1AZ9 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AZ9 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E  2 HEM   1   801  750 HEM   HEM A . 
F  3 H4B   1   802  760 H4B   BH4 A . 
G  4 A1AZ9 1   803  800 A1AZ9 2V9 A . 
H  5 GOL   1   804  881 GOL   GOL A . 
I  5 GOL   1   805  882 GOL   GOL A . 
J  6 ZN    1   806  900 ZN    ZN  A . 
K  2 HEM   1   801  750 HEM   HEM B . 
L  3 H4B   1   802  760 H4B   BH4 B . 
M  4 A1AZ9 1   803  800 A1AZ9 2V9 B . 
N  5 GOL   1   804  881 GOL   GOL B . 
O  2 HEM   1   801  750 HEM   HEM C . 
P  3 H4B   1   802  760 H4B   BH4 C . 
Q  4 A1AZ9 1   803  800 A1AZ9 2V9 C . 
R  5 GOL   1   804  881 GOL   GOL C . 
S  5 GOL   1   805  882 GOL   GOL C . 
T  6 ZN    1   806  900 ZN    ZN  C . 
U  2 HEM   1   801  750 HEM   HEM D . 
V  3 H4B   1   802  760 H4B   BH4 D . 
W  4 A1AZ9 1   803  800 A1AZ9 2V9 D . 
X  5 GOL   1   804  881 GOL   GOL D . 
Y  7 HOH   1   901  247 HOH   HOH A . 
Y  7 HOH   2   902  254 HOH   HOH A . 
Y  7 HOH   3   903  18  HOH   HOH A . 
Y  7 HOH   4   904  1   HOH   HOH A . 
Y  7 HOH   5   905  236 HOH   HOH A . 
Y  7 HOH   6   906  25  HOH   HOH A . 
Y  7 HOH   7   907  163 HOH   HOH A . 
Y  7 HOH   8   908  251 HOH   HOH A . 
Y  7 HOH   9   909  222 HOH   HOH A . 
Y  7 HOH   10  910  248 HOH   HOH A . 
Y  7 HOH   11  911  2   HOH   HOH A . 
Y  7 HOH   12  912  121 HOH   HOH A . 
Y  7 HOH   13  913  45  HOH   HOH A . 
Y  7 HOH   14  914  50  HOH   HOH A . 
Y  7 HOH   15  915  10  HOH   HOH A . 
Y  7 HOH   16  916  11  HOH   HOH A . 
Y  7 HOH   17  917  259 HOH   HOH A . 
Y  7 HOH   18  918  80  HOH   HOH A . 
Y  7 HOH   19  919  238 HOH   HOH A . 
Y  7 HOH   20  920  48  HOH   HOH A . 
Y  7 HOH   21  921  241 HOH   HOH A . 
Y  7 HOH   22  922  253 HOH   HOH A . 
Y  7 HOH   23  923  44  HOH   HOH A . 
Y  7 HOH   24  924  96  HOH   HOH A . 
Y  7 HOH   25  925  57  HOH   HOH A . 
Y  7 HOH   26  926  194 HOH   HOH A . 
Y  7 HOH   27  927  13  HOH   HOH A . 
Y  7 HOH   28  928  8   HOH   HOH A . 
Y  7 HOH   29  929  138 HOH   HOH A . 
Y  7 HOH   30  930  28  HOH   HOH A . 
Y  7 HOH   31  931  223 HOH   HOH A . 
Y  7 HOH   32  932  95  HOH   HOH A . 
Y  7 HOH   33  933  221 HOH   HOH A . 
Y  7 HOH   34  934  63  HOH   HOH A . 
Y  7 HOH   35  935  155 HOH   HOH A . 
Y  7 HOH   36  936  99  HOH   HOH A . 
Y  7 HOH   37  937  9   HOH   HOH A . 
Y  7 HOH   38  938  119 HOH   HOH A . 
Y  7 HOH   39  939  49  HOH   HOH A . 
Y  7 HOH   40  940  76  HOH   HOH A . 
Y  7 HOH   41  941  134 HOH   HOH A . 
Y  7 HOH   42  942  249 HOH   HOH A . 
Y  7 HOH   43  943  256 HOH   HOH A . 
Y  7 HOH   44  944  136 HOH   HOH A . 
Y  7 HOH   45  945  36  HOH   HOH A . 
Y  7 HOH   46  946  68  HOH   HOH A . 
Y  7 HOH   47  947  139 HOH   HOH A . 
Y  7 HOH   48  948  123 HOH   HOH A . 
Y  7 HOH   49  949  78  HOH   HOH A . 
Y  7 HOH   50  950  276 HOH   HOH A . 
Y  7 HOH   51  951  73  HOH   HOH A . 
Y  7 HOH   52  952  37  HOH   HOH A . 
Y  7 HOH   53  953  15  HOH   HOH A . 
Y  7 HOH   54  954  129 HOH   HOH A . 
Y  7 HOH   55  955  252 HOH   HOH A . 
Y  7 HOH   56  956  33  HOH   HOH A . 
Y  7 HOH   57  957  124 HOH   HOH A . 
Y  7 HOH   58  958  210 HOH   HOH A . 
Y  7 HOH   59  959  107 HOH   HOH A . 
Y  7 HOH   60  960  40  HOH   HOH A . 
Y  7 HOH   61  961  29  HOH   HOH A . 
Y  7 HOH   62  962  258 HOH   HOH A . 
Y  7 HOH   63  963  189 HOH   HOH A . 
Y  7 HOH   64  964  105 HOH   HOH A . 
Y  7 HOH   65  965  197 HOH   HOH A . 
Y  7 HOH   66  966  257 HOH   HOH A . 
Y  7 HOH   67  967  70  HOH   HOH A . 
Y  7 HOH   68  968  23  HOH   HOH A . 
Y  7 HOH   69  969  209 HOH   HOH A . 
Y  7 HOH   70  970  208 HOH   HOH A . 
Y  7 HOH   71  971  250 HOH   HOH A . 
Y  7 HOH   72  972  20  HOH   HOH A . 
Y  7 HOH   73  973  244 HOH   HOH A . 
Y  7 HOH   74  974  43  HOH   HOH A . 
Y  7 HOH   75  975  255 HOH   HOH A . 
Y  7 HOH   76  976  240 HOH   HOH A . 
Y  7 HOH   77  977  260 HOH   HOH A . 
Y  7 HOH   78  978  101 HOH   HOH A . 
Y  7 HOH   79  979  220 HOH   HOH A . 
Y  7 HOH   80  980  232 HOH   HOH A . 
Y  7 HOH   81  981  186 HOH   HOH A . 
Y  7 HOH   82  982  213 HOH   HOH A . 
Y  7 HOH   83  983  245 HOH   HOH A . 
Y  7 HOH   84  984  242 HOH   HOH A . 
Y  7 HOH   85  985  233 HOH   HOH A . 
Y  7 HOH   86  986  214 HOH   HOH A . 
Y  7 HOH   87  987  224 HOH   HOH A . 
Y  7 HOH   88  988  195 HOH   HOH A . 
Y  7 HOH   89  989  243 HOH   HOH A . 
Y  7 HOH   90  990  246 HOH   HOH A . 
Y  7 HOH   91  991  239 HOH   HOH A . 
Y  7 HOH   92  992  98  HOH   HOH A . 
Y  7 HOH   93  993  237 HOH   HOH A . 
Y  7 HOH   94  994  199 HOH   HOH A . 
Z  7 HOH   1   901  277 HOH   HOH B . 
Z  7 HOH   2   902  218 HOH   HOH B . 
Z  7 HOH   3   903  172 HOH   HOH B . 
Z  7 HOH   4   904  145 HOH   HOH B . 
Z  7 HOH   5   905  215 HOH   HOH B . 
Z  7 HOH   6   906  234 HOH   HOH B . 
Z  7 HOH   7   907  24  HOH   HOH B . 
Z  7 HOH   8   908  81  HOH   HOH B . 
Z  7 HOH   9   909  157 HOH   HOH B . 
Z  7 HOH   10  910  118 HOH   HOH B . 
Z  7 HOH   11  911  267 HOH   HOH B . 
Z  7 HOH   12  912  103 HOH   HOH B . 
Z  7 HOH   13  913  51  HOH   HOH B . 
Z  7 HOH   14  914  19  HOH   HOH B . 
Z  7 HOH   15  915  58  HOH   HOH B . 
Z  7 HOH   16  916  143 HOH   HOH B . 
Z  7 HOH   17  917  47  HOH   HOH B . 
Z  7 HOH   18  918  39  HOH   HOH B . 
Z  7 HOH   19  919  16  HOH   HOH B . 
Z  7 HOH   20  920  203 HOH   HOH B . 
Z  7 HOH   21  921  173 HOH   HOH B . 
Z  7 HOH   22  922  108 HOH   HOH B . 
Z  7 HOH   23  923  217 HOH   HOH B . 
Z  7 HOH   24  924  92  HOH   HOH B . 
Z  7 HOH   25  925  278 HOH   HOH B . 
Z  7 HOH   26  926  54  HOH   HOH B . 
Z  7 HOH   27  927  67  HOH   HOH B . 
Z  7 HOH   28  928  27  HOH   HOH B . 
Z  7 HOH   29  929  212 HOH   HOH B . 
Z  7 HOH   30  930  132 HOH   HOH B . 
Z  7 HOH   31  931  56  HOH   HOH B . 
Z  7 HOH   32  932  41  HOH   HOH B . 
Z  7 HOH   33  933  275 HOH   HOH B . 
Z  7 HOH   34  934  82  HOH   HOH B . 
Z  7 HOH   35  935  261 HOH   HOH B . 
Z  7 HOH   36  936  151 HOH   HOH B . 
Z  7 HOH   37  937  205 HOH   HOH B . 
Z  7 HOH   38  938  153 HOH   HOH B . 
Z  7 HOH   39  939  133 HOH   HOH B . 
Z  7 HOH   40  940  201 HOH   HOH B . 
Z  7 HOH   41  941  280 HOH   HOH B . 
Z  7 HOH   42  942  126 HOH   HOH B . 
Z  7 HOH   43  943  264 HOH   HOH B . 
Z  7 HOH   44  944  216 HOH   HOH B . 
Z  7 HOH   45  945  235 HOH   HOH B . 
Z  7 HOH   46  946  53  HOH   HOH B . 
Z  7 HOH   47  947  64  HOH   HOH B . 
Z  7 HOH   48  948  193 HOH   HOH B . 
Z  7 HOH   49  949  114 HOH   HOH B . 
Z  7 HOH   50  950  273 HOH   HOH B . 
Z  7 HOH   51  951  272 HOH   HOH B . 
Z  7 HOH   52  952  188 HOH   HOH B . 
Z  7 HOH   53  953  270 HOH   HOH B . 
Z  7 HOH   54  954  268 HOH   HOH B . 
Z  7 HOH   55  955  274 HOH   HOH B . 
Z  7 HOH   56  956  211 HOH   HOH B . 
Z  7 HOH   57  957  336 HOH   HOH B . 
Z  7 HOH   58  958  166 HOH   HOH B . 
Z  7 HOH   59  959  262 HOH   HOH B . 
Z  7 HOH   60  960  219 HOH   HOH B . 
Z  7 HOH   61  961  263 HOH   HOH B . 
Z  7 HOH   62  962  266 HOH   HOH B . 
Z  7 HOH   63  963  279 HOH   HOH B . 
Z  7 HOH   64  964  271 HOH   HOH B . 
Z  7 HOH   65  965  269 HOH   HOH B . 
Z  7 HOH   66  966  265 HOH   HOH B . 
AA 7 HOH   1   901  304 HOH   HOH C . 
AA 7 HOH   2   902  307 HOH   HOH C . 
AA 7 HOH   3   903  62  HOH   HOH C . 
AA 7 HOH   4   904  141 HOH   HOH C . 
AA 7 HOH   5   905  42  HOH   HOH C . 
AA 7 HOH   6   906  284 HOH   HOH C . 
AA 7 HOH   7   907  122 HOH   HOH C . 
AA 7 HOH   8   908  60  HOH   HOH C . 
AA 7 HOH   9   909  12  HOH   HOH C . 
AA 7 HOH   10  910  147 HOH   HOH C . 
AA 7 HOH   11  911  165 HOH   HOH C . 
AA 7 HOH   12  912  87  HOH   HOH C . 
AA 7 HOH   13  913  5   HOH   HOH C . 
AA 7 HOH   14  914  4   HOH   HOH C . 
AA 7 HOH   15  915  85  HOH   HOH C . 
AA 7 HOH   16  916  174 HOH   HOH C . 
AA 7 HOH   17  917  298 HOH   HOH C . 
AA 7 HOH   18  918  164 HOH   HOH C . 
AA 7 HOH   19  919  168 HOH   HOH C . 
AA 7 HOH   20  920  137 HOH   HOH C . 
AA 7 HOH   21  921  120 HOH   HOH C . 
AA 7 HOH   22  922  184 HOH   HOH C . 
AA 7 HOH   23  923  17  HOH   HOH C . 
AA 7 HOH   24  924  297 HOH   HOH C . 
AA 7 HOH   25  925  281 HOH   HOH C . 
AA 7 HOH   26  926  302 HOH   HOH C . 
AA 7 HOH   27  927  83  HOH   HOH C . 
AA 7 HOH   28  928  167 HOH   HOH C . 
AA 7 HOH   29  929  309 HOH   HOH C . 
AA 7 HOH   30  930  144 HOH   HOH C . 
AA 7 HOH   31  931  55  HOH   HOH C . 
AA 7 HOH   32  932  32  HOH   HOH C . 
AA 7 HOH   33  933  112 HOH   HOH C . 
AA 7 HOH   34  934  46  HOH   HOH C . 
AA 7 HOH   35  935  159 HOH   HOH C . 
AA 7 HOH   36  936  7   HOH   HOH C . 
AA 7 HOH   37  937  38  HOH   HOH C . 
AA 7 HOH   38  938  22  HOH   HOH C . 
AA 7 HOH   39  939  91  HOH   HOH C . 
AA 7 HOH   40  940  125 HOH   HOH C . 
AA 7 HOH   41  941  207 HOH   HOH C . 
AA 7 HOH   42  942  130 HOH   HOH C . 
AA 7 HOH   43  943  289 HOH   HOH C . 
AA 7 HOH   44  944  86  HOH   HOH C . 
AA 7 HOH   45  945  140 HOH   HOH C . 
AA 7 HOH   46  946  111 HOH   HOH C . 
AA 7 HOH   47  947  190 HOH   HOH C . 
AA 7 HOH   48  948  109 HOH   HOH C . 
AA 7 HOH   49  949  75  HOH   HOH C . 
AA 7 HOH   50  950  162 HOH   HOH C . 
AA 7 HOH   51  951  226 HOH   HOH C . 
AA 7 HOH   52  952  148 HOH   HOH C . 
AA 7 HOH   53  953  299 HOH   HOH C . 
AA 7 HOH   54  954  61  HOH   HOH C . 
AA 7 HOH   55  955  181 HOH   HOH C . 
AA 7 HOH   56  956  303 HOH   HOH C . 
AA 7 HOH   57  957  128 HOH   HOH C . 
AA 7 HOH   58  958  191 HOH   HOH C . 
AA 7 HOH   59  959  102 HOH   HOH C . 
AA 7 HOH   60  960  308 HOH   HOH C . 
AA 7 HOH   61  961  228 HOH   HOH C . 
AA 7 HOH   62  962  294 HOH   HOH C . 
AA 7 HOH   63  963  288 HOH   HOH C . 
AA 7 HOH   64  964  286 HOH   HOH C . 
AA 7 HOH   65  965  90  HOH   HOH C . 
AA 7 HOH   66  966  106 HOH   HOH C . 
AA 7 HOH   67  967  295 HOH   HOH C . 
AA 7 HOH   68  968  300 HOH   HOH C . 
AA 7 HOH   69  969  301 HOH   HOH C . 
AA 7 HOH   70  970  291 HOH   HOH C . 
AA 7 HOH   71  971  292 HOH   HOH C . 
AA 7 HOH   72  972  290 HOH   HOH C . 
AA 7 HOH   73  973  175 HOH   HOH C . 
AA 7 HOH   74  974  225 HOH   HOH C . 
AA 7 HOH   75  975  293 HOH   HOH C . 
AA 7 HOH   76  976  182 HOH   HOH C . 
AA 7 HOH   77  977  170 HOH   HOH C . 
AA 7 HOH   78  978  283 HOH   HOH C . 
AA 7 HOH   79  979  169 HOH   HOH C . 
AA 7 HOH   80  980  282 HOH   HOH C . 
AA 7 HOH   81  981  296 HOH   HOH C . 
AA 7 HOH   82  982  306 HOH   HOH C . 
AA 7 HOH   83  983  161 HOH   HOH C . 
BA 7 HOH   1   901  339 HOH   HOH D . 
BA 7 HOH   2   902  327 HOH   HOH D . 
BA 7 HOH   3   903  332 HOH   HOH D . 
BA 7 HOH   4   904  341 HOH   HOH D . 
BA 7 HOH   5   905  315 HOH   HOH D . 
BA 7 HOH   6   906  71  HOH   HOH D . 
BA 7 HOH   7   907  34  HOH   HOH D . 
BA 7 HOH   8   908  326 HOH   HOH D . 
BA 7 HOH   9   909  311 HOH   HOH D . 
BA 7 HOH   10  910  59  HOH   HOH D . 
BA 7 HOH   11  911  285 HOH   HOH D . 
BA 7 HOH   12  912  342 HOH   HOH D . 
BA 7 HOH   13  913  94  HOH   HOH D . 
BA 7 HOH   14  914  117 HOH   HOH D . 
BA 7 HOH   15  915  69  HOH   HOH D . 
BA 7 HOH   16  916  26  HOH   HOH D . 
BA 7 HOH   17  917  3   HOH   HOH D . 
BA 7 HOH   18  918  287 HOH   HOH D . 
BA 7 HOH   19  919  154 HOH   HOH D . 
BA 7 HOH   20  920  158 HOH   HOH D . 
BA 7 HOH   21  921  146 HOH   HOH D . 
BA 7 HOH   22  922  113 HOH   HOH D . 
BA 7 HOH   23  923  346 HOH   HOH D . 
BA 7 HOH   24  924  142 HOH   HOH D . 
BA 7 HOH   25  925  100 HOH   HOH D . 
BA 7 HOH   26  926  345 HOH   HOH D . 
BA 7 HOH   27  927  21  HOH   HOH D . 
BA 7 HOH   28  928  338 HOH   HOH D . 
BA 7 HOH   29  929  180 HOH   HOH D . 
BA 7 HOH   30  930  160 HOH   HOH D . 
BA 7 HOH   31  931  192 HOH   HOH D . 
BA 7 HOH   32  932  72  HOH   HOH D . 
BA 7 HOH   33  933  202 HOH   HOH D . 
BA 7 HOH   34  934  65  HOH   HOH D . 
BA 7 HOH   35  935  79  HOH   HOH D . 
BA 7 HOH   36  936  347 HOH   HOH D . 
BA 7 HOH   37  937  230 HOH   HOH D . 
BA 7 HOH   38  938  231 HOH   HOH D . 
BA 7 HOH   39  939  6   HOH   HOH D . 
BA 7 HOH   40  940  316 HOH   HOH D . 
BA 7 HOH   41  941  149 HOH   HOH D . 
BA 7 HOH   42  942  89  HOH   HOH D . 
BA 7 HOH   43  943  152 HOH   HOH D . 
BA 7 HOH   44  944  30  HOH   HOH D . 
BA 7 HOH   45  945  77  HOH   HOH D . 
BA 7 HOH   46  946  31  HOH   HOH D . 
BA 7 HOH   47  947  93  HOH   HOH D . 
BA 7 HOH   48  948  343 HOH   HOH D . 
BA 7 HOH   49  949  150 HOH   HOH D . 
BA 7 HOH   50  950  330 HOH   HOH D . 
BA 7 HOH   51  951  183 HOH   HOH D . 
BA 7 HOH   52  952  340 HOH   HOH D . 
BA 7 HOH   53  953  229 HOH   HOH D . 
BA 7 HOH   54  954  227 HOH   HOH D . 
BA 7 HOH   55  955  333 HOH   HOH D . 
BA 7 HOH   56  956  104 HOH   HOH D . 
BA 7 HOH   57  957  116 HOH   HOH D . 
BA 7 HOH   58  958  198 HOH   HOH D . 
BA 7 HOH   59  959  334 HOH   HOH D . 
BA 7 HOH   60  960  35  HOH   HOH D . 
BA 7 HOH   61  961  74  HOH   HOH D . 
BA 7 HOH   62  962  331 HOH   HOH D . 
BA 7 HOH   63  963  66  HOH   HOH D . 
BA 7 HOH   64  964  84  HOH   HOH D . 
BA 7 HOH   65  965  177 HOH   HOH D . 
BA 7 HOH   66  966  328 HOH   HOH D . 
BA 7 HOH   67  967  187 HOH   HOH D . 
BA 7 HOH   68  968  206 HOH   HOH D . 
BA 7 HOH   69  969  314 HOH   HOH D . 
BA 7 HOH   70  970  135 HOH   HOH D . 
BA 7 HOH   71  971  131 HOH   HOH D . 
BA 7 HOH   72  972  88  HOH   HOH D . 
BA 7 HOH   73  973  52  HOH   HOH D . 
BA 7 HOH   74  974  200 HOH   HOH D . 
BA 7 HOH   75  975  110 HOH   HOH D . 
BA 7 HOH   76  976  178 HOH   HOH D . 
BA 7 HOH   77  977  156 HOH   HOH D . 
BA 7 HOH   78  978  319 HOH   HOH D . 
BA 7 HOH   79  979  305 HOH   HOH D . 
BA 7 HOH   80  980  14  HOH   HOH D . 
BA 7 HOH   81  981  97  HOH   HOH D . 
BA 7 HOH   82  982  127 HOH   HOH D . 
BA 7 HOH   83  983  115 HOH   HOH D . 
BA 7 HOH   84  984  318 HOH   HOH D . 
BA 7 HOH   85  985  196 HOH   HOH D . 
BA 7 HOH   86  986  320 HOH   HOH D . 
BA 7 HOH   87  987  204 HOH   HOH D . 
BA 7 HOH   88  988  323 HOH   HOH D . 
BA 7 HOH   89  989  322 HOH   HOH D . 
BA 7 HOH   90  990  329 HOH   HOH D . 
BA 7 HOH   91  991  310 HOH   HOH D . 
BA 7 HOH   92  992  171 HOH   HOH D . 
BA 7 HOH   93  993  337 HOH   HOH D . 
BA 7 HOH   94  994  344 HOH   HOH D . 
BA 7 HOH   95  995  185 HOH   HOH D . 
BA 7 HOH   96  996  321 HOH   HOH D . 
BA 7 HOH   97  997  317 HOH   HOH D . 
BA 7 HOH   98  998  335 HOH   HOH D . 
BA 7 HOH   99  999  179 HOH   HOH D . 
BA 7 HOH   100 1000 312 HOH   HOH D . 
BA 7 HOH   101 1001 324 HOH   HOH D . 
BA 7 HOH   102 1002 313 HOH   HOH D . 
BA 7 HOH   103 1003 325 HOH   HOH D . 
BA 7 HOH   104 1004 176 HOH   HOH D . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.11.1_2575 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? .           4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9CVZ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     118.764 
_cell.length_a_esd                 ? 
_cell.length_b                     52.174 
_cell.length_b_esd                 ? 
_cell.length_c                     164.487 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9CVZ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9CVZ 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.74 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.2 
_exptl_crystal.description                  plates 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.2 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '8% PEG3350, 35 mM citric acid, 65 mM Bis-Tris propane, 10% glycerol, 5 mM TCEP' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            278 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      mirrors 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-03-18 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    'DOUBLE CRYSTAL SI(III)' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.000 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ALS BEAMLINE 5.0.2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   5.0.2 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9CVZ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.18 
_reflns.d_resolution_low                               48.14 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     105088 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          3.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.311 
_reflns.pdbx_Rpim_I_all                                0.140 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       500573 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.986 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.276 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.18 
_reflns_shell.d_res_low                                     2.22 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           24426 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5105 
_reflns_shell.percent_possible_obs                          99.0 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               4.8 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.4 
_reflns_shell.pdbx_Rrim_I_all                               4.984 
_reflns_shell.pdbx_Rpim_I_all                               2.260 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.127 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  4.419 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9CVZ 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.180 
_refine.ls_d_res_low                             48.14 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     91063 
_refine.ls_number_reflns_R_free                  8764 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    84.91 
_refine.ls_percent_reflns_R_free                 5.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2128 
_refine.ls_R_factor_R_free                       0.2774 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2093 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.57 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            random 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 37.18 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.43 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        13600 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         362 
_refine_hist.number_atoms_solvent             347 
_refine_hist.number_atoms_total               14309 
_refine_hist.d_res_high                       2.180 
_refine_hist.d_res_low                        48.14 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008  ? 14444 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.041  ? 19660 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 18.670 ? 8442  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.054  ? 2025  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006  ? 2486  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.1800 2.2048 . . 144 2517 39.00  . . . . 0.3966 . . . . . . . . . . . 0.4237 
'X-RAY DIFFRACTION' 2.2048 2.2307 . . 92  1632 25.00  . . . . 0.4457 . . . . . . . . . . . 0.5033 
'X-RAY DIFFRACTION' 2.2307 2.2580 . . 252 4875 74.00  . . . . 0.4124 . . . . . . . . . . . 0.5109 
'X-RAY DIFFRACTION' 2.2580 2.2865 . . 41  1202 18.00  . . . . 0.4109 . . . . . . . . . . . 0.5482 
'X-RAY DIFFRACTION' 2.2865 2.3166 . . 157 3321 51.00  . . . . 0.3622 . . . . . . . . . . . 0.3661 
'X-RAY DIFFRACTION' 2.3166 2.3484 . . 230 3963 60.00  . . . . 0.3627 . . . . . . . . . . . 0.3859 
'X-RAY DIFFRACTION' 2.3484 2.3819 . . 211 4061 62.00  . . . . 0.3651 . . . . . . . . . . . 0.3946 
'X-RAY DIFFRACTION' 2.3819 2.4175 . . 287 4724 74.00  . . . . 0.3516 . . . . . . . . . . . 0.3953 
'X-RAY DIFFRACTION' 2.4175 2.4552 . . 270 5654 85.00  . . . . 0.3502 . . . . . . . . . . . 0.4034 
'X-RAY DIFFRACTION' 2.4552 2.4955 . . 327 6061 93.00  . . . . 0.3508 . . . . . . . . . . . 0.4152 
'X-RAY DIFFRACTION' 2.4955 2.5385 . . 346 6222 96.00  . . . . 0.3115 . . . . . . . . . . . 0.3855 
'X-RAY DIFFRACTION' 2.5385 2.5847 . . 332 6340 98.00  . . . . 0.3086 . . . . . . . . . . . 0.3288 
'X-RAY DIFFRACTION' 2.5847 2.6344 . . 360 6349 98.00  . . . . 0.3069 . . . . . . . . . . . 0.3619 
'X-RAY DIFFRACTION' 2.6344 2.6881 . . 380 6355 98.00  . . . . 0.3180 . . . . . . . . . . . 0.3171 
'X-RAY DIFFRACTION' 2.6881 2.7466 . . 313 6611 99.00  . . . . 0.3115 . . . . . . . . . . . 0.3614 
'X-RAY DIFFRACTION' 2.7466 2.8105 . . 327 6278 99.00  . . . . 0.2908 . . . . . . . . . . . 0.3715 
'X-RAY DIFFRACTION' 2.8105 2.8807 . . 279 6644 99.00  . . . . 0.2962 . . . . . . . . . . . 0.3663 
'X-RAY DIFFRACTION' 2.8807 2.9586 . . 342 6358 99.00  . . . . 0.2894 . . . . . . . . . . . 0.3395 
'X-RAY DIFFRACTION' 2.9586 3.0457 . . 345 6574 99.00  . . . . 0.2803 . . . . . . . . . . . 0.3635 
'X-RAY DIFFRACTION' 3.0457 3.1440 . . 314 6372 99.00  . . . . 0.2644 . . . . . . . . . . . 0.3736 
'X-RAY DIFFRACTION' 3.1440 3.2563 . . 355 6531 99.00  . . . . 0.2486 . . . . . . . . . . . 0.3287 
'X-RAY DIFFRACTION' 3.2563 3.3866 . . 325 6344 97.00  . . . . 0.2253 . . . . . . . . . . . 0.3223 
'X-RAY DIFFRACTION' 3.3866 3.5407 . . 335 6070 94.00  . . . . 0.2092 . . . . . . . . . . . 0.2897 
'X-RAY DIFFRACTION' 3.5407 3.7273 . . 354 6570 100.00 . . . . 0.1744 . . . . . . . . . . . 0.2626 
'X-RAY DIFFRACTION' 3.7273 3.9608 . . 372 6431 99.00  . . . . 0.1623 . . . . . . . . . . . 0.2377 
'X-RAY DIFFRACTION' 3.9608 4.2664 . . 303 6524 100.00 . . . . 0.1300 . . . . . . . . . . . 0.1836 
'X-RAY DIFFRACTION' 4.2664 4.6954 . . 306 6494 99.00  . . . . 0.1210 . . . . . . . . . . . 0.1785 
'X-RAY DIFFRACTION' 4.6954 5.3741 . . 391 6401 99.00  . . . . 0.1302 . . . . . . . . . . . 0.2093 
'X-RAY DIFFRACTION' 5.3741 6.7678 . . 329 6247 96.00  . . . . 0.1577 . . . . . . . . . . . 0.2267 
'X-RAY DIFFRACTION' 6.7678 48.14  . . 345 6484 99.00  . . . . 0.1487 . . . . . . . . . . . 0.2135 
# 
_struct.entry_id                     9CVZ 
_struct.title                        
;structure of human neuronal nitric oxide synthase R354A/G357D mutant heme domain bound with 6-(2,3-difluoro-5-(((2-fluoroethyl)amino)methyl)phenyl)-4-methylpyridin-2-amine dihydrochloride
;
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9CVZ 
_struct_keywords.text            'nitric oxide synthase inhibitor binding, OXIDOREDUCTASE-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE/INHIBITOR 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 1 ? 
C  N N 1 ? 
D  N N 1 ? 
E  N N 2 ? 
F  N N 3 ? 
G  N N 4 ? 
H  N N 5 ? 
I  N N 5 ? 
J  N N 6 ? 
K  N N 2 ? 
L  N N 3 ? 
M  N N 4 ? 
N  N N 5 ? 
O  N N 2 ? 
P  N N 3 ? 
Q  N N 4 ? 
R  N N 5 ? 
S  N N 5 ? 
T  N N 6 ? 
U  N N 2 ? 
V  N N 3 ? 
W  N N 4 ? 
X  N N 5 ? 
Y  N N 7 ? 
Z  N N 7 ? 
AA N N 7 ? 
BA N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    NOS1_HUMAN 
_struct_ref.pdbx_db_accession          P29475 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;CPRFLKVKNWETEVVLTDTLHLKSTLETGCTEYICMGSIMHPSQHARRPEDVRTKGQLFPLAKEFIDQYYSSIKRFGSKA
HMERLEEVNKEIDTTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLR
SAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKPPRGRFDVLPLLLQANGNDPELFQI
PPELVLEVPIRHPKFEWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEEVAKKMNL
DMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEML
NYRLTPSFEYQPDPWNTHVWK
;
_struct_ref.pdbx_align_begin           302 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9CVZ A 1 ? 421 ? P29475 302 ? 722 ? 302 722 
2 1 9CVZ B 1 ? 421 ? P29475 302 ? 722 ? 302 722 
3 1 9CVZ C 1 ? 421 ? P29475 302 ? 722 ? 302 722 
4 1 9CVZ D 1 ? 421 ? P29475 302 ? 722 ? 302 722 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9CVZ ALA A 53  ? UNP P29475 ARG 354 'engineered mutation' 354 1  
1 9CVZ ASP A 56  ? UNP P29475 GLY 357 'engineered mutation' 357 2  
1 9CVZ LEU A 422 ? UNP P29475 ?   ?   'expression tag'      723 3  
1 9CVZ VAL A 423 ? UNP P29475 ?   ?   'expression tag'      724 4  
2 9CVZ ALA B 53  ? UNP P29475 ARG 354 'engineered mutation' 354 5  
2 9CVZ ASP B 56  ? UNP P29475 GLY 357 'engineered mutation' 357 6  
2 9CVZ LEU B 422 ? UNP P29475 ?   ?   'expression tag'      723 7  
2 9CVZ VAL B 423 ? UNP P29475 ?   ?   'expression tag'      724 8  
3 9CVZ ALA C 53  ? UNP P29475 ARG 354 'engineered mutation' 354 9  
3 9CVZ ASP C 56  ? UNP P29475 GLY 357 'engineered mutation' 357 10 
3 9CVZ LEU C 422 ? UNP P29475 ?   ?   'expression tag'      723 11 
3 9CVZ VAL C 423 ? UNP P29475 ?   ?   'expression tag'      724 12 
4 9CVZ ALA D 53  ? UNP P29475 ARG 354 'engineered mutation' 354 13 
4 9CVZ ASP D 56  ? UNP P29475 GLY 357 'engineered mutation' 357 14 
4 9CVZ LEU D 422 ? UNP P29475 ?   ?   'expression tag'      723 15 
4 9CVZ VAL D 423 ? UNP P29475 ?   ?   'expression tag'      724 16 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 9950  ? 
1 MORE         -82   ? 
1 'SSA (A^2)'  34330 ? 
2 'ABSA (A^2)' 9930  ? 
2 MORE         -82   ? 
2 'SSA (A^2)'  34410 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,E,F,G,H,I,J,K,L,M,N,Y,Z   
2 1 C,D,O,P,Q,R,S,T,U,V,W,X,AA,BA 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 THR A 19  ? SER A 24  ? THR A 320 SER A 325 5 ? 6  
HELX_P HELX_P2  AA2 THR A 54  ? ILE A 73  ? THR A 355 ILE A 374 1 ? 20 
HELX_P HELX_P3  AA3 SER A 78  ? SER A 96  ? SER A 379 SER A 397 1 ? 19 
HELX_P HELX_P4  AA4 LYS A 101 ? ALA A 116 ? LYS A 402 ALA A 417 1 ? 16 
HELX_P HELX_P5  AA5 GLY A 121 ? TRP A 125 ? GLY A 422 TRP A 426 5 ? 5  
HELX_P HELX_P6  AA6 THR A 138 ? ASN A 155 ? THR A 439 ASN A 456 1 ? 18 
HELX_P HELX_P7  AA7 LYS A 156 ? ASN A 158 ? LYS A 457 ASN A 459 5 ? 3  
HELX_P HELX_P8  AA8 ASN A 202 ? GLN A 212 ? ASN A 503 GLN A 513 1 ? 11 
HELX_P HELX_P9  AA9 PRO A 241 ? VAL A 245 ? PRO A 542 VAL A 546 5 ? 5  
HELX_P HELX_P10 AB1 TRP A 257 ? GLY A 262 ? TRP A 558 GLY A 563 5 ? 6  
HELX_P HELX_P11 AB2 MET A 293 ? VAL A 299 ? MET A 594 VAL A 600 1 ? 7  
HELX_P HELX_P12 AB3 VAL A 299 ? ASP A 304 ? VAL A 600 ASP A 605 1 ? 6  
HELX_P HELX_P13 AB4 ILE A 310 ? ASN A 319 ? ILE A 611 ASN A 620 1 ? 10 
HELX_P HELX_P14 AB5 LYS A 324 ? SER A 327 ? LYS A 625 SER A 628 5 ? 4  
HELX_P HELX_P15 AB6 LEU A 328 ? ASP A 348 ? LEU A 629 ASP A 649 1 ? 21 
HELX_P HELX_P16 AB7 ASP A 354 ? GLY A 374 ? ASP A 655 GLY A 675 1 ? 21 
HELX_P HELX_P17 AB8 ASP A 379 ? VAL A 384 ? ASP A 680 VAL A 685 1 ? 6  
HELX_P HELX_P18 AB9 SER A 388 ? THR A 392 ? SER A 689 THR A 693 5 ? 5  
HELX_P HELX_P19 AC1 ASP A 413 ? HIS A 418 ? ASP A 714 HIS A 719 1 ? 6  
HELX_P HELX_P20 AC2 THR B 19  ? SER B 24  ? THR B 320 SER B 325 5 ? 6  
HELX_P HELX_P21 AC3 THR B 54  ? ILE B 73  ? THR B 355 ILE B 374 1 ? 20 
HELX_P HELX_P22 AC4 SER B 78  ? SER B 96  ? SER B 379 SER B 397 1 ? 19 
HELX_P HELX_P23 AC5 LYS B 101 ? ASN B 115 ? LYS B 402 ASN B 416 1 ? 15 
HELX_P HELX_P24 AC6 GLY B 121 ? TRP B 125 ? GLY B 422 TRP B 426 5 ? 5  
HELX_P HELX_P25 AC7 THR B 138 ? ASN B 155 ? THR B 439 ASN B 456 1 ? 18 
HELX_P HELX_P26 AC8 LYS B 156 ? ASN B 158 ? LYS B 457 ASN B 459 5 ? 3  
HELX_P HELX_P27 AC9 ASN B 202 ? GLN B 212 ? ASN B 503 GLN B 513 1 ? 11 
HELX_P HELX_P28 AD1 PRO B 241 ? VAL B 245 ? PRO B 542 VAL B 546 5 ? 5  
HELX_P HELX_P29 AD2 PHE B 255 ? GLY B 262 ? PHE B 556 GLY B 563 5 ? 8  
HELX_P HELX_P30 AD3 MET B 293 ? VAL B 299 ? MET B 594 VAL B 600 1 ? 7  
HELX_P HELX_P31 AD4 VAL B 299 ? ASP B 304 ? VAL B 600 ASP B 605 1 ? 6  
HELX_P HELX_P32 AD5 ILE B 310 ? MET B 318 ? ILE B 611 MET B 619 1 ? 9  
HELX_P HELX_P33 AD6 LYS B 324 ? SER B 327 ? LYS B 625 SER B 628 5 ? 4  
HELX_P HELX_P34 AD7 LEU B 328 ? ASP B 348 ? LEU B 629 ASP B 649 1 ? 21 
HELX_P HELX_P35 AD8 ASP B 354 ? GLY B 374 ? ASP B 655 GLY B 675 1 ? 21 
HELX_P HELX_P36 AD9 ASP B 379 ? VAL B 384 ? ASP B 680 VAL B 685 1 ? 6  
HELX_P HELX_P37 AE1 SER B 388 ? GLN B 397 ? SER B 689 GLN B 698 5 ? 10 
HELX_P HELX_P38 AE2 ASP B 413 ? THR B 417 ? ASP B 714 THR B 718 5 ? 5  
HELX_P HELX_P39 AE3 THR C 19  ? SER C 24  ? THR C 320 SER C 325 5 ? 6  
HELX_P HELX_P40 AE4 THR C 54  ? ILE C 73  ? THR C 355 ILE C 374 1 ? 20 
HELX_P HELX_P41 AE5 SER C 78  ? SER C 96  ? SER C 379 SER C 397 1 ? 19 
HELX_P HELX_P42 AE6 LYS C 101 ? ASN C 115 ? LYS C 402 ASN C 416 1 ? 15 
HELX_P HELX_P43 AE7 GLY C 121 ? TRP C 125 ? GLY C 422 TRP C 426 5 ? 5  
HELX_P HELX_P44 AE8 THR C 138 ? ASN C 155 ? THR C 439 ASN C 456 1 ? 18 
HELX_P HELX_P45 AE9 LYS C 156 ? ASN C 158 ? LYS C 457 ASN C 459 5 ? 3  
HELX_P HELX_P46 AF1 ASN C 202 ? GLN C 212 ? ASN C 503 GLN C 513 1 ? 11 
HELX_P HELX_P47 AF2 PRO C 241 ? VAL C 245 ? PRO C 542 VAL C 546 5 ? 5  
HELX_P HELX_P48 AF3 PHE C 255 ? GLY C 262 ? PHE C 556 GLY C 563 5 ? 8  
HELX_P HELX_P49 AF4 MET C 293 ? VAL C 299 ? MET C 594 VAL C 600 1 ? 7  
HELX_P HELX_P50 AF5 ILE C 310 ? ASN C 319 ? ILE C 611 ASN C 620 1 ? 10 
HELX_P HELX_P51 AF6 LYS C 324 ? SER C 327 ? LYS C 625 SER C 628 5 ? 4  
HELX_P HELX_P52 AF7 LEU C 328 ? ASP C 348 ? LEU C 629 ASP C 649 1 ? 21 
HELX_P HELX_P53 AF8 ASP C 354 ? GLY C 374 ? ASP C 655 GLY C 675 1 ? 21 
HELX_P HELX_P54 AF9 ASP C 379 ? VAL C 384 ? ASP C 680 VAL C 685 1 ? 6  
HELX_P HELX_P55 AG1 SER C 388 ? THR C 392 ? SER C 689 THR C 693 5 ? 5  
HELX_P HELX_P56 AG2 ASP C 413 ? THR C 417 ? ASP C 714 THR C 718 5 ? 5  
HELX_P HELX_P57 AG3 THR D 19  ? SER D 24  ? THR D 320 SER D 325 5 ? 6  
HELX_P HELX_P58 AG4 THR D 54  ? ILE D 73  ? THR D 355 ILE D 374 1 ? 20 
HELX_P HELX_P59 AG5 SER D 78  ? SER D 96  ? SER D 379 SER D 397 1 ? 19 
HELX_P HELX_P60 AG6 LYS D 101 ? ALA D 116 ? LYS D 402 ALA D 417 1 ? 16 
HELX_P HELX_P61 AG7 GLY D 121 ? TRP D 125 ? GLY D 422 TRP D 426 5 ? 5  
HELX_P HELX_P62 AG8 THR D 138 ? ASN D 155 ? THR D 439 ASN D 456 1 ? 18 
HELX_P HELX_P63 AG9 LYS D 156 ? ASN D 158 ? LYS D 457 ASN D 459 5 ? 3  
HELX_P HELX_P64 AH1 ASN D 202 ? GLN D 212 ? ASN D 503 GLN D 513 1 ? 11 
HELX_P HELX_P65 AH2 PRO D 241 ? VAL D 245 ? PRO D 542 VAL D 546 5 ? 5  
HELX_P HELX_P66 AH3 PHE D 255 ? GLY D 262 ? PHE D 556 GLY D 563 5 ? 8  
HELX_P HELX_P67 AH4 GLY D 294 ? VAL D 299 ? GLY D 595 VAL D 600 1 ? 6  
HELX_P HELX_P68 AH5 ILE D 310 ? ASN D 319 ? ILE D 611 ASN D 620 1 ? 10 
HELX_P HELX_P69 AH6 LYS D 324 ? SER D 327 ? LYS D 625 SER D 628 5 ? 4  
HELX_P HELX_P70 AH7 LEU D 328 ? ASP D 348 ? LEU D 629 ASP D 649 1 ? 21 
HELX_P HELX_P71 AH8 ASP D 354 ? GLY D 374 ? ASP D 655 GLY D 675 1 ? 21 
HELX_P HELX_P72 AH9 ASP D 379 ? VAL D 384 ? ASP D 680 VAL D 685 1 ? 6  
HELX_P HELX_P73 AI1 SER D 388 ? GLN D 397 ? SER D 689 GLN D 698 5 ? 10 
HELX_P HELX_P74 AI2 ASP D 413 ? HIS D 418 ? ASP D 714 HIS D 719 1 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A CYS 30  SG ? ? ? 1_555 J ZN  .  ZN ? ? A CYS 331 A ZN  806 1_555 ? ? ? ? ? ? ? 2.333 ? ? 
metalc2  metalc ? ? A CYS 35  SG ? ? ? 1_555 J ZN  .  ZN ? ? A CYS 336 A ZN  806 1_555 ? ? ? ? ? ? ? 2.408 ? ? 
metalc3  metalc ? ? A CYS 119 SG ? ? ? 1_555 E HEM .  FE ? ? A CYS 420 A HEM 801 1_555 ? ? ? ? ? ? ? 2.299 ? ? 
metalc4  metalc ? ? J ZN  .   ZN ? ? ? 1_555 B CYS 30 SG ? ? A ZN  806 B CYS 331 1_555 ? ? ? ? ? ? ? 2.345 ? ? 
metalc5  metalc ? ? J ZN  .   ZN ? ? ? 1_555 B CYS 35 SG ? ? A ZN  806 B CYS 336 1_555 ? ? ? ? ? ? ? 2.441 ? ? 
metalc6  metalc ? ? B CYS 119 SG ? ? ? 1_555 K HEM .  FE ? ? B CYS 420 B HEM 801 1_555 ? ? ? ? ? ? ? 2.413 ? ? 
metalc7  metalc ? ? C CYS 30  SG ? ? ? 1_555 T ZN  .  ZN ? ? C CYS 331 C ZN  806 1_555 ? ? ? ? ? ? ? 2.332 ? ? 
metalc8  metalc ? ? C CYS 35  SG ? ? ? 1_555 T ZN  .  ZN ? ? C CYS 336 C ZN  806 1_555 ? ? ? ? ? ? ? 2.568 ? ? 
metalc9  metalc ? ? C CYS 119 SG ? ? ? 1_555 O HEM .  FE ? ? C CYS 420 C HEM 801 1_555 ? ? ? ? ? ? ? 2.359 ? ? 
metalc10 metalc ? ? T ZN  .   ZN ? ? ? 1_555 D CYS 30 SG ? ? C ZN  806 D CYS 331 1_555 ? ? ? ? ? ? ? 2.265 ? ? 
metalc11 metalc ? ? T ZN  .   ZN ? ? ? 1_555 D CYS 35 SG ? ? C ZN  806 D CYS 336 1_555 ? ? ? ? ? ? ? 2.331 ? ? 
metalc12 metalc ? ? D CYS 119 SG ? ? ? 1_555 U HEM .  FE ? ? D CYS 420 D HEM 801 1_555 ? ? ? ? ? ? ? 2.229 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG ? A CYS 30  ? A CYS 331 ? 1_555 ZN ? J ZN  . ? A ZN  806 ? 1_555 SG ? A CYS 35 ? A CYS 336 ? 1_555 107.5 ? 
2  SG ? A CYS 30  ? A CYS 331 ? 1_555 ZN ? J ZN  . ? A ZN  806 ? 1_555 SG ? B CYS 30 ? B CYS 331 ? 1_555 115.4 ? 
3  SG ? A CYS 35  ? A CYS 336 ? 1_555 ZN ? J ZN  . ? A ZN  806 ? 1_555 SG ? B CYS 30 ? B CYS 331 ? 1_555 107.5 ? 
4  SG ? A CYS 30  ? A CYS 331 ? 1_555 ZN ? J ZN  . ? A ZN  806 ? 1_555 SG ? B CYS 35 ? B CYS 336 ? 1_555 102.0 ? 
5  SG ? A CYS 35  ? A CYS 336 ? 1_555 ZN ? J ZN  . ? A ZN  806 ? 1_555 SG ? B CYS 35 ? B CYS 336 ? 1_555 111.4 ? 
6  SG ? B CYS 30  ? B CYS 331 ? 1_555 ZN ? J ZN  . ? A ZN  806 ? 1_555 SG ? B CYS 35 ? B CYS 336 ? 1_555 113.0 ? 
7  SG ? A CYS 119 ? A CYS 420 ? 1_555 FE ? E HEM . ? A HEM 801 ? 1_555 NA ? E HEM .  ? A HEM 801 ? 1_555 98.6  ? 
8  SG ? A CYS 119 ? A CYS 420 ? 1_555 FE ? E HEM . ? A HEM 801 ? 1_555 NB ? E HEM .  ? A HEM 801 ? 1_555 100.4 ? 
9  NA ? E HEM .   ? A HEM 801 ? 1_555 FE ? E HEM . ? A HEM 801 ? 1_555 NB ? E HEM .  ? A HEM 801 ? 1_555 86.5  ? 
10 SG ? A CYS 119 ? A CYS 420 ? 1_555 FE ? E HEM . ? A HEM 801 ? 1_555 NC ? E HEM .  ? A HEM 801 ? 1_555 91.7  ? 
11 NA ? E HEM .   ? A HEM 801 ? 1_555 FE ? E HEM . ? A HEM 801 ? 1_555 NC ? E HEM .  ? A HEM 801 ? 1_555 169.7 ? 
12 NB ? E HEM .   ? A HEM 801 ? 1_555 FE ? E HEM . ? A HEM 801 ? 1_555 NC ? E HEM .  ? A HEM 801 ? 1_555 92.3  ? 
13 SG ? A CYS 119 ? A CYS 420 ? 1_555 FE ? E HEM . ? A HEM 801 ? 1_555 ND ? E HEM .  ? A HEM 801 ? 1_555 97.1  ? 
14 NA ? E HEM .   ? A HEM 801 ? 1_555 FE ? E HEM . ? A HEM 801 ? 1_555 ND ? E HEM .  ? A HEM 801 ? 1_555 90.6  ? 
15 NB ? E HEM .   ? A HEM 801 ? 1_555 FE ? E HEM . ? A HEM 801 ? 1_555 ND ? E HEM .  ? A HEM 801 ? 1_555 162.5 ? 
16 NC ? E HEM .   ? A HEM 801 ? 1_555 FE ? E HEM . ? A HEM 801 ? 1_555 ND ? E HEM .  ? A HEM 801 ? 1_555 87.5  ? 
17 SG ? B CYS 119 ? B CYS 420 ? 1_555 FE ? K HEM . ? B HEM 801 ? 1_555 NA ? K HEM .  ? B HEM 801 ? 1_555 103.6 ? 
18 SG ? B CYS 119 ? B CYS 420 ? 1_555 FE ? K HEM . ? B HEM 801 ? 1_555 NB ? K HEM .  ? B HEM 801 ? 1_555 95.1  ? 
19 NA ? K HEM .   ? B HEM 801 ? 1_555 FE ? K HEM . ? B HEM 801 ? 1_555 NB ? K HEM .  ? B HEM 801 ? 1_555 87.4  ? 
20 SG ? B CYS 119 ? B CYS 420 ? 1_555 FE ? K HEM . ? B HEM 801 ? 1_555 NC ? K HEM .  ? B HEM 801 ? 1_555 96.2  ? 
21 NA ? K HEM .   ? B HEM 801 ? 1_555 FE ? K HEM . ? B HEM 801 ? 1_555 NC ? K HEM .  ? B HEM 801 ? 1_555 159.8 ? 
22 NB ? K HEM .   ? B HEM 801 ? 1_555 FE ? K HEM . ? B HEM 801 ? 1_555 NC ? K HEM .  ? B HEM 801 ? 1_555 87.2  ? 
23 SG ? B CYS 119 ? B CYS 420 ? 1_555 FE ? K HEM . ? B HEM 801 ? 1_555 ND ? K HEM .  ? B HEM 801 ? 1_555 108.8 ? 
24 NA ? K HEM .   ? B HEM 801 ? 1_555 FE ? K HEM . ? B HEM 801 ? 1_555 ND ? K HEM .  ? B HEM 801 ? 1_555 87.5  ? 
25 NB ? K HEM .   ? B HEM 801 ? 1_555 FE ? K HEM . ? B HEM 801 ? 1_555 ND ? K HEM .  ? B HEM 801 ? 1_555 156.2 ? 
26 NC ? K HEM .   ? B HEM 801 ? 1_555 FE ? K HEM . ? B HEM 801 ? 1_555 ND ? K HEM .  ? B HEM 801 ? 1_555 89.6  ? 
27 SG ? C CYS 30  ? C CYS 331 ? 1_555 ZN ? T ZN  . ? C ZN  806 ? 1_555 SG ? C CYS 35 ? C CYS 336 ? 1_555 112.7 ? 
28 SG ? C CYS 30  ? C CYS 331 ? 1_555 ZN ? T ZN  . ? C ZN  806 ? 1_555 SG ? D CYS 30 ? D CYS 331 ? 1_555 113.6 ? 
29 SG ? C CYS 35  ? C CYS 336 ? 1_555 ZN ? T ZN  . ? C ZN  806 ? 1_555 SG ? D CYS 30 ? D CYS 331 ? 1_555 102.6 ? 
30 SG ? C CYS 30  ? C CYS 331 ? 1_555 ZN ? T ZN  . ? C ZN  806 ? 1_555 SG ? D CYS 35 ? D CYS 336 ? 1_555 109.5 ? 
31 SG ? C CYS 35  ? C CYS 336 ? 1_555 ZN ? T ZN  . ? C ZN  806 ? 1_555 SG ? D CYS 35 ? D CYS 336 ? 1_555 113.4 ? 
32 SG ? D CYS 30  ? D CYS 331 ? 1_555 ZN ? T ZN  . ? C ZN  806 ? 1_555 SG ? D CYS 35 ? D CYS 336 ? 1_555 104.6 ? 
33 SG ? C CYS 119 ? C CYS 420 ? 1_555 FE ? O HEM . ? C HEM 801 ? 1_555 NA ? O HEM .  ? C HEM 801 ? 1_555 103.4 ? 
34 SG ? C CYS 119 ? C CYS 420 ? 1_555 FE ? O HEM . ? C HEM 801 ? 1_555 NB ? O HEM .  ? C HEM 801 ? 1_555 100.5 ? 
35 NA ? O HEM .   ? C HEM 801 ? 1_555 FE ? O HEM . ? C HEM 801 ? 1_555 NB ? O HEM .  ? C HEM 801 ? 1_555 88.9  ? 
36 SG ? C CYS 119 ? C CYS 420 ? 1_555 FE ? O HEM . ? C HEM 801 ? 1_555 NC ? O HEM .  ? C HEM 801 ? 1_555 95.7  ? 
37 NA ? O HEM .   ? C HEM 801 ? 1_555 FE ? O HEM . ? C HEM 801 ? 1_555 NC ? O HEM .  ? C HEM 801 ? 1_555 160.9 ? 
38 NB ? O HEM .   ? C HEM 801 ? 1_555 FE ? O HEM . ? C HEM 801 ? 1_555 NC ? O HEM .  ? C HEM 801 ? 1_555 86.4  ? 
39 SG ? C CYS 119 ? C CYS 420 ? 1_555 FE ? O HEM . ? C HEM 801 ? 1_555 ND ? O HEM .  ? C HEM 801 ? 1_555 103.0 ? 
40 NA ? O HEM .   ? C HEM 801 ? 1_555 FE ? O HEM . ? C HEM 801 ? 1_555 ND ? O HEM .  ? C HEM 801 ? 1_555 89.3  ? 
41 NB ? O HEM .   ? C HEM 801 ? 1_555 FE ? O HEM . ? C HEM 801 ? 1_555 ND ? O HEM .  ? C HEM 801 ? 1_555 156.2 ? 
42 NC ? O HEM .   ? C HEM 801 ? 1_555 FE ? O HEM . ? C HEM 801 ? 1_555 ND ? O HEM .  ? C HEM 801 ? 1_555 87.6  ? 
43 SG ? D CYS 119 ? D CYS 420 ? 1_555 FE ? U HEM . ? D HEM 801 ? 1_555 NA ? U HEM .  ? D HEM 801 ? 1_555 102.4 ? 
44 SG ? D CYS 119 ? D CYS 420 ? 1_555 FE ? U HEM . ? D HEM 801 ? 1_555 NB ? U HEM .  ? D HEM 801 ? 1_555 102.0 ? 
45 NA ? U HEM .   ? D HEM 801 ? 1_555 FE ? U HEM . ? D HEM 801 ? 1_555 NB ? U HEM .  ? D HEM 801 ? 1_555 84.1  ? 
46 SG ? D CYS 119 ? D CYS 420 ? 1_555 FE ? U HEM . ? D HEM 801 ? 1_555 NC ? U HEM .  ? D HEM 801 ? 1_555 96.6  ? 
47 NA ? U HEM .   ? D HEM 801 ? 1_555 FE ? U HEM . ? D HEM 801 ? 1_555 NC ? U HEM .  ? D HEM 801 ? 1_555 160.9 ? 
48 NB ? U HEM .   ? D HEM 801 ? 1_555 FE ? U HEM . ? D HEM 801 ? 1_555 NC ? U HEM .  ? D HEM 801 ? 1_555 89.8  ? 
49 SG ? D CYS 119 ? D CYS 420 ? 1_555 FE ? U HEM . ? D HEM 801 ? 1_555 ND ? U HEM .  ? D HEM 801 ? 1_555 102.9 ? 
50 NA ? U HEM .   ? D HEM 801 ? 1_555 FE ? U HEM . ? D HEM 801 ? 1_555 ND ? U HEM .  ? D HEM 801 ? 1_555 91.6  ? 
51 NB ? U HEM .   ? D HEM 801 ? 1_555 FE ? U HEM . ? D HEM 801 ? 1_555 ND ? U HEM .  ? D HEM 801 ? 1_555 155.1 ? 
52 NC ? U HEM .   ? D HEM 801 ? 1_555 FE ? U HEM . ? D HEM 801 ? 1_555 ND ? U HEM .  ? D HEM 801 ? 1_555 86.3  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 THR 405 A . ? THR 706 A PRO 406 A ? PRO 707 A 1 2.37  
2 THR 405 A . ? THR 706 A PRO 406 A ? PRO 707 A 1 0.27  
3 THR 405 B . ? THR 706 B PRO 406 B ? PRO 707 B 1 -4.02 
4 THR 405 C . ? THR 706 C PRO 406 C ? PRO 707 C 1 -1.25 
5 THR 405 C . ? THR 706 C PRO 406 C ? PRO 707 C 1 0.12  
6 THR 405 D . ? THR 706 D PRO 406 D ? PRO 707 D 1 5.97  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 4 ? 
AA3 ? 3 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 3 ? 
AA7 ? 2 ? 
AA8 ? 4 ? 
AA9 ? 3 ? 
AB1 ? 2 ? 
AB2 ? 2 ? 
AB3 ? 3 ? 
AB4 ? 2 ? 
AB5 ? 4 ? 
AB6 ? 3 ? 
AB7 ? 2 ? 
AB8 ? 2 ? 
AB9 ? 3 ? 
AC1 ? 2 ? 
AC2 ? 4 ? 
AC3 ? 3 ? 
AC4 ? 2 ? 
AC5 ? 2 ? 
AC6 ? 3 ? 
AC7 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? parallel      
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB5 1 2 ? parallel      
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB6 2 3 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB9 1 2 ? anti-parallel 
AB9 2 3 ? anti-parallel 
AC1 1 2 ? anti-parallel 
AC2 1 2 ? parallel      
AC2 2 3 ? anti-parallel 
AC2 3 4 ? anti-parallel 
AC3 1 2 ? anti-parallel 
AC3 2 3 ? anti-parallel 
AC4 1 2 ? anti-parallel 
AC5 1 2 ? anti-parallel 
AC6 1 2 ? anti-parallel 
AC6 2 3 ? anti-parallel 
AC7 1 2 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LYS A 6   ? LYS A 8   ? LYS A 307 LYS A 309 
AA1 2 VAL A 15  ? THR A 17  ? VAL A 316 THR A 318 
AA2 1 GLN A 129 ? ASP A 132 ? GLN A 430 ASP A 433 
AA2 2 ALA A 162 ? ILE A 165 ? ALA A 463 ILE A 466 
AA2 3 PHE A 288 ? SER A 289 ? PHE A 589 SER A 590 
AA2 4 ALA A 270 ? VAL A 271 ? ALA A 571 VAL A 572 
AA3 1 ARG A 177 ? VAL A 178 ? ARG A 478 VAL A 479 
AA3 2 LEU A 226 ? GLN A 229 ? LEU A 527 GLN A 530 
AA3 3 GLU A 236 ? PHE A 238 ? GLU A 537 PHE A 539 
AA4 1 GLY A 188 ? LYS A 190 ? GLY A 489 LYS A 491 
AA4 2 THR A 196 ? GLY A 198 ? THR A 497 GLY A 499 
AA5 1 GLU A 247 ? PRO A 249 ? GLU A 548 PRO A 550 
AA5 2 LYS A 264 ? TYR A 266 ? LYS A 565 TYR A 567 
AA6 1 LEU A 281 ? PHE A 283 ? LEU A 582 PHE A 584 
AA6 2 MET A 274 ? ILE A 278 ? MET A 575 ILE A 579 
AA6 3 SER A 407 ? TYR A 410 ? SER A 708 TYR A 711 
AA7 1 LEU B 5   ? LYS B 8   ? LEU B 306 LYS B 309 
AA7 2 VAL B 15  ? ASP B 18  ? VAL B 316 ASP B 319 
AA8 1 GLN B 129 ? ASP B 132 ? GLN B 430 ASP B 433 
AA8 2 ALA B 162 ? ILE B 165 ? ALA B 463 ILE B 466 
AA8 3 PHE B 288 ? SER B 289 ? PHE B 589 SER B 590 
AA8 4 ALA B 270 ? VAL B 271 ? ALA B 571 VAL B 572 
AA9 1 ARG B 177 ? VAL B 178 ? ARG B 478 VAL B 479 
AA9 2 LEU B 226 ? GLN B 229 ? LEU B 527 GLN B 530 
AA9 3 GLU B 236 ? PHE B 238 ? GLU B 537 PHE B 539 
AB1 1 GLY B 188 ? LYS B 190 ? GLY B 489 LYS B 491 
AB1 2 THR B 196 ? GLY B 198 ? THR B 497 GLY B 499 
AB2 1 GLU B 247 ? PRO B 249 ? GLU B 548 PRO B 550 
AB2 2 LYS B 264 ? TYR B 266 ? LYS B 565 TYR B 567 
AB3 1 LEU B 281 ? PHE B 283 ? LEU B 582 PHE B 584 
AB3 2 LEU B 275 ? ILE B 278 ? LEU B 576 ILE B 579 
AB3 3 SER B 407 ? GLU B 409 ? SER B 708 GLU B 710 
AB4 1 LEU C 5   ? LYS C 8   ? LEU C 306 LYS C 309 
AB4 2 VAL C 15  ? ASP C 18  ? VAL C 316 ASP C 319 
AB5 1 GLN C 129 ? ASP C 132 ? GLN C 430 ASP C 433 
AB5 2 ALA C 162 ? ILE C 165 ? ALA C 463 ILE C 466 
AB5 3 PHE C 288 ? SER C 289 ? PHE C 589 SER C 590 
AB5 4 ALA C 270 ? VAL C 271 ? ALA C 571 VAL C 572 
AB6 1 ARG C 177 ? VAL C 178 ? ARG C 478 VAL C 479 
AB6 2 LEU C 226 ? GLN C 229 ? LEU C 527 GLN C 530 
AB6 3 GLU C 236 ? PHE C 238 ? GLU C 537 PHE C 539 
AB7 1 GLY C 188 ? LYS C 190 ? GLY C 489 LYS C 491 
AB7 2 THR C 196 ? GLY C 198 ? THR C 497 GLY C 499 
AB8 1 GLU C 247 ? PRO C 249 ? GLU C 548 PRO C 550 
AB8 2 LYS C 264 ? TYR C 266 ? LYS C 565 TYR C 567 
AB9 1 LEU C 281 ? PHE C 283 ? LEU C 582 PHE C 584 
AB9 2 LEU C 275 ? ILE C 278 ? LEU C 576 ILE C 579 
AB9 3 SER C 407 ? GLU C 409 ? SER C 708 GLU C 710 
AC1 1 LYS D 6   ? LYS D 8   ? LYS D 307 LYS D 309 
AC1 2 VAL D 15  ? THR D 17  ? VAL D 316 THR D 318 
AC2 1 GLN D 129 ? ASP D 132 ? GLN D 430 ASP D 433 
AC2 2 ALA D 162 ? ILE D 165 ? ALA D 463 ILE D 466 
AC2 3 PHE D 288 ? SER D 289 ? PHE D 589 SER D 590 
AC2 4 ALA D 270 ? VAL D 271 ? ALA D 571 VAL D 572 
AC3 1 ARG D 177 ? VAL D 178 ? ARG D 478 VAL D 479 
AC3 2 LEU D 226 ? GLN D 229 ? LEU D 527 GLN D 530 
AC3 3 GLU D 236 ? PHE D 238 ? GLU D 537 PHE D 539 
AC4 1 GLY D 188 ? LYS D 190 ? GLY D 489 LYS D 491 
AC4 2 THR D 196 ? GLY D 198 ? THR D 497 GLY D 499 
AC5 1 GLU D 247 ? PRO D 249 ? GLU D 548 PRO D 550 
AC5 2 LYS D 264 ? TYR D 266 ? LYS D 565 TYR D 567 
AC6 1 LEU D 281 ? PHE D 283 ? LEU D 582 PHE D 584 
AC6 2 LEU D 275 ? ILE D 278 ? LEU D 576 ILE D 579 
AC6 3 SER D 407 ? GLU D 409 ? SER D 708 GLU D 710 
AC7 1 TYR D 292 ? MET D 293 ? TYR D 593 MET D 594 
AC7 2 ILE D 352 ? VAL D 353 ? ILE D 653 VAL D 654 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 7   ? N VAL A 308 O LEU A 16  ? O LEU A 317 
AA2 1 2 N PHE A 131 ? N PHE A 432 O ILE A 163 ? O ILE A 464 
AA2 2 3 N ALA A 162 ? N ALA A 463 O SER A 289 ? O SER A 590 
AA2 3 4 O PHE A 288 ? O PHE A 589 N VAL A 271 ? N VAL A 572 
AA3 1 2 N ARG A 177 ? N ARG A 478 O GLN A 229 ? O GLN A 530 
AA3 2 3 N LEU A 228 ? N LEU A 529 O GLU A 236 ? O GLU A 537 
AA4 1 2 N TYR A 189 ? N TYR A 490 O LEU A 197 ? O LEU A 498 
AA5 1 2 N VAL A 248 ? N VAL A 549 O TRP A 265 ? O TRP A 566 
AA6 1 2 O PHE A 283 ? O PHE A 584 N LEU A 276 ? N LEU A 577 
AA6 2 3 N LEU A 275 ? N LEU A 576 O GLU A 409 ? O GLU A 710 
AA7 1 2 N LEU B 5   ? N LEU B 306 O ASP B 18  ? O ASP B 319 
AA8 1 2 N PHE B 131 ? N PHE B 432 O ILE B 163 ? O ILE B 464 
AA8 2 3 N ALA B 162 ? N ALA B 463 O SER B 289 ? O SER B 590 
AA8 3 4 O PHE B 288 ? O PHE B 589 N VAL B 271 ? N VAL B 572 
AA9 1 2 N ARG B 177 ? N ARG B 478 O GLN B 229 ? O GLN B 530 
AA9 2 3 N LEU B 226 ? N LEU B 527 O PHE B 238 ? O PHE B 539 
AB1 1 2 N TYR B 189 ? N TYR B 490 O LEU B 197 ? O LEU B 498 
AB2 1 2 N VAL B 248 ? N VAL B 549 O TRP B 265 ? O TRP B 566 
AB3 1 2 O PHE B 283 ? O PHE B 584 N LEU B 276 ? N LEU B 577 
AB3 2 3 N LEU B 275 ? N LEU B 576 O GLU B 409 ? O GLU B 710 
AB4 1 2 N LEU C 5   ? N LEU C 306 O ASP C 18  ? O ASP C 319 
AB5 1 2 N PHE C 131 ? N PHE C 432 O ILE C 163 ? O ILE C 464 
AB5 2 3 N ALA C 162 ? N ALA C 463 O SER C 289 ? O SER C 590 
AB5 3 4 O PHE C 288 ? O PHE C 589 N VAL C 271 ? N VAL C 572 
AB6 1 2 N ARG C 177 ? N ARG C 478 O GLN C 229 ? O GLN C 530 
AB6 2 3 N LEU C 226 ? N LEU C 527 O PHE C 238 ? O PHE C 539 
AB7 1 2 N TYR C 189 ? N TYR C 490 O LEU C 197 ? O LEU C 498 
AB8 1 2 N VAL C 248 ? N VAL C 549 O TRP C 265 ? O TRP C 566 
AB9 1 2 O LEU C 281 ? O LEU C 582 N ILE C 278 ? N ILE C 579 
AB9 2 3 N GLU C 277 ? N GLU C 578 O SER C 407 ? O SER C 708 
AC1 1 2 N VAL D 7   ? N VAL D 308 O LEU D 16  ? O LEU D 317 
AC2 1 2 N PHE D 131 ? N PHE D 432 O ILE D 163 ? O ILE D 464 
AC2 2 3 N ALA D 162 ? N ALA D 463 O SER D 289 ? O SER D 590 
AC2 3 4 O PHE D 288 ? O PHE D 589 N VAL D 271 ? N VAL D 572 
AC3 1 2 N ARG D 177 ? N ARG D 478 O GLN D 229 ? O GLN D 530 
AC3 2 3 N LEU D 228 ? N LEU D 529 O GLU D 236 ? O GLU D 537 
AC4 1 2 N TYR D 189 ? N TYR D 490 O LEU D 197 ? O LEU D 498 
AC5 1 2 N VAL D 248 ? N VAL D 549 O TRP D 265 ? O TRP D 566 
AC6 1 2 O PHE D 283 ? O PHE D 584 N LEU D 276 ? N LEU D 577 
AC6 2 3 N LEU D 275 ? N LEU D 576 O GLU D 409 ? O GLU D 710 
AC7 1 2 N TYR D 292 ? N TYR D 593 O VAL D 353 ? O VAL D 654 
# 
_pdbx_entry_details.entry_id                   9CVZ 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OH  B TYR 711 ? ? O1D B HEM 801 ? ? 2.11 
2 1 NH1 D ARG 521 ? ? O   D HOH 901 ? ? 2.17 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_1              327 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_2              327 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_3              327 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                129.25 
_pdbx_validate_rmsd_angle.angle_target_value         115.30 
_pdbx_validate_rmsd_angle.angle_deviation            13.95 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.30 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP A 352 ? ? -68.31  32.96   
2  1 THR A 395 ? ? -76.21  -74.73  
3  1 LYS A 428 ? ? -111.00 70.50   
4  1 GLN A 469 ? ? -57.43  176.18  
5  1 THR A 471 ? ? -124.44 -85.76  
6  1 CYS A 587 ? ? -152.27 51.96   
7  1 ARG A 608 ? ? -111.48 -138.37 
8  1 CYS A 677 ? ? -169.51 101.17  
9  1 PRO B 350 ? ? -73.72  -149.18 
10 1 ASP B 352 ? ? -114.37 -149.52 
11 1 ARG B 376 ? ? -119.31 -116.69 
12 1 PHE B 377 ? ? 70.77   114.47  
13 1 LYS B 428 ? ? -105.90 67.94   
14 1 THR B 471 ? ? -118.01 -71.72  
15 1 PHE B 522 ? ? -107.23 66.84   
16 1 ASN B 532 ? ? 26.72   59.78   
17 1 SER B 573 ? ? -140.88 13.83   
18 1 CYS B 587 ? ? -154.21 59.77   
19 1 VAL B 600 ? ? -91.09  -61.99  
20 1 ASP B 605 ? ? -41.92  151.40  
21 1 ARG B 608 ? ? -132.52 -131.19 
22 1 ASN B 620 ? ? 63.24   66.03   
23 1 LYS B 650 ? ? 26.40   48.61   
24 1 CYS B 677 ? ? -160.47 108.12  
25 1 PHE C 305 ? ? 173.34  144.49  
26 1 HIS C 342 ? ? -118.14 77.45   
27 1 PRO C 350 ? ? -59.60  -159.12 
28 1 ASP C 352 ? ? -112.38 -153.84 
29 1 THR C 355 ? ? -68.69  -179.82 
30 1 ARG C 376 ? ? -100.94 -121.66 
31 1 PHE C 377 ? ? 85.83   117.84  
32 1 THR C 398 ? ? -138.75 -159.91 
33 1 ARG C 423 ? ? -68.82  2.50    
34 1 LYS C 428 ? ? -114.22 68.12   
35 1 SER C 496 ? ? -72.30  -167.68 
36 1 ARG C 519 ? ? 56.56   75.49   
37 1 PHE C 522 ? ? -102.78 61.53   
38 1 ASN C 532 ? ? 30.90   61.94   
39 1 CYS C 587 ? ? -148.22 55.28   
40 1 ARG C 608 ? ? -127.23 -136.92 
41 1 ASP C 622 ? ? -60.87  86.59   
42 1 CYS C 677 ? ? -162.41 108.39  
43 1 THR D 326 ? ? -143.32 44.34   
44 1 THR D 471 ? ? -120.12 -64.24  
45 1 CYS D 587 ? ? -146.76 46.60   
46 1 ARG D 608 ? ? -120.43 -130.59 
47 1 LYS D 650 ? ? 33.57   46.68   
48 1 CYS D 677 ? ? -169.73 103.32  
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -34.5830 7.7739  -38.4633 0.2593 ? 0.0048  ? 0.0330  ? 0.2291 ? 0.0518 ? 0.2527 ? 0.9003 ? -0.2319 
? 0.0646  ? 0.4962 ? 0.2923  ? 2.1461 ? -0.0304 ? -0.0721 ? -0.0263 ? -0.0147 ? 0.0353 ? 0.0445  ? 0.1388  ? 0.0375 ? 0.0077 ? 
2 'X-RAY DIFFRACTION' ? refined -34.8101 9.7050  -0.9753  0.3019 ? 0.0010  ? -0.0176 ? 0.2633 ? 0.0339 ? 0.2448 ? 0.9490 ? -0.1662 
? -0.1599 ? 0.5487 ? -0.0557 ? 3.0441 ? -0.0791 ? 0.0442  ? 0.0520  ? 0.0586  ? 0.0280 ? -0.0107 ? -0.1334 ? 0.1193 ? 0.0444 ? 
3 'X-RAY DIFFRACTION' ? refined 24.5113  31.6470 -81.2329 0.3563 ? -0.0106 ? -0.0031 ? 0.3165 ? 0.0317 ? 0.2956 ? 0.9463 ? 0.0961  
? -0.0432 ? 0.5738 ? 0.0014  ? 3.0684 ? -0.0785 ? -0.0952 ? -0.0509 ? -0.0526 ? 0.0234 ? -0.0025 ? 0.1258  ? 0.0545 ? 0.0513 ? 
4 'X-RAY DIFFRACTION' ? refined 24.8578  33.5649 -43.7881 0.2496 ? 0.0104  ? -0.0334 ? 0.2312 ? 0.0372 ? 0.2605 ? 0.7676 ? 0.2092  
? -0.0296 ? 0.5538 ? 0.1654  ? 2.2624 ? -0.0688 ? 0.0564  ? 0.0380  ? -0.0187 ? 0.0511 ? 0.0436  ? -0.1069 ? 0.0498 ? 0.0169 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? '(chain A and resid 304:722)' 
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? '(chain B and resid 304:722)' 
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? '(chain C and resid 303:722)' 
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? '(chain D and resid 304:722)' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A CYS 302 ? A CYS 1   
2  1 Y 1 A PRO 303 ? A PRO 2   
3  1 Y 1 A SER 344 ? A SER 43  
4  1 Y 1 A GLN 345 ? A GLN 44  
5  1 Y 1 A HIS 346 ? A HIS 45  
6  1 Y 1 A ALA 347 ? A ALA 46  
7  1 Y 1 A ARG 348 ? A ARG 47  
8  1 Y 1 A LEU 723 ? A LEU 422 
9  1 Y 1 A VAL 724 ? A VAL 423 
10 1 Y 1 B CYS 302 ? B CYS 1   
11 1 Y 1 B PRO 303 ? B PRO 2   
12 1 Y 1 B LEU 723 ? B LEU 422 
13 1 Y 1 B VAL 724 ? B VAL 423 
14 1 Y 1 C CYS 302 ? C CYS 1   
15 1 Y 1 C LEU 723 ? C LEU 422 
16 1 Y 1 C VAL 724 ? C VAL 423 
17 1 Y 1 D CYS 302 ? D CYS 1   
18 1 Y 1 D PRO 303 ? D PRO 2   
19 1 Y 1 D GLN 345 ? D GLN 44  
20 1 Y 1 D HIS 346 ? D HIS 45  
21 1 Y 1 D ALA 347 ? D ALA 46  
22 1 Y 1 D ARG 348 ? D ARG 47  
23 1 Y 1 D ARG 349 ? D ARG 48  
24 1 Y 1 D LEU 723 ? D LEU 422 
25 1 Y 1 D VAL 724 ? D VAL 423 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1AZ9 C14  C  Y N 1   
A1AZ9 C13  C  Y N 2   
A1AZ9 C12  C  Y N 3   
A1AZ9 C11  C  Y N 4   
A1AZ9 C15  C  Y N 5   
A1AZ9 C16  C  Y N 6   
A1AZ9 C17  C  N N 7   
A1AZ9 C19  C  N N 8   
A1AZ9 C20  C  N N 9   
A1AZ9 C02  C  Y N 10  
A1AZ9 C03  C  Y N 11  
A1AZ9 C04  C  Y N 12  
A1AZ9 C05  C  Y N 13  
A1AZ9 C06  C  Y N 14  
A1AZ9 C07  C  N N 15  
A1AZ9 F12  F  N N 16  
A1AZ9 F13  F  N N 17  
A1AZ9 F21  F  N N 18  
A1AZ9 N01  N  Y N 19  
A1AZ9 N02  N  N N 20  
A1AZ9 N18  N  N N 21  
A1AZ9 H1   H  N N 22  
A1AZ9 H2   H  N N 23  
A1AZ9 H3   H  N N 24  
A1AZ9 H4   H  N N 25  
A1AZ9 H5   H  N N 26  
A1AZ9 H6   H  N N 27  
A1AZ9 H7   H  N N 28  
A1AZ9 H8   H  N N 29  
A1AZ9 H9   H  N N 30  
A1AZ9 H10  H  N N 31  
A1AZ9 H11  H  N N 32  
A1AZ9 H12  H  N N 33  
A1AZ9 H13  H  N N 34  
A1AZ9 H14  H  N N 35  
A1AZ9 H15  H  N N 36  
A1AZ9 H16  H  N N 37  
ALA   N    N  N N 38  
ALA   CA   C  N S 39  
ALA   C    C  N N 40  
ALA   O    O  N N 41  
ALA   CB   C  N N 42  
ALA   OXT  O  N N 43  
ALA   H    H  N N 44  
ALA   H2   H  N N 45  
ALA   HA   H  N N 46  
ALA   HB1  H  N N 47  
ALA   HB2  H  N N 48  
ALA   HB3  H  N N 49  
ALA   HXT  H  N N 50  
ARG   N    N  N N 51  
ARG   CA   C  N S 52  
ARG   C    C  N N 53  
ARG   O    O  N N 54  
ARG   CB   C  N N 55  
ARG   CG   C  N N 56  
ARG   CD   C  N N 57  
ARG   NE   N  N N 58  
ARG   CZ   C  N N 59  
ARG   NH1  N  N N 60  
ARG   NH2  N  N N 61  
ARG   OXT  O  N N 62  
ARG   H    H  N N 63  
ARG   H2   H  N N 64  
ARG   HA   H  N N 65  
ARG   HB2  H  N N 66  
ARG   HB3  H  N N 67  
ARG   HG2  H  N N 68  
ARG   HG3  H  N N 69  
ARG   HD2  H  N N 70  
ARG   HD3  H  N N 71  
ARG   HE   H  N N 72  
ARG   HH11 H  N N 73  
ARG   HH12 H  N N 74  
ARG   HH21 H  N N 75  
ARG   HH22 H  N N 76  
ARG   HXT  H  N N 77  
ASN   N    N  N N 78  
ASN   CA   C  N S 79  
ASN   C    C  N N 80  
ASN   O    O  N N 81  
ASN   CB   C  N N 82  
ASN   CG   C  N N 83  
ASN   OD1  O  N N 84  
ASN   ND2  N  N N 85  
ASN   OXT  O  N N 86  
ASN   H    H  N N 87  
ASN   H2   H  N N 88  
ASN   HA   H  N N 89  
ASN   HB2  H  N N 90  
ASN   HB3  H  N N 91  
ASN   HD21 H  N N 92  
ASN   HD22 H  N N 93  
ASN   HXT  H  N N 94  
ASP   N    N  N N 95  
ASP   CA   C  N S 96  
ASP   C    C  N N 97  
ASP   O    O  N N 98  
ASP   CB   C  N N 99  
ASP   CG   C  N N 100 
ASP   OD1  O  N N 101 
ASP   OD2  O  N N 102 
ASP   OXT  O  N N 103 
ASP   H    H  N N 104 
ASP   H2   H  N N 105 
ASP   HA   H  N N 106 
ASP   HB2  H  N N 107 
ASP   HB3  H  N N 108 
ASP   HD2  H  N N 109 
ASP   HXT  H  N N 110 
CYS   N    N  N N 111 
CYS   CA   C  N R 112 
CYS   C    C  N N 113 
CYS   O    O  N N 114 
CYS   CB   C  N N 115 
CYS   SG   S  N N 116 
CYS   OXT  O  N N 117 
CYS   H    H  N N 118 
CYS   H2   H  N N 119 
CYS   HA   H  N N 120 
CYS   HB2  H  N N 121 
CYS   HB3  H  N N 122 
CYS   HG   H  N N 123 
CYS   HXT  H  N N 124 
GLN   N    N  N N 125 
GLN   CA   C  N S 126 
GLN   C    C  N N 127 
GLN   O    O  N N 128 
GLN   CB   C  N N 129 
GLN   CG   C  N N 130 
GLN   CD   C  N N 131 
GLN   OE1  O  N N 132 
GLN   NE2  N  N N 133 
GLN   OXT  O  N N 134 
GLN   H    H  N N 135 
GLN   H2   H  N N 136 
GLN   HA   H  N N 137 
GLN   HB2  H  N N 138 
GLN   HB3  H  N N 139 
GLN   HG2  H  N N 140 
GLN   HG3  H  N N 141 
GLN   HE21 H  N N 142 
GLN   HE22 H  N N 143 
GLN   HXT  H  N N 144 
GLU   N    N  N N 145 
GLU   CA   C  N S 146 
GLU   C    C  N N 147 
GLU   O    O  N N 148 
GLU   CB   C  N N 149 
GLU   CG   C  N N 150 
GLU   CD   C  N N 151 
GLU   OE1  O  N N 152 
GLU   OE2  O  N N 153 
GLU   OXT  O  N N 154 
GLU   H    H  N N 155 
GLU   H2   H  N N 156 
GLU   HA   H  N N 157 
GLU   HB2  H  N N 158 
GLU   HB3  H  N N 159 
GLU   HG2  H  N N 160 
GLU   HG3  H  N N 161 
GLU   HE2  H  N N 162 
GLU   HXT  H  N N 163 
GLY   N    N  N N 164 
GLY   CA   C  N N 165 
GLY   C    C  N N 166 
GLY   O    O  N N 167 
GLY   OXT  O  N N 168 
GLY   H    H  N N 169 
GLY   H2   H  N N 170 
GLY   HA2  H  N N 171 
GLY   HA3  H  N N 172 
GLY   HXT  H  N N 173 
GOL   C1   C  N N 174 
GOL   O1   O  N N 175 
GOL   C2   C  N N 176 
GOL   O2   O  N N 177 
GOL   C3   C  N N 178 
GOL   O3   O  N N 179 
GOL   H11  H  N N 180 
GOL   H12  H  N N 181 
GOL   HO1  H  N N 182 
GOL   H2   H  N N 183 
GOL   HO2  H  N N 184 
GOL   H31  H  N N 185 
GOL   H32  H  N N 186 
GOL   HO3  H  N N 187 
H4B   N1   N  Y N 188 
H4B   C2   C  Y N 189 
H4B   N2   N  N N 190 
H4B   N3   N  Y N 191 
H4B   C4   C  Y N 192 
H4B   O4   O  N N 193 
H4B   C4A  C  Y N 194 
H4B   C8A  C  Y N 195 
H4B   N5   N  N N 196 
H4B   N8   N  N N 197 
H4B   C6   C  N R 198 
H4B   C7   C  N N 199 
H4B   C9   C  N R 200 
H4B   O9   O  N N 201 
H4B   C10  C  N S 202 
H4B   C11  C  N N 203 
H4B   O10  O  N N 204 
H4B   HN21 H  N N 205 
H4B   HN22 H  N N 206 
H4B   HN3  H  N N 207 
H4B   HN5  H  N N 208 
H4B   HN8  H  N N 209 
H4B   H6   H  N N 210 
H4B   H71  H  N N 211 
H4B   H72  H  N N 212 
H4B   H9   H  N N 213 
H4B   HO9  H  N N 214 
H4B   H10  H  N N 215 
H4B   H111 H  N N 216 
H4B   H112 H  N N 217 
H4B   H113 H  N N 218 
H4B   HO0  H  N N 219 
HEM   CHA  C  N N 220 
HEM   CHB  C  N N 221 
HEM   CHC  C  N N 222 
HEM   CHD  C  N N 223 
HEM   C1A  C  Y N 224 
HEM   C2A  C  Y N 225 
HEM   C3A  C  Y N 226 
HEM   C4A  C  Y N 227 
HEM   CMA  C  N N 228 
HEM   CAA  C  N N 229 
HEM   CBA  C  N N 230 
HEM   CGA  C  N N 231 
HEM   O1A  O  N N 232 
HEM   O2A  O  N N 233 
HEM   C1B  C  N N 234 
HEM   C2B  C  N N 235 
HEM   C3B  C  N N 236 
HEM   C4B  C  N N 237 
HEM   CMB  C  N N 238 
HEM   CAB  C  N N 239 
HEM   CBB  C  N N 240 
HEM   C1C  C  Y N 241 
HEM   C2C  C  Y N 242 
HEM   C3C  C  Y N 243 
HEM   C4C  C  Y N 244 
HEM   CMC  C  N N 245 
HEM   CAC  C  N N 246 
HEM   CBC  C  N N 247 
HEM   C1D  C  N N 248 
HEM   C2D  C  N N 249 
HEM   C3D  C  N N 250 
HEM   C4D  C  N N 251 
HEM   CMD  C  N N 252 
HEM   CAD  C  N N 253 
HEM   CBD  C  N N 254 
HEM   CGD  C  N N 255 
HEM   O1D  O  N N 256 
HEM   O2D  O  N N 257 
HEM   NA   N  Y N 258 
HEM   NB   N  N N 259 
HEM   NC   N  Y N 260 
HEM   ND   N  N N 261 
HEM   FE   FE N N 262 
HEM   HHB  H  N N 263 
HEM   HHC  H  N N 264 
HEM   HHD  H  N N 265 
HEM   HMA  H  N N 266 
HEM   HMAA H  N N 267 
HEM   HMAB H  N N 268 
HEM   HAA  H  N N 269 
HEM   HAAA H  N N 270 
HEM   HBA  H  N N 271 
HEM   HBAA H  N N 272 
HEM   HMB  H  N N 273 
HEM   HMBA H  N N 274 
HEM   HMBB H  N N 275 
HEM   HAB  H  N N 276 
HEM   HBB  H  N N 277 
HEM   HBBA H  N N 278 
HEM   HMC  H  N N 279 
HEM   HMCA H  N N 280 
HEM   HMCB H  N N 281 
HEM   HAC  H  N N 282 
HEM   HBC  H  N N 283 
HEM   HBCA H  N N 284 
HEM   HMD  H  N N 285 
HEM   HMDA H  N N 286 
HEM   HMDB H  N N 287 
HEM   HAD  H  N N 288 
HEM   HADA H  N N 289 
HEM   HBD  H  N N 290 
HEM   HBDA H  N N 291 
HEM   H2A  H  N N 292 
HEM   H2D  H  N N 293 
HEM   HHA  H  N N 294 
HIS   N    N  N N 295 
HIS   CA   C  N S 296 
HIS   C    C  N N 297 
HIS   O    O  N N 298 
HIS   CB   C  N N 299 
HIS   CG   C  Y N 300 
HIS   ND1  N  Y N 301 
HIS   CD2  C  Y N 302 
HIS   CE1  C  Y N 303 
HIS   NE2  N  Y N 304 
HIS   OXT  O  N N 305 
HIS   H    H  N N 306 
HIS   H2   H  N N 307 
HIS   HA   H  N N 308 
HIS   HB2  H  N N 309 
HIS   HB3  H  N N 310 
HIS   HD1  H  N N 311 
HIS   HD2  H  N N 312 
HIS   HE1  H  N N 313 
HIS   HE2  H  N N 314 
HIS   HXT  H  N N 315 
HOH   O    O  N N 316 
HOH   H1   H  N N 317 
HOH   H2   H  N N 318 
ILE   N    N  N N 319 
ILE   CA   C  N S 320 
ILE   C    C  N N 321 
ILE   O    O  N N 322 
ILE   CB   C  N S 323 
ILE   CG1  C  N N 324 
ILE   CG2  C  N N 325 
ILE   CD1  C  N N 326 
ILE   OXT  O  N N 327 
ILE   H    H  N N 328 
ILE   H2   H  N N 329 
ILE   HA   H  N N 330 
ILE   HB   H  N N 331 
ILE   HG12 H  N N 332 
ILE   HG13 H  N N 333 
ILE   HG21 H  N N 334 
ILE   HG22 H  N N 335 
ILE   HG23 H  N N 336 
ILE   HD11 H  N N 337 
ILE   HD12 H  N N 338 
ILE   HD13 H  N N 339 
ILE   HXT  H  N N 340 
LEU   N    N  N N 341 
LEU   CA   C  N S 342 
LEU   C    C  N N 343 
LEU   O    O  N N 344 
LEU   CB   C  N N 345 
LEU   CG   C  N N 346 
LEU   CD1  C  N N 347 
LEU   CD2  C  N N 348 
LEU   OXT  O  N N 349 
LEU   H    H  N N 350 
LEU   H2   H  N N 351 
LEU   HA   H  N N 352 
LEU   HB2  H  N N 353 
LEU   HB3  H  N N 354 
LEU   HG   H  N N 355 
LEU   HD11 H  N N 356 
LEU   HD12 H  N N 357 
LEU   HD13 H  N N 358 
LEU   HD21 H  N N 359 
LEU   HD22 H  N N 360 
LEU   HD23 H  N N 361 
LEU   HXT  H  N N 362 
LYS   N    N  N N 363 
LYS   CA   C  N S 364 
LYS   C    C  N N 365 
LYS   O    O  N N 366 
LYS   CB   C  N N 367 
LYS   CG   C  N N 368 
LYS   CD   C  N N 369 
LYS   CE   C  N N 370 
LYS   NZ   N  N N 371 
LYS   OXT  O  N N 372 
LYS   H    H  N N 373 
LYS   H2   H  N N 374 
LYS   HA   H  N N 375 
LYS   HB2  H  N N 376 
LYS   HB3  H  N N 377 
LYS   HG2  H  N N 378 
LYS   HG3  H  N N 379 
LYS   HD2  H  N N 380 
LYS   HD3  H  N N 381 
LYS   HE2  H  N N 382 
LYS   HE3  H  N N 383 
LYS   HZ1  H  N N 384 
LYS   HZ2  H  N N 385 
LYS   HZ3  H  N N 386 
LYS   HXT  H  N N 387 
MET   N    N  N N 388 
MET   CA   C  N S 389 
MET   C    C  N N 390 
MET   O    O  N N 391 
MET   CB   C  N N 392 
MET   CG   C  N N 393 
MET   SD   S  N N 394 
MET   CE   C  N N 395 
MET   OXT  O  N N 396 
MET   H    H  N N 397 
MET   H2   H  N N 398 
MET   HA   H  N N 399 
MET   HB2  H  N N 400 
MET   HB3  H  N N 401 
MET   HG2  H  N N 402 
MET   HG3  H  N N 403 
MET   HE1  H  N N 404 
MET   HE2  H  N N 405 
MET   HE3  H  N N 406 
MET   HXT  H  N N 407 
PHE   N    N  N N 408 
PHE   CA   C  N S 409 
PHE   C    C  N N 410 
PHE   O    O  N N 411 
PHE   CB   C  N N 412 
PHE   CG   C  Y N 413 
PHE   CD1  C  Y N 414 
PHE   CD2  C  Y N 415 
PHE   CE1  C  Y N 416 
PHE   CE2  C  Y N 417 
PHE   CZ   C  Y N 418 
PHE   OXT  O  N N 419 
PHE   H    H  N N 420 
PHE   H2   H  N N 421 
PHE   HA   H  N N 422 
PHE   HB2  H  N N 423 
PHE   HB3  H  N N 424 
PHE   HD1  H  N N 425 
PHE   HD2  H  N N 426 
PHE   HE1  H  N N 427 
PHE   HE2  H  N N 428 
PHE   HZ   H  N N 429 
PHE   HXT  H  N N 430 
PRO   N    N  N N 431 
PRO   CA   C  N S 432 
PRO   C    C  N N 433 
PRO   O    O  N N 434 
PRO   CB   C  N N 435 
PRO   CG   C  N N 436 
PRO   CD   C  N N 437 
PRO   OXT  O  N N 438 
PRO   H    H  N N 439 
PRO   HA   H  N N 440 
PRO   HB2  H  N N 441 
PRO   HB3  H  N N 442 
PRO   HG2  H  N N 443 
PRO   HG3  H  N N 444 
PRO   HD2  H  N N 445 
PRO   HD3  H  N N 446 
PRO   HXT  H  N N 447 
SER   N    N  N N 448 
SER   CA   C  N S 449 
SER   C    C  N N 450 
SER   O    O  N N 451 
SER   CB   C  N N 452 
SER   OG   O  N N 453 
SER   OXT  O  N N 454 
SER   H    H  N N 455 
SER   H2   H  N N 456 
SER   HA   H  N N 457 
SER   HB2  H  N N 458 
SER   HB3  H  N N 459 
SER   HG   H  N N 460 
SER   HXT  H  N N 461 
THR   N    N  N N 462 
THR   CA   C  N S 463 
THR   C    C  N N 464 
THR   O    O  N N 465 
THR   CB   C  N R 466 
THR   OG1  O  N N 467 
THR   CG2  C  N N 468 
THR   OXT  O  N N 469 
THR   H    H  N N 470 
THR   H2   H  N N 471 
THR   HA   H  N N 472 
THR   HB   H  N N 473 
THR   HG1  H  N N 474 
THR   HG21 H  N N 475 
THR   HG22 H  N N 476 
THR   HG23 H  N N 477 
THR   HXT  H  N N 478 
TRP   N    N  N N 479 
TRP   CA   C  N S 480 
TRP   C    C  N N 481 
TRP   O    O  N N 482 
TRP   CB   C  N N 483 
TRP   CG   C  Y N 484 
TRP   CD1  C  Y N 485 
TRP   CD2  C  Y N 486 
TRP   NE1  N  Y N 487 
TRP   CE2  C  Y N 488 
TRP   CE3  C  Y N 489 
TRP   CZ2  C  Y N 490 
TRP   CZ3  C  Y N 491 
TRP   CH2  C  Y N 492 
TRP   OXT  O  N N 493 
TRP   H    H  N N 494 
TRP   H2   H  N N 495 
TRP   HA   H  N N 496 
TRP   HB2  H  N N 497 
TRP   HB3  H  N N 498 
TRP   HD1  H  N N 499 
TRP   HE1  H  N N 500 
TRP   HE3  H  N N 501 
TRP   HZ2  H  N N 502 
TRP   HZ3  H  N N 503 
TRP   HH2  H  N N 504 
TRP   HXT  H  N N 505 
TYR   N    N  N N 506 
TYR   CA   C  N S 507 
TYR   C    C  N N 508 
TYR   O    O  N N 509 
TYR   CB   C  N N 510 
TYR   CG   C  Y N 511 
TYR   CD1  C  Y N 512 
TYR   CD2  C  Y N 513 
TYR   CE1  C  Y N 514 
TYR   CE2  C  Y N 515 
TYR   CZ   C  Y N 516 
TYR   OH   O  N N 517 
TYR   OXT  O  N N 518 
TYR   H    H  N N 519 
TYR   H2   H  N N 520 
TYR   HA   H  N N 521 
TYR   HB2  H  N N 522 
TYR   HB3  H  N N 523 
TYR   HD1  H  N N 524 
TYR   HD2  H  N N 525 
TYR   HE1  H  N N 526 
TYR   HE2  H  N N 527 
TYR   HH   H  N N 528 
TYR   HXT  H  N N 529 
VAL   N    N  N N 530 
VAL   CA   C  N S 531 
VAL   C    C  N N 532 
VAL   O    O  N N 533 
VAL   CB   C  N N 534 
VAL   CG1  C  N N 535 
VAL   CG2  C  N N 536 
VAL   OXT  O  N N 537 
VAL   H    H  N N 538 
VAL   H2   H  N N 539 
VAL   HA   H  N N 540 
VAL   HB   H  N N 541 
VAL   HG11 H  N N 542 
VAL   HG12 H  N N 543 
VAL   HG13 H  N N 544 
VAL   HG21 H  N N 545 
VAL   HG22 H  N N 546 
VAL   HG23 H  N N 547 
VAL   HXT  H  N N 548 
ZN    ZN   ZN N N 549 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1AZ9 C07 C04  sing N N 1   
A1AZ9 C04 C05  doub Y N 2   
A1AZ9 C04 C03  sing Y N 3   
A1AZ9 C05 C06  sing Y N 4   
A1AZ9 C03 C02  doub Y N 5   
A1AZ9 C06 C11  sing N N 6   
A1AZ9 C06 N01  doub Y N 7   
A1AZ9 C02 N01  sing Y N 8   
A1AZ9 C02 N02  sing N N 9   
A1AZ9 F12 C12  sing N N 10  
A1AZ9 C11 C12  doub Y N 11  
A1AZ9 C11 C16  sing Y N 12  
A1AZ9 C12 C13  sing Y N 13  
A1AZ9 C16 C15  doub Y N 14  
A1AZ9 C13 F13  sing N N 15  
A1AZ9 C13 C14  doub Y N 16  
A1AZ9 C15 C14  sing Y N 17  
A1AZ9 C15 C17  sing N N 18  
A1AZ9 C17 N18  sing N N 19  
A1AZ9 C20 C19  sing N N 20  
A1AZ9 C20 F21  sing N N 21  
A1AZ9 N18 C19  sing N N 22  
A1AZ9 C14 H1   sing N N 23  
A1AZ9 C16 H2   sing N N 24  
A1AZ9 C17 H3   sing N N 25  
A1AZ9 C17 H4   sing N N 26  
A1AZ9 C19 H5   sing N N 27  
A1AZ9 C19 H6   sing N N 28  
A1AZ9 C20 H7   sing N N 29  
A1AZ9 C20 H8   sing N N 30  
A1AZ9 C03 H9   sing N N 31  
A1AZ9 C05 H10  sing N N 32  
A1AZ9 C07 H11  sing N N 33  
A1AZ9 C07 H12  sing N N 34  
A1AZ9 C07 H13  sing N N 35  
A1AZ9 N02 H14  sing N N 36  
A1AZ9 N02 H15  sing N N 37  
A1AZ9 N18 H16  sing N N 38  
ALA   N   CA   sing N N 39  
ALA   N   H    sing N N 40  
ALA   N   H2   sing N N 41  
ALA   CA  C    sing N N 42  
ALA   CA  CB   sing N N 43  
ALA   CA  HA   sing N N 44  
ALA   C   O    doub N N 45  
ALA   C   OXT  sing N N 46  
ALA   CB  HB1  sing N N 47  
ALA   CB  HB2  sing N N 48  
ALA   CB  HB3  sing N N 49  
ALA   OXT HXT  sing N N 50  
ARG   N   CA   sing N N 51  
ARG   N   H    sing N N 52  
ARG   N   H2   sing N N 53  
ARG   CA  C    sing N N 54  
ARG   CA  CB   sing N N 55  
ARG   CA  HA   sing N N 56  
ARG   C   O    doub N N 57  
ARG   C   OXT  sing N N 58  
ARG   CB  CG   sing N N 59  
ARG   CB  HB2  sing N N 60  
ARG   CB  HB3  sing N N 61  
ARG   CG  CD   sing N N 62  
ARG   CG  HG2  sing N N 63  
ARG   CG  HG3  sing N N 64  
ARG   CD  NE   sing N N 65  
ARG   CD  HD2  sing N N 66  
ARG   CD  HD3  sing N N 67  
ARG   NE  CZ   sing N N 68  
ARG   NE  HE   sing N N 69  
ARG   CZ  NH1  sing N N 70  
ARG   CZ  NH2  doub N N 71  
ARG   NH1 HH11 sing N N 72  
ARG   NH1 HH12 sing N N 73  
ARG   NH2 HH21 sing N N 74  
ARG   NH2 HH22 sing N N 75  
ARG   OXT HXT  sing N N 76  
ASN   N   CA   sing N N 77  
ASN   N   H    sing N N 78  
ASN   N   H2   sing N N 79  
ASN   CA  C    sing N N 80  
ASN   CA  CB   sing N N 81  
ASN   CA  HA   sing N N 82  
ASN   C   O    doub N N 83  
ASN   C   OXT  sing N N 84  
ASN   CB  CG   sing N N 85  
ASN   CB  HB2  sing N N 86  
ASN   CB  HB3  sing N N 87  
ASN   CG  OD1  doub N N 88  
ASN   CG  ND2  sing N N 89  
ASN   ND2 HD21 sing N N 90  
ASN   ND2 HD22 sing N N 91  
ASN   OXT HXT  sing N N 92  
ASP   N   CA   sing N N 93  
ASP   N   H    sing N N 94  
ASP   N   H2   sing N N 95  
ASP   CA  C    sing N N 96  
ASP   CA  CB   sing N N 97  
ASP   CA  HA   sing N N 98  
ASP   C   O    doub N N 99  
ASP   C   OXT  sing N N 100 
ASP   CB  CG   sing N N 101 
ASP   CB  HB2  sing N N 102 
ASP   CB  HB3  sing N N 103 
ASP   CG  OD1  doub N N 104 
ASP   CG  OD2  sing N N 105 
ASP   OD2 HD2  sing N N 106 
ASP   OXT HXT  sing N N 107 
CYS   N   CA   sing N N 108 
CYS   N   H    sing N N 109 
CYS   N   H2   sing N N 110 
CYS   CA  C    sing N N 111 
CYS   CA  CB   sing N N 112 
CYS   CA  HA   sing N N 113 
CYS   C   O    doub N N 114 
CYS   C   OXT  sing N N 115 
CYS   CB  SG   sing N N 116 
CYS   CB  HB2  sing N N 117 
CYS   CB  HB3  sing N N 118 
CYS   SG  HG   sing N N 119 
CYS   OXT HXT  sing N N 120 
GLN   N   CA   sing N N 121 
GLN   N   H    sing N N 122 
GLN   N   H2   sing N N 123 
GLN   CA  C    sing N N 124 
GLN   CA  CB   sing N N 125 
GLN   CA  HA   sing N N 126 
GLN   C   O    doub N N 127 
GLN   C   OXT  sing N N 128 
GLN   CB  CG   sing N N 129 
GLN   CB  HB2  sing N N 130 
GLN   CB  HB3  sing N N 131 
GLN   CG  CD   sing N N 132 
GLN   CG  HG2  sing N N 133 
GLN   CG  HG3  sing N N 134 
GLN   CD  OE1  doub N N 135 
GLN   CD  NE2  sing N N 136 
GLN   NE2 HE21 sing N N 137 
GLN   NE2 HE22 sing N N 138 
GLN   OXT HXT  sing N N 139 
GLU   N   CA   sing N N 140 
GLU   N   H    sing N N 141 
GLU   N   H2   sing N N 142 
GLU   CA  C    sing N N 143 
GLU   CA  CB   sing N N 144 
GLU   CA  HA   sing N N 145 
GLU   C   O    doub N N 146 
GLU   C   OXT  sing N N 147 
GLU   CB  CG   sing N N 148 
GLU   CB  HB2  sing N N 149 
GLU   CB  HB3  sing N N 150 
GLU   CG  CD   sing N N 151 
GLU   CG  HG2  sing N N 152 
GLU   CG  HG3  sing N N 153 
GLU   CD  OE1  doub N N 154 
GLU   CD  OE2  sing N N 155 
GLU   OE2 HE2  sing N N 156 
GLU   OXT HXT  sing N N 157 
GLY   N   CA   sing N N 158 
GLY   N   H    sing N N 159 
GLY   N   H2   sing N N 160 
GLY   CA  C    sing N N 161 
GLY   CA  HA2  sing N N 162 
GLY   CA  HA3  sing N N 163 
GLY   C   O    doub N N 164 
GLY   C   OXT  sing N N 165 
GLY   OXT HXT  sing N N 166 
GOL   C1  O1   sing N N 167 
GOL   C1  C2   sing N N 168 
GOL   C1  H11  sing N N 169 
GOL   C1  H12  sing N N 170 
GOL   O1  HO1  sing N N 171 
GOL   C2  O2   sing N N 172 
GOL   C2  C3   sing N N 173 
GOL   C2  H2   sing N N 174 
GOL   O2  HO2  sing N N 175 
GOL   C3  O3   sing N N 176 
GOL   C3  H31  sing N N 177 
GOL   C3  H32  sing N N 178 
GOL   O3  HO3  sing N N 179 
H4B   N1  C2   doub Y N 180 
H4B   N1  C8A  sing Y N 181 
H4B   C2  N2   sing N N 182 
H4B   C2  N3   sing Y N 183 
H4B   N2  HN21 sing N N 184 
H4B   N2  HN22 sing N N 185 
H4B   N3  C4   sing Y N 186 
H4B   N3  HN3  sing N N 187 
H4B   C4  O4   doub N N 188 
H4B   C4  C4A  sing Y N 189 
H4B   C4A C8A  doub Y N 190 
H4B   C4A N5   sing N N 191 
H4B   C8A N8   sing N N 192 
H4B   N5  C6   sing N N 193 
H4B   N5  HN5  sing N N 194 
H4B   N8  C7   sing N N 195 
H4B   N8  HN8  sing N N 196 
H4B   C6  C7   sing N N 197 
H4B   C6  C9   sing N N 198 
H4B   C6  H6   sing N N 199 
H4B   C7  H71  sing N N 200 
H4B   C7  H72  sing N N 201 
H4B   C9  O9   sing N N 202 
H4B   C9  C10  sing N N 203 
H4B   C9  H9   sing N N 204 
H4B   O9  HO9  sing N N 205 
H4B   C10 C11  sing N N 206 
H4B   C10 O10  sing N N 207 
H4B   C10 H10  sing N N 208 
H4B   C11 H111 sing N N 209 
H4B   C11 H112 sing N N 210 
H4B   C11 H113 sing N N 211 
H4B   O10 HO0  sing N N 212 
HEM   CHA C1A  sing N N 213 
HEM   CHA C4D  doub N N 214 
HEM   CHA HHA  sing N N 215 
HEM   CHB C4A  sing N N 216 
HEM   CHB C1B  doub N N 217 
HEM   CHB HHB  sing N N 218 
HEM   CHC C4B  sing N N 219 
HEM   CHC C1C  doub N N 220 
HEM   CHC HHC  sing N N 221 
HEM   CHD C4C  doub N N 222 
HEM   CHD C1D  sing N N 223 
HEM   CHD HHD  sing N N 224 
HEM   C1A C2A  doub Y N 225 
HEM   C1A NA   sing Y N 226 
HEM   C2A C3A  sing Y N 227 
HEM   C2A CAA  sing N N 228 
HEM   C3A C4A  doub Y N 229 
HEM   C3A CMA  sing N N 230 
HEM   C4A NA   sing Y N 231 
HEM   CMA HMA  sing N N 232 
HEM   CMA HMAA sing N N 233 
HEM   CMA HMAB sing N N 234 
HEM   CAA CBA  sing N N 235 
HEM   CAA HAA  sing N N 236 
HEM   CAA HAAA sing N N 237 
HEM   CBA CGA  sing N N 238 
HEM   CBA HBA  sing N N 239 
HEM   CBA HBAA sing N N 240 
HEM   CGA O1A  doub N N 241 
HEM   CGA O2A  sing N N 242 
HEM   C1B C2B  sing N N 243 
HEM   C1B NB   sing N N 244 
HEM   C2B C3B  doub N N 245 
HEM   C2B CMB  sing N N 246 
HEM   C3B C4B  sing N N 247 
HEM   C3B CAB  sing N N 248 
HEM   C4B NB   doub N N 249 
HEM   CMB HMB  sing N N 250 
HEM   CMB HMBA sing N N 251 
HEM   CMB HMBB sing N N 252 
HEM   CAB CBB  doub N N 253 
HEM   CAB HAB  sing N N 254 
HEM   CBB HBB  sing N N 255 
HEM   CBB HBBA sing N N 256 
HEM   C1C C2C  sing Y N 257 
HEM   C1C NC   sing Y N 258 
HEM   C2C C3C  doub Y N 259 
HEM   C2C CMC  sing N N 260 
HEM   C3C C4C  sing Y N 261 
HEM   C3C CAC  sing N N 262 
HEM   C4C NC   sing Y N 263 
HEM   CMC HMC  sing N N 264 
HEM   CMC HMCA sing N N 265 
HEM   CMC HMCB sing N N 266 
HEM   CAC CBC  doub N N 267 
HEM   CAC HAC  sing N N 268 
HEM   CBC HBC  sing N N 269 
HEM   CBC HBCA sing N N 270 
HEM   C1D C2D  sing N N 271 
HEM   C1D ND   doub N N 272 
HEM   C2D C3D  doub N N 273 
HEM   C2D CMD  sing N N 274 
HEM   C3D C4D  sing N N 275 
HEM   C3D CAD  sing N N 276 
HEM   C4D ND   sing N N 277 
HEM   CMD HMD  sing N N 278 
HEM   CMD HMDA sing N N 279 
HEM   CMD HMDB sing N N 280 
HEM   CAD CBD  sing N N 281 
HEM   CAD HAD  sing N N 282 
HEM   CAD HADA sing N N 283 
HEM   CBD CGD  sing N N 284 
HEM   CBD HBD  sing N N 285 
HEM   CBD HBDA sing N N 286 
HEM   CGD O1D  doub N N 287 
HEM   CGD O2D  sing N N 288 
HEM   O2A H2A  sing N N 289 
HEM   O2D H2D  sing N N 290 
HEM   FE  NA   sing N N 291 
HEM   FE  NB   sing N N 292 
HEM   FE  NC   sing N N 293 
HEM   FE  ND   sing N N 294 
HIS   N   CA   sing N N 295 
HIS   N   H    sing N N 296 
HIS   N   H2   sing N N 297 
HIS   CA  C    sing N N 298 
HIS   CA  CB   sing N N 299 
HIS   CA  HA   sing N N 300 
HIS   C   O    doub N N 301 
HIS   C   OXT  sing N N 302 
HIS   CB  CG   sing N N 303 
HIS   CB  HB2  sing N N 304 
HIS   CB  HB3  sing N N 305 
HIS   CG  ND1  sing Y N 306 
HIS   CG  CD2  doub Y N 307 
HIS   ND1 CE1  doub Y N 308 
HIS   ND1 HD1  sing N N 309 
HIS   CD2 NE2  sing Y N 310 
HIS   CD2 HD2  sing N N 311 
HIS   CE1 NE2  sing Y N 312 
HIS   CE1 HE1  sing N N 313 
HIS   NE2 HE2  sing N N 314 
HIS   OXT HXT  sing N N 315 
HOH   O   H1   sing N N 316 
HOH   O   H2   sing N N 317 
ILE   N   CA   sing N N 318 
ILE   N   H    sing N N 319 
ILE   N   H2   sing N N 320 
ILE   CA  C    sing N N 321 
ILE   CA  CB   sing N N 322 
ILE   CA  HA   sing N N 323 
ILE   C   O    doub N N 324 
ILE   C   OXT  sing N N 325 
ILE   CB  CG1  sing N N 326 
ILE   CB  CG2  sing N N 327 
ILE   CB  HB   sing N N 328 
ILE   CG1 CD1  sing N N 329 
ILE   CG1 HG12 sing N N 330 
ILE   CG1 HG13 sing N N 331 
ILE   CG2 HG21 sing N N 332 
ILE   CG2 HG22 sing N N 333 
ILE   CG2 HG23 sing N N 334 
ILE   CD1 HD11 sing N N 335 
ILE   CD1 HD12 sing N N 336 
ILE   CD1 HD13 sing N N 337 
ILE   OXT HXT  sing N N 338 
LEU   N   CA   sing N N 339 
LEU   N   H    sing N N 340 
LEU   N   H2   sing N N 341 
LEU   CA  C    sing N N 342 
LEU   CA  CB   sing N N 343 
LEU   CA  HA   sing N N 344 
LEU   C   O    doub N N 345 
LEU   C   OXT  sing N N 346 
LEU   CB  CG   sing N N 347 
LEU   CB  HB2  sing N N 348 
LEU   CB  HB3  sing N N 349 
LEU   CG  CD1  sing N N 350 
LEU   CG  CD2  sing N N 351 
LEU   CG  HG   sing N N 352 
LEU   CD1 HD11 sing N N 353 
LEU   CD1 HD12 sing N N 354 
LEU   CD1 HD13 sing N N 355 
LEU   CD2 HD21 sing N N 356 
LEU   CD2 HD22 sing N N 357 
LEU   CD2 HD23 sing N N 358 
LEU   OXT HXT  sing N N 359 
LYS   N   CA   sing N N 360 
LYS   N   H    sing N N 361 
LYS   N   H2   sing N N 362 
LYS   CA  C    sing N N 363 
LYS   CA  CB   sing N N 364 
LYS   CA  HA   sing N N 365 
LYS   C   O    doub N N 366 
LYS   C   OXT  sing N N 367 
LYS   CB  CG   sing N N 368 
LYS   CB  HB2  sing N N 369 
LYS   CB  HB3  sing N N 370 
LYS   CG  CD   sing N N 371 
LYS   CG  HG2  sing N N 372 
LYS   CG  HG3  sing N N 373 
LYS   CD  CE   sing N N 374 
LYS   CD  HD2  sing N N 375 
LYS   CD  HD3  sing N N 376 
LYS   CE  NZ   sing N N 377 
LYS   CE  HE2  sing N N 378 
LYS   CE  HE3  sing N N 379 
LYS   NZ  HZ1  sing N N 380 
LYS   NZ  HZ2  sing N N 381 
LYS   NZ  HZ3  sing N N 382 
LYS   OXT HXT  sing N N 383 
MET   N   CA   sing N N 384 
MET   N   H    sing N N 385 
MET   N   H2   sing N N 386 
MET   CA  C    sing N N 387 
MET   CA  CB   sing N N 388 
MET   CA  HA   sing N N 389 
MET   C   O    doub N N 390 
MET   C   OXT  sing N N 391 
MET   CB  CG   sing N N 392 
MET   CB  HB2  sing N N 393 
MET   CB  HB3  sing N N 394 
MET   CG  SD   sing N N 395 
MET   CG  HG2  sing N N 396 
MET   CG  HG3  sing N N 397 
MET   SD  CE   sing N N 398 
MET   CE  HE1  sing N N 399 
MET   CE  HE2  sing N N 400 
MET   CE  HE3  sing N N 401 
MET   OXT HXT  sing N N 402 
PHE   N   CA   sing N N 403 
PHE   N   H    sing N N 404 
PHE   N   H2   sing N N 405 
PHE   CA  C    sing N N 406 
PHE   CA  CB   sing N N 407 
PHE   CA  HA   sing N N 408 
PHE   C   O    doub N N 409 
PHE   C   OXT  sing N N 410 
PHE   CB  CG   sing N N 411 
PHE   CB  HB2  sing N N 412 
PHE   CB  HB3  sing N N 413 
PHE   CG  CD1  doub Y N 414 
PHE   CG  CD2  sing Y N 415 
PHE   CD1 CE1  sing Y N 416 
PHE   CD1 HD1  sing N N 417 
PHE   CD2 CE2  doub Y N 418 
PHE   CD2 HD2  sing N N 419 
PHE   CE1 CZ   doub Y N 420 
PHE   CE1 HE1  sing N N 421 
PHE   CE2 CZ   sing Y N 422 
PHE   CE2 HE2  sing N N 423 
PHE   CZ  HZ   sing N N 424 
PHE   OXT HXT  sing N N 425 
PRO   N   CA   sing N N 426 
PRO   N   CD   sing N N 427 
PRO   N   H    sing N N 428 
PRO   CA  C    sing N N 429 
PRO   CA  CB   sing N N 430 
PRO   CA  HA   sing N N 431 
PRO   C   O    doub N N 432 
PRO   C   OXT  sing N N 433 
PRO   CB  CG   sing N N 434 
PRO   CB  HB2  sing N N 435 
PRO   CB  HB3  sing N N 436 
PRO   CG  CD   sing N N 437 
PRO   CG  HG2  sing N N 438 
PRO   CG  HG3  sing N N 439 
PRO   CD  HD2  sing N N 440 
PRO   CD  HD3  sing N N 441 
PRO   OXT HXT  sing N N 442 
SER   N   CA   sing N N 443 
SER   N   H    sing N N 444 
SER   N   H2   sing N N 445 
SER   CA  C    sing N N 446 
SER   CA  CB   sing N N 447 
SER   CA  HA   sing N N 448 
SER   C   O    doub N N 449 
SER   C   OXT  sing N N 450 
SER   CB  OG   sing N N 451 
SER   CB  HB2  sing N N 452 
SER   CB  HB3  sing N N 453 
SER   OG  HG   sing N N 454 
SER   OXT HXT  sing N N 455 
THR   N   CA   sing N N 456 
THR   N   H    sing N N 457 
THR   N   H2   sing N N 458 
THR   CA  C    sing N N 459 
THR   CA  CB   sing N N 460 
THR   CA  HA   sing N N 461 
THR   C   O    doub N N 462 
THR   C   OXT  sing N N 463 
THR   CB  OG1  sing N N 464 
THR   CB  CG2  sing N N 465 
THR   CB  HB   sing N N 466 
THR   OG1 HG1  sing N N 467 
THR   CG2 HG21 sing N N 468 
THR   CG2 HG22 sing N N 469 
THR   CG2 HG23 sing N N 470 
THR   OXT HXT  sing N N 471 
TRP   N   CA   sing N N 472 
TRP   N   H    sing N N 473 
TRP   N   H2   sing N N 474 
TRP   CA  C    sing N N 475 
TRP   CA  CB   sing N N 476 
TRP   CA  HA   sing N N 477 
TRP   C   O    doub N N 478 
TRP   C   OXT  sing N N 479 
TRP   CB  CG   sing N N 480 
TRP   CB  HB2  sing N N 481 
TRP   CB  HB3  sing N N 482 
TRP   CG  CD1  doub Y N 483 
TRP   CG  CD2  sing Y N 484 
TRP   CD1 NE1  sing Y N 485 
TRP   CD1 HD1  sing N N 486 
TRP   CD2 CE2  doub Y N 487 
TRP   CD2 CE3  sing Y N 488 
TRP   NE1 CE2  sing Y N 489 
TRP   NE1 HE1  sing N N 490 
TRP   CE2 CZ2  sing Y N 491 
TRP   CE3 CZ3  doub Y N 492 
TRP   CE3 HE3  sing N N 493 
TRP   CZ2 CH2  doub Y N 494 
TRP   CZ2 HZ2  sing N N 495 
TRP   CZ3 CH2  sing Y N 496 
TRP   CZ3 HZ3  sing N N 497 
TRP   CH2 HH2  sing N N 498 
TRP   OXT HXT  sing N N 499 
TYR   N   CA   sing N N 500 
TYR   N   H    sing N N 501 
TYR   N   H2   sing N N 502 
TYR   CA  C    sing N N 503 
TYR   CA  CB   sing N N 504 
TYR   CA  HA   sing N N 505 
TYR   C   O    doub N N 506 
TYR   C   OXT  sing N N 507 
TYR   CB  CG   sing N N 508 
TYR   CB  HB2  sing N N 509 
TYR   CB  HB3  sing N N 510 
TYR   CG  CD1  doub Y N 511 
TYR   CG  CD2  sing Y N 512 
TYR   CD1 CE1  sing Y N 513 
TYR   CD1 HD1  sing N N 514 
TYR   CD2 CE2  doub Y N 515 
TYR   CD2 HD2  sing N N 516 
TYR   CE1 CZ   doub Y N 517 
TYR   CE1 HE1  sing N N 518 
TYR   CE2 CZ   sing Y N 519 
TYR   CE2 HE2  sing N N 520 
TYR   CZ  OH   sing N N 521 
TYR   OH  HH   sing N N 522 
TYR   OXT HXT  sing N N 523 
VAL   N   CA   sing N N 524 
VAL   N   H    sing N N 525 
VAL   N   H2   sing N N 526 
VAL   CA  C    sing N N 527 
VAL   CA  CB   sing N N 528 
VAL   CA  HA   sing N N 529 
VAL   C   O    doub N N 530 
VAL   C   OXT  sing N N 531 
VAL   CB  CG1  sing N N 532 
VAL   CB  CG2  sing N N 533 
VAL   CB  HB   sing N N 534 
VAL   CG1 HG11 sing N N 535 
VAL   CG1 HG12 sing N N 536 
VAL   CG1 HG13 sing N N 537 
VAL   CG2 HG21 sing N N 538 
VAL   CG2 HG22 sing N N 539 
VAL   CG2 HG23 sing N N 540 
VAL   OXT HXT  sing N N 541 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           GM131920 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7TS7 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9CVZ 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.008420 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.019167 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.006080 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
F  
FE 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N   . ARG   A  1 3   ? -51.259 27.981  -21.003  1.00 83.84  ? 304  ARG   A N   1 
ATOM   2     C  CA  . ARG   A  1 3   ? -50.910 29.312  -21.498  1.00 92.21  ? 304  ARG   A CA  1 
ATOM   3     C  C   . ARG   A  1 3   ? -49.403 29.429  -21.761  1.00 94.16  ? 304  ARG   A C   1 
ATOM   4     O  O   . ARG   A  1 3   ? -48.978 29.859  -22.835  1.00 99.70  ? 304  ARG   A O   1 
ATOM   5     C  CB  . ARG   A  1 3   ? -51.368 30.387  -20.506  1.00 101.37 ? 304  ARG   A CB  1 
ATOM   6     C  CG  . ARG   A  1 3   ? -51.162 31.829  -20.956  1.00 104.78 ? 304  ARG   A CG  1 
ATOM   7     C  CD  . ARG   A  1 3   ? -52.083 32.207  -22.106  1.00 108.91 ? 304  ARG   A CD  1 
ATOM   8     N  NE  . ARG   A  1 3   ? -51.609 31.711  -23.397  1.00 109.97 ? 304  ARG   A NE  1 
ATOM   9     C  CZ  . ARG   A  1 3   ? -52.148 32.041  -24.566  1.00 112.91 ? 304  ARG   A CZ  1 
ATOM   10    N  NH1 . ARG   A  1 3   ? -53.176 32.878  -24.603  1.00 115.83 ? 304  ARG   A NH1 1 
ATOM   11    N  NH2 . ARG   A  1 3   ? -51.656 31.544  -25.698  1.00 111.57 ? 304  ARG   A NH2 1 
ATOM   12    N  N   . PHE   A  1 4   ? -48.598 29.057  -20.769  1.00 82.97  ? 305  PHE   A N   1 
ATOM   13    C  CA  . PHE   A  1 4   ? -47.158 28.935  -20.931  1.00 79.97  ? 305  PHE   A CA  1 
ATOM   14    C  C   . PHE   A  1 4   ? -46.709 27.708  -20.156  1.00 74.26  ? 305  PHE   A C   1 
ATOM   15    O  O   . PHE   A  1 4   ? -47.480 27.119  -19.398  1.00 81.17  ? 305  PHE   A O   1 
ATOM   16    C  CB  . PHE   A  1 4   ? -46.402 30.182  -20.446  1.00 90.69  ? 305  PHE   A CB  1 
ATOM   17    C  CG  . PHE   A  1 4   ? -46.699 31.434  -21.236  1.00 107.62 ? 305  PHE   A CG  1 
ATOM   18    C  CD1 . PHE   A  1 4   ? -47.741 32.279  -20.864  1.00 116.19 ? 305  PHE   A CD1 1 
ATOM   19    C  CD2 . PHE   A  1 4   ? -45.926 31.783  -22.338  1.00 108.26 ? 305  PHE   A CD2 1 
ATOM   20    C  CE1 . PHE   A  1 4   ? -48.016 33.444  -21.586  1.00 115.51 ? 305  PHE   A CE1 1 
ATOM   21    C  CE2 . PHE   A  1 4   ? -46.190 32.950  -23.064  1.00 108.64 ? 305  PHE   A CE2 1 
ATOM   22    C  CZ  . PHE   A  1 4   ? -47.236 33.779  -22.686  1.00 111.56 ? 305  PHE   A CZ  1 
ATOM   23    N  N   . LEU   A  1 5   ? -45.453 27.315  -20.358  1.00 57.84  ? 306  LEU   A N   1 
ATOM   24    C  CA  . LEU   A  1 5   ? -44.861 26.192  -19.643  1.00 49.22  ? 306  LEU   A CA  1 
ATOM   25    C  C   . LEU   A  1 5   ? -43.359 26.403  -19.604  1.00 60.04  ? 306  LEU   A C   1 
ATOM   26    O  O   . LEU   A  1 5   ? -42.771 26.844  -20.592  1.00 67.64  ? 306  LEU   A O   1 
ATOM   27    C  CB  . LEU   A  1 5   ? -45.184 24.848  -20.301  1.00 44.71  ? 306  LEU   A CB  1 
ATOM   28    C  CG  . LEU   A  1 5   ? -46.492 24.157  -19.902  1.00 50.34  ? 306  LEU   A CG  1 
ATOM   29    C  CD1 . LEU   A  1 5   ? -46.733 22.880  -20.695  1.00 51.79  ? 306  LEU   A CD1 1 
ATOM   30    C  CD2 . LEU   A  1 5   ? -46.502 23.863  -18.423  1.00 56.79  ? 306  LEU   A CD2 1 
ATOM   31    N  N   . LYS   A  1 6   ? -42.746 26.092  -18.467  1.00 64.64  ? 307  LYS   A N   1 
ATOM   32    C  CA  . LYS   A  1 6   ? -41.330 26.347  -18.260  1.00 59.13  ? 307  LYS   A CA  1 
ATOM   33    C  C   . LYS   A  1 6   ? -40.571 25.035  -18.151  1.00 54.21  ? 307  LYS   A C   1 
ATOM   34    O  O   . LYS   A  1 6   ? -41.048 24.073  -17.535  1.00 50.24  ? 307  LYS   A O   1 
ATOM   35    C  CB  . LYS   A  1 6   ? -41.097 27.203  -17.017  1.00 58.28  ? 307  LYS   A CB  1 
ATOM   36    C  CG  . LYS   A  1 6   ? -41.329 28.683  -17.272  1.00 65.93  ? 307  LYS   A CG  1 
ATOM   37    C  CD  . LYS   A  1 6   ? -40.819 29.539  -16.123  1.00 77.04  ? 307  LYS   A CD  1 
ATOM   38    C  CE  . LYS   A  1 6   ? -41.467 30.931  -16.104  1.00 87.43  ? 307  LYS   A CE  1 
ATOM   39    N  NZ  . LYS   A  1 6   ? -41.329 31.679  -17.397  1.00 87.75  ? 307  LYS   A NZ  1 
ATOM   40    N  N   . VAL   A  1 7   ? -39.411 24.995  -18.802  1.00 48.84  ? 308  VAL   A N   1 
ATOM   41    C  CA  . VAL   A  1 7   ? -38.440 23.921  -18.649  1.00 50.86  ? 308  VAL   A CA  1 
ATOM   42    C  C   . VAL   A  1 7   ? -37.190 24.561  -18.083  1.00 51.37  ? 308  VAL   A C   1 
ATOM   43    O  O   . VAL   A  1 7   ? -36.841 25.684  -18.462  1.00 47.90  ? 308  VAL   A O   1 
ATOM   44    C  CB  . VAL   A  1 7   ? -38.131 23.165  -19.970  1.00 40.83  ? 308  VAL   A CB  1 
ATOM   45    C  CG1 . VAL   A  1 7   ? -39.367 22.478  -20.476  1.00 36.82  ? 308  VAL   A CG1 1 
ATOM   46    C  CG2 . VAL   A  1 7   ? -37.564 24.087  -21.025  1.00 38.99  ? 308  VAL   A CG2 1 
ATOM   47    N  N   . LYS   A  1 8   ? -36.544 23.861  -17.158  1.00 51.45  ? 309  LYS   A N   1 
ATOM   48    C  CA  . LYS   A  1 8   ? -35.378 24.358  -16.451  1.00 44.84  ? 309  LYS   A CA  1 
ATOM   49    C  C   . LYS   A  1 8   ? -34.212 23.424  -16.725  1.00 46.24  ? 309  LYS   A C   1 
ATOM   50    O  O   . LYS   A  1 8   ? -34.393 22.205  -16.796  1.00 56.57  ? 309  LYS   A O   1 
ATOM   51    C  CB  . LYS   A  1 8   ? -35.659 24.451  -14.946  1.00 38.53  ? 309  LYS   A CB  1 
ATOM   52    C  CG  . LYS   A  1 8   ? -34.422 24.616  -14.057  1.00 46.69  ? 309  LYS   A CG  1 
ATOM   53    C  CD  . LYS   A  1 8   ? -34.827 24.783  -12.584  1.00 53.85  ? 309  LYS   A CD  1 
ATOM   54    C  CE  . LYS   A  1 8   ? -33.638 24.829  -11.653  1.00 53.79  ? 309  LYS   A CE  1 
ATOM   55    N  NZ  . LYS   A  1 8   ? -34.095 25.083  -10.255  1.00 68.01  ? 309  LYS   A NZ  1 
ATOM   56    N  N   . ASN   A  1 9   ? -33.027 23.995  -16.912  1.00 46.70  ? 310  ASN   A N   1 
ATOM   57    C  CA  . ASN   A  1 9   ? -31.800 23.210  -16.961  1.00 55.37  ? 310  ASN   A CA  1 
ATOM   58    C  C   . ASN   A  1 9   ? -31.220 23.154  -15.557  1.00 54.02  ? 310  ASN   A C   1 
ATOM   59    O  O   . ASN   A  1 9   ? -30.860 24.190  -14.990  1.00 57.44  ? 310  ASN   A O   1 
ATOM   60    C  CB  . ASN   A  1 9   ? -30.784 23.806  -17.934  1.00 57.44  ? 310  ASN   A CB  1 
ATOM   61    C  CG  . ASN   A  1 9   ? -29.608 22.876  -18.177  1.00 58.98  ? 310  ASN   A CG  1 
ATOM   62    O  OD1 . ASN   A  1 9   ? -28.740 22.713  -17.317  1.00 56.76  ? 310  ASN   A OD1 1 
ATOM   63    N  ND2 . ASN   A  1 9   ? -29.581 22.251  -19.352  1.00 66.53  ? 310  ASN   A ND2 1 
ATOM   64    N  N   . TRP   A  1 10  ? -31.142 21.955  -14.988  1.00 53.65  ? 311  TRP   A N   1 
ATOM   65    C  CA  . TRP   A  1 10  ? -30.732 21.847  -13.595  1.00 48.96  ? 311  TRP   A CA  1 
ATOM   66    C  C   . TRP   A  1 10  ? -29.223 21.938  -13.413  1.00 50.61  ? 311  TRP   A C   1 
ATOM   67    O  O   . TRP   A  1 10  ? -28.749 21.930  -12.274  1.00 57.54  ? 311  TRP   A O   1 
ATOM   68    C  CB  . TRP   A  1 10  ? -31.291 20.557  -12.987  1.00 42.57  ? 311  TRP   A CB  1 
ATOM   69    C  CG  . TRP   A  1 10  ? -32.766 20.650  -12.695  1.00 48.47  ? 311  TRP   A CG  1 
ATOM   70    C  CD1 . TRP   A  1 10  ? -33.792 20.317  -13.533  1.00 47.68  ? 311  TRP   A CD1 1 
ATOM   71    C  CD2 . TRP   A  1 10  ? -33.378 21.141  -11.494  1.00 49.02  ? 311  TRP   A CD2 1 
ATOM   72    N  NE1 . TRP   A  1 10  ? -35.002 20.552  -12.919  1.00 50.35  ? 311  TRP   A NE1 1 
ATOM   73    C  CE2 . TRP   A  1 10  ? -34.772 21.058  -11.668  1.00 54.07  ? 311  TRP   A CE2 1 
ATOM   74    C  CE3 . TRP   A  1 10  ? -32.881 21.633  -10.285  1.00 58.66  ? 311  TRP   A CE3 1 
ATOM   75    C  CZ2 . TRP   A  1 10  ? -35.673 21.449  -10.675  1.00 60.98  ? 311  TRP   A CZ2 1 
ATOM   76    C  CZ3 . TRP   A  1 10  ? -33.783 22.019  -9.297   1.00 57.28  ? 311  TRP   A CZ3 1 
ATOM   77    C  CH2 . TRP   A  1 10  ? -35.157 21.922  -9.498   1.00 57.56  ? 311  TRP   A CH2 1 
ATOM   78    N  N   . GLU   A  1 11  ? -28.463 22.058  -14.497  1.00 56.15  ? 312  GLU   A N   1 
ATOM   79    C  CA  . GLU   A  1 11  ? -27.015 22.234  -14.449  1.00 52.56  ? 312  GLU   A CA  1 
ATOM   80    C  C   . GLU   A  1 11  ? -26.599 23.692  -14.576  1.00 56.45  ? 312  GLU   A C   1 
ATOM   81    O  O   . GLU   A  1 11  ? -25.586 24.090  -13.993  1.00 62.39  ? 312  GLU   A O   1 
ATOM   82    C  CB  . GLU   A  1 11  ? -26.349 21.410  -15.567  1.00 40.42  ? 312  GLU   A CB  1 
ATOM   83    C  CG  . GLU   A  1 11  ? -24.830 21.384  -15.541  1.00 46.87  ? 312  GLU   A CG  1 
ATOM   84    C  CD  . GLU   A  1 11  ? -24.228 20.941  -16.869  1.00 68.03  ? 312  GLU   A CD  1 
ATOM   85    O  OE1 . GLU   A  1 11  ? -24.986 20.409  -17.720  1.00 74.05  ? 312  GLU   A OE1 1 
ATOM   86    O  OE2 . GLU   A  1 11  ? -23.000 21.134  -17.060  1.00 72.26  ? 312  GLU   A OE2 1 
ATOM   87    N  N   . THR   A  1 12  ? -27.381 24.492  -15.306  1.00 59.21  ? 313  THR   A N   1 
ATOM   88    C  CA  . THR   A  1 12  ? -27.089 25.889  -15.591  1.00 49.02  ? 313  THR   A CA  1 
ATOM   89    C  C   . THR   A  1 12  ? -28.174 26.843  -15.114  1.00 54.71  ? 313  THR   A C   1 
ATOM   90    O  O   . THR   A  1 12  ? -28.043 28.051  -15.325  1.00 57.65  ? 313  THR   A O   1 
ATOM   91    C  CB  . THR   A  1 12  ? -26.899 26.099  -17.096  1.00 54.57  ? 313  THR   A CB  1 
ATOM   92    O  OG1 . THR   A  1 12  ? -28.140 25.849  -17.776  1.00 55.30  ? 313  THR   A OG1 1 
ATOM   93    C  CG2 . THR   A  1 12  ? -25.833 25.166  -17.636  1.00 56.18  ? 313  THR   A CG2 1 
ATOM   94    N  N   . GLU   A  1 13  ? -29.256 26.337  -14.518  1.00 60.53  ? 314  GLU   A N   1 
ATOM   95    C  CA  . GLU   A  1 13  ? -30.386 27.135  -14.033  1.00 63.28  ? 314  GLU   A CA  1 
ATOM   96    C  C   . GLU   A  1 13  ? -31.141 27.884  -15.143  1.00 65.59  ? 314  GLU   A C   1 
ATOM   97    O  O   . GLU   A  1 13  ? -32.092 28.618  -14.846  1.00 65.31  ? 314  GLU   A O   1 
ATOM   98    C  CB  . GLU   A  1 13  ? -29.925 28.126  -12.953  1.00 65.17  ? 314  GLU   A CB  1 
ATOM   99    C  CG  . GLU   A  1 13  ? -28.928 27.572  -11.938  1.00 61.91  ? 314  GLU   A CG  1 
ATOM   100   C  CD  . GLU   A  1 13  ? -29.567 27.093  -10.653  1.00 78.46  ? 314  GLU   A CD  1 
ATOM   101   O  OE1 . GLU   A  1 13  ? -30.721 26.605  -10.671  1.00 83.37  ? 314  GLU   A OE1 1 
ATOM   102   O  OE2 . GLU   A  1 13  ? -28.896 27.205  -9.608   1.00 87.01  ? 314  GLU   A OE2 1 
ATOM   103   N  N   . VAL   A  1 14  ? -30.752 27.685  -16.414  1.00 64.10  ? 315  VAL   A N   1 
ATOM   104   C  CA  . VAL   A  1 14  ? -31.414 28.341  -17.543  1.00 60.86  ? 315  VAL   A CA  1 
ATOM   105   C  C   . VAL   A  1 14  ? -32.859 27.870  -17.664  1.00 66.97  ? 315  VAL   A C   1 
ATOM   106   O  O   . VAL   A  1 14  ? -33.150 26.671  -17.559  1.00 70.04  ? 315  VAL   A O   1 
ATOM   107   C  CB  . VAL   A  1 14  ? -30.643 28.057  -18.845  1.00 60.55  ? 315  VAL   A CB  1 
ATOM   108   C  CG1 . VAL   A  1 14  ? -31.439 28.498  -20.063  1.00 50.76  ? 315  VAL   A CG1 1 
ATOM   109   C  CG2 . VAL   A  1 14  ? -29.296 28.737  -18.823  1.00 66.68  ? 315  VAL   A CG2 1 
ATOM   110   N  N   . VAL   A  1 15  ? -33.777 28.811  -17.909  1.00 62.64  ? 316  VAL   A N   1 
ATOM   111   C  CA  . VAL   A  1 15  ? -35.200 28.492  -18.007  1.00 59.22  ? 316  VAL   A CA  1 
ATOM   112   C  C   . VAL   A  1 15  ? -35.781 29.029  -19.313  1.00 59.71  ? 316  VAL   A C   1 
ATOM   113   O  O   . VAL   A  1 15  ? -35.560 30.193  -19.663  1.00 63.61  ? 316  VAL   A O   1 
ATOM   114   C  CB  . VAL   A  1 15  ? -35.979 29.040  -16.800  1.00 54.87  ? 316  VAL   A CB  1 
ATOM   115   C  CG1 . VAL   A  1 15  ? -37.433 28.583  -16.849  1.00 50.96  ? 316  VAL   A CG1 1 
ATOM   116   C  CG2 . VAL   A  1 15  ? -35.317 28.586  -15.530  1.00 54.03  ? 316  VAL   A CG2 1 
ATOM   117   N  N   . LEU   A  1 16  ? -36.552 28.186  -20.007  1.00 61.64  ? 317  LEU   A N   1 
ATOM   118   C  CA  . LEU   A  1 16  ? -37.107 28.453  -21.332  1.00 53.72  ? 317  LEU   A CA  1 
ATOM   119   C  C   . LEU   A  1 16  ? -38.620 28.317  -21.284  1.00 58.87  ? 317  LEU   A C   1 
ATOM   120   O  O   . LEU   A  1 16  ? -39.152 27.491  -20.540  1.00 64.82  ? 317  LEU   A O   1 
ATOM   121   C  CB  . LEU   A  1 16  ? -36.563 27.473  -22.370  1.00 38.82  ? 317  LEU   A CB  1 
ATOM   122   C  CG  . LEU   A  1 16  ? -35.056 27.257  -22.298  1.00 39.71  ? 317  LEU   A CG  1 
ATOM   123   C  CD1 . LEU   A  1 16  ? -34.635 26.083  -23.151  1.00 27.37  ? 317  LEU   A CD1 1 
ATOM   124   C  CD2 . LEU   A  1 16  ? -34.338 28.537  -22.706  1.00 43.42  ? 317  LEU   A CD2 1 
ATOM   125   N  N   . THR   A  1 17  ? -39.316 29.109  -22.101  1.00 61.75  ? 318  THR   A N   1 
ATOM   126   C  CA  . THR   A  1 17  ? -40.775 29.201  -22.026  1.00 62.77  ? 318  THR   A CA  1 
ATOM   127   C  C   . THR   A  1 17  ? -41.411 28.664  -23.302  1.00 60.31  ? 318  THR   A C   1 
ATOM   128   O  O   . THR   A  1 17  ? -41.374 29.314  -24.350  1.00 55.33  ? 318  THR   A O   1 
ATOM   129   C  CB  . THR   A  1 17  ? -41.224 30.634  -21.769  1.00 64.24  ? 318  THR   A CB  1 
ATOM   130   O  OG1 . THR   A  1 17  ? -40.596 31.120  -20.576  1.00 63.50  ? 318  THR   A OG1 1 
ATOM   131   C  CG2 . THR   A  1 17  ? -42.730 30.672  -21.589  1.00 66.20  ? 318  THR   A CG2 1 
ATOM   132   N  N   . ASP   A  1 18  ? -42.047 27.507  -23.188  1.00 60.57  ? 319  ASP   A N   1 
ATOM   133   C  CA  . ASP   A  1 18  ? -42.601 26.788  -24.328  1.00 55.84  ? 319  ASP   A CA  1 
ATOM   134   C  C   . ASP   A  1 18  ? -44.039 27.234  -24.557  1.00 61.83  ? 319  ASP   A C   1 
ATOM   135   O  O   . ASP   A  1 18  ? -44.944 26.847  -23.816  1.00 64.71  ? 319  ASP   A O   1 
ATOM   136   C  CB  . ASP   A  1 18  ? -42.511 25.290  -24.073  1.00 59.31  ? 319  ASP   A CB  1 
ATOM   137   C  CG  . ASP   A  1 18  ? -42.998 24.480  -25.231  1.00 63.28  ? 319  ASP   A CG  1 
ATOM   138   O  OD1 . ASP   A  1 18  ? -44.189 24.632  -25.582  1.00 64.31  ? 319  ASP   A OD1 1 
ATOM   139   O  OD2 . ASP   A  1 18  ? -42.190 23.698  -25.788  1.00 61.52  ? 319  ASP   A OD2 1 
ATOM   140   N  N   . THR   A  1 19  ? -44.254 28.036  -25.602  1.00 52.65  ? 320  THR   A N   1 
ATOM   141   C  CA  . THR   A  1 19  ? -45.597 28.345  -26.077  1.00 49.55  ? 320  THR   A CA  1 
ATOM   142   C  C   . THR   A  1 19  ? -46.027 27.479  -27.254  1.00 56.93  ? 320  THR   A C   1 
ATOM   143   O  O   . THR   A  1 19  ? -47.230 27.389  -27.531  1.00 61.45  ? 320  THR   A O   1 
ATOM   144   C  CB  . THR   A  1 19  ? -45.678 29.802  -26.524  1.00 45.45  ? 320  THR   A CB  1 
ATOM   145   O  OG1 . THR   A  1 19  ? -44.949 29.940  -27.752  1.00 40.88  ? 320  THR   A OG1 1 
ATOM   146   C  CG2 . THR   A  1 19  ? -45.064 30.712  -25.490  1.00 36.99  ? 320  THR   A CG2 1 
ATOM   147   N  N   . LEU   A  1 20  ? -45.065 26.854  -27.947  1.00 46.75  ? 321  LEU   A N   1 
ATOM   148   C  CA  . LEU   A  1 20  ? -45.341 26.112  -29.175  1.00 54.71  ? 321  LEU   A CA  1 
ATOM   149   C  C   . LEU   A  1 20  ? -46.232 24.898  -28.938  1.00 54.17  ? 321  LEU   A C   1 
ATOM   150   O  O   . LEU   A  1 20  ? -46.963 24.488  -29.848  1.00 54.17  ? 321  LEU   A O   1 
ATOM   151   C  CB  . LEU   A  1 20  ? -44.027 25.672  -29.821  1.00 57.10  ? 321  LEU   A CB  1 
ATOM   152   C  CG  . LEU   A  1 20  ? -44.136 25.006  -31.195  1.00 62.74  ? 321  LEU   A CG  1 
ATOM   153   C  CD1 . LEU   A  1 20  ? -44.699 26.001  -32.199  1.00 65.39  ? 321  LEU   A CD1 1 
ATOM   154   C  CD2 . LEU   A  1 20  ? -42.793 24.448  -31.671  1.00 58.70  ? 321  LEU   A CD2 1 
ATOM   155   N  N   . HIS   A  1 21  ? -46.176 24.312  -27.732  1.00 50.38  ? 322  HIS   A N   1 
ATOM   156   C  CA  . HIS   A  1 21  ? -46.946 23.117  -27.394  1.00 41.07  ? 322  HIS   A CA  1 
ATOM   157   C  C   . HIS   A  1 21  ? -48.433 23.335  -27.544  1.00 43.95  ? 322  HIS   A C   1 
ATOM   158   O  O   . HIS   A  1 21  ? -49.182 22.356  -27.637  1.00 48.66  ? 322  HIS   A O   1 
ATOM   159   C  CB  . HIS   A  1 21  ? -46.660 22.679  -25.953  1.00 50.96  ? 322  HIS   A CB  1 
ATOM   160   C  CG  . HIS   A  1 21  ? -47.241 23.593  -24.916  1.00 45.44  ? 322  HIS   A CG  1 
ATOM   161   N  ND1 . HIS   A  1 21  ? -46.629 24.770  -24.528  1.00 46.96  ? 322  HIS   A ND1 1 
ATOM   162   C  CD2 . HIS   A  1 21  ? -48.385 23.509  -24.195  1.00 45.95  ? 322  HIS   A CD2 1 
ATOM   163   C  CE1 . HIS   A  1 21  ? -47.377 25.373  -23.617  1.00 49.68  ? 322  HIS   A CE1 1 
ATOM   164   N  NE2 . HIS   A  1 21  ? -48.445 24.628  -23.395  1.00 47.95  ? 322  HIS   A NE2 1 
ATOM   165   N  N   . LEU   A  1 22  ? -48.877 24.594  -27.556  1.00 47.58  ? 323  LEU   A N   1 
ATOM   166   C  CA  . LEU   A  1 22  ? -50.289 24.879  -27.760  1.00 55.58  ? 323  LEU   A CA  1 
ATOM   167   C  C   . LEU   A  1 22  ? -50.745 24.457  -29.144  1.00 64.57  ? 323  LEU   A C   1 
ATOM   168   O  O   . LEU   A  1 22  ? -51.940 24.212  -29.352  1.00 70.14  ? 323  LEU   A O   1 
ATOM   169   C  CB  . LEU   A  1 22  ? -50.555 26.371  -27.539  1.00 57.65  ? 323  LEU   A CB  1 
ATOM   170   C  CG  . LEU   A  1 22  ? -50.296 26.900  -26.117  1.00 59.08  ? 323  LEU   A CG  1 
ATOM   171   C  CD1 . LEU   A  1 22  ? -50.654 28.378  -25.991  1.00 58.46  ? 323  LEU   A CD1 1 
ATOM   172   C  CD2 . LEU   A  1 22  ? -51.028 26.072  -25.051  1.00 49.32  ? 323  LEU   A CD2 1 
ATOM   173   N  N   . LYS   A  1 23  ? -49.805 24.327  -30.078  1.00 63.04  ? 324  LYS   A N   1 
ATOM   174   C  CA  . LYS   A  1 23  ? -50.078 24.058  -31.478  1.00 48.02  ? 324  LYS   A CA  1 
ATOM   175   C  C   . LYS   A  1 23  ? -49.964 22.586  -31.828  1.00 52.30  ? 324  LYS   A C   1 
ATOM   176   O  O   . LYS   A  1 23  ? -49.719 22.254  -32.989  1.00 55.02  ? 324  LYS   A O   1 
ATOM   177   C  CB  . LYS   A  1 23  ? -49.125 24.874  -32.354  1.00 52.63  ? 324  LYS   A CB  1 
ATOM   178   C  CG  . LYS   A  1 23  ? -49.574 26.314  -32.554  1.00 63.32  ? 324  LYS   A CG  1 
ATOM   179   C  CD  . LYS   A  1 23  ? -48.509 27.139  -33.246  1.00 70.87  ? 324  LYS   A CD  1 
ATOM   180   C  CE  . LYS   A  1 23  ? -48.463 28.563  -32.688  1.00 77.84  ? 324  LYS   A CE  1 
ATOM   181   N  NZ  . LYS   A  1 23  ? -47.818 28.660  -31.324  1.00 69.51  ? 324  LYS   A NZ  1 
ATOM   182   N  N   . SER   A  1 24  ? -50.120 21.694  -30.865  1.00 58.66  ? 325  SER   A N   1 
ATOM   183   C  CA  . SER   A  1 24  ? -50.087 20.272  -31.159  1.00 67.68  ? 325  SER   A CA  1 
ATOM   184   C  C   . SER   A  1 24  ? -51.485 19.706  -30.976  1.00 77.71  ? 325  SER   A C   1 
ATOM   185   O  O   . SER   A  1 24  ? -52.239 20.167  -30.118  1.00 86.82  ? 325  SER   A O   1 
ATOM   186   C  CB  . SER   A  1 24  ? -49.083 19.535  -30.268  1.00 63.25  ? 325  SER   A CB  1 
ATOM   187   O  OG  . SER   A  1 24  ? -49.731 18.815  -29.241  1.00 67.41  ? 325  SER   A OG  1 
ATOM   188   N  N   . THR   A  1 25  ? -51.847 18.724  -31.810  1.00 82.90  ? 326  THR   A N   1 
ATOM   189   C  CA  . THR   A  1 25  ? -53.187 18.153  -31.697  1.00 92.72  ? 326  THR   A CA  1 
ATOM   190   C  C   . THR   A  1 25  ? -53.176 16.633  -31.782  1.00 87.30  ? 326  THR   A C   1 
ATOM   191   O  O   . THR   A  1 25  ? -54.214 16.033  -32.071  1.00 95.20  ? 326  THR   A O   1 
ATOM   192   C  CB  . THR   A  1 25  ? -54.147 18.702  -32.773  1.00 95.24  ? 326  THR   A CB  1 
ATOM   193   O  OG1 . THR   A  1 25  ? -53.404 19.345  -33.819  1.00 101.93 ? 326  THR   A OG1 1 
ATOM   194   C  CG2 . THR   A  1 25  ? -55.183 19.658  -32.147  1.00 75.99  ? 326  THR   A CG2 1 
ATOM   195   N  N   . LEU   A  1 26  ? -52.040 16.001  -31.526  1.00 78.60  ? 327  LEU   A N   1 
ATOM   196   C  CA  . LEU   A  1 26  ? -51.901 14.560  -31.636  1.00 82.72  ? 327  LEU   A CA  1 
ATOM   197   C  C   . LEU   A  1 26  ? -51.556 13.978  -30.265  1.00 81.48  ? 327  LEU   A C   1 
ATOM   198   O  O   . LEU   A  1 26  ? -50.861 14.610  -29.461  1.00 82.94  ? 327  LEU   A O   1 
ATOM   199   C  CB  . LEU   A  1 26  ? -50.809 14.175  -32.660  1.00 89.25  ? 327  LEU   A CB  1 
ATOM   200   C  CG  . LEU   A  1 26  ? -50.445 14.852  -34.010  1.00 89.07  ? 327  LEU   A CG  1 
ATOM   201   C  CD1 . LEU   A  1 26  ? -50.886 14.009  -35.220  1.00 81.00  ? 327  LEU   A CD1 1 
ATOM   202   C  CD2 . LEU   A  1 26  ? -50.874 16.330  -34.195  1.00 90.94  ? 327  LEU   A CD2 1 
ATOM   203   N  N   . GLU   A  1 27  ? -52.039 12.765  -30.003  1.00 70.45  ? 328  GLU   A N   1 
ATOM   204   C  CA  . GLU   A  1 27  ? -51.802 12.126  -28.715  1.00 61.62  ? 328  GLU   A CA  1 
ATOM   205   C  C   . GLU   A  1 27  ? -50.321 11.823  -28.512  1.00 60.93  ? 328  GLU   A C   1 
ATOM   206   O  O   . GLU   A  1 27  ? -49.584 11.566  -29.466  1.00 68.48  ? 328  GLU   A O   1 
ATOM   207   C  CB  . GLU   A  1 27  ? -52.597 10.825  -28.606  1.00 64.23  ? 328  GLU   A CB  1 
ATOM   208   C  CG  . GLU   A  1 27  ? -54.076 10.999  -28.330  1.00 76.67  ? 328  GLU   A CG  1 
ATOM   209   C  CD  . GLU   A  1 27  ? -54.807 9.668   -28.254  1.00 92.37  ? 328  GLU   A CD  1 
ATOM   210   O  OE1 . GLU   A  1 27  ? -54.285 8.667   -28.799  1.00 97.81  ? 328  GLU   A OE1 1 
ATOM   211   O  OE2 . GLU   A  1 27  ? -55.900 9.626   -27.647  1.00 97.01  ? 328  GLU   A OE2 1 
ATOM   212   N  N   . THR   A  1 28  ? -49.889 11.869  -27.245  1.00 49.49  ? 329  THR   A N   1 
ATOM   213   C  CA  . THR   A  1 28  ? -48.602 11.324  -26.836  1.00 45.52  ? 329  THR   A CA  1 
ATOM   214   C  C   . THR   A  1 28  ? -48.724 9.921   -26.277  1.00 46.04  ? 329  THR   A C   1 
ATOM   215   O  O   . THR   A  1 28  ? -47.725 9.198   -26.227  1.00 60.74  ? 329  THR   A O   1 
ATOM   216   C  CB  . THR   A  1 28  ? -47.949 12.185  -25.747  1.00 64.88  ? 329  THR   A CB  1 
ATOM   217   O  OG1 . THR   A  1 28  ? -48.738 12.108  -24.547  1.00 70.52  ? 329  THR   A OG1 1 
ATOM   218   C  CG2 . THR   A  1 28  ? -47.802 13.636  -26.192  1.00 71.90  ? 329  THR   A CG2 1 
ATOM   219   N  N   . GLY   A  1 29  ? -49.912 9.529   -25.842  1.00 44.34  ? 330  GLY   A N   1 
ATOM   220   C  CA  . GLY   A  1 29  ? -50.119 8.281   -25.156  1.00 53.48  ? 330  GLY   A CA  1 
ATOM   221   C  C   . GLY   A  1 29  ? -50.272 8.439   -23.663  1.00 61.21  ? 330  GLY   A C   1 
ATOM   222   O  O   . GLY   A  1 29  ? -50.892 7.586   -23.019  1.00 68.51  ? 330  GLY   A O   1 
ATOM   223   N  N   . CYS   A  1 30  ? -49.739 9.520   -23.105  1.00 53.61  ? 331  CYS   A N   1 
ATOM   224   C  CA  . CYS   A  1 30  ? -49.887 9.794   -21.685  1.00 48.38  ? 331  CYS   A CA  1 
ATOM   225   C  C   . CYS   A  1 30  ? -51.294 10.289  -21.386  1.00 50.98  ? 331  CYS   A C   1 
ATOM   226   O  O   . CYS   A  1 30  ? -51.871 11.058  -22.158  1.00 54.36  ? 331  CYS   A O   1 
ATOM   227   C  CB  . CYS   A  1 30  ? -48.862 10.837  -21.240  1.00 46.56  ? 331  CYS   A CB  1 
ATOM   228   S  SG  . CYS   A  1 30  ? -47.105 10.339  -21.365  1.00 50.79  ? 331  CYS   A SG  1 
ATOM   229   N  N   . THR   A  1 31  ? -51.851 9.847   -20.261  1.00 51.72  ? 332  THR   A N   1 
ATOM   230   C  CA  . THR   A  1 31  ? -53.104 10.407  -19.784  1.00 53.18  ? 332  THR   A CA  1 
ATOM   231   C  C   . THR   A  1 31  ? -52.787 11.371  -18.651  1.00 45.46  ? 332  THR   A C   1 
ATOM   232   O  O   . THR   A  1 31  ? -51.631 11.555  -18.277  1.00 58.60  ? 332  THR   A O   1 
ATOM   233   C  CB  . THR   A  1 31  ? -54.085 9.313   -19.351  1.00 62.63  ? 332  THR   A CB  1 
ATOM   234   O  OG1 . THR   A  1 31  ? -53.930 9.048   -17.952  1.00 61.98  ? 332  THR   A OG1 1 
ATOM   235   C  CG2 . THR   A  1 31  ? -53.861 8.026   -20.160  1.00 59.94  ? 332  THR   A CG2 1 
ATOM   236   N  N   . GLU   A  1 32  ? -53.822 12.013  -18.111  1.00 47.15  ? 333  GLU   A N   1 
ATOM   237   C  CA  . GLU   A  1 32  ? -53.595 12.979  -17.044  1.00 54.18  ? 333  GLU   A CA  1 
ATOM   238   C  C   . GLU   A  1 32  ? -53.064 12.327  -15.776  1.00 57.10  ? 333  GLU   A C   1 
ATOM   239   O  O   . GLU   A  1 32  ? -52.398 13.010  -14.985  1.00 52.86  ? 333  GLU   A O   1 
ATOM   240   C  CB  . GLU   A  1 32  ? -54.885 13.744  -16.724  1.00 66.30  ? 333  GLU   A CB  1 
ATOM   241   C  CG  . GLU   A  1 32  ? -55.551 14.362  -17.944  1.00 77.77  ? 333  GLU   A CG  1 
ATOM   242   C  CD  . GLU   A  1 32  ? -56.637 15.355  -17.578  1.00 86.96  ? 333  GLU   A CD  1 
ATOM   243   O  OE1 . GLU   A  1 32  ? -56.450 16.564  -17.864  1.00 84.08  ? 333  GLU   A OE1 1 
ATOM   244   O  OE2 . GLU   A  1 32  ? -57.668 14.925  -17.000  1.00 89.49  ? 333  GLU   A OE2 1 
ATOM   245   N  N   . TYR   A  1 33  ? -53.332 11.024  -15.583  1.00 53.26  ? 334  TYR   A N   1 
ATOM   246   C  CA  . TYR   A  1 33  ? -52.994 10.303  -14.362  1.00 46.26  ? 334  TYR   A CA  1 
ATOM   247   C  C   . TYR   A  1 33  ? -52.064 9.128   -14.585  1.00 44.92  ? 334  TYR   A C   1 
ATOM   248   O  O   . TYR   A  1 33  ? -51.805 8.385   -13.635  1.00 59.41  ? 334  TYR   A O   1 
ATOM   249   C  CB  . TYR   A  1 33  ? -54.259 9.777   -13.656  1.00 50.63  ? 334  TYR   A CB  1 
ATOM   250   C  CG  . TYR   A  1 33  ? -55.177 10.848  -13.112  1.00 59.31  ? 334  TYR   A CG  1 
ATOM   251   C  CD1 . TYR   A  1 33  ? -55.069 11.275  -11.796  1.00 67.65  ? 334  TYR   A CD1 1 
ATOM   252   C  CD2 . TYR   A  1 33  ? -56.148 11.428  -13.912  1.00 68.18  ? 334  TYR   A CD2 1 
ATOM   253   C  CE1 . TYR   A  1 33  ? -55.902 12.254  -11.285  1.00 71.55  ? 334  TYR   A CE1 1 
ATOM   254   C  CE2 . TYR   A  1 33  ? -56.983 12.408  -13.414  1.00 76.88  ? 334  TYR   A CE2 1 
ATOM   255   C  CZ  . TYR   A  1 33  ? -56.858 12.818  -12.096  1.00 76.66  ? 334  TYR   A CZ  1 
ATOM   256   O  OH  . TYR   A  1 33  ? -57.685 13.798  -11.586  1.00 78.60  ? 334  TYR   A OH  1 
ATOM   257   N  N   . ILE   A  1 34  ? -51.576 8.909   -15.798  1.00 55.02  ? 335  ILE   A N   1 
ATOM   258   C  CA  . ILE   A  1 34  ? -50.539 7.908   -16.025  1.00 50.78  ? 335  ILE   A CA  1 
ATOM   259   C  C   . ILE   A  1 34  ? -49.628 8.424   -17.115  1.00 44.17  ? 335  ILE   A C   1 
ATOM   260   O  O   . ILE   A  1 34  ? -50.079 9.106   -18.040  1.00 61.15  ? 335  ILE   A O   1 
ATOM   261   C  CB  . ILE   A  1 34  ? -51.115 6.507   -16.354  1.00 53.22  ? 335  ILE   A CB  1 
ATOM   262   C  CG1 . ILE   A  1 34  ? -50.196 5.744   -17.298  1.00 58.42  ? 335  ILE   A CG1 1 
ATOM   263   C  CG2 . ILE   A  1 34  ? -52.541 6.570   -16.853  1.00 55.63  ? 335  ILE   A CG2 1 
ATOM   264   C  CD1 . ILE   A  1 34  ? -49.925 4.332   -16.840  1.00 69.02  ? 335  ILE   A CD1 1 
ATOM   265   N  N   . CYS   A  1 35  ? -48.335 8.147   -16.979  1.00 45.34  ? 336  CYS   A N   1 
ATOM   266   C  CA  . CYS   A  1 35  ? -47.338 8.607   -17.932  1.00 38.34  ? 336  CYS   A CA  1 
ATOM   267   C  C   . CYS   A  1 35  ? -46.762 7.426   -18.684  1.00 52.44  ? 336  CYS   A C   1 
ATOM   268   O  O   . CYS   A  1 35  ? -46.432 6.402   -18.079  1.00 46.08  ? 336  CYS   A O   1 
ATOM   269   C  CB  . CYS   A  1 35  ? -46.200 9.356   -17.244  1.00 40.99  ? 336  CYS   A CB  1 
ATOM   270   S  SG  . CYS   A  1 35  ? -44.823 9.758   -18.352  1.00 50.23  ? 336  CYS   A SG  1 
ATOM   271   N  N   . MET   A  1 36  ? -46.620 7.583   -20.007  1.00 57.03  ? 337  MET   A N   1 
ATOM   272   C  CA  . MET   A  1 36  ? -46.086 6.518   -20.847  1.00 50.34  ? 337  MET   A CA  1 
ATOM   273   C  C   . MET   A  1 36  ? -44.825 6.938   -21.588  1.00 42.82  ? 337  MET   A C   1 
ATOM   274   O  O   . MET   A  1 36  ? -44.503 6.356   -22.622  1.00 49.53  ? 337  MET   A O   1 
ATOM   275   C  CB  . MET   A  1 36  ? -47.153 6.027   -21.824  1.00 47.58  ? 337  MET   A CB  1 
ATOM   276   C  CG  . MET   A  1 36  ? -48.345 5.452   -21.083  1.00 61.61  ? 337  MET   A CG  1 
ATOM   277   S  SD  . MET   A  1 36  ? -49.407 4.460   -22.116  1.00 69.68  ? 337  MET   A SD  1 
ATOM   278   C  CE  . MET   A  1 36  ? -50.996 4.830   -21.376  1.00 68.10  ? 337  MET   A CE  1 
ATOM   279   N  N   . GLY   A  1 37  ? -44.071 7.894   -21.042  1.00 42.90  ? 338  GLY   A N   1 
ATOM   280   C  CA  . GLY   A  1 37  ? -42.919 8.466   -21.719  1.00 32.92  ? 338  GLY   A CA  1 
ATOM   281   C  C   . GLY   A  1 37  ? -41.810 7.495   -22.066  1.00 42.10  ? 338  GLY   A C   1 
ATOM   282   O  O   . GLY   A  1 37  ? -40.887 7.879   -22.801  1.00 54.45  ? 338  GLY   A O   1 
ATOM   283   N  N   . SER   A  1 38  ? -41.854 6.255   -21.545  1.00 39.29  ? 339  SER   A N   1 
ATOM   284   C  CA  . SER   A  1 38  ? -40.861 5.229   -21.884  1.00 44.46  ? 339  SER   A CA  1 
ATOM   285   C  C   . SER   A  1 38  ? -41.417 4.096   -22.743  1.00 47.66  ? 339  SER   A C   1 
ATOM   286   O  O   . SER   A  1 38  ? -40.647 3.221   -23.171  1.00 48.55  ? 339  SER   A O   1 
ATOM   287   C  CB  . SER   A  1 38  ? -40.213 4.636   -20.622  1.00 49.42  ? 339  SER   A CB  1 
ATOM   288   O  OG  . SER   A  1 38  ? -41.110 3.887   -19.806  1.00 54.08  ? 339  SER   A OG  1 
ATOM   289   N  N   . ILE   A  1 39  ? -42.729 4.080   -22.995  1.00 53.00  ? 340  ILE   A N   1 
ATOM   290   C  CA  . ILE   A  1 39  ? -43.318 3.137   -23.942  1.00 57.57  ? 340  ILE   A CA  1 
ATOM   291   C  C   . ILE   A  1 39  ? -42.845 3.480   -25.348  1.00 58.49  ? 340  ILE   A C   1 
ATOM   292   O  O   . ILE   A  1 39  ? -42.887 4.648   -25.764  1.00 58.24  ? 340  ILE   A O   1 
ATOM   293   C  CB  . ILE   A  1 39  ? -44.851 3.177   -23.861  1.00 54.31  ? 340  ILE   A CB  1 
ATOM   294   C  CG1 . ILE   A  1 39  ? -45.316 3.185   -22.409  1.00 45.55  ? 340  ILE   A CG1 1 
ATOM   295   C  CG2 . ILE   A  1 39  ? -45.451 1.995   -24.609  1.00 67.07  ? 340  ILE   A CG2 1 
ATOM   296   C  CD1 . ILE   A  1 39  ? -44.937 1.954   -21.650  1.00 51.87  ? 340  ILE   A CD1 1 
ATOM   297   N  N   . MET   A  1 40  ? -42.413 2.459   -26.098  1.00 58.54  ? 341  MET   A N   1 
ATOM   298   C  CA  . MET   A  1 40  ? -41.793 2.717   -27.397  1.00 65.97  ? 341  MET   A CA  1 
ATOM   299   C  C   . MET   A  1 40  ? -42.815 3.134   -28.452  1.00 62.85  ? 341  MET   A C   1 
ATOM   300   O  O   . MET   A  1 40  ? -42.572 4.076   -29.217  1.00 64.58  ? 341  MET   A O   1 
ATOM   301   C  CB  . MET   A  1 40  ? -41.010 1.498   -27.867  1.00 75.00  ? 341  MET   A CB  1 
ATOM   302   C  CG  . MET   A  1 40  ? -40.240 1.790   -29.144  1.00 87.36  ? 341  MET   A CG  1 
ATOM   303   S  SD  . MET   A  1 40  ? -38.781 0.761   -29.337  1.00 94.50  ? 341  MET   A SD  1 
ATOM   304   C  CE  . MET   A  1 40  ? -37.853 1.198   -27.880  1.00 82.98  ? 341  MET   A CE  1 
ATOM   305   N  N   . HIS   A  1 41  ? -43.936 2.421   -28.542  1.00 66.12  ? 342  HIS   A N   1 
ATOM   306   C  CA  . HIS   A  1 41  ? -45.066 2.814   -29.388  1.00 72.89  ? 342  HIS   A CA  1 
ATOM   307   C  C   . HIS   A  1 41  ? -46.311 2.800   -28.504  1.00 73.06  ? 342  HIS   A C   1 
ATOM   308   O  O   . HIS   A  1 41  ? -46.812 1.715   -28.158  1.00 81.51  ? 342  HIS   A O   1 
ATOM   309   C  CB  . HIS   A  1 41  ? -45.263 1.885   -30.595  1.00 76.41  ? 342  HIS   A CB  1 
ATOM   310   C  CG  . HIS   A  1 41  ? -43.995 1.335   -31.198  1.00 80.23  ? 342  HIS   A CG  1 
ATOM   311   N  ND1 . HIS   A  1 41  ? -43.164 2.079   -32.012  1.00 79.04  ? 342  HIS   A ND1 1 
ATOM   312   C  CD2 . HIS   A  1 41  ? -43.455 0.090   -31.157  1.00 77.73  ? 342  HIS   A CD2 1 
ATOM   313   C  CE1 . HIS   A  1 41  ? -42.150 1.329   -32.413  1.00 74.48  ? 342  HIS   A CE1 1 
ATOM   314   N  NE2 . HIS   A  1 41  ? -42.305 0.117   -31.913  1.00 73.04  ? 342  HIS   A NE2 1 
ATOM   315   N  N   . PRO   A  1 42  ? -46.836 3.967   -28.095  1.00 65.29  ? 343  PRO   A N   1 
ATOM   316   C  CA  . PRO   A  1 42  ? -47.995 3.914   -27.189  1.00 62.44  ? 343  PRO   A CA  1 
ATOM   317   C  C   . PRO   A  1 42  ? -49.312 3.580   -27.898  1.00 57.40  ? 343  PRO   A C   1 
ATOM   318   O  O   . PRO   A  1 42  ? -49.895 4.442   -28.558  1.00 62.55  ? 343  PRO   A O   1 
ATOM   319   C  CB  . PRO   A  1 42  ? -48.040 5.331   -26.581  1.00 57.43  ? 343  PRO   A CB  1 
ATOM   320   C  CG  . PRO   A  1 42  ? -46.695 5.921   -26.861  1.00 60.63  ? 343  PRO   A CG  1 
ATOM   321   C  CD  . PRO   A  1 42  ? -46.288 5.325   -28.190  1.00 66.48  ? 343  PRO   A CD  1 
ATOM   322   N  N   . ARG   A  1 48  ? -54.231 0.192   -39.546  1.00 114.72 ? 349  ARG   A N   1 
ATOM   323   C  CA  . ARG   A  1 48  ? -54.933 -0.453  -40.653  1.00 121.54 ? 349  ARG   A CA  1 
ATOM   324   C  C   . ARG   A  1 48  ? -54.663 0.256   -41.995  1.00 129.14 ? 349  ARG   A C   1 
ATOM   325   O  O   . ARG   A  1 48  ? -54.330 1.447   -42.016  1.00 123.60 ? 349  ARG   A O   1 
ATOM   326   C  CB  . ARG   A  1 48  ? -56.435 -0.498  -40.366  1.00 117.47 ? 349  ARG   A CB  1 
ATOM   327   C  CG  . ARG   A  1 48  ? -57.042 -1.880  -40.496  1.00 116.88 ? 349  ARG   A CG  1 
ATOM   328   C  CD  . ARG   A  1 48  ? -58.471 -1.805  -40.995  1.00 120.82 ? 349  ARG   A CD  1 
ATOM   329   N  NE  . ARG   A  1 48  ? -58.649 -2.480  -42.281  1.00 122.79 ? 349  ARG   A NE  1 
ATOM   330   C  CZ  . ARG   A  1 48  ? -59.833 -2.809  -42.795  1.00 127.93 ? 349  ARG   A CZ  1 
ATOM   331   N  NH1 . ARG   A  1 48  ? -60.947 -2.525  -42.127  1.00 130.81 ? 349  ARG   A NH1 1 
ATOM   332   N  NH2 . ARG   A  1 48  ? -59.904 -3.425  -43.972  1.00 126.90 ? 349  ARG   A NH2 1 
ATOM   333   N  N   . PRO   A  1 49  ? -54.789 -0.486  -43.123  1.00 137.82 ? 350  PRO   A N   1 
ATOM   334   C  CA  . PRO   A  1 49  ? -54.562 0.132   -44.440  1.00 142.41 ? 350  PRO   A CA  1 
ATOM   335   C  C   . PRO   A  1 49  ? -55.822 0.736   -45.044  1.00 148.54 ? 350  PRO   A C   1 
ATOM   336   O  O   . PRO   A  1 49  ? -55.746 1.622   -45.901  1.00 148.45 ? 350  PRO   A O   1 
ATOM   337   C  CB  . PRO   A  1 49  ? -54.048 -1.040  -45.281  1.00 139.62 ? 350  PRO   A CB  1 
ATOM   338   C  CG  . PRO   A  1 49  ? -54.782 -2.215  -44.717  1.00 138.76 ? 350  PRO   A CG  1 
ATOM   339   C  CD  . PRO   A  1 49  ? -54.921 -1.953  -43.229  1.00 138.30 ? 350  PRO   A CD  1 
ATOM   340   N  N   . GLU   A  1 50  ? -56.991 0.243   -44.627  1.00 152.05 ? 351  GLU   A N   1 
ATOM   341   C  CA  . GLU   A  1 50  ? -58.242 0.912   -44.963  1.00 151.70 ? 351  GLU   A CA  1 
ATOM   342   C  C   . GLU   A  1 50  ? -58.389 2.228   -44.208  1.00 147.33 ? 351  GLU   A C   1 
ATOM   343   O  O   . GLU   A  1 50  ? -59.192 3.078   -44.612  1.00 146.95 ? 351  GLU   A O   1 
ATOM   344   C  CB  . GLU   A  1 50  ? -59.428 -0.010  -44.658  1.00 154.01 ? 351  GLU   A CB  1 
ATOM   345   C  CG  . GLU   A  1 50  ? -60.590 0.042   -45.655  1.00 149.65 ? 351  GLU   A CG  1 
ATOM   346   C  CD  . GLU   A  1 50  ? -60.652 -1.187  -46.555  1.00 141.58 ? 351  GLU   A CD  1 
ATOM   347   O  OE1 . GLU   A  1 50  ? -60.056 -1.150  -47.656  1.00 140.48 ? 351  GLU   A OE1 1 
ATOM   348   O  OE2 . GLU   A  1 50  ? -61.286 -2.190  -46.153  1.00 135.15 ? 351  GLU   A OE2 1 
ATOM   349   N  N   . ASP   A  1 51  ? -57.615 2.418   -43.134  1.00 142.77 ? 352  ASP   A N   1 
ATOM   350   C  CA  . ASP   A  1 51  ? -57.630 3.627   -42.311  1.00 134.32 ? 352  ASP   A CA  1 
ATOM   351   C  C   . ASP   A  1 51  ? -57.076 4.841   -43.059  1.00 120.59 ? 352  ASP   A C   1 
ATOM   352   O  O   . ASP   A  1 51  ? -56.460 5.719   -42.443  1.00 121.86 ? 352  ASP   A O   1 
ATOM   353   C  CB  . ASP   A  1 51  ? -56.821 3.404   -41.018  1.00 130.36 ? 352  ASP   A CB  1 
ATOM   354   C  CG  . ASP   A  1 51  ? -57.678 2.919   -39.836  1.00 121.99 ? 352  ASP   A CG  1 
ATOM   355   O  OD1 . ASP   A  1 51  ? -58.491 1.985   -40.011  1.00 120.68 ? 352  ASP   A OD1 1 
ATOM   356   O  OD2 . ASP   A  1 51  ? -57.511 3.462   -38.719  1.00 113.87 ? 352  ASP   A OD2 1 
ATOM   357   N  N   . VAL   A  1 52  ? -57.286 4.908   -44.386  1.00 101.90 ? 353  VAL   A N   1 
ATOM   358   C  CA  . VAL   A  1 52  ? -56.875 6.065   -45.175  1.00 81.70  ? 353  VAL   A CA  1 
ATOM   359   C  C   . VAL   A  1 52  ? -57.954 7.134   -45.098  1.00 65.55  ? 353  VAL   A C   1 
ATOM   360   O  O   . VAL   A  1 52  ? -59.156 6.842   -45.051  1.00 64.93  ? 353  VAL   A O   1 
ATOM   361   C  CB  . VAL   A  1 52  ? -56.582 5.672   -46.633  1.00 86.15  ? 353  VAL   A CB  1 
ATOM   362   C  CG1 . VAL   A  1 52  ? -55.467 4.653   -46.674  1.00 90.61  ? 353  VAL   A CG1 1 
ATOM   363   C  CG2 . VAL   A  1 52  ? -57.842 5.136   -47.314  1.00 85.35  ? 353  VAL   A CG2 1 
ATOM   364   N  N   . ALA   A  1 53  ? -57.518 8.387   -45.102  1.00 57.12  ? 354  ALA   A N   1 
ATOM   365   C  CA  . ALA   A  1 53  ? -58.383 9.482   -44.687  1.00 59.74  ? 354  ALA   A CA  1 
ATOM   366   C  C   . ALA   A  1 53  ? -59.557 9.660   -45.636  1.00 59.00  ? 354  ALA   A C   1 
ATOM   367   O  O   . ALA   A  1 53  ? -59.418 9.531   -46.854  1.00 73.39  ? 354  ALA   A O   1 
ATOM   368   C  CB  . ALA   A  1 53  ? -57.582 10.778  -44.597  1.00 64.88  ? 354  ALA   A CB  1 
ATOM   369   N  N   . THR   A  1 54  ? -60.721 9.945   -45.064  1.00 58.62  ? 355  THR   A N   1 
ATOM   370   C  CA  . THR   A  1 54  ? -61.896 10.310  -45.837  1.00 71.59  ? 355  THR   A CA  1 
ATOM   371   C  C   . THR   A  1 54  ? -61.785 11.759  -46.304  1.00 78.08  ? 355  THR   A C   1 
ATOM   372   O  O   . THR   A  1 54  ? -60.921 12.519  -45.852  1.00 75.83  ? 355  THR   A O   1 
ATOM   373   C  CB  . THR   A  1 54  ? -63.166 10.136  -45.003  1.00 75.11  ? 355  THR   A CB  1 
ATOM   374   O  OG1 . THR   A  1 54  ? -63.306 11.255  -44.118  1.00 77.55  ? 355  THR   A OG1 1 
ATOM   375   C  CG2 . THR   A  1 54  ? -63.089 8.859   -44.174  1.00 78.95  ? 355  THR   A CG2 1 
ATOM   376   N  N   . LYS   A  1 55  ? -62.692 12.147  -47.209  1.00 79.63  ? 356  LYS   A N   1 
ATOM   377   C  CA  . LYS   A  1 55  ? -62.719 13.526  -47.692  1.00 76.60  ? 356  LYS   A CA  1 
ATOM   378   C  C   . LYS   A  1 55  ? -62.847 14.516  -46.538  1.00 80.89  ? 356  LYS   A C   1 
ATOM   379   O  O   . LYS   A  1 55  ? -62.031 15.432  -46.400  1.00 83.23  ? 356  LYS   A O   1 
ATOM   380   C  CB  . LYS   A  1 55  ? -63.865 13.728  -48.687  1.00 73.80  ? 356  LYS   A CB  1 
ATOM   381   C  CG  . LYS   A  1 55  ? -63.739 12.970  -49.987  1.00 68.55  ? 356  LYS   A CG  1 
ATOM   382   C  CD  . LYS   A  1 55  ? -64.553 13.642  -51.078  1.00 69.37  ? 356  LYS   A CD  1 
ATOM   383   C  CE  . LYS   A  1 55  ? -65.190 12.617  -51.997  1.00 83.16  ? 356  LYS   A CE  1 
ATOM   384   N  NZ  . LYS   A  1 55  ? -65.511 13.164  -53.355  1.00 85.02  ? 356  LYS   A NZ  1 
ATOM   385   N  N   . ASP   A  1 56  ? -63.870 14.346  -45.694  1.00 83.06  ? 357  ASP   A N   1 
ATOM   386   C  CA  . ASP   A  1 56  ? -64.076 15.277  -44.585  1.00 85.20  ? 357  ASP   A CA  1 
ATOM   387   C  C   . ASP   A  1 56  ? -62.941 15.210  -43.575  1.00 78.22  ? 357  ASP   A C   1 
ATOM   388   O  O   . ASP   A  1 56  ? -62.623 16.220  -42.940  1.00 82.99  ? 357  ASP   A O   1 
ATOM   389   C  CB  . ASP   A  1 56  ? -65.403 14.997  -43.879  1.00 87.52  ? 357  ASP   A CB  1 
ATOM   390   C  CG  . ASP   A  1 56  ? -66.593 15.138  -44.797  1.00 81.46  ? 357  ASP   A CG  1 
ATOM   391   O  OD1 . ASP   A  1 56  ? -66.452 15.777  -45.866  1.00 63.25  ? 357  ASP   A OD1 1 
ATOM   392   O  OD2 . ASP   A  1 56  ? -67.669 14.613  -44.436  1.00 90.34  ? 357  ASP   A OD2 1 
ATOM   393   N  N   . GLN   A  1 57  ? -62.342 14.033  -43.392  1.00 63.16  ? 358  GLN   A N   1 
ATOM   394   C  CA  . GLN   A  1 57  ? -61.126 13.951  -42.597  1.00 50.89  ? 358  GLN   A CA  1 
ATOM   395   C  C   . GLN   A  1 57  ? -60.021 14.821  -43.184  1.00 55.97  ? 358  GLN   A C   1 
ATOM   396   O  O   . GLN   A  1 57  ? -59.309 15.506  -42.445  1.00 55.81  ? 358  GLN   A O   1 
ATOM   397   C  CB  . GLN   A  1 57  ? -60.661 12.501  -42.505  1.00 60.32  ? 358  GLN   A CB  1 
ATOM   398   C  CG  . GLN   A  1 57  ? -61.524 11.612  -41.637  1.00 74.59  ? 358  GLN   A CG  1 
ATOM   399   C  CD  . GLN   A  1 57  ? -60.825 10.311  -41.272  1.00 82.14  ? 358  GLN   A CD  1 
ATOM   400   O  OE1 . GLN   A  1 57  ? -60.675 9.412   -42.106  1.00 83.32  ? 358  GLN   A OE1 1 
ATOM   401   N  NE2 . GLN   A  1 57  ? -60.382 10.210  -40.020  1.00 82.73  ? 358  GLN   A NE2 1 
ATOM   402   N  N   . LEU   A  1 58  ? -59.872 14.825  -44.518  1.00 61.93  ? 359  LEU   A N   1 
ATOM   403   C  CA  . LEU   A  1 58  ? -58.674 15.406  -45.132  1.00 56.19  ? 359  LEU   A CA  1 
ATOM   404   C  C   . LEU   A  1 58  ? -58.715 16.935  -45.192  1.00 56.58  ? 359  LEU   A C   1 
ATOM   405   O  O   . LEU   A  1 58  ? -57.667 17.579  -45.056  1.00 50.63  ? 359  LEU   A O   1 
ATOM   406   C  CB  . LEU   A  1 58  ? -58.463 14.826  -46.539  1.00 46.71  ? 359  LEU   A CB  1 
ATOM   407   C  CG  . LEU   A  1 58  ? -57.038 14.959  -47.077  1.00 52.76  ? 359  LEU   A CG  1 
ATOM   408   C  CD1 . LEU   A  1 58  ? -56.048 14.484  -46.026  1.00 55.75  ? 359  LEU   A CD1 1 
ATOM   409   C  CD2 . LEU   A  1 58  ? -56.825 14.202  -48.393  1.00 46.68  ? 359  LEU   A CD2 1 
ATOM   410   N  N   . PHE   A  1 59  ? -59.894 17.532  -45.384  1.00 62.86  ? 360  PHE   A N   1 
ATOM   411   C  CA  . PHE   A  1 59  ? -59.987 18.986  -45.526  1.00 69.65  ? 360  PHE   A CA  1 
ATOM   412   C  C   . PHE   A  1 59  ? -59.312 19.753  -44.400  1.00 68.21  ? 360  PHE   A C   1 
ATOM   413   O  O   . PHE   A  1 59  ? -58.455 20.601  -44.697  1.00 71.91  ? 360  PHE   A O   1 
ATOM   414   C  CB  . PHE   A  1 59  ? -61.451 19.426  -45.646  1.00 80.03  ? 360  PHE   A CB  1 
ATOM   415   C  CG  . PHE   A  1 59  ? -62.088 19.101  -46.961  1.00 92.15  ? 360  PHE   A CG  1 
ATOM   416   C  CD1 . PHE   A  1 59  ? -61.583 19.619  -48.140  1.00 91.41  ? 360  PHE   A CD1 1 
ATOM   417   C  CD2 . PHE   A  1 59  ? -63.219 18.300  -47.019  1.00 98.94  ? 360  PHE   A CD2 1 
ATOM   418   C  CE1 . PHE   A  1 59  ? -62.190 19.325  -49.345  1.00 90.18  ? 360  PHE   A CE1 1 
ATOM   419   C  CE2 . PHE   A  1 59  ? -63.826 18.002  -48.227  1.00 92.81  ? 360  PHE   A CE2 1 
ATOM   420   C  CZ  . PHE   A  1 59  ? -63.312 18.514  -49.386  1.00 88.78  ? 360  PHE   A CZ  1 
ATOM   421   N  N   . PRO   A  1 60  ? -59.623 19.521  -43.117  1.00 62.75  ? 361  PRO   A N   1 
ATOM   422   C  CA  . PRO   A  1 60  ? -58.993 20.348  -42.084  1.00 50.02  ? 361  PRO   A CA  1 
ATOM   423   C  C   . PRO   A  1 60  ? -57.502 20.131  -41.994  1.00 48.08  ? 361  PRO   A C   1 
ATOM   424   O  O   . PRO   A  1 60  ? -56.767 21.095  -41.750  1.00 55.17  ? 361  PRO   A O   1 
ATOM   425   C  CB  . PRO   A  1 60  ? -59.710 19.914  -40.806  1.00 58.94  ? 361  PRO   A CB  1 
ATOM   426   C  CG  . PRO   A  1 60  ? -60.071 18.519  -41.064  1.00 60.05  ? 361  PRO   A CG  1 
ATOM   427   C  CD  . PRO   A  1 60  ? -60.422 18.441  -42.515  1.00 60.68  ? 361  PRO   A CD  1 
ATOM   428   N  N   . LEU   A  1 61  ? -57.025 18.902  -42.210  1.00 43.95  ? 362  LEU   A N   1 
ATOM   429   C  CA  . LEU   A  1 61  ? -55.588 18.654  -42.117  1.00 46.16  ? 362  LEU   A CA  1 
ATOM   430   C  C   . LEU   A  1 61  ? -54.841 19.440  -43.178  1.00 60.54  ? 362  LEU   A C   1 
ATOM   431   O  O   . LEU   A  1 61  ? -53.856 20.131  -42.880  1.00 57.06  ? 362  LEU   A O   1 
ATOM   432   C  CB  . LEU   A  1 61  ? -55.284 17.163  -42.255  1.00 39.67  ? 362  LEU   A CB  1 
ATOM   433   C  CG  . LEU   A  1 61  ? -55.976 16.205  -41.294  1.00 45.68  ? 362  LEU   A CG  1 
ATOM   434   C  CD1 . LEU   A  1 61  ? -55.763 14.765  -41.747  1.00 45.71  ? 362  LEU   A CD1 1 
ATOM   435   C  CD2 . LEU   A  1 61  ? -55.424 16.409  -39.902  1.00 44.24  ? 362  LEU   A CD2 1 
ATOM   436   N  N   . ALA   A  1 62  ? -55.305 19.344  -44.431  1.00 61.50  ? 363  ALA   A N   1 
ATOM   437   C  CA  . ALA   A  1 62  ? -54.711 20.133  -45.499  1.00 50.42  ? 363  ALA   A CA  1 
ATOM   438   C  C   . ALA   A  1 62  ? -54.740 21.622  -45.161  1.00 48.99  ? 363  ALA   A C   1 
ATOM   439   O  O   . ALA   A  1 62  ? -53.734 22.324  -45.337  1.00 54.57  ? 363  ALA   A O   1 
ATOM   440   C  CB  . ALA   A  1 62  ? -55.428 19.847  -46.819  1.00 55.00  ? 363  ALA   A CB  1 
ATOM   441   N  N   . LYS   A  1 63  ? -55.863 22.119  -44.634  1.00 48.39  ? 364  LYS   A N   1 
ATOM   442   C  CA  . LYS   A  1 63  ? -55.941 23.544  -44.334  1.00 52.39  ? 364  LYS   A CA  1 
ATOM   443   C  C   . LYS   A  1 63  ? -54.908 23.942  -43.290  1.00 65.32  ? 364  LYS   A C   1 
ATOM   444   O  O   . LYS   A  1 63  ? -54.287 25.007  -43.399  1.00 70.21  ? 364  LYS   A O   1 
ATOM   445   C  CB  . LYS   A  1 63  ? -57.344 23.946  -43.869  1.00 44.48  ? 364  LYS   A CB  1 
ATOM   446   C  CG  . LYS   A  1 63  ? -57.604 25.477  -43.998  1.00 54.04  ? 364  LYS   A CG  1 
ATOM   447   C  CD  . LYS   A  1 63  ? -58.297 26.091  -42.768  1.00 66.59  ? 364  LYS   A CD  1 
ATOM   448   C  CE  . LYS   A  1 63  ? -58.605 27.592  -42.952  1.00 73.20  ? 364  LYS   A CE  1 
ATOM   449   N  NZ  . LYS   A  1 63  ? -57.424 28.516  -42.818  1.00 71.72  ? 364  LYS   A NZ  1 
ATOM   450   N  N   . GLU   A  1 64  ? -54.703 23.105  -42.268  1.00 63.67  ? 365  GLU   A N   1 
ATOM   451   C  CA  . GLU   A  1 64  ? -53.727 23.468  -41.245  1.00 61.24  ? 365  GLU   A CA  1 
ATOM   452   C  C   . GLU   A  1 64  ? -52.336 23.560  -41.846  1.00 55.29  ? 365  GLU   A C   1 
ATOM   453   O  O   . GLU   A  1 64  ? -51.589 24.509  -41.572  1.00 54.61  ? 365  GLU   A O   1 
ATOM   454   C  CB  . GLU   A  1 64  ? -53.751 22.465  -40.092  1.00 67.40  ? 365  GLU   A CB  1 
ATOM   455   C  CG  . GLU   A  1 64  ? -53.940 23.120  -38.733  1.00 74.78  ? 365  GLU   A CG  1 
ATOM   456   C  CD  . GLU   A  1 64  ? -52.846 22.753  -37.750  1.00 87.50  ? 365  GLU   A CD  1 
ATOM   457   O  OE1 . GLU   A  1 64  ? -52.272 23.672  -37.123  1.00 93.24  ? 365  GLU   A OE1 1 
ATOM   458   O  OE2 . GLU   A  1 64  ? -52.559 21.543  -37.605  1.00 88.91  ? 365  GLU   A OE2 1 
ATOM   459   N  N   . PHE   A  1 65  ? -51.994 22.609  -42.715  1.00 53.35  ? 366  PHE   A N   1 
ATOM   460   C  CA  . PHE   A  1 65  ? -50.664 22.595  -43.305  1.00 52.28  ? 366  PHE   A CA  1 
ATOM   461   C  C   . PHE   A  1 65  ? -50.454 23.774  -44.251  1.00 56.74  ? 366  PHE   A C   1 
ATOM   462   O  O   . PHE   A  1 65  ? -49.406 24.429  -44.206  1.00 63.34  ? 366  PHE   A O   1 
ATOM   463   C  CB  . PHE   A  1 65  ? -50.417 21.277  -44.030  1.00 44.65  ? 366  PHE   A CB  1 
ATOM   464   C  CG  . PHE   A  1 65  ? -49.152 21.272  -44.816  1.00 44.87  ? 366  PHE   A CG  1 
ATOM   465   C  CD1 . PHE   A  1 65  ? -47.927 21.254  -44.169  1.00 43.01  ? 366  PHE   A CD1 1 
ATOM   466   C  CD2 . PHE   A  1 65  ? -49.181 21.313  -46.205  1.00 48.77  ? 366  PHE   A CD2 1 
ATOM   467   C  CE1 . PHE   A  1 65  ? -46.749 21.272  -44.895  1.00 46.69  ? 366  PHE   A CE1 1 
ATOM   468   C  CE2 . PHE   A  1 65  ? -48.015 21.328  -46.934  1.00 46.17  ? 366  PHE   A CE2 1 
ATOM   469   C  CZ  . PHE   A  1 65  ? -46.793 21.303  -46.278  1.00 46.05  ? 366  PHE   A CZ  1 
ATOM   470   N  N   . ILE   A  1 66  ? -51.424 24.055  -45.127  1.00 51.72  ? 367  ILE   A N   1 
ATOM   471   C  CA  . ILE   A  1 66  ? -51.236 25.152  -46.078  1.00 53.72  ? 367  ILE   A CA  1 
ATOM   472   C  C   . ILE   A  1 66  ? -51.124 26.477  -45.332  1.00 58.29  ? 367  ILE   A C   1 
ATOM   473   O  O   . ILE   A  1 66  ? -50.268 27.316  -45.653  1.00 55.70  ? 367  ILE   A O   1 
ATOM   474   C  CB  . ILE   A  1 66  ? -52.368 25.181  -47.126  1.00 50.38  ? 367  ILE   A CB  1 
ATOM   475   C  CG1 . ILE   A  1 66  ? -52.473 23.848  -47.870  1.00 43.51  ? 367  ILE   A CG1 1 
ATOM   476   C  CG2 . ILE   A  1 66  ? -52.145 26.315  -48.128  1.00 42.51  ? 367  ILE   A CG2 1 
ATOM   477   C  CD1 . ILE   A  1 66  ? -51.268 23.530  -48.752  1.00 42.66  ? 367  ILE   A CD1 1 
ATOM   478   N  N   . ASP   A  1 67  ? -51.980 26.682  -44.321  1.00 57.96  ? 368  ASP   A N   1 
ATOM   479   C  CA  . ASP   A  1 67  ? -51.873 27.874  -43.483  1.00 54.63  ? 368  ASP   A CA  1 
ATOM   480   C  C   . ASP   A  1 67  ? -50.507 27.930  -42.830  1.00 56.11  ? 368  ASP   A C   1 
ATOM   481   O  O   . ASP   A  1 67  ? -49.829 28.964  -42.854  1.00 59.36  ? 368  ASP   A O   1 
ATOM   482   C  CB  . ASP   A  1 67  ? -52.955 27.882  -42.402  1.00 45.92  ? 368  ASP   A CB  1 
ATOM   483   C  CG  . ASP   A  1 67  ? -54.370 27.922  -42.959  1.00 57.78  ? 368  ASP   A CG  1 
ATOM   484   O  OD1 . ASP   A  1 67  ? -54.599 28.374  -44.111  1.00 59.06  ? 368  ASP   A OD1 1 
ATOM   485   O  OD2 . ASP   A  1 67  ? -55.275 27.507  -42.206  1.00 65.09  ? 368  ASP   A OD2 1 
ATOM   486   N  N   . GLN   A  1 68  ? -50.094 26.812  -42.236  1.00 51.60  ? 369  GLN   A N   1 
ATOM   487   C  CA  . GLN   A  1 68  ? -48.781 26.729  -41.618  1.00 51.57  ? 369  GLN   A CA  1 
ATOM   488   C  C   . GLN   A  1 68  ? -47.688 27.125  -42.604  1.00 55.59  ? 369  GLN   A C   1 
ATOM   489   O  O   . GLN   A  1 68  ? -46.765 27.881  -42.264  1.00 58.44  ? 369  GLN   A O   1 
ATOM   490   C  CB  . GLN   A  1 68  ? -48.577 25.309  -41.094  1.00 49.27  ? 369  GLN   A CB  1 
ATOM   491   C  CG  . GLN   A  1 68  ? -47.270 25.053  -40.369  1.00 52.97  ? 369  GLN   A CG  1 
ATOM   492   C  CD  . GLN   A  1 68  ? -47.095 23.584  -40.029  1.00 66.51  ? 369  GLN   A CD  1 
ATOM   493   O  OE1 . GLN   A  1 68  ? -48.080 22.861  -39.841  1.00 69.48  ? 369  GLN   A OE1 1 
ATOM   494   N  NE2 . GLN   A  1 68  ? -45.839 23.127  -39.978  1.00 70.23  ? 369  GLN   A NE2 1 
ATOM   495   N  N   . TYR   A  1 69  ? -47.805 26.662  -43.849  1.00 54.81  ? 370  TYR   A N   1 
ATOM   496   C  CA  . TYR   A  1 69  ? -46.779 26.949  -44.842  1.00 48.00  ? 370  TYR   A CA  1 
ATOM   497   C  C   . TYR   A  1 69  ? -46.803 28.413  -45.264  1.00 46.99  ? 370  TYR   A C   1 
ATOM   498   O  O   . TYR   A  1 69  ? -45.746 29.049  -45.384  1.00 39.95  ? 370  TYR   A O   1 
ATOM   499   C  CB  . TYR   A  1 69  ? -46.948 26.042  -46.056  1.00 47.16  ? 370  TYR   A CB  1 
ATOM   500   C  CG  . TYR   A  1 69  ? -46.043 26.434  -47.190  1.00 54.93  ? 370  TYR   A CG  1 
ATOM   501   C  CD1 . TYR   A  1 69  ? -44.711 26.057  -47.201  1.00 59.18  ? 370  TYR   A CD1 1 
ATOM   502   C  CD2 . TYR   A  1 69  ? -46.515 27.198  -48.246  1.00 49.43  ? 370  TYR   A CD2 1 
ATOM   503   C  CE1 . TYR   A  1 69  ? -43.876 26.424  -48.244  1.00 64.37  ? 370  TYR   A CE1 1 
ATOM   504   C  CE2 . TYR   A  1 69  ? -45.686 27.572  -49.282  1.00 52.15  ? 370  TYR   A CE2 1 
ATOM   505   C  CZ  . TYR   A  1 69  ? -44.369 27.188  -49.280  1.00 59.93  ? 370  TYR   A CZ  1 
ATOM   506   O  OH  . TYR   A  1 69  ? -43.535 27.562  -50.322  1.00 66.04  ? 370  TYR   A OH  1 
ATOM   507   N  N   . TYR   A  1 70  ? -47.990 28.968  -45.504  1.00 40.35  ? 371  TYR   A N   1 
ATOM   508   C  CA  . TYR   A  1 70  ? -48.016 30.361  -45.912  1.00 50.23  ? 371  TYR   A CA  1 
ATOM   509   C  C   . TYR   A  1 70  ? -47.632 31.276  -44.764  1.00 57.31  ? 371  TYR   A C   1 
ATOM   510   O  O   . TYR   A  1 70  ? -47.073 32.354  -44.995  1.00 59.81  ? 371  TYR   A O   1 
ATOM   511   C  CB  . TYR   A  1 70  ? -49.377 30.718  -46.514  1.00 52.94  ? 371  TYR   A CB  1 
ATOM   512   C  CG  . TYR   A  1 70  ? -49.382 30.329  -47.968  1.00 50.73  ? 371  TYR   A CG  1 
ATOM   513   C  CD1 . TYR   A  1 70  ? -49.864 29.097  -48.361  1.00 48.07  ? 371  TYR   A CD1 1 
ATOM   514   C  CD2 . TYR   A  1 70  ? -48.801 31.142  -48.923  1.00 41.29  ? 371  TYR   A CD2 1 
ATOM   515   C  CE1 . TYR   A  1 70  ? -49.825 28.702  -49.658  1.00 52.92  ? 371  TYR   A CE1 1 
ATOM   516   C  CE2 . TYR   A  1 70  ? -48.762 30.748  -50.246  1.00 51.93  ? 371  TYR   A CE2 1 
ATOM   517   C  CZ  . TYR   A  1 70  ? -49.279 29.525  -50.598  1.00 50.51  ? 371  TYR   A CZ  1 
ATOM   518   O  OH  . TYR   A  1 70  ? -49.259 29.088  -51.888  1.00 56.67  ? 371  TYR   A OH  1 
ATOM   519   N  N   . SER   A  1 71  ? -47.884 30.853  -43.527  1.00 66.80  ? 372  SER   A N   1 
ATOM   520   C  CA  . SER   A  1 71  ? -47.376 31.611  -42.393  1.00 64.69  ? 372  SER   A CA  1 
ATOM   521   C  C   . SER   A  1 71  ? -45.854 31.630  -42.410  1.00 56.89  ? 372  SER   A C   1 
ATOM   522   O  O   . SER   A  1 71  ? -45.232 32.700  -42.389  1.00 61.74  ? 372  SER   A O   1 
ATOM   523   C  CB  . SER   A  1 71  ? -47.909 31.021  -41.093  1.00 63.23  ? 372  SER   A CB  1 
ATOM   524   O  OG  . SER   A  1 71  ? -46.998 31.257  -40.041  1.00 77.75  ? 372  SER   A OG  1 
ATOM   525   N  N   . SER   A  1 72  ? -45.240 30.451  -42.522  1.00 47.70  ? 373  SER   A N   1 
ATOM   526   C  CA  . SER   A  1 72  ? -43.784 30.355  -42.484  1.00 46.13  ? 373  SER   A CA  1 
ATOM   527   C  C   . SER   A  1 72  ? -43.095 31.284  -43.474  1.00 56.88  ? 373  SER   A C   1 
ATOM   528   O  O   . SER   A  1 72  ? -41.985 31.754  -43.205  1.00 59.28  ? 373  SER   A O   1 
ATOM   529   C  CB  . SER   A  1 72  ? -43.363 28.930  -42.786  1.00 51.50  ? 373  SER   A CB  1 
ATOM   530   O  OG  . SER   A  1 72  ? -43.461 28.712  -44.184  1.00 68.21  ? 373  SER   A OG  1 
ATOM   531   N  N   . ILE   A  1 73  ? -43.718 31.550  -44.620  1.00 57.87  ? 374  ILE   A N   1 
ATOM   532   C  CA  . ILE   A  1 73  ? -43.070 32.268  -45.709  1.00 53.49  ? 374  ILE   A CA  1 
ATOM   533   C  C   . ILE   A  1 73  ? -43.621 33.684  -45.869  1.00 59.43  ? 374  ILE   A C   1 
ATOM   534   O  O   . ILE   A  1 73  ? -43.480 34.276  -46.942  1.00 57.63  ? 374  ILE   A O   1 
ATOM   535   C  CB  . ILE   A  1 73  ? -43.182 31.493  -47.028  1.00 52.06  ? 374  ILE   A CB  1 
ATOM   536   C  CG1 . ILE   A  1 73  ? -44.647 31.449  -47.474  1.00 60.04  ? 374  ILE   A CG1 1 
ATOM   537   C  CG2 . ILE   A  1 73  ? -42.649 30.089  -46.843  1.00 51.80  ? 374  ILE   A CG2 1 
ATOM   538   C  CD1 . ILE   A  1 73  ? -44.865 31.387  -48.974  1.00 59.84  ? 374  ILE   A CD1 1 
ATOM   539   N  N   . LYS   A  1 74  ? -44.257 34.234  -44.829  1.00 60.60  ? 375  LYS   A N   1 
ATOM   540   C  CA  . LYS   A  1 74  ? -44.668 35.639  -44.810  1.00 77.59  ? 375  LYS   A CA  1 
ATOM   541   C  C   . LYS   A  1 74  ? -45.795 35.933  -45.795  1.00 76.95  ? 375  LYS   A C   1 
ATOM   542   O  O   . LYS   A  1 74  ? -45.943 37.072  -46.242  1.00 79.75  ? 375  LYS   A O   1 
ATOM   543   C  CB  . LYS   A  1 74  ? -43.480 36.571  -45.094  1.00 89.67  ? 375  LYS   A CB  1 
ATOM   544   C  CG  . LYS   A  1 74  ? -42.891 37.246  -43.882  1.00 97.18  ? 375  LYS   A CG  1 
ATOM   545   C  CD  . LYS   A  1 74  ? -43.547 38.597  -43.642  1.00 97.51  ? 375  LYS   A CD  1 
ATOM   546   C  CE  . LYS   A  1 74  ? -43.093 39.144  -42.312  1.00 97.40  ? 375  LYS   A CE  1 
ATOM   547   N  NZ  . LYS   A  1 74  ? -42.966 38.048  -41.295  1.00 94.86  ? 375  LYS   A NZ  1 
ATOM   548   N  N   . ARG   A  1 75  ? -46.601 34.926  -46.149  1.00 73.34  ? 376  ARG   A N   1 
ATOM   549   C  CA  . ARG   A  1 75  ? -47.651 35.108  -47.149  1.00 71.39  ? 376  ARG   A CA  1 
ATOM   550   C  C   . ARG   A  1 75  ? -49.030 34.716  -46.629  1.00 72.05  ? 376  ARG   A C   1 
ATOM   551   O  O   . ARG   A  1 75  ? -49.926 34.439  -47.433  1.00 72.41  ? 376  ARG   A O   1 
ATOM   552   C  CB  . ARG   A  1 75  ? -47.337 34.315  -48.419  1.00 65.16  ? 376  ARG   A CB  1 
ATOM   553   C  CG  . ARG   A  1 75  ? -46.129 34.818  -49.165  1.00 65.15  ? 376  ARG   A CG  1 
ATOM   554   C  CD  . ARG   A  1 75  ? -46.273 36.289  -49.443  1.00 68.07  ? 376  ARG   A CD  1 
ATOM   555   N  NE  . ARG   A  1 75  ? -45.303 36.762  -50.424  1.00 76.01  ? 376  ARG   A NE  1 
ATOM   556   C  CZ  . ARG   A  1 75  ? -44.089 37.218  -50.129  1.00 82.33  ? 376  ARG   A CZ  1 
ATOM   557   N  NH1 . ARG   A  1 75  ? -43.290 37.635  -51.101  1.00 77.03  ? 376  ARG   A NH1 1 
ATOM   558   N  NH2 . ARG   A  1 75  ? -43.672 37.254  -48.869  1.00 89.06  ? 376  ARG   A NH2 1 
ATOM   559   N  N   . PHE   A  1 76  ? -49.225 34.704  -45.310  1.00 63.98  ? 377  PHE   A N   1 
ATOM   560   C  CA  . PHE   A  1 76  ? -50.492 34.257  -44.745  1.00 58.03  ? 377  PHE   A CA  1 
ATOM   561   C  C   . PHE   A  1 76  ? -51.608 35.227  -45.108  1.00 65.01  ? 377  PHE   A C   1 
ATOM   562   O  O   . PHE   A  1 76  ? -51.422 36.444  -45.082  1.00 77.86  ? 377  PHE   A O   1 
ATOM   563   C  CB  . PHE   A  1 76  ? -50.385 34.118  -43.222  1.00 61.08  ? 377  PHE   A CB  1 
ATOM   564   C  CG  . PHE   A  1 76  ? -51.642 33.590  -42.576  1.00 66.11  ? 377  PHE   A CG  1 
ATOM   565   C  CD1 . PHE   A  1 76  ? -51.831 32.231  -42.416  1.00 57.05  ? 377  PHE   A CD1 1 
ATOM   566   C  CD2 . PHE   A  1 76  ? -52.644 34.458  -42.142  1.00 74.76  ? 377  PHE   A CD2 1 
ATOM   567   C  CE1 . PHE   A  1 76  ? -52.984 31.746  -41.846  1.00 59.07  ? 377  PHE   A CE1 1 
ATOM   568   C  CE2 . PHE   A  1 76  ? -53.807 33.973  -41.565  1.00 67.96  ? 377  PHE   A CE2 1 
ATOM   569   C  CZ  . PHE   A  1 76  ? -53.975 32.619  -41.416  1.00 63.77  ? 377  PHE   A CZ  1 
ATOM   570   N  N   . GLY   A  1 77  ? -52.777 34.683  -45.444  1.00 68.52  ? 378  GLY   A N   1 
ATOM   571   C  CA  . GLY   A  1 77  ? -53.886 35.494  -45.916  1.00 73.28  ? 378  GLY   A CA  1 
ATOM   572   C  C   . GLY   A  1 77  ? -53.701 36.116  -47.287  1.00 75.78  ? 378  GLY   A C   1 
ATOM   573   O  O   . GLY   A  1 77  ? -54.609 36.808  -47.765  1.00 69.23  ? 378  GLY   A O   1 
ATOM   574   N  N   . SER   A  1 78  ? -52.562 35.892  -47.939  1.00 76.27  ? 379  SER   A N   1 
ATOM   575   C  CA  . SER   A  1 78  ? -52.285 36.515  -49.221  1.00 72.10  ? 379  SER   A CA  1 
ATOM   576   C  C   . SER   A  1 78  ? -53.157 35.911  -50.317  1.00 71.88  ? 379  SER   A C   1 
ATOM   577   O  O   . SER   A  1 78  ? -53.843 34.901  -50.129  1.00 63.48  ? 379  SER   A O   1 
ATOM   578   C  CB  . SER   A  1 78  ? -50.819 36.341  -49.596  1.00 70.42  ? 379  SER   A CB  1 
ATOM   579   O  OG  . SER   A  1 78  ? -50.589 35.017  -50.037  1.00 67.10  ? 379  SER   A OG  1 
ATOM   580   N  N   . LYS   A  1 79  ? -53.102 36.547  -51.488  1.00 77.36  ? 380  LYS   A N   1 
ATOM   581   C  CA  . LYS   A  1 79  ? -53.852 36.054  -52.637  1.00 82.67  ? 380  LYS   A CA  1 
ATOM   582   C  C   . LYS   A  1 79  ? -53.424 34.633  -53.000  1.00 77.97  ? 380  LYS   A C   1 
ATOM   583   O  O   . LYS   A  1 79  ? -54.266 33.747  -53.193  1.00 71.84  ? 380  LYS   A O   1 
ATOM   584   C  CB  . LYS   A  1 79  ? -53.663 37.010  -53.816  1.00 89.29  ? 380  LYS   A CB  1 
ATOM   585   C  CG  . LYS   A  1 79  ? -54.901 37.198  -54.692  1.00 98.02  ? 380  LYS   A CG  1 
ATOM   586   C  CD  . LYS   A  1 79  ? -54.645 38.228  -55.794  1.00 103.26 ? 380  LYS   A CD  1 
ATOM   587   C  CE  . LYS   A  1 79  ? -55.925 38.633  -56.529  1.00 101.55 ? 380  LYS   A CE  1 
ATOM   588   N  NZ  . LYS   A  1 79  ? -56.400 37.586  -57.481  1.00 93.46  ? 380  LYS   A NZ  1 
ATOM   589   N  N   . ALA   A  1 80  ? -52.110 34.391  -53.074  1.00 74.93  ? 381  ALA   A N   1 
ATOM   590   C  CA  . ALA   A  1 80  ? -51.622 33.055  -53.402  1.00 71.19  ? 381  ALA   A CA  1 
ATOM   591   C  C   . ALA   A  1 80  ? -51.955 32.046  -52.310  1.00 69.21  ? 381  ALA   A C   1 
ATOM   592   O  O   . ALA   A  1 80  ? -52.115 30.852  -52.599  1.00 65.29  ? 381  ALA   A O   1 
ATOM   593   C  CB  . ALA   A  1 80  ? -50.116 33.088  -53.648  1.00 66.15  ? 381  ALA   A CB  1 
ATOM   594   N  N   . HIS   A  1 81  ? -52.060 32.500  -51.057  1.00 62.14  ? 382  HIS   A N   1 
ATOM   595   C  CA  . HIS   A  1 81  ? -52.513 31.613  -49.988  1.00 60.59  ? 382  HIS   A CA  1 
ATOM   596   C  C   . HIS   A  1 81  ? -53.966 31.206  -50.205  1.00 56.84  ? 382  HIS   A C   1 
ATOM   597   O  O   . HIS   A  1 81  ? -54.295 30.014  -50.203  1.00 57.61  ? 382  HIS   A O   1 
ATOM   598   C  CB  . HIS   A  1 81  ? -52.332 32.301  -48.629  1.00 60.74  ? 382  HIS   A CB  1 
ATOM   599   C  CG  . HIS   A  1 81  ? -52.777 31.482  -47.453  1.00 57.90  ? 382  HIS   A CG  1 
ATOM   600   N  ND1 . HIS   A  1 81  ? -52.963 32.025  -46.197  1.00 58.80  ? 382  HIS   A ND1 1 
ATOM   601   C  CD2 . HIS   A  1 81  ? -53.054 30.162  -47.332  1.00 57.38  ? 382  HIS   A CD2 1 
ATOM   602   C  CE1 . HIS   A  1 81  ? -53.349 31.079  -45.360  1.00 54.09  ? 382  HIS   A CE1 1 
ATOM   603   N  NE2 . HIS   A  1 81  ? -53.408 29.937  -46.022  1.00 56.98  ? 382  HIS   A NE2 1 
ATOM   604   N  N   . MET   A  1 82  ? -54.847 32.187  -50.417  1.00 52.67  ? 383  MET   A N   1 
ATOM   605   C  CA  . MET   A  1 82  ? -56.273 31.900  -50.555  1.00 62.12  ? 383  MET   A CA  1 
ATOM   606   C  C   . MET   A  1 82  ? -56.584 31.071  -51.801  1.00 68.30  ? 383  MET   A C   1 
ATOM   607   O  O   . MET   A  1 82  ? -57.511 30.250  -51.782  1.00 70.79  ? 383  MET   A O   1 
ATOM   608   C  CB  . MET   A  1 82  ? -57.068 33.207  -50.579  1.00 63.80  ? 383  MET   A CB  1 
ATOM   609   C  CG  . MET   A  1 82  ? -57.022 34.013  -49.286  1.00 75.40  ? 383  MET   A CG  1 
ATOM   610   S  SD  . MET   A  1 82  ? -57.604 33.102  -47.826  1.00 83.16  ? 383  MET   A SD  1 
ATOM   611   C  CE  . MET   A  1 82  ? -57.544 34.379  -46.566  1.00 76.58  ? 383  MET   A CE  1 
ATOM   612   N  N   . GLU   A  1 83  ? -55.840 31.273  -52.895  1.00 63.38  ? 384  GLU   A N   1 
ATOM   613   C  CA  . GLU   A  1 83  ? -56.088 30.478  -54.096  1.00 64.15  ? 384  GLU   A CA  1 
ATOM   614   C  C   . GLU   A  1 83  ? -55.595 29.054  -53.921  1.00 63.43  ? 384  GLU   A C   1 
ATOM   615   O  O   . GLU   A  1 83  ? -56.269 28.102  -54.334  1.00 59.53  ? 384  GLU   A O   1 
ATOM   616   C  CB  . GLU   A  1 83  ? -55.420 31.118  -55.310  1.00 72.93  ? 384  GLU   A CB  1 
ATOM   617   C  CG  . GLU   A  1 83  ? -56.187 32.291  -55.879  1.00 84.51  ? 384  GLU   A CG  1 
ATOM   618   C  CD  . GLU   A  1 83  ? -55.385 33.063  -56.894  1.00 86.30  ? 384  GLU   A CD  1 
ATOM   619   O  OE1 . GLU   A  1 83  ? -54.264 32.600  -57.225  1.00 80.59  ? 384  GLU   A OE1 1 
ATOM   620   O  OE2 . GLU   A  1 83  ? -55.881 34.126  -57.346  1.00 87.00  ? 384  GLU   A OE2 1 
ATOM   621   N  N   . ARG   A  1 84  ? -54.409 28.895  -53.327  1.00 62.63  ? 385  ARG   A N   1 
ATOM   622   C  CA  . ARG   A  1 84  ? -53.894 27.565  -53.035  1.00 57.60  ? 385  ARG   A CA  1 
ATOM   623   C  C   . ARG   A  1 84  ? -54.868 26.794  -52.159  1.00 61.81  ? 385  ARG   A C   1 
ATOM   624   O  O   . ARG   A  1 84  ? -55.047 25.582  -52.331  1.00 58.38  ? 385  ARG   A O   1 
ATOM   625   C  CB  . ARG   A  1 84  ? -52.529 27.687  -52.359  1.00 55.97  ? 385  ARG   A CB  1 
ATOM   626   C  CG  . ARG   A  1 84  ? -51.911 26.373  -51.916  1.00 55.47  ? 385  ARG   A CG  1 
ATOM   627   C  CD  . ARG   A  1 84  ? -51.774 25.430  -53.079  1.00 46.89  ? 385  ARG   A CD  1 
ATOM   628   N  NE  . ARG   A  1 84  ? -51.243 24.141  -52.662  1.00 55.69  ? 385  ARG   A NE  1 
ATOM   629   C  CZ  . ARG   A  1 84  ? -51.220 23.073  -53.450  1.00 56.15  ? 385  ARG   A CZ  1 
ATOM   630   N  NH1 . ARG   A  1 84  ? -51.706 23.168  -54.680  1.00 63.76  ? 385  ARG   A NH1 1 
ATOM   631   N  NH2 . ARG   A  1 84  ? -50.719 21.922  -53.016  1.00 47.94  ? 385  ARG   A NH2 1 
ATOM   632   N  N   . LEU   A  1 85  ? -55.529 27.495  -51.232  1.00 65.78  ? 386  LEU   A N   1 
ATOM   633   C  CA  . LEU   A  1 85  ? -56.471 26.854  -50.320  1.00 61.99  ? 386  LEU   A CA  1 
ATOM   634   C  C   . LEU   A  1 85  ? -57.625 26.239  -51.088  1.00 71.00  ? 386  LEU   A C   1 
ATOM   635   O  O   . LEU   A  1 85  ? -57.899 25.040  -50.970  1.00 72.48  ? 386  LEU   A O   1 
ATOM   636   C  CB  . LEU   A  1 85  ? -56.993 27.867  -49.303  1.00 62.30  ? 386  LEU   A CB  1 
ATOM   637   C  CG  . LEU   A  1 85  ? -56.950 27.426  -47.842  1.00 56.54  ? 386  LEU   A CG  1 
ATOM   638   C  CD1 . LEU   A  1 85  ? -57.527 26.024  -47.683  1.00 63.17  ? 386  LEU   A CD1 1 
ATOM   639   C  CD2 . LEU   A  1 85  ? -55.528 27.476  -47.346  1.00 55.41  ? 386  LEU   A CD2 1 
ATOM   640   N  N   . GLU   A  1 86  ? -58.315 27.058  -51.892  1.00 75.92  ? 387  GLU   A N   1 
ATOM   641   C  CA  . GLU   A  1 86  ? -59.446 26.558  -52.665  1.00 76.84  ? 387  GLU   A CA  1 
ATOM   642   C  C   . GLU   A  1 86  ? -58.995 25.555  -53.719  1.00 67.90  ? 387  GLU   A C   1 
ATOM   643   O  O   . GLU   A  1 86  ? -59.758 24.652  -54.083  1.00 66.33  ? 387  GLU   A O   1 
ATOM   644   C  CB  . GLU   A  1 86  ? -60.205 27.729  -53.296  1.00 90.60  ? 387  GLU   A CB  1 
ATOM   645   C  CG  . GLU   A  1 86  ? -60.185 27.779  -54.818  1.00 96.92  ? 387  GLU   A CG  1 
ATOM   646   C  CD  . GLU   A  1 86  ? -61.439 28.427  -55.389  1.00 102.89 ? 387  GLU   A CD  1 
ATOM   647   O  OE1 . GLU   A  1 86  ? -62.527 27.825  -55.251  1.00 107.82 ? 387  GLU   A OE1 1 
ATOM   648   O  OE2 . GLU   A  1 86  ? -61.339 29.538  -55.957  1.00 101.16 ? 387  GLU   A OE2 1 
ATOM   649   N  N   . GLU   A  1 87  ? -57.752 25.674  -54.191  1.00 57.65  ? 388  GLU   A N   1 
ATOM   650   C  CA  . GLU   A  1 87  ? -57.229 24.695  -55.132  1.00 50.24  ? 388  GLU   A CA  1 
ATOM   651   C  C   . GLU   A  1 87  ? -57.117 23.315  -54.501  1.00 61.06  ? 388  GLU   A C   1 
ATOM   652   O  O   . GLU   A  1 87  ? -57.276 22.306  -55.203  1.00 64.37  ? 388  GLU   A O   1 
ATOM   653   C  CB  . GLU   A  1 87  ? -55.865 25.145  -55.661  1.00 45.72  ? 388  GLU   A CB  1 
ATOM   654   C  CG  . GLU   A  1 87  ? -55.378 24.394  -56.901  1.00 41.85  ? 388  GLU   A CG  1 
ATOM   655   C  CD  . GLU   A  1 87  ? -53.880 24.507  -57.104  1.00 54.05  ? 388  GLU   A CD  1 
ATOM   656   O  OE1 . GLU   A  1 87  ? -53.161 24.794  -56.125  1.00 60.84  ? 388  GLU   A OE1 1 
ATOM   657   O  OE2 . GLU   A  1 87  ? -53.408 24.292  -58.238  1.00 59.97  ? 388  GLU   A OE2 1 
ATOM   658   N  N   . VAL   A  1 88  ? -56.824 23.241  -53.194  1.00 50.77  ? 389  VAL   A N   1 
ATOM   659   C  CA  . VAL   A  1 88  ? -56.728 21.937  -52.539  1.00 45.29  ? 389  VAL   A CA  1 
ATOM   660   C  C   . VAL   A  1 88  ? -58.113 21.365  -52.331  1.00 57.03  ? 389  VAL   A C   1 
ATOM   661   O  O   . VAL   A  1 88  ? -58.331 20.155  -52.475  1.00 50.06  ? 389  VAL   A O   1 
ATOM   662   C  CB  . VAL   A  1 88  ? -55.968 22.023  -51.199  1.00 37.23  ? 389  VAL   A CB  1 
ATOM   663   C  CG1 . VAL   A  1 88  ? -56.030 20.683  -50.498  1.00 42.04  ? 389  VAL   A CG1 1 
ATOM   664   C  CG2 . VAL   A  1 88  ? -54.514 22.426  -51.396  1.00 36.83  ? 389  VAL   A CG2 1 
ATOM   665   N  N   . ASN   A  1 89  ? -59.066 22.235  -51.990  1.00 70.95  ? 390  ASN   A N   1 
ATOM   666   C  CA  . ASN   A  1 89  ? -60.433 21.795  -51.751  1.00 73.10  ? 390  ASN   A CA  1 
ATOM   667   C  C   . ASN   A  1 89  ? -61.034 21.184  -53.001  1.00 71.22  ? 390  ASN   A C   1 
ATOM   668   O  O   . ASN   A  1 89  ? -61.733 20.168  -52.925  1.00 77.11  ? 390  ASN   A O   1 
ATOM   669   C  CB  . ASN   A  1 89  ? -61.276 22.968  -51.257  1.00 81.58  ? 390  ASN   A CB  1 
ATOM   670   C  CG  . ASN   A  1 89  ? -61.221 23.132  -49.743  1.00 84.04  ? 390  ASN   A CG  1 
ATOM   671   O  OD1 . ASN   A  1 89  ? -62.264 23.225  -49.087  1.00 93.31  ? 390  ASN   A OD1 1 
ATOM   672   N  ND2 . ASN   A  1 89  ? -60.003 23.147  -49.177  1.00 71.04  ? 390  ASN   A ND2 1 
ATOM   673   N  N   . LYS   A  1 90  ? -60.762 21.778  -54.164  1.00 68.45  ? 391  LYS   A N   1 
ATOM   674   C  CA  . LYS   A  1 90  ? -61.265 21.206  -55.405  1.00 66.19  ? 391  LYS   A CA  1 
ATOM   675   C  C   . LYS   A  1 90  ? -60.710 19.809  -55.610  1.00 57.95  ? 391  LYS   A C   1 
ATOM   676   O  O   . LYS   A  1 90  ? -61.439 18.894  -56.009  1.00 67.57  ? 391  LYS   A O   1 
ATOM   677   C  CB  . LYS   A  1 90  ? -60.925 22.116  -56.591  1.00 66.19  ? 391  LYS   A CB  1 
ATOM   678   C  CG  . LYS   A  1 90  ? -61.858 23.327  -56.738  1.00 71.80  ? 391  LYS   A CG  1 
ATOM   679   C  CD  . LYS   A  1 90  ? -61.264 24.406  -57.634  1.00 80.71  ? 391  LYS   A CD  1 
ATOM   680   C  CE  . LYS   A  1 90  ? -62.180 25.626  -57.708  1.00 92.78  ? 391  LYS   A CE  1 
ATOM   681   N  NZ  . LYS   A  1 90  ? -61.702 26.657  -58.694  1.00 98.50  ? 391  LYS   A NZ  1 
ATOM   682   N  N   . GLU   A  1 91  ? -59.430 19.617  -55.303  1.00 50.78  ? 392  GLU   A N   1 
ATOM   683   C  CA  . GLU   A  1 91  ? -58.819 18.305  -55.471  1.00 56.43  ? 392  GLU   A CA  1 
ATOM   684   C  C   . GLU   A  1 91  ? -59.399 17.282  -54.489  1.00 65.42  ? 392  GLU   A C   1 
ATOM   685   O  O   . GLU   A  1 91  ? -59.744 16.161  -54.882  1.00 73.66  ? 392  GLU   A O   1 
ATOM   686   C  CB  . GLU   A  1 91  ? -57.305 18.422  -55.319  1.00 55.19  ? 392  GLU   A CB  1 
ATOM   687   C  CG  . GLU   A  1 91  ? -56.531 18.034  -56.558  1.00 58.91  ? 392  GLU   A CG  1 
ATOM   688   C  CD  . GLU   A  1 91  ? -55.063 18.366  -56.444  1.00 60.62  ? 392  GLU   A CD  1 
ATOM   689   O  OE1 . GLU   A  1 91  ? -54.225 17.502  -56.767  1.00 61.11  ? 392  GLU   A OE1 1 
ATOM   690   O  OE2 . GLU   A  1 91  ? -54.742 19.494  -56.028  1.00 59.74  ? 392  GLU   A OE2 1 
ATOM   691   N  N   . ILE   A  1 92  ? -59.507 17.633  -53.206  1.00 60.69  ? 393  ILE   A N   1 
ATOM   692   C  CA  . ILE   A  1 92  ? -60.075 16.676  -52.257  1.00 63.13  ? 393  ILE   A CA  1 
ATOM   693   C  C   . ILE   A  1 92  ? -61.541 16.406  -52.593  1.00 75.67  ? 393  ILE   A C   1 
ATOM   694   O  O   . ILE   A  1 92  ? -62.019 15.273  -52.473  1.00 82.77  ? 393  ILE   A O   1 
ATOM   695   C  CB  . ILE   A  1 92  ? -59.909 17.163  -50.806  1.00 54.92  ? 393  ILE   A CB  1 
ATOM   696   C  CG1 . ILE   A  1 92  ? -58.471 17.593  -50.512  1.00 50.79  ? 393  ILE   A CG1 1 
ATOM   697   C  CG2 . ILE   A  1 92  ? -60.312 16.073  -49.836  1.00 55.32  ? 393  ILE   A CG2 1 
ATOM   698   C  CD1 . ILE   A  1 92  ? -58.316 18.234  -49.136  1.00 44.38  ? 393  ILE   A CD1 1 
ATOM   699   N  N   . ASP   A  1 93  ? -62.274 17.436  -53.029  1.00 80.18  ? 394  ASP   A N   1 
ATOM   700   C  CA  . ASP   A  1 93  ? -63.654 17.236  -53.469  1.00 77.77  ? 394  ASP   A CA  1 
ATOM   701   C  C   . ASP   A  1 93  ? -63.717 16.267  -54.643  1.00 78.29  ? 394  ASP   A C   1 
ATOM   702   O  O   . ASP   A  1 93  ? -64.450 15.271  -54.602  1.00 79.95  ? 394  ASP   A O   1 
ATOM   703   C  CB  . ASP   A  1 93  ? -64.286 18.570  -53.858  1.00 84.96  ? 394  ASP   A CB  1 
ATOM   704   C  CG  . ASP   A  1 93  ? -65.361 19.011  -52.897  1.00 94.56  ? 394  ASP   A CG  1 
ATOM   705   O  OD1 . ASP   A  1 93  ? -66.065 19.995  -53.220  1.00 96.39  ? 394  ASP   A OD1 1 
ATOM   706   O  OD2 . ASP   A  1 93  ? -65.492 18.388  -51.820  1.00 99.24  ? 394  ASP   A OD2 1 
ATOM   707   N  N   . THR   A  1 94  ? -62.947 16.539  -55.702  1.00 69.71  ? 395  THR   A N   1 
ATOM   708   C  CA  . THR   A  1 94  ? -62.958 15.653  -56.865  1.00 75.60  ? 395  THR   A CA  1 
ATOM   709   C  C   . THR   A  1 94  ? -62.162 14.382  -56.585  1.00 83.60  ? 395  THR   A C   1 
ATOM   710   O  O   . THR   A  1 94  ? -62.739 13.316  -56.354  1.00 90.74  ? 395  THR   A O   1 
ATOM   711   C  CB  . THR   A  1 94  ? -62.433 16.380  -58.111  1.00 71.38  ? 395  THR   A CB  1 
ATOM   712   O  OG1 . THR   A  1 94  ? -61.097 16.833  -57.889  1.00 67.36  ? 395  THR   A OG1 1 
ATOM   713   C  CG2 . THR   A  1 94  ? -63.301 17.569  -58.419  1.00 74.00  ? 395  THR   A CG2 1 
ATOM   714   N  N   . THR   A  1 95  ? -60.829 14.479  -56.579  1.00 83.07  ? 396  THR   A N   1 
ATOM   715   C  CA  . THR   A  1 95  ? -59.992 13.283  -56.552  1.00 71.35  ? 396  THR   A CA  1 
ATOM   716   C  C   . THR   A  1 95  ? -59.991 12.570  -55.206  1.00 70.37  ? 396  THR   A C   1 
ATOM   717   O  O   . THR   A  1 95  ? -59.440 11.468  -55.126  1.00 76.55  ? 396  THR   A O   1 
ATOM   718   C  CB  . THR   A  1 95  ? -58.551 13.634  -56.949  1.00 63.37  ? 396  THR   A CB  1 
ATOM   719   O  OG1 . THR   A  1 95  ? -57.923 14.399  -55.905  1.00 63.23  ? 396  THR   A OG1 1 
ATOM   720   C  CG2 . THR   A  1 95  ? -58.537 14.440  -58.256  1.00 47.54  ? 396  THR   A CG2 1 
ATOM   721   N  N   . SER   A  1 96  ? -60.587 13.156  -54.164  1.00 67.64  ? 397  SER   A N   1 
ATOM   722   C  CA  . SER   A  1 96  ? -60.581 12.618  -52.800  1.00 62.22  ? 397  SER   A CA  1 
ATOM   723   C  C   . SER   A  1 96  ? -59.203 12.635  -52.155  1.00 59.26  ? 397  SER   A C   1 
ATOM   724   O  O   . SER   A  1 96  ? -58.992 11.983  -51.130  1.00 53.07  ? 397  SER   A O   1 
ATOM   725   C  CB  . SER   A  1 96  ? -61.162 11.206  -52.740  1.00 62.62  ? 397  SER   A CB  1 
ATOM   726   O  OG  . SER   A  1 96  ? -62.575 11.260  -52.707  1.00 70.91  ? 397  SER   A OG  1 
ATOM   727   N  N   . THR   A  1 97  ? -58.264 13.368  -52.741  1.00 61.64  ? 398  THR   A N   1 
ATOM   728   C  CA  . THR   A  1 97  ? -56.916 13.568  -52.219  1.00 55.92  ? 398  THR   A CA  1 
ATOM   729   C  C   . THR   A  1 97  ? -56.380 14.828  -52.885  1.00 56.15  ? 398  THR   A C   1 
ATOM   730   O  O   . THR   A  1 97  ? -57.128 15.547  -53.555  1.00 61.47  ? 398  THR   A O   1 
ATOM   731   C  CB  . THR   A  1 97  ? -56.033 12.346  -52.481  1.00 55.96  ? 398  THR   A CB  1 
ATOM   732   O  OG1 . THR   A  1 97  ? -54.726 12.570  -51.940  1.00 49.53  ? 398  THR   A OG1 1 
ATOM   733   C  CG2 . THR   A  1 97  ? -55.936 12.075  -53.993  1.00 53.68  ? 398  THR   A CG2 1 
ATOM   734   N  N   . TYR   A  1 98  ? -55.095 15.116  -52.696  1.00 50.38  ? 399  TYR   A N   1 
ATOM   735   C  CA  . TYR   A  1 98  ? -54.501 16.252  -53.389  1.00 41.80  ? 399  TYR   A CA  1 
ATOM   736   C  C   . TYR   A  1 98  ? -53.003 16.029  -53.522  1.00 50.64  ? 399  TYR   A C   1 
ATOM   737   O  O   . TYR   A  1 98  ? -52.454 15.030  -53.045  1.00 59.51  ? 399  TYR   A O   1 
ATOM   738   C  CB  . TYR   A  1 98  ? -54.839 17.570  -52.688  1.00 40.09  ? 399  TYR   A CB  1 
ATOM   739   C  CG  . TYR   A  1 98  ? -54.164 17.801  -51.355  1.00 43.94  ? 399  TYR   A CG  1 
ATOM   740   C  CD1 . TYR   A  1 98  ? -53.163 18.758  -51.222  1.00 38.51  ? 399  TYR   A CD1 1 
ATOM   741   C  CD2 . TYR   A  1 98  ? -54.528 17.075  -50.228  1.00 50.91  ? 399  TYR   A CD2 1 
ATOM   742   C  CE1 . TYR   A  1 98  ? -52.542 18.975  -50.009  1.00 47.37  ? 399  TYR   A CE1 1 
ATOM   743   C  CE2 . TYR   A  1 98  ? -53.907 17.293  -48.992  1.00 42.19  ? 399  TYR   A CE2 1 
ATOM   744   C  CZ  . TYR   A  1 98  ? -52.917 18.246  -48.900  1.00 46.18  ? 399  TYR   A CZ  1 
ATOM   745   O  OH  . TYR   A  1 98  ? -52.289 18.496  -47.702  1.00 50.34  ? 399  TYR   A OH  1 
ATOM   746   N  N   . GLN   A  1 99  ? -52.346 16.967  -54.195  1.00 45.44  ? 400  GLN   A N   1 
ATOM   747   C  CA  . GLN   A  1 99  ? -50.946 16.827  -54.557  1.00 49.85  ? 400  GLN   A CA  1 
ATOM   748   C  C   . GLN   A  1 99  ? -50.168 18.023  -54.031  1.00 57.55  ? 400  GLN   A C   1 
ATOM   749   O  O   . GLN   A  1 99  ? -50.527 19.173  -54.305  1.00 58.11  ? 400  GLN   A O   1 
ATOM   750   C  CB  . GLN   A  1 99  ? -50.778 16.714  -56.080  1.00 53.22  ? 400  GLN   A CB  1 
ATOM   751   C  CG  . GLN   A  1 99  ? -51.261 15.413  -56.673  1.00 46.87  ? 400  GLN   A CG  1 
ATOM   752   C  CD  . GLN   A  1 99  ? -50.481 14.228  -56.152  1.00 50.70  ? 400  GLN   A CD  1 
ATOM   753   O  OE1 . GLN   A  1 99  ? -49.255 14.263  -56.072  1.00 52.88  ? 400  GLN   A OE1 1 
ATOM   754   N  NE2 . GLN   A  1 99  ? -51.191 13.169  -55.783  1.00 49.80  ? 400  GLN   A NE2 1 
ATOM   755   N  N   . LEU   A  1 100 ? -49.098 17.756  -53.290  1.00 56.50  ? 401  LEU   A N   1 
ATOM   756   C  CA  . LEU   A  1 100 ? -48.297 18.846  -52.753  1.00 51.42  ? 401  LEU   A CA  1 
ATOM   757   C  C   . LEU   A  1 100 ? -47.487 19.501  -53.859  1.00 43.38  ? 401  LEU   A C   1 
ATOM   758   O  O   . LEU   A  1 100 ? -46.881 18.814  -54.678  1.00 46.45  ? 401  LEU   A O   1 
ATOM   759   C  CB  . LEU   A  1 100 ? -47.353 18.331  -51.676  1.00 44.12  ? 401  LEU   A CB  1 
ATOM   760   C  CG  . LEU   A  1 100 ? -47.986 17.798  -50.396  1.00 34.40  ? 401  LEU   A CG  1 
ATOM   761   C  CD1 . LEU   A  1 100 ? -46.901 17.113  -49.635  1.00 37.61  ? 401  LEU   A CD1 1 
ATOM   762   C  CD2 . LEU   A  1 100 ? -48.558 18.948  -49.613  1.00 36.75  ? 401  LEU   A CD2 1 
ATOM   763   N  N   . LYS   A  1 101 ? -47.454 20.833  -53.864  1.00 39.37  ? 402  LYS   A N   1 
ATOM   764   C  CA  . LYS   A  1 101 ? -46.468 21.545  -54.666  1.00 34.46  ? 402  LYS   A CA  1 
ATOM   765   C  C   . LYS   A  1 101 ? -45.063 21.143  -54.229  1.00 44.51  ? 402  LYS   A C   1 
ATOM   766   O  O   . LYS   A  1 101 ? -44.859 20.578  -53.155  1.00 58.84  ? 402  LYS   A O   1 
ATOM   767   C  CB  . LYS   A  1 101 ? -46.655 23.056  -54.532  1.00 34.48  ? 402  LYS   A CB  1 
ATOM   768   C  CG  . LYS   A  1 101 ? -48.069 23.539  -54.930  1.00 54.92  ? 402  LYS   A CG  1 
ATOM   769   C  CD  . LYS   A  1 101 ? -48.052 24.537  -56.112  1.00 65.95  ? 402  LYS   A CD  1 
ATOM   770   C  CE  . LYS   A  1 101 ? -48.630 23.937  -57.386  1.00 74.39  ? 402  LYS   A CE  1 
ATOM   771   N  NZ  . LYS   A  1 101 ? -50.074 23.605  -57.223  1.00 81.01  ? 402  LYS   A NZ  1 
ATOM   772   N  N   . ASP   A  1 102 ? -44.081 21.430  -55.081  1.00 56.75  ? 403  ASP   A N   1 
ATOM   773   C  CA  . ASP   A  1 102 ? -42.710 21.042  -54.765  1.00 54.41  ? 403  ASP   A CA  1 
ATOM   774   C  C   . ASP   A  1 102 ? -42.200 21.782  -53.538  1.00 50.34  ? 403  ASP   A C   1 
ATOM   775   O  O   . ASP   A  1 102 ? -41.501 21.204  -52.696  1.00 60.14  ? 403  ASP   A O   1 
ATOM   776   C  CB  . ASP   A  1 102 ? -41.798 21.313  -55.963  1.00 67.62  ? 403  ASP   A CB  1 
ATOM   777   C  CG  . ASP   A  1 102 ? -41.989 20.316  -57.082  1.00 75.89  ? 403  ASP   A CG  1 
ATOM   778   O  OD1 . ASP   A  1 102 ? -42.927 19.496  -56.996  1.00 76.47  ? 403  ASP   A OD1 1 
ATOM   779   O  OD2 . ASP   A  1 102 ? -41.191 20.350  -58.044  1.00 79.10  ? 403  ASP   A OD2 1 
ATOM   780   N  N   . THR   A  1 103 ? -42.539 23.066  -53.418  1.00 43.40  ? 404  THR   A N   1 
ATOM   781   C  CA  . THR   A  1 103 ? -42.081 23.846  -52.276  1.00 43.37  ? 404  THR   A CA  1 
ATOM   782   C  C   . THR   A  1 103 ? -42.691 23.338  -50.978  1.00 44.82  ? 404  THR   A C   1 
ATOM   783   O  O   . THR   A  1 103 ? -42.022 23.283  -49.943  1.00 42.14  ? 404  THR   A O   1 
ATOM   784   C  CB  . THR   A  1 103 ? -42.447 25.305  -52.477  1.00 37.01  ? 404  THR   A CB  1 
ATOM   785   O  OG1 . THR   A  1 103 ? -43.812 25.374  -52.904  1.00 44.34  ? 404  THR   A OG1 1 
ATOM   786   C  CG2 . THR   A  1 103 ? -41.535 25.954  -53.516  1.00 37.74  ? 404  THR   A CG2 1 
ATOM   787   N  N   . GLU   A  1 104 ? -43.975 23.003  -51.016  1.00 52.81  ? 405  GLU   A N   1 
ATOM   788   C  CA  . GLU   A  1 104 ? -44.649 22.453  -49.853  1.00 47.45  ? 405  GLU   A CA  1 
ATOM   789   C  C   . GLU   A  1 104 ? -43.985 21.156  -49.414  1.00 48.42  ? 405  GLU   A C   1 
ATOM   790   O  O   . GLU   A  1 104 ? -43.788 20.928  -48.218  1.00 53.84  ? 405  GLU   A O   1 
ATOM   791   C  CB  . GLU   A  1 104 ? -46.140 22.239  -50.179  1.00 41.08  ? 405  GLU   A CB  1 
ATOM   792   C  CG  . GLU   A  1 104 ? -46.882 23.531  -50.580  1.00 35.93  ? 405  GLU   A CG  1 
ATOM   793   C  CD  . GLU   A  1 104 ? -48.238 23.306  -51.247  1.00 43.13  ? 405  GLU   A CD  1 
ATOM   794   O  OE1 . GLU   A  1 104 ? -48.970 24.312  -51.428  1.00 50.15  ? 405  GLU   A OE1 1 
ATOM   795   O  OE2 . GLU   A  1 104 ? -48.570 22.151  -51.598  1.00 44.47  ? 405  GLU   A OE2 1 
ATOM   796   N  N   . LEU   A  1 105 ? -43.606 20.308  -50.371  1.00 46.22  ? 406  LEU   A N   1 
ATOM   797   C  CA  . LEU   A  1 105 ? -43.025 19.016  -50.021  1.00 47.09  ? 406  LEU   A CA  1 
ATOM   798   C  C   . LEU   A  1 105 ? -41.689 19.181  -49.309  1.00 47.64  ? 406  LEU   A C   1 
ATOM   799   O  O   . LEU   A  1 105 ? -41.399 18.454  -48.358  1.00 44.06  ? 406  LEU   A O   1 
ATOM   800   C  CB  . LEU   A  1 105 ? -42.854 18.162  -51.276  1.00 31.68  ? 406  LEU   A CB  1 
ATOM   801   C  CG  . LEU   A  1 105 ? -42.336 16.723  -51.128  1.00 34.38  ? 406  LEU   A CG  1 
ATOM   802   C  CD1 . LEU   A  1 105 ? -43.463 15.752  -50.777  1.00 31.08  ? 406  LEU   A CD1 1 
ATOM   803   C  CD2 . LEU   A  1 105 ? -41.599 16.261  -52.389  1.00 36.54  ? 406  LEU   A CD2 1 
ATOM   804   N  N   . ILE   A  1 106 ? -40.864 20.123  -49.765  1.00 46.68  ? 407  ILE   A N   1 
ATOM   805   C  CA  . ILE   A  1 106 ? -39.571 20.372  -49.134  1.00 39.58  ? 407  ILE   A CA  1 
ATOM   806   C  C   . ILE   A  1 106 ? -39.751 20.938  -47.732  1.00 43.37  ? 407  ILE   A C   1 
ATOM   807   O  O   . ILE   A  1 106 ? -39.047 20.541  -46.794  1.00 33.71  ? 407  ILE   A O   1 
ATOM   808   C  CB  . ILE   A  1 106 ? -38.737 21.317  -50.010  1.00 38.25  ? 407  ILE   A CB  1 
ATOM   809   C  CG1 . ILE   A  1 106 ? -38.109 20.541  -51.161  1.00 38.00  ? 407  ILE   A CG1 1 
ATOM   810   C  CG2 . ILE   A  1 106 ? -37.689 22.044  -49.183  1.00 38.44  ? 407  ILE   A CG2 1 
ATOM   811   C  CD1 . ILE   A  1 106 ? -37.734 21.448  -52.338  1.00 41.55  ? 407  ILE   A CD1 1 
ATOM   812   N  N   . TYR   A  1 107 ? -40.670 21.902  -47.581  1.00 40.70  ? 408  TYR   A N   1 
ATOM   813   C  CA  . TYR   A  1 107 ? -40.996 22.447  -46.269  1.00 45.08  ? 408  TYR   A CA  1 
ATOM   814   C  C   . TYR   A  1 107 ? -41.527 21.355  -45.356  1.00 48.49  ? 408  TYR   A C   1 
ATOM   815   O  O   . TYR   A  1 107 ? -41.160 21.268  -44.172  1.00 49.87  ? 408  TYR   A O   1 
ATOM   816   C  CB  . TYR   A  1 107 ? -42.031 23.574  -46.406  1.00 45.43  ? 408  TYR   A CB  1 
ATOM   817   C  CG  . TYR   A  1 107 ? -42.665 23.983  -45.093  1.00 42.50  ? 408  TYR   A CG  1 
ATOM   818   C  CD1 . TYR   A  1 107 ? -42.160 25.043  -44.361  1.00 47.46  ? 408  TYR   A CD1 1 
ATOM   819   C  CD2 . TYR   A  1 107 ? -43.788 23.327  -44.597  1.00 37.56  ? 408  TYR   A CD2 1 
ATOM   820   C  CE1 . TYR   A  1 107 ? -42.733 25.430  -43.155  1.00 44.59  ? 408  TYR   A CE1 1 
ATOM   821   C  CE2 . TYR   A  1 107 ? -44.369 23.698  -43.388  1.00 45.14  ? 408  TYR   A CE2 1 
ATOM   822   C  CZ  . TYR   A  1 107 ? -43.830 24.753  -42.663  1.00 47.39  ? 408  TYR   A CZ  1 
ATOM   823   O  OH  . TYR   A  1 107 ? -44.388 25.143  -41.449  1.00 47.56  ? 408  TYR   A OH  1 
ATOM   824   N  N   . GLY   A  1 108 ? -42.421 20.525  -45.891  1.00 47.14  ? 409  GLY   A N   1 
ATOM   825   C  CA  . GLY   A  1 108 ? -42.963 19.404  -45.160  1.00 43.88  ? 409  GLY   A CA  1 
ATOM   826   C  C   . GLY   A  1 108 ? -41.889 18.477  -44.639  1.00 44.29  ? 409  GLY   A C   1 
ATOM   827   O  O   . GLY   A  1 108 ? -41.784 18.269  -43.431  1.00 59.85  ? 409  GLY   A O   1 
ATOM   828   N  N   . ALA   A  1 109 ? -41.043 17.958  -45.535  1.00 41.26  ? 410  ALA   A N   1 
ATOM   829   C  CA  . ALA   A  1 109 ? -40.027 17.002  -45.106  1.00 39.79  ? 410  ALA   A CA  1 
ATOM   830   C  C   . ALA   A  1 109 ? -39.029 17.632  -44.147  1.00 40.62  ? 410  ALA   A C   1 
ATOM   831   O  O   . ALA   A  1 109 ? -38.498 16.952  -43.269  1.00 37.49  ? 410  ALA   A O   1 
ATOM   832   C  CB  . ALA   A  1 109 ? -39.298 16.424  -46.317  1.00 32.30  ? 410  ALA   A CB  1 
ATOM   833   N  N   . LYS   A  1 110 ? -38.768 18.927  -44.289  1.00 40.12  ? 411  LYS   A N   1 
ATOM   834   C  CA  . LYS   A  1 110 ? -37.843 19.586  -43.385  1.00 38.03  ? 411  LYS   A CA  1 
ATOM   835   C  C   . LYS   A  1 110 ? -38.461 19.766  -42.005  1.00 55.12  ? 411  LYS   A C   1 
ATOM   836   O  O   . LYS   A  1 110 ? -37.766 19.668  -40.986  1.00 52.77  ? 411  LYS   A O   1 
ATOM   837   C  CB  . LYS   A  1 110 ? -37.415 20.932  -43.961  1.00 32.91  ? 411  LYS   A CB  1 
ATOM   838   C  CG  . LYS   A  1 110 ? -36.292 20.829  -44.970  1.00 30.80  ? 411  LYS   A CG  1 
ATOM   839   C  CD  . LYS   A  1 110 ? -36.190 22.095  -45.784  1.00 30.45  ? 411  LYS   A CD  1 
ATOM   840   C  CE  . LYS   A  1 110 ? -34.831 22.228  -46.439  1.00 37.41  ? 411  LYS   A CE  1 
ATOM   841   N  NZ  . LYS   A  1 110 ? -34.730 23.571  -47.093  1.00 43.92  ? 411  LYS   A NZ  1 
ATOM   842   N  N   . HIS   A  1 111 ? -39.763 20.012  -41.945  1.00 52.53  ? 412  HIS   A N   1 
ATOM   843   C  CA  . HIS   A  1 111 ? -40.351 20.218  -40.634  1.00 46.87  ? 412  HIS   A CA  1 
ATOM   844   C  C   . HIS   A  1 111 ? -40.620 18.903  -39.906  1.00 46.90  ? 412  HIS   A C   1 
ATOM   845   O  O   . HIS   A  1 111 ? -40.516 18.853  -38.671  1.00 45.68  ? 412  HIS   A O   1 
ATOM   846   C  CB  . HIS   A  1 111 ? -41.597 21.086  -40.772  1.00 41.07  ? 412  HIS   A CB  1 
ATOM   847   C  CG  . HIS   A  1 111 ? -41.280 22.549  -40.782  1.00 42.04  ? 412  HIS   A CG  1 
ATOM   848   N  ND1 . HIS   A  1 111 ? -40.468 23.119  -41.735  1.00 42.62  ? 412  HIS   A ND1 1 
ATOM   849   C  CD2 . HIS   A  1 111 ? -41.613 23.546  -39.927  1.00 44.21  ? 412  HIS   A CD2 1 
ATOM   850   C  CE1 . HIS   A  1 111 ? -40.319 24.405  -41.473  1.00 46.87  ? 412  HIS   A CE1 1 
ATOM   851   N  NE2 . HIS   A  1 111 ? -41.014 24.693  -40.389  1.00 40.68  ? 412  HIS   A NE2 1 
ATOM   852   N  N   . ALA   A  1 112 ? -40.902 17.820  -40.633  1.00 33.47  ? 413  ALA   A N   1 
ATOM   853   C  CA  . ALA   A  1 112 ? -41.050 16.544  -39.950  1.00 34.64  ? 413  ALA   A CA  1 
ATOM   854   C  C   . ALA   A  1 112 ? -39.775 16.185  -39.205  1.00 42.23  ? 413  ALA   A C   1 
ATOM   855   O  O   . ALA   A  1 112 ? -39.824 15.692  -38.073  1.00 55.19  ? 413  ALA   A O   1 
ATOM   856   C  CB  . ALA   A  1 112 ? -41.427 15.452  -40.933  1.00 39.06  ? 413  ALA   A CB  1 
ATOM   857   N  N   . TRP   A  1 113 ? -38.623 16.447  -39.814  1.00 45.10  ? 414  TRP   A N   1 
ATOM   858   C  CA  . TRP   A  1 113 ? -37.363 16.278  -39.104  1.00 43.38  ? 414  TRP   A CA  1 
ATOM   859   C  C   . TRP   A  1 113 ? -37.288 17.226  -37.918  1.00 47.37  ? 414  TRP   A C   1 
ATOM   860   O  O   . TRP   A  1 113 ? -36.965 16.819  -36.798  1.00 55.25  ? 414  TRP   A O   1 
ATOM   861   C  CB  . TRP   A  1 113 ? -36.194 16.524  -40.056  1.00 32.91  ? 414  TRP   A CB  1 
ATOM   862   C  CG  . TRP   A  1 113 ? -34.866 16.247  -39.476  1.00 37.84  ? 414  TRP   A CG  1 
ATOM   863   C  CD1 . TRP   A  1 113 ? -34.600 15.648  -38.265  1.00 36.29  ? 414  TRP   A CD1 1 
ATOM   864   C  CD2 . TRP   A  1 113 ? -33.591 16.553  -40.063  1.00 52.92  ? 414  TRP   A CD2 1 
ATOM   865   N  NE1 . TRP   A  1 113 ? -33.246 15.559  -38.074  1.00 35.96  ? 414  TRP   A NE1 1 
ATOM   866   C  CE2 . TRP   A  1 113 ? -32.600 16.113  -39.153  1.00 49.79  ? 414  TRP   A CE2 1 
ATOM   867   C  CE3 . TRP   A  1 113 ? -33.187 17.148  -41.271  1.00 48.94  ? 414  TRP   A CE3 1 
ATOM   868   C  CZ2 . TRP   A  1 113 ? -31.228 16.253  -39.411  1.00 45.43  ? 414  TRP   A CZ2 1 
ATOM   869   C  CZ3 . TRP   A  1 113 ? -31.819 17.286  -41.524  1.00 33.62  ? 414  TRP   A CZ3 1 
ATOM   870   C  CH2 . TRP   A  1 113 ? -30.860 16.844  -40.595  1.00 39.01  ? 414  TRP   A CH2 1 
ATOM   871   N  N   . ARG   A  1 114 ? -37.581 18.504  -38.158  1.00 38.96  ? 415  ARG   A N   1 
ATOM   872   C  CA  . ARG   A  1 114 ? -37.566 19.505  -37.100  1.00 30.88  ? 415  ARG   A CA  1 
ATOM   873   C  C   . ARG   A  1 114 ? -38.450 19.077  -35.936  1.00 41.35  ? 415  ARG   A C   1 
ATOM   874   O  O   . ARG   A  1 114 ? -38.110 19.294  -34.766  1.00 51.30  ? 415  ARG   A O   1 
ATOM   875   C  CB  . ARG   A  1 114 ? -38.028 20.845  -37.683  1.00 33.28  ? 415  ARG   A CB  1 
ATOM   876   C  CG  . ARG   A  1 114 ? -37.835 22.065  -36.790  1.00 38.44  ? 415  ARG   A CG  1 
ATOM   877   C  CD  . ARG   A  1 114 ? -38.438 23.322  -37.431  1.00 33.82  ? 415  ARG   A CD  1 
ATOM   878   N  NE  . ARG   A  1 114 ? -37.988 24.536  -36.753  1.00 40.79  ? 415  ARG   A NE  1 
ATOM   879   C  CZ  . ARG   A  1 114 ? -38.389 25.761  -37.084  1.00 45.42  ? 415  ARG   A CZ  1 
ATOM   880   N  NH1 . ARG   A  1 114 ? -37.939 26.826  -36.437  1.00 35.95  ? 415  ARG   A NH1 1 
ATOM   881   N  NH2 . ARG   A  1 114 ? -39.245 25.918  -38.075  1.00 45.29  ? 415  ARG   A NH2 1 
ATOM   882   N  N   . ASN   A  1 115 ? -39.576 18.445  -36.239  1.00 39.80  ? 416  ASN   A N   1 
ATOM   883   C  CA  . ASN   A  1 115 ? -40.544 18.071  -35.231  1.00 30.62  ? 416  ASN   A CA  1 
ATOM   884   C  C   . ASN   A  1 115 ? -40.274 16.702  -34.631  1.00 38.62  ? 416  ASN   A C   1 
ATOM   885   O  O   . ASN   A  1 115 ? -40.967 16.327  -33.674  1.00 48.61  ? 416  ASN   A O   1 
ATOM   886   C  CB  . ASN   A  1 115 ? -41.951 18.087  -35.829  1.00 32.49  ? 416  ASN   A CB  1 
ATOM   887   C  CG  . ASN   A  1 115 ? -42.411 19.481  -36.249  1.00 39.71  ? 416  ASN   A CG  1 
ATOM   888   O  OD1 . ASN   A  1 115 ? -41.927 20.497  -35.743  1.00 48.58  ? 416  ASN   A OD1 1 
ATOM   889   N  ND2 . ASN   A  1 115 ? -43.390 19.528  -37.154  1.00 38.59  ? 416  ASN   A ND2 1 
ATOM   890   N  N   . ALA   A  1 116 ? -39.294 15.950  -35.151  1.00 24.36  ? 417  ALA   A N   1 
ATOM   891   C  CA  . ALA   A  1 116 ? -38.982 14.623  -34.601  1.00 38.34  ? 417  ALA   A CA  1 
ATOM   892   C  C   . ALA   A  1 116 ? -38.392 14.760  -33.191  1.00 45.45  ? 417  ALA   A C   1 
ATOM   893   O  O   . ALA   A  1 116 ? -37.210 15.060  -33.019  1.00 41.71  ? 417  ALA   A O   1 
ATOM   894   C  CB  . ALA   A  1 116 ? -38.024 13.877  -35.517  1.00 19.86  ? 417  ALA   A CB  1 
ATOM   895   N  N   . SER   A  1 117 ? -39.195 14.475  -32.163  1.00 43.78  ? 418  SER   A N   1 
ATOM   896   C  CA  A SER   A  1 117 ? -38.746 14.785  -30.809  0.71 44.77  ? 418  SER   A CA  1 
ATOM   897   C  CA  B SER   A  1 117 ? -38.792 14.747  -30.781  0.29 44.04  ? 418  SER   A CA  1 
ATOM   898   C  C   . SER   A  1 117 ? -37.653 13.846  -30.315  1.00 44.54  ? 418  SER   A C   1 
ATOM   899   O  O   . SER   A  1 117 ? -36.913 14.218  -29.404  1.00 52.03  ? 418  SER   A O   1 
ATOM   900   C  CB  A SER   A  1 117 ? -39.929 14.769  -29.835  0.71 42.26  ? 418  SER   A CB  1 
ATOM   901   C  CB  B SER   A  1 117 ? -39.990 14.589  -29.844  0.29 42.47  ? 418  SER   A CB  1 
ATOM   902   O  OG  A SER   A  1 117 ? -40.580 13.507  -29.836  0.71 39.97  ? 418  SER   A OG  1 
ATOM   903   O  OG  B SER   A  1 117 ? -41.042 15.475  -30.182  0.29 40.35  ? 418  SER   A OG  1 
ATOM   904   N  N   . ARG   A  1 118 ? -37.509 12.657  -30.902  1.00 45.06  ? 419  ARG   A N   1 
ATOM   905   C  CA  . ARG   A  1 118 ? -36.484 11.702  -30.489  1.00 43.94  ? 419  ARG   A CA  1 
ATOM   906   C  C   . ARG   A  1 118 ? -35.127 11.905  -31.154  1.00 45.00  ? 419  ARG   A C   1 
ATOM   907   O  O   . ARG   A  1 118 ? -34.191 11.164  -30.837  1.00 53.07  ? 419  ARG   A O   1 
ATOM   908   C  CB  . ARG   A  1 118 ? -36.942 10.270  -30.771  1.00 36.73  ? 419  ARG   A CB  1 
ATOM   909   C  CG  . ARG   A  1 118 ? -38.200 9.894   -30.033  1.00 31.31  ? 419  ARG   A CG  1 
ATOM   910   C  CD  . ARG   A  1 118 ? -38.564 8.448   -30.220  1.00 34.33  ? 419  ARG   A CD  1 
ATOM   911   N  NE  . ARG   A  1 118 ? -39.558 8.076   -29.221  1.00 47.96  ? 419  ARG   A NE  1 
ATOM   912   C  CZ  . ARG   A  1 118 ? -40.275 6.957   -29.241  1.00 47.15  ? 419  ARG   A CZ  1 
ATOM   913   N  NH1 . ARG   A  1 118 ? -40.120 6.087   -30.231  1.00 34.29  ? 419  ARG   A NH1 1 
ATOM   914   N  NH2 . ARG   A  1 118 ? -41.159 6.728   -28.268  1.00 39.03  ? 419  ARG   A NH2 1 
ATOM   915   N  N   . CYS   A  1 119 ? -34.984 12.851  -32.078  1.00 39.09  ? 420  CYS   A N   1 
ATOM   916   C  CA  . CYS   A  1 119 ? -33.759 12.968  -32.866  1.00 38.78  ? 420  CYS   A CA  1 
ATOM   917   C  C   . CYS   A  1 119 ? -32.879 14.045  -32.257  1.00 36.90  ? 420  CYS   A C   1 
ATOM   918   O  O   . CYS   A  1 119 ? -33.293 15.206  -32.159  1.00 33.39  ? 420  CYS   A O   1 
ATOM   919   C  CB  . CYS   A  1 119 ? -34.054 13.288  -34.336  1.00 38.68  ? 420  CYS   A CB  1 
ATOM   920   S  SG  . CYS   A  1 119 ? -32.563 13.574  -35.371  1.00 39.83  ? 420  CYS   A SG  1 
ATOM   921   N  N   . VAL   A  1 120 ? -31.667 13.654  -31.859  1.00 37.38  ? 421  VAL   A N   1 
ATOM   922   C  CA  . VAL   A  1 120 ? -30.711 14.582  -31.264  1.00 43.68  ? 421  VAL   A CA  1 
ATOM   923   C  C   . VAL   A  1 120 ? -29.965 15.407  -32.298  1.00 45.52  ? 421  VAL   A C   1 
ATOM   924   O  O   . VAL   A  1 120 ? -29.203 16.307  -31.928  1.00 46.47  ? 421  VAL   A O   1 
ATOM   925   C  CB  . VAL   A  1 120 ? -29.722 13.775  -30.400  1.00 53.07  ? 421  VAL   A CB  1 
ATOM   926   C  CG1 . VAL   A  1 120 ? -28.652 13.171  -31.263  1.00 42.94  ? 421  VAL   A CG1 1 
ATOM   927   C  CG2 . VAL   A  1 120 ? -29.099 14.638  -29.292  1.00 58.68  ? 421  VAL   A CG2 1 
ATOM   928   N  N   . GLY   A  1 121 ? -30.160 15.141  -33.589  1.00 47.61  ? 422  GLY   A N   1 
ATOM   929   C  CA  . GLY   A  1 121 ? -29.390 15.787  -34.635  1.00 32.58  ? 422  GLY   A CA  1 
ATOM   930   C  C   . GLY   A  1 121 ? -30.065 16.946  -35.332  1.00 36.84  ? 422  GLY   A C   1 
ATOM   931   O  O   . GLY   A  1 121 ? -29.583 17.381  -36.385  1.00 43.59  ? 422  GLY   A O   1 
ATOM   932   N  N   . ARG   A  1 122 ? -31.161 17.467  -34.784  1.00 32.70  ? 423  ARG   A N   1 
ATOM   933   C  CA  . ARG   A  1 122 ? -32.006 18.424  -35.492  1.00 31.69  ? 423  ARG   A CA  1 
ATOM   934   C  C   . ARG   A  1 122 ? -31.379 19.798  -35.688  1.00 35.99  ? 423  ARG   A C   1 
ATOM   935   O  O   . ARG   A  1 122 ? -31.980 20.631  -36.373  1.00 39.88  ? 423  ARG   A O   1 
ATOM   936   C  CB  . ARG   A  1 122 ? -33.331 18.586  -34.752  1.00 31.91  ? 423  ARG   A CB  1 
ATOM   937   C  CG  . ARG   A  1 122 ? -34.183 17.331  -34.777  1.00 29.88  ? 423  ARG   A CG  1 
ATOM   938   C  CD  . ARG   A  1 122 ? -35.454 17.567  -33.978  1.00 37.69  ? 423  ARG   A CD  1 
ATOM   939   N  NE  . ARG   A  1 122 ? -35.346 17.156  -32.574  1.00 34.91  ? 423  ARG   A NE  1 
ATOM   940   C  CZ  . ARG   A  1 122 ? -36.265 17.450  -31.662  1.00 41.47  ? 423  ARG   A CZ  1 
ATOM   941   N  NH1 . ARG   A  1 122 ? -37.327 18.152  -32.040  1.00 38.22  ? 423  ARG   A NH1 1 
ATOM   942   N  NH2 . ARG   A  1 122 ? -36.131 17.055  -30.392  1.00 38.07  ? 423  ARG   A NH2 1 
ATOM   943   N  N   . ILE   A  1 123 ? -30.204 20.081  -35.133  1.00 32.74  ? 424  ILE   A N   1 
ATOM   944   C  CA  . ILE   A  1 123 ? -29.661 21.410  -35.392  1.00 41.76  ? 424  ILE   A CA  1 
ATOM   945   C  C   . ILE   A  1 123 ? -29.386 21.574  -36.880  1.00 47.62  ? 424  ILE   A C   1 
ATOM   946   O  O   . ILE   A  1 123 ? -29.426 22.690  -37.408  1.00 50.17  ? 424  ILE   A O   1 
ATOM   947   C  CB  . ILE   A  1 123 ? -28.406 21.682  -34.540  1.00 40.14  ? 424  ILE   A CB  1 
ATOM   948   C  CG1 . ILE   A  1 123 ? -27.891 23.097  -34.827  1.00 41.03  ? 424  ILE   A CG1 1 
ATOM   949   C  CG2 . ILE   A  1 123 ? -27.337 20.647  -34.814  1.00 45.17  ? 424  ILE   A CG2 1 
ATOM   950   C  CD1 . ILE   A  1 123 ? -26.901 23.614  -33.846  1.00 35.96  ? 424  ILE   A CD1 1 
ATOM   951   N  N   . GLN   A  1 124 ? -29.132 20.470  -37.579  1.00 48.17  ? 425  GLN   A N   1 
ATOM   952   C  CA  . GLN   A  1 124 ? -28.925 20.432  -39.025  1.00 58.17  ? 425  GLN   A CA  1 
ATOM   953   C  C   . GLN   A  1 124 ? -30.229 20.402  -39.828  1.00 55.23  ? 425  GLN   A C   1 
ATOM   954   O  O   . GLN   A  1 124 ? -30.165 20.190  -41.044  1.00 56.42  ? 425  GLN   A O   1 
ATOM   955   C  CB  . GLN   A  1 124 ? -28.104 19.193  -39.408  1.00 58.53  ? 425  GLN   A CB  1 
ATOM   956   C  CG  . GLN   A  1 124 ? -26.674 19.175  -38.941  1.00 57.77  ? 425  GLN   A CG  1 
ATOM   957   C  CD  . GLN   A  1 124 ? -25.773 20.030  -39.808  1.00 70.07  ? 425  GLN   A CD  1 
ATOM   958   O  OE1 . GLN   A  1 124 ? -26.179 21.080  -40.311  1.00 82.73  ? 425  GLN   A OE1 1 
ATOM   959   N  NE2 . GLN   A  1 124 ? -24.544 19.582  -39.995  1.00 70.79  ? 425  GLN   A NE2 1 
ATOM   960   N  N   . TRP   A  1 125 ? -31.389 20.604  -39.188  1.00 50.11  ? 426  TRP   A N   1 
ATOM   961   C  CA  . TRP   A  1 125 ? -32.654 20.202  -39.801  1.00 47.27  ? 426  TRP   A CA  1 
ATOM   962   C  C   . TRP   A  1 125 ? -32.906 20.927  -41.116  1.00 53.15  ? 426  TRP   A C   1 
ATOM   963   O  O   . TRP   A  1 125 ? -33.410 20.336  -42.075  1.00 50.98  ? 426  TRP   A O   1 
ATOM   964   C  CB  . TRP   A  1 125 ? -33.819 20.440  -38.843  1.00 48.16  ? 426  TRP   A CB  1 
ATOM   965   C  CG  . TRP   A  1 125 ? -34.256 21.871  -38.661  1.00 46.28  ? 426  TRP   A CG  1 
ATOM   966   C  CD1 . TRP   A  1 125 ? -33.885 22.720  -37.657  1.00 51.43  ? 426  TRP   A CD1 1 
ATOM   967   C  CD2 . TRP   A  1 125 ? -35.178 22.600  -39.480  1.00 46.67  ? 426  TRP   A CD2 1 
ATOM   968   N  NE1 . TRP   A  1 125 ? -34.499 23.943  -37.813  1.00 49.69  ? 426  TRP   A NE1 1 
ATOM   969   C  CE2 . TRP   A  1 125 ? -35.298 23.897  -38.926  1.00 47.83  ? 426  TRP   A CE2 1 
ATOM   970   C  CE3 . TRP   A  1 125 ? -35.907 22.288  -40.635  1.00 49.43  ? 426  TRP   A CE3 1 
ATOM   971   C  CZ2 . TRP   A  1 125 ? -36.116 24.880  -39.493  1.00 44.53  ? 426  TRP   A CZ2 1 
ATOM   972   C  CZ3 . TRP   A  1 125 ? -36.712 23.260  -41.193  1.00 46.24  ? 426  TRP   A CZ3 1 
ATOM   973   C  CH2 . TRP   A  1 125 ? -36.808 24.542  -40.626  1.00 45.33  ? 426  TRP   A CH2 1 
ATOM   974   N  N   . SER   A  1 126 ? -32.569 22.205  -41.185  1.00 42.10  ? 427  SER   A N   1 
ATOM   975   C  CA  . SER   A  1 126 ? -32.938 23.001  -42.338  1.00 44.51  ? 427  SER   A CA  1 
ATOM   976   C  C   . SER   A  1 126 ? -31.932 22.909  -43.473  1.00 55.82  ? 427  SER   A C   1 
ATOM   977   O  O   . SER   A  1 126 ? -32.070 23.641  -44.454  1.00 56.62  ? 427  SER   A O   1 
ATOM   978   C  CB  . SER   A  1 126 ? -33.124 24.462  -41.930  1.00 47.55  ? 427  SER   A CB  1 
ATOM   979   O  OG  . SER   A  1 126 ? -31.894 25.016  -41.488  1.00 63.91  ? 427  SER   A OG  1 
ATOM   980   N  N   . LYS   A  1 127 ? -30.904 22.074  -43.349  1.00 53.06  ? 428  LYS   A N   1 
ATOM   981   C  CA  . LYS   A  1 127 ? -30.059 21.716  -44.482  1.00 43.04  ? 428  LYS   A CA  1 
ATOM   982   C  C   . LYS   A  1 127 ? -30.319 20.252  -44.812  1.00 51.81  ? 428  LYS   A C   1 
ATOM   983   O  O   . LYS   A  1 127 ? -29.504 19.373  -44.545  1.00 63.47  ? 428  LYS   A O   1 
ATOM   984   C  CB  . LYS   A  1 127 ? -28.568 21.975  -44.179  1.00 44.28  ? 428  LYS   A CB  1 
ATOM   985   C  CG  . LYS   A  1 127 ? -28.177 23.458  -44.057  1.00 59.31  ? 428  LYS   A CG  1 
ATOM   986   C  CD  . LYS   A  1 127 ? -26.672 23.672  -44.288  1.00 76.10  ? 428  LYS   A CD  1 
ATOM   987   C  CE  . LYS   A  1 127 ? -26.305 23.632  -45.791  1.00 85.28  ? 428  LYS   A CE  1 
ATOM   988   N  NZ  . LYS   A  1 127 ? -25.411 22.489  -46.176  1.00 83.59  ? 428  LYS   A NZ  1 
ATOM   989   N  N   . LEU   A  1 128 ? -31.507 19.993  -45.348  1.00 49.32  ? 429  LEU   A N   1 
ATOM   990   C  CA  . LEU   A  1 128 ? -31.900 18.671  -45.806  1.00 33.99  ? 429  LEU   A CA  1 
ATOM   991   C  C   . LEU   A  1 128 ? -32.072 18.737  -47.311  1.00 41.63  ? 429  LEU   A C   1 
ATOM   992   O  O   . LEU   A  1 128 ? -32.486 19.766  -47.846  1.00 42.62  ? 429  LEU   A O   1 
ATOM   993   C  CB  . LEU   A  1 128 ? -33.194 18.216  -45.150  1.00 28.16  ? 429  LEU   A CB  1 
ATOM   994   C  CG  . LEU   A  1 128 ? -33.761 16.874  -45.603  1.00 34.65  ? 429  LEU   A CG  1 
ATOM   995   C  CD1 . LEU   A  1 128 ? -32.927 15.712  -45.076  1.00 36.27  ? 429  LEU   A CD1 1 
ATOM   996   C  CD2 . LEU   A  1 128 ? -35.189 16.736  -45.188  1.00 23.71  ? 429  LEU   A CD2 1 
ATOM   997   N  N   . GLN   A  1 129 ? -31.732 17.654  -47.996  1.00 47.28  ? 430  GLN   A N   1 
ATOM   998   C  CA  . GLN   A  1 129 ? -31.768 17.611  -49.453  1.00 43.18  ? 430  GLN   A CA  1 
ATOM   999   C  C   . GLN   A  1 129 ? -32.888 16.663  -49.860  1.00 41.04  ? 430  GLN   A C   1 
ATOM   1000  O  O   . GLN   A  1 129 ? -32.770 15.446  -49.680  1.00 38.33  ? 430  GLN   A O   1 
ATOM   1001  C  CB  . GLN   A  1 129 ? -30.412 17.176  -50.012  1.00 44.93  ? 430  GLN   A CB  1 
ATOM   1002  C  CG  . GLN   A  1 129 ? -30.294 17.290  -51.517  1.00 52.10  ? 430  GLN   A CG  1 
ATOM   1003  C  CD  . GLN   A  1 129 ? -30.697 18.665  -52.029  1.00 53.24  ? 430  GLN   A CD  1 
ATOM   1004  O  OE1 . GLN   A  1 129 ? -31.754 18.824  -52.639  1.00 54.59  ? 430  GLN   A OE1 1 
ATOM   1005  N  NE2 . GLN   A  1 129 ? -29.859 19.667  -51.774  1.00 42.82  ? 430  GLN   A NE2 1 
ATOM   1006  N  N   . VAL   A  1 130 ? -33.985 17.213  -50.386  1.00 41.09  ? 431  VAL   A N   1 
ATOM   1007  C  CA  . VAL   A  1 130 ? -35.186 16.427  -50.652  1.00 40.85  ? 431  VAL   A CA  1 
ATOM   1008  C  C   . VAL   A  1 130 ? -35.182 16.006  -52.113  1.00 46.72  ? 431  VAL   A C   1 
ATOM   1009  O  O   . VAL   A  1 130 ? -34.991 16.835  -53.008  1.00 53.80  ? 431  VAL   A O   1 
ATOM   1010  C  CB  . VAL   A  1 130 ? -36.463 17.207  -50.308  1.00 39.07  ? 431  VAL   A CB  1 
ATOM   1011  C  CG1 . VAL   A  1 130 ? -37.685 16.302  -50.497  1.00 28.85  ? 431  VAL   A CG1 1 
ATOM   1012  C  CG2 . VAL   A  1 130 ? -36.404 17.696  -48.878  1.00 39.51  ? 431  VAL   A CG2 1 
ATOM   1013  N  N   . PHE   A  1 131 ? -35.366 14.716  -52.349  1.00 41.75  ? 432  PHE   A N   1 
ATOM   1014  C  CA  . PHE   A  1 131 ? -35.427 14.137  -53.682  1.00 36.85  ? 432  PHE   A CA  1 
ATOM   1015  C  C   . PHE   A  1 131 ? -36.875 13.726  -53.925  1.00 34.86  ? 432  PHE   A C   1 
ATOM   1016  O  O   . PHE   A  1 131 ? -37.349 12.762  -53.320  1.00 50.04  ? 432  PHE   A O   1 
ATOM   1017  C  CB  . PHE   A  1 131 ? -34.475 12.942  -53.789  1.00 41.18  ? 432  PHE   A CB  1 
ATOM   1018  C  CG  . PHE   A  1 131 ? -33.020 13.320  -53.747  1.00 35.02  ? 432  PHE   A CG  1 
ATOM   1019  C  CD1 . PHE   A  1 131 ? -32.448 14.048  -54.779  1.00 36.39  ? 432  PHE   A CD1 1 
ATOM   1020  C  CD2 . PHE   A  1 131 ? -32.222 12.945  -52.692  1.00 31.26  ? 432  PHE   A CD2 1 
ATOM   1021  C  CE1 . PHE   A  1 131 ? -31.111 14.398  -54.750  1.00 30.05  ? 432  PHE   A CE1 1 
ATOM   1022  C  CE2 . PHE   A  1 131 ? -30.871 13.306  -52.650  1.00 31.49  ? 432  PHE   A CE2 1 
ATOM   1023  C  CZ  . PHE   A  1 131 ? -30.330 14.028  -53.674  1.00 33.40  ? 432  PHE   A CZ  1 
ATOM   1024  N  N   . ASP   A  1 132 ? -37.572 14.458  -54.799  1.00 34.81  ? 433  ASP   A N   1 
ATOM   1025  C  CA  . ASP   A  1 132 ? -38.951 14.146  -55.180  1.00 35.31  ? 433  ASP   A CA  1 
ATOM   1026  C  C   . ASP   A  1 132 ? -38.970 12.920  -56.071  1.00 42.74  ? 433  ASP   A C   1 
ATOM   1027  O  O   . ASP   A  1 132 ? -38.590 13.000  -57.239  1.00 39.88  ? 433  ASP   A O   1 
ATOM   1028  C  CB  . ASP   A  1 132 ? -39.577 15.311  -55.931  1.00 35.80  ? 433  ASP   A CB  1 
ATOM   1029  C  CG  . ASP   A  1 132 ? -41.084 15.200  -56.021  1.00 43.31  ? 433  ASP   A CG  1 
ATOM   1030  O  OD1 . ASP   A  1 132 ? -41.742 16.236  -56.280  1.00 47.18  ? 433  ASP   A OD1 1 
ATOM   1031  O  OD2 . ASP   A  1 132 ? -41.621 14.090  -55.822  1.00 35.24  ? 433  ASP   A OD2 1 
ATOM   1032  N  N   . ALA   A  1 133 ? -39.425 11.788  -55.550  1.00 43.22  ? 434  ALA   A N   1 
ATOM   1033  C  CA  . ALA   A  1 133 ? -39.559 10.590  -56.366  1.00 43.25  ? 434  ALA   A CA  1 
ATOM   1034  C  C   . ALA   A  1 133 ? -41.019 10.243  -56.616  1.00 38.69  ? 434  ALA   A C   1 
ATOM   1035  O  O   . ALA   A  1 133 ? -41.361 9.082   -56.883  1.00 30.24  ? 434  ALA   A O   1 
ATOM   1036  C  CB  . ALA   A  1 133 ? -38.833 9.419   -55.714  1.00 47.00  ? 434  ALA   A CB  1 
ATOM   1037  N  N   . ARG   A  1 134 ? -41.891 11.237  -56.548  1.00 33.49  ? 435  ARG   A N   1 
ATOM   1038  C  CA  . ARG   A  1 134 ? -43.302 10.937  -56.675  1.00 36.47  ? 435  ARG   A CA  1 
ATOM   1039  C  C   . ARG   A  1 134 ? -43.703 10.436  -58.058  1.00 38.23  ? 435  ARG   A C   1 
ATOM   1040  O  O   . ARG   A  1 134 ? -44.788 9.863   -58.186  1.00 48.65  ? 435  ARG   A O   1 
ATOM   1041  C  CB  . ARG   A  1 134 ? -44.086 12.168  -56.275  1.00 31.57  ? 435  ARG   A CB  1 
ATOM   1042  C  CG  . ARG   A  1 134 ? -44.170 12.280  -54.756  1.00 32.55  ? 435  ARG   A CG  1 
ATOM   1043  C  CD  . ARG   A  1 134 ? -44.900 13.523  -54.357  1.00 27.84  ? 435  ARG   A CD  1 
ATOM   1044  N  NE  . ARG   A  1 134 ? -44.189 14.682  -54.881  1.00 29.04  ? 435  ARG   A NE  1 
ATOM   1045  C  CZ  . ARG   A  1 134 ? -44.730 15.891  -54.919  1.00 36.47  ? 435  ARG   A CZ  1 
ATOM   1046  N  NH1 . ARG   A  1 134 ? -45.976 16.043  -54.468  1.00 33.07  ? 435  ARG   A NH1 1 
ATOM   1047  N  NH2 . ARG   A  1 134 ? -44.053 16.928  -55.407  1.00 34.32  ? 435  ARG   A NH2 1 
ATOM   1048  N  N   . ASP   A  1 135 ? -42.856 10.571  -59.080  1.00 48.64  ? 436  ASP   A N   1 
ATOM   1049  C  CA  . ASP   A  1 135 ? -43.216 10.080  -60.410  1.00 50.78  ? 436  ASP   A CA  1 
ATOM   1050  C  C   . ASP   A  1 135 ? -42.889 8.605   -60.602  1.00 49.92  ? 436  ASP   A C   1 
ATOM   1051  O  O   . ASP   A  1 135 ? -43.127 8.068   -61.692  1.00 49.71  ? 436  ASP   A O   1 
ATOM   1052  C  CB  . ASP   A  1 135 ? -42.524 10.916  -61.501  1.00 50.38  ? 436  ASP   A CB  1 
ATOM   1053  C  CG  . ASP   A  1 135 ? -41.012 10.942  -61.357  1.00 50.25  ? 436  ASP   A CG  1 
ATOM   1054  O  OD1 . ASP   A  1 135 ? -40.326 11.382  -62.306  1.00 39.11  ? 436  ASP   A OD1 1 
ATOM   1055  O  OD2 . ASP   A  1 135 ? -40.512 10.535  -60.289  1.00 50.87  ? 436  ASP   A OD2 1 
ATOM   1056  N  N   . CYS   A  1 136 ? -42.376 7.943   -59.563  1.00 47.48  ? 437  CYS   A N   1 
ATOM   1057  C  CA  . CYS   A  1 136 ? -41.924 6.561   -59.670  1.00 38.62  ? 437  CYS   A CA  1 
ATOM   1058  C  C   . CYS   A  1 136 ? -43.126 5.622   -59.758  1.00 49.02  ? 437  CYS   A C   1 
ATOM   1059  O  O   . CYS   A  1 136 ? -44.172 5.876   -59.155  1.00 52.55  ? 437  CYS   A O   1 
ATOM   1060  C  CB  . CYS   A  1 136 ? -41.026 6.233   -58.467  1.00 30.48  ? 437  CYS   A CB  1 
ATOM   1061  S  SG  . CYS   A  1 136 ? -40.108 4.658   -58.435  1.00 42.30  ? 437  CYS   A SG  1 
ATOM   1062  N  N   . THR   A  1 137 ? -42.998 4.556   -60.564  1.00 45.09  ? 438  THR   A N   1 
ATOM   1063  C  CA  . THR   A  1 137 ? -44.088 3.595   -60.736  1.00 41.74  ? 438  THR   A CA  1 
ATOM   1064  C  C   . THR   A  1 137 ? -43.685 2.146   -60.490  1.00 36.79  ? 438  THR   A C   1 
ATOM   1065  O  O   . THR   A  1 137 ? -44.572 1.314   -60.267  1.00 41.35  ? 438  THR   A O   1 
ATOM   1066  C  CB  . THR   A  1 137 ? -44.734 3.712   -62.150  1.00 47.15  ? 438  THR   A CB  1 
ATOM   1067  O  OG1 . THR   A  1 137 ? -43.873 3.206   -63.193  1.00 34.50  ? 438  THR   A OG1 1 
ATOM   1068  C  CG2 . THR   A  1 137 ? -45.119 5.165   -62.481  1.00 41.81  ? 438  THR   A CG2 1 
ATOM   1069  N  N   . THR   A  1 138 ? -42.398 1.814   -60.493  1.00 34.91  ? 439  THR   A N   1 
ATOM   1070  C  CA  . THR   A  1 138 ? -41.966 0.426   -60.401  1.00 40.41  ? 439  THR   A CA  1 
ATOM   1071  C  C   . THR   A  1 138 ? -40.866 0.249   -59.359  1.00 39.86  ? 439  THR   A C   1 
ATOM   1072  O  O   . THR   A  1 138 ? -40.175 1.202   -58.967  1.00 41.92  ? 439  THR   A O   1 
ATOM   1073  C  CB  . THR   A  1 138 ? -41.433 -0.063  -61.745  1.00 43.11  ? 439  THR   A CB  1 
ATOM   1074  O  OG1 . THR   A  1 138 ? -40.420 0.850   -62.186  1.00 50.36  ? 439  THR   A OG1 1 
ATOM   1075  C  CG2 . THR   A  1 138 ? -42.546 -0.119  -62.780  1.00 46.18  ? 439  THR   A CG2 1 
ATOM   1076  N  N   . ALA   A  1 139 ? -40.676 -1.006  -58.945  1.00 41.61  ? 440  ALA   A N   1 
ATOM   1077  C  CA  . ALA   A  1 139 ? -39.545 -1.317  -58.072  1.00 44.78  ? 440  ALA   A CA  1 
ATOM   1078  C  C   . ALA   A  1 139 ? -38.225 -0.900  -58.712  1.00 50.51  ? 440  ALA   A C   1 
ATOM   1079  O  O   . ALA   A  1 139 ? -37.346 -0.343  -58.041  1.00 54.42  ? 440  ALA   A O   1 
ATOM   1080  C  CB  . ALA   A  1 139 ? -39.519 -2.808  -57.734  1.00 42.87  ? 440  ALA   A CB  1 
ATOM   1081  N  N   . HIS   A  1 140 ? -38.068 -1.162  -60.013  1.00 53.22  ? 441  HIS   A N   1 
ATOM   1082  C  CA  . HIS   A  1 140 ? -36.833 -0.789  -60.694  1.00 41.93  ? 441  HIS   A CA  1 
ATOM   1083  C  C   . HIS   A  1 140 ? -36.580 0.706   -60.575  1.00 41.23  ? 441  HIS   A C   1 
ATOM   1084  O  O   . HIS   A  1 140 ? -35.446 1.132   -60.324  1.00 45.64  ? 441  HIS   A O   1 
ATOM   1085  C  CB  . HIS   A  1 140 ? -36.881 -1.235  -62.166  1.00 44.80  ? 441  HIS   A CB  1 
ATOM   1086  C  CG  . HIS   A  1 140 ? -36.377 -2.629  -62.381  1.00 37.84  ? 441  HIS   A CG  1 
ATOM   1087  N  ND1 . HIS   A  1 140 ? -37.180 -3.741  -62.232  1.00 38.50  ? 441  HIS   A ND1 1 
ATOM   1088  C  CD2 . HIS   A  1 140 ? -35.135 -3.094  -62.657  1.00 37.93  ? 441  HIS   A CD2 1 
ATOM   1089  C  CE1 . HIS   A  1 140 ? -36.459 -4.832  -62.439  1.00 41.83  ? 441  HIS   A CE1 1 
ATOM   1090  N  NE2 . HIS   A  1 140 ? -35.214 -4.467  -62.692  1.00 37.53  ? 441  HIS   A NE2 1 
ATOM   1091  N  N   . GLY   A  1 141 ? -37.629 1.518   -60.718  1.00 45.22  ? 442  GLY   A N   1 
ATOM   1092  C  CA  . GLY   A  1 141 ? -37.469 2.948   -60.542  1.00 48.87  ? 442  GLY   A CA  1 
ATOM   1093  C  C   . GLY   A  1 141 ? -37.071 3.311   -59.124  1.00 52.75  ? 442  GLY   A C   1 
ATOM   1094  O  O   . GLY   A  1 141 ? -36.245 4.206   -58.910  1.00 45.21  ? 442  GLY   A O   1 
ATOM   1095  N  N   . MET   A  1 142 ? -37.642 2.611   -58.137  1.00 55.02  ? 443  MET   A N   1 
ATOM   1096  C  CA  . MET   A  1 142 ? -37.260 2.842   -56.746  1.00 45.40  ? 443  MET   A CA  1 
ATOM   1097  C  C   . MET   A  1 142 ? -35.777 2.546   -56.527  1.00 46.08  ? 443  MET   A C   1 
ATOM   1098  O  O   . MET   A  1 142 ? -35.031 3.395   -56.017  1.00 38.79  ? 443  MET   A O   1 
ATOM   1099  C  CB  . MET   A  1 142 ? -38.124 1.992   -55.815  1.00 47.77  ? 443  MET   A CB  1 
ATOM   1100  C  CG  . MET   A  1 142 ? -39.493 2.582   -55.475  1.00 36.66  ? 443  MET   A CG  1 
ATOM   1101  S  SD  . MET   A  1 142 ? -40.618 1.306   -54.825  1.00 41.90  ? 443  MET   A SD  1 
ATOM   1102  C  CE  . MET   A  1 142 ? -40.222 1.378   -53.038  1.00 27.99  ? 443  MET   A CE  1 
ATOM   1103  N  N   . PHE   A  1 143 ? -35.322 1.355   -56.938  1.00 37.59  ? 444  PHE   A N   1 
ATOM   1104  C  CA  . PHE   A  1 143 ? -33.903 1.026   -56.816  1.00 34.62  ? 444  PHE   A CA  1 
ATOM   1105  C  C   . PHE   A  1 143 ? -33.006 2.112   -57.420  1.00 46.62  ? 444  PHE   A C   1 
ATOM   1106  O  O   . PHE   A  1 143 ? -31.950 2.435   -56.869  1.00 57.28  ? 444  PHE   A O   1 
ATOM   1107  C  CB  . PHE   A  1 143 ? -33.631 -0.333  -57.463  1.00 35.18  ? 444  PHE   A CB  1 
ATOM   1108  C  CG  . PHE   A  1 143 ? -32.178 -0.642  -57.621  1.00 43.61  ? 444  PHE   A CG  1 
ATOM   1109  C  CD1 . PHE   A  1 143 ? -31.568 -0.574  -58.865  1.00 56.65  ? 444  PHE   A CD1 1 
ATOM   1110  C  CD2 . PHE   A  1 143 ? -31.416 -0.997  -56.535  1.00 30.76  ? 444  PHE   A CD2 1 
ATOM   1111  C  CE1 . PHE   A  1 143 ? -30.216 -0.861  -59.009  1.00 57.03  ? 444  PHE   A CE1 1 
ATOM   1112  C  CE2 . PHE   A  1 143 ? -30.068 -1.277  -56.673  1.00 41.08  ? 444  PHE   A CE2 1 
ATOM   1113  C  CZ  . PHE   A  1 143 ? -29.467 -1.207  -57.906  1.00 51.97  ? 444  PHE   A CZ  1 
ATOM   1114  N  N   . ASN   A  1 144 ? -33.417 2.705   -58.539  1.00 45.66  ? 445  ASN   A N   1 
ATOM   1115  C  CA  . ASN   A  1 144 ? -32.616 3.761   -59.153  1.00 36.81  ? 445  ASN   A CA  1 
ATOM   1116  C  C   . ASN   A  1 144 ? -32.556 5.000   -58.262  1.00 35.83  ? 445  ASN   A C   1 
ATOM   1117  O  O   . ASN   A  1 144 ? -31.469 5.469   -57.909  1.00 48.43  ? 445  ASN   A O   1 
ATOM   1118  C  CB  . ASN   A  1 144 ? -33.186 4.100   -60.538  1.00 40.79  ? 445  ASN   A CB  1 
ATOM   1119  C  CG  . ASN   A  1 144 ? -32.294 5.050   -61.325  1.00 49.92  ? 445  ASN   A CG  1 
ATOM   1120  O  OD1 . ASN   A  1 144 ? -32.665 6.191   -61.617  1.00 56.27  ? 445  ASN   A OD1 1 
ATOM   1121  N  ND2 . ASN   A  1 144 ? -31.115 4.576   -61.675  1.00 50.04  ? 445  ASN   A ND2 1 
ATOM   1122  N  N   . TYR   A  1 145 ? -33.725 5.558   -57.911  1.00 40.86  ? 446  TYR   A N   1 
ATOM   1123  C  CA  . TYR   A  1 145 ? -33.815 6.676   -56.967  1.00 48.47  ? 446  TYR   A CA  1 
ATOM   1124  C  C   . TYR   A  1 145 ? -33.017 6.423   -55.683  1.00 44.66  ? 446  TYR   A C   1 
ATOM   1125  O  O   . TYR   A  1 145 ? -32.385 7.338   -55.133  1.00 27.25  ? 446  TYR   A O   1 
ATOM   1126  C  CB  . TYR   A  1 145 ? -35.287 6.938   -56.603  1.00 50.33  ? 446  TYR   A CB  1 
ATOM   1127  C  CG  . TYR   A  1 145 ? -36.027 7.935   -57.485  1.00 40.88  ? 446  TYR   A CG  1 
ATOM   1128  C  CD1 . TYR   A  1 145 ? -37.031 7.518   -58.367  1.00 28.27  ? 446  TYR   A CD1 1 
ATOM   1129  C  CD2 . TYR   A  1 145 ? -35.725 9.297   -57.428  1.00 31.96  ? 446  TYR   A CD2 1 
ATOM   1130  C  CE1 . TYR   A  1 145 ? -37.706 8.425   -59.148  1.00 26.69  ? 446  TYR   A CE1 1 
ATOM   1131  C  CE2 . TYR   A  1 145 ? -36.399 10.208  -58.215  1.00 38.42  ? 446  TYR   A CE2 1 
ATOM   1132  C  CZ  . TYR   A  1 145 ? -37.379 9.770   -59.074  1.00 41.00  ? 446  TYR   A CZ  1 
ATOM   1133  O  OH  . TYR   A  1 145 ? -38.032 10.687  -59.857  1.00 46.33  ? 446  TYR   A OH  1 
ATOM   1134  N  N   . ILE   A  1 146 ? -33.056 5.197   -55.173  1.00 46.41  ? 447  ILE   A N   1 
ATOM   1135  C  CA  . ILE   A  1 146 ? -32.397 4.928   -53.904  1.00 45.44  ? 447  ILE   A CA  1 
ATOM   1136  C  C   . ILE   A  1 146 ? -30.880 4.947   -54.075  1.00 48.59  ? 447  ILE   A C   1 
ATOM   1137  O  O   . ILE   A  1 146 ? -30.156 5.472   -53.217  1.00 39.80  ? 447  ILE   A O   1 
ATOM   1138  C  CB  . ILE   A  1 146 ? -32.913 3.601   -53.311  1.00 40.59  ? 447  ILE   A CB  1 
ATOM   1139  C  CG1 . ILE   A  1 146 ? -34.344 3.791   -52.792  1.00 40.04  ? 447  ILE   A CG1 1 
ATOM   1140  C  CG2 . ILE   A  1 146 ? -31.980 3.084   -52.243  1.00 36.62  ? 447  ILE   A CG2 1 
ATOM   1141  C  CD1 . ILE   A  1 146 ? -34.929 2.589   -52.076  1.00 43.98  ? 447  ILE   A CD1 1 
ATOM   1142  N  N   . CYS   A  1 147 ? -30.376 4.416   -55.200  1.00 49.83  ? 448  CYS   A N   1 
ATOM   1143  C  CA  . CYS   A  1 147 ? -28.934 4.455   -55.461  1.00 47.61  ? 448  CYS   A CA  1 
ATOM   1144  C  C   . CYS   A  1 147 ? -28.426 5.893   -55.565  1.00 48.62  ? 448  CYS   A C   1 
ATOM   1145  O  O   . CYS   A  1 147 ? -27.362 6.237   -55.026  1.00 46.24  ? 448  CYS   A O   1 
ATOM   1146  C  CB  . CYS   A  1 147 ? -28.598 3.692   -56.747  1.00 42.46  ? 448  CYS   A CB  1 
ATOM   1147  S  SG  . CYS   A  1 147 ? -28.623 1.893   -56.636  1.00 46.25  ? 448  CYS   A SG  1 
ATOM   1148  N  N   . ASN   A  1 148 ? -29.165 6.748   -56.272  1.00 39.53  ? 449  ASN   A N   1 
ATOM   1149  C  CA  . ASN   A  1 148 ? -28.728 8.129   -56.388  1.00 37.97  ? 449  ASN   A CA  1 
ATOM   1150  C  C   . ASN   A  1 148 ? -28.769 8.823   -55.028  1.00 41.01  ? 449  ASN   A C   1 
ATOM   1151  O  O   . ASN   A  1 148 ? -27.941 9.697   -54.751  1.00 41.15  ? 449  ASN   A O   1 
ATOM   1152  C  CB  . ASN   A  1 148 ? -29.591 8.846   -57.435  1.00 38.65  ? 449  ASN   A CB  1 
ATOM   1153  C  CG  . ASN   A  1 148 ? -29.454 8.232   -58.852  1.00 48.39  ? 449  ASN   A CG  1 
ATOM   1154  O  OD1 . ASN   A  1 148 ? -28.449 7.574   -59.182  1.00 43.26  ? 449  ASN   A OD1 1 
ATOM   1155  N  ND2 . ASN   A  1 148 ? -30.464 8.462   -59.691  1.00 43.81  ? 449  ASN   A ND2 1 
ATOM   1156  N  N   . HIS   A  1 149 ? -29.710 8.428   -54.165  1.00 41.17  ? 450  HIS   A N   1 
ATOM   1157  C  CA  . HIS   A  1 149 ? -29.737 8.916   -52.788  1.00 37.97  ? 450  HIS   A CA  1 
ATOM   1158  C  C   . HIS   A  1 149 ? -28.470 8.497   -52.044  1.00 41.99  ? 450  HIS   A C   1 
ATOM   1159  O  O   . HIS   A  1 149 ? -27.715 9.341   -51.543  1.00 41.60  ? 450  HIS   A O   1 
ATOM   1160  C  CB  . HIS   A  1 149 ? -31.000 8.394   -52.087  1.00 34.03  ? 450  HIS   A CB  1 
ATOM   1161  C  CG  . HIS   A  1 149 ? -31.166 8.870   -50.666  1.00 40.07  ? 450  HIS   A CG  1 
ATOM   1162  N  ND1 . HIS   A  1 149 ? -32.400 9.126   -50.109  1.00 36.96  ? 450  HIS   A ND1 1 
ATOM   1163  C  CD2 . HIS   A  1 149 ? -30.257 9.131   -49.692  1.00 43.77  ? 450  HIS   A CD2 1 
ATOM   1164  C  CE1 . HIS   A  1 149 ? -32.243 9.546   -48.865  1.00 44.44  ? 450  HIS   A CE1 1 
ATOM   1165  N  NE2 . HIS   A  1 149 ? -30.951 9.560   -48.588  1.00 35.98  ? 450  HIS   A NE2 1 
ATOM   1166  N  N   . VAL   A  1 150 ? -28.224 7.183   -51.972  1.00 30.65  ? 451  VAL   A N   1 
ATOM   1167  C  CA  . VAL   A  1 150 ? -27.019 6.649   -51.344  1.00 31.09  ? 451  VAL   A CA  1 
ATOM   1168  C  C   . VAL   A  1 150 ? -25.768 7.363   -51.849  1.00 39.44  ? 451  VAL   A C   1 
ATOM   1169  O  O   . VAL   A  1 150 ? -24.927 7.815   -51.064  1.00 51.83  ? 451  VAL   A O   1 
ATOM   1170  C  CB  . VAL   A  1 150 ? -26.934 5.132   -51.587  1.00 28.24  ? 451  VAL   A CB  1 
ATOM   1171  C  CG1 . VAL   A  1 150 ? -25.588 4.609   -51.142  1.00 24.53  ? 451  VAL   A CG1 1 
ATOM   1172  C  CG2 . VAL   A  1 150 ? -28.025 4.439   -50.828  1.00 26.31  ? 451  VAL   A CG2 1 
ATOM   1173  N  N   . LYS   A  1 151 ? -25.625 7.468   -53.171  1.00 49.00  ? 452  LYS   A N   1 
ATOM   1174  C  CA  . LYS   A  1 151 ? -24.409 8.038   -53.745  1.00 44.58  ? 452  LYS   A CA  1 
ATOM   1175  C  C   . LYS   A  1 151 ? -24.248 9.497   -53.354  1.00 36.58  ? 452  LYS   A C   1 
ATOM   1176  O  O   . LYS   A  1 151 ? -23.145 9.944   -53.032  1.00 40.26  ? 452  LYS   A O   1 
ATOM   1177  C  CB  . LYS   A  1 151 ? -24.437 7.890   -55.269  1.00 40.13  ? 452  LYS   A CB  1 
ATOM   1178  C  CG  . LYS   A  1 151 ? -23.156 8.320   -56.002  1.00 40.44  ? 452  LYS   A CG  1 
ATOM   1179  C  CD  . LYS   A  1 151 ? -23.109 7.644   -57.394  1.00 36.72  ? 452  LYS   A CD  1 
ATOM   1180  C  CE  . LYS   A  1 151 ? -21.825 7.905   -58.159  1.00 41.10  ? 452  LYS   A CE  1 
ATOM   1181  N  NZ  . LYS   A  1 151 ? -21.611 6.839   -59.188  1.00 49.40  ? 452  LYS   A NZ  1 
ATOM   1182  N  N   . TYR   A  1 152 ? -25.340 10.253  -53.368  1.00 38.09  ? 453  TYR   A N   1 
ATOM   1183  C  CA  . TYR   A  1 152 ? -25.269 11.661  -52.996  1.00 43.62  ? 453  TYR   A CA  1 
ATOM   1184  C  C   . TYR   A  1 152 ? -24.982 11.829  -51.506  1.00 45.36  ? 453  TYR   A C   1 
ATOM   1185  O  O   . TYR   A  1 152 ? -24.086 12.590  -51.115  1.00 43.63  ? 453  TYR   A O   1 
ATOM   1186  C  CB  . TYR   A  1 152 ? -26.577 12.347  -53.365  1.00 47.61  ? 453  TYR   A CB  1 
ATOM   1187  C  CG  . TYR   A  1 152 ? -26.691 13.739  -52.808  1.00 49.68  ? 453  TYR   A CG  1 
ATOM   1188  C  CD1 . TYR   A  1 152 ? -26.164 14.815  -53.498  1.00 48.42  ? 453  TYR   A CD1 1 
ATOM   1189  C  CD2 . TYR   A  1 152 ? -27.335 13.980  -51.602  1.00 38.70  ? 453  TYR   A CD2 1 
ATOM   1190  C  CE1 . TYR   A  1 152 ? -26.260 16.082  -53.007  1.00 54.30  ? 453  TYR   A CE1 1 
ATOM   1191  C  CE2 . TYR   A  1 152 ? -27.438 15.257  -51.107  1.00 44.54  ? 453  TYR   A CE2 1 
ATOM   1192  C  CZ  . TYR   A  1 152 ? -26.893 16.305  -51.814  1.00 48.26  ? 453  TYR   A CZ  1 
ATOM   1193  O  OH  . TYR   A  1 152 ? -26.975 17.595  -51.348  1.00 56.99  ? 453  TYR   A OH  1 
ATOM   1194  N  N   . ALA   A  1 153 ? -25.746 11.123  -50.665  1.00 43.59  ? 454  ALA   A N   1 
ATOM   1195  C  CA  . ALA   A  1 153 ? -25.591 11.213  -49.211  1.00 42.31  ? 454  ALA   A CA  1 
ATOM   1196  C  C   . ALA   A  1 153 ? -24.194 10.801  -48.761  1.00 41.24  ? 454  ALA   A C   1 
ATOM   1197  O  O   . ALA   A  1 153 ? -23.581 11.482  -47.937  1.00 39.56  ? 454  ALA   A O   1 
ATOM   1198  C  CB  . ALA   A  1 153 ? -26.640 10.340  -48.539  1.00 27.18  ? 454  ALA   A CB  1 
ATOM   1199  N  N   . THR   A  1 154 ? -23.669 9.698   -49.301  1.00 43.66  ? 455  THR   A N   1 
ATOM   1200  C  CA  . THR   A  1 154 ? -22.346 9.238   -48.899  1.00 40.96  ? 455  THR   A CA  1 
ATOM   1201  C  C   . THR   A  1 154 ? -21.260 10.239  -49.293  1.00 56.18  ? 455  THR   A C   1 
ATOM   1202  O  O   . THR   A  1 154 ? -20.333 10.486  -48.511  1.00 70.28  ? 455  THR   A O   1 
ATOM   1203  C  CB  . THR   A  1 154 ? -22.063 7.866   -49.503  1.00 32.28  ? 455  THR   A CB  1 
ATOM   1204  O  OG1 . THR   A  1 154 ? -23.052 6.929   -49.058  1.00 32.12  ? 455  THR   A OG1 1 
ATOM   1205  C  CG2 . THR   A  1 154 ? -20.705 7.374   -49.063  1.00 31.37  ? 455  THR   A CG2 1 
ATOM   1206  N  N   . ASN   A  1 155 ? -21.360 10.827  -50.501  1.00 47.17  ? 456  ASN   A N   1 
ATOM   1207  C  CA  . ASN   A  1 155 ? -20.464 11.881  -50.995  1.00 31.02  ? 456  ASN   A CA  1 
ATOM   1208  C  C   . ASN   A  1 155 ? -19.000 11.611  -50.647  1.00 42.99  ? 456  ASN   A C   1 
ATOM   1209  O  O   . ASN   A  1 155 ? -18.267 12.521  -50.245  1.00 41.87  ? 456  ASN   A O   1 
ATOM   1210  C  CB  . ASN   A  1 155 ? -20.913 13.242  -50.451  1.00 28.83  ? 456  ASN   A CB  1 
ATOM   1211  C  CG  . ASN   A  1 155 ? -20.076 14.397  -50.953  1.00 36.90  ? 456  ASN   A CG  1 
ATOM   1212  O  OD1 . ASN   A  1 155 ? -19.493 14.342  -52.028  1.00 49.05  ? 456  ASN   A OD1 1 
ATOM   1213  N  ND2 . ASN   A  1 155 ? -20.013 15.456  -50.173  1.00 36.26  ? 456  ASN   A ND2 1 
ATOM   1214  N  N   . LYS   A  1 156 ? -18.565 10.357  -50.804  1.00 48.90  ? 457  LYS   A N   1 
ATOM   1215  C  CA  . LYS   A  1 156 ? -17.166 9.955   -50.625  1.00 45.44  ? 457  LYS   A CA  1 
ATOM   1216  C  C   . LYS   A  1 156 ? -16.679 10.117  -49.187  1.00 48.74  ? 457  LYS   A C   1 
ATOM   1217  O  O   . LYS   A  1 156 ? -15.489 10.351  -48.948  1.00 39.90  ? 457  LYS   A O   1 
ATOM   1218  C  CB  . LYS   A  1 156 ? -16.233 10.714  -51.567  1.00 52.05  ? 457  LYS   A CB  1 
ATOM   1219  C  CG  . LYS   A  1 156 ? -16.316 10.314  -53.007  1.00 52.86  ? 457  LYS   A CG  1 
ATOM   1220  C  CD  . LYS   A  1 156 ? -15.415 11.214  -53.811  1.00 65.06  ? 457  LYS   A CD  1 
ATOM   1221  C  CE  . LYS   A  1 156 ? -15.653 11.054  -55.301  1.00 68.63  ? 457  LYS   A CE  1 
ATOM   1222  N  NZ  . LYS   A  1 156 ? -14.466 10.426  -55.940  1.00 70.05  ? 457  LYS   A NZ  1 
ATOM   1223  N  N   . GLY   A  1 157 ? -17.573 9.956   -48.217  1.00 50.58  ? 458  GLY   A N   1 
ATOM   1224  C  CA  . GLY   A  1 157 ? -17.231 10.038  -46.826  1.00 53.31  ? 458  GLY   A CA  1 
ATOM   1225  C  C   . GLY   A  1 157 ? -17.687 11.312  -46.158  1.00 54.76  ? 458  GLY   A C   1 
ATOM   1226  O  O   . GLY   A  1 157 ? -17.894 11.319  -44.940  1.00 50.57  ? 458  GLY   A O   1 
ATOM   1227  N  N   . ASN   A  1 158 ? -17.853 12.390  -46.922  1.00 47.33  ? 459  ASN   A N   1 
ATOM   1228  C  CA  . ASN   A  1 158 ? -18.295 13.659  -46.353  1.00 47.48  ? 459  ASN   A CA  1 
ATOM   1229  C  C   . ASN   A  1 158 ? -19.819 13.726  -46.411  1.00 51.00  ? 459  ASN   A C   1 
ATOM   1230  O  O   . ASN   A  1 158 ? -20.399 14.430  -47.235  1.00 58.20  ? 459  ASN   A O   1 
ATOM   1231  C  CB  . ASN   A  1 158 ? -17.654 14.816  -47.099  1.00 39.39  ? 459  ASN   A CB  1 
ATOM   1232  C  CG  . ASN   A  1 158 ? -18.104 16.148  -46.570  1.00 51.70  ? 459  ASN   A CG  1 
ATOM   1233  O  OD1 . ASN   A  1 158 ? -18.533 16.259  -45.423  1.00 64.45  ? 459  ASN   A OD1 1 
ATOM   1234  N  ND2 . ASN   A  1 158 ? -18.034 17.167  -47.403  1.00 51.27  ? 459  ASN   A ND2 1 
ATOM   1235  N  N   . LEU   A  1 159 ? -20.473 13.019  -45.481  1.00 47.80  ? 460  LEU   A N   1 
ATOM   1236  C  CA  . LEU   A  1 159 ? -21.896 12.711  -45.621  1.00 46.10  ? 460  LEU   A CA  1 
ATOM   1237  C  C   . LEU   A  1 159 ? -22.785 13.948  -45.621  1.00 46.19  ? 460  LEU   A C   1 
ATOM   1238  O  O   . LEU   A  1 159 ? -22.542 14.914  -44.895  1.00 38.61  ? 460  LEU   A O   1 
ATOM   1239  C  CB  . LEU   A  1 159 ? -22.387 11.802  -44.504  1.00 39.14  ? 460  LEU   A CB  1 
ATOM   1240  C  CG  . LEU   A  1 159 ? -21.636 10.540  -44.120  1.00 51.21  ? 460  LEU   A CG  1 
ATOM   1241  C  CD1 . LEU   A  1 159 ? -22.594 9.633   -43.361  1.00 56.97  ? 460  LEU   A CD1 1 
ATOM   1242  C  CD2 . LEU   A  1 159 ? -21.039 9.840   -45.309  1.00 37.47  ? 460  LEU   A CD2 1 
ATOM   1243  N  N   . ARG   A  1 160 ? -23.852 13.880  -46.417  1.00 45.95  ? 461  ARG   A N   1 
ATOM   1244  C  CA  . ARG   A  1 160 ? -24.902 14.885  -46.454  1.00 44.75  ? 461  ARG   A CA  1 
ATOM   1245  C  C   . ARG   A  1 160 ? -26.240 14.258  -46.082  1.00 45.57  ? 461  ARG   A C   1 
ATOM   1246  O  O   . ARG   A  1 160 ? -26.491 13.071  -46.323  1.00 45.55  ? 461  ARG   A O   1 
ATOM   1247  C  CB  . ARG   A  1 160 ? -24.986 15.517  -47.831  1.00 41.45  ? 461  ARG   A CB  1 
ATOM   1248  C  CG  . ARG   A  1 160 ? -23.674 16.104  -48.269  1.00 41.44  ? 461  ARG   A CG  1 
ATOM   1249  C  CD  . ARG   A  1 160 ? -23.743 16.652  -49.673  1.00 55.20  ? 461  ARG   A CD  1 
ATOM   1250  N  NE  . ARG   A  1 160 ? -23.512 15.614  -50.666  1.00 56.12  ? 461  ARG   A NE  1 
ATOM   1251  C  CZ  . ARG   A  1 160 ? -23.167 15.874  -51.908  1.00 46.56  ? 461  ARG   A CZ  1 
ATOM   1252  N  NH1 . ARG   A  1 160 ? -23.030 17.134  -52.281  1.00 43.09  ? 461  ARG   A NH1 1 
ATOM   1253  N  NH2 . ARG   A  1 160 ? -22.973 14.890  -52.762  1.00 51.79  ? 461  ARG   A NH2 1 
ATOM   1254  N  N   . SER   A  1 161 ? -27.101 15.048  -45.470  1.00 47.24  ? 462  SER   A N   1 
ATOM   1255  C  CA  . SER   A  1 161 ? -28.395 14.502  -45.114  1.00 48.57  ? 462  SER   A CA  1 
ATOM   1256  C  C   . SER   A  1 161 ? -29.345 14.688  -46.287  1.00 37.81  ? 462  SER   A C   1 
ATOM   1257  O  O   . SER   A  1 161 ? -29.218 15.638  -47.070  1.00 31.03  ? 462  SER   A O   1 
ATOM   1258  C  CB  . SER   A  1 161 ? -28.948 15.136  -43.833  1.00 53.40  ? 462  SER   A CB  1 
ATOM   1259  O  OG  . SER   A  1 161 ? -28.899 16.548  -43.868  1.00 69.47  ? 462  SER   A OG  1 
ATOM   1260  N  N   . ALA   A  1 162 ? -30.296 13.762  -46.404  1.00 27.93  ? 463  ALA   A N   1 
ATOM   1261  C  CA  . ALA   A  1 162 ? -31.078 13.625  -47.619  1.00 37.72  ? 463  ALA   A CA  1 
ATOM   1262  C  C   . ALA   A  1 162 ? -32.261 12.706  -47.365  1.00 42.40  ? 463  ALA   A C   1 
ATOM   1263  O  O   . ALA   A  1 162 ? -32.183 11.774  -46.558  1.00 43.05  ? 463  ALA   A O   1 
ATOM   1264  C  CB  . ALA   A  1 162 ? -30.225 13.065  -48.769  1.00 31.38  ? 463  ALA   A CB  1 
ATOM   1265  N  N   . ILE   A  1 163 ? -33.349 12.979  -48.083  1.00 45.09  ? 464  ILE   A N   1 
ATOM   1266  C  CA  . ILE   A  1 163 ? -34.569 12.182  -48.057  1.00 38.63  ? 464  ILE   A CA  1 
ATOM   1267  C  C   . ILE   A  1 163 ? -35.063 12.023  -49.497  1.00 41.89  ? 464  ILE   A C   1 
ATOM   1268  O  O   . ILE   A  1 163 ? -34.974 12.953  -50.310  1.00 40.07  ? 464  ILE   A O   1 
ATOM   1269  C  CB  . ILE   A  1 163 ? -35.647 12.826  -47.148  1.00 25.57  ? 464  ILE   A CB  1 
ATOM   1270  C  CG1 . ILE   A  1 163 ? -36.847 11.894  -46.958  1.00 23.19  ? 464  ILE   A CG1 1 
ATOM   1271  C  CG2 . ILE   A  1 163 ? -36.093 14.194  -47.672  1.00 25.38  ? 464  ILE   A CG2 1 
ATOM   1272  C  CD1 . ILE   A  1 163 ? -37.932 12.472  -46.080  1.00 25.18  ? 464  ILE   A CD1 1 
ATOM   1273  N  N   . THR   A  1 164 ? -35.567 10.833  -49.810  1.00 37.59  ? 465  THR   A N   1 
ATOM   1274  C  CA  . THR   A  1 164 ? -36.219 10.544  -51.079  1.00 41.55  ? 465  THR   A CA  1 
ATOM   1275  C  C   . THR   A  1 164 ? -37.660 10.106  -50.833  1.00 39.99  ? 465  THR   A C   1 
ATOM   1276  O  O   . THR   A  1 164 ? -37.899 9.093   -50.169  1.00 33.67  ? 465  THR   A O   1 
ATOM   1277  C  CB  . THR   A  1 164 ? -35.453 9.467   -51.834  1.00 45.56  ? 465  THR   A CB  1 
ATOM   1278  O  OG1 . THR   A  1 164 ? -34.228 10.027  -52.329  1.00 53.58  ? 465  THR   A OG1 1 
ATOM   1279  C  CG2 . THR   A  1 164 ? -36.289 8.938   -52.993  1.00 34.80  ? 465  THR   A CG2 1 
ATOM   1280  N  N   . ILE   A  1 165 ? -38.611 10.834  -51.415  1.00 44.79  ? 466  ILE   A N   1 
ATOM   1281  C  CA  . ILE   A  1 165 ? -40.036 10.681  -51.140  1.00 41.37  ? 466  ILE   A CA  1 
ATOM   1282  C  C   . ILE   A  1 165 ? -40.725 10.053  -52.357  1.00 50.31  ? 466  ILE   A C   1 
ATOM   1283  O  O   . ILE   A  1 165 ? -40.826 10.677  -53.424  1.00 44.93  ? 466  ILE   A O   1 
ATOM   1284  C  CB  . ILE   A  1 165 ? -40.662 12.035  -50.793  1.00 42.10  ? 466  ILE   A CB  1 
ATOM   1285  C  CG1 . ILE   A  1 165 ? -39.871 12.725  -49.692  1.00 40.40  ? 466  ILE   A CG1 1 
ATOM   1286  C  CG2 . ILE   A  1 165 ? -42.109 11.876  -50.386  1.00 45.20  ? 466  ILE   A CG2 1 
ATOM   1287  C  CD1 . ILE   A  1 165 ? -40.536 14.029  -49.254  1.00 39.36  ? 466  ILE   A CD1 1 
ATOM   1288  N  N   . PHE   A  1 166 ? -41.236 8.835   -52.181  1.00 44.58  ? 467  PHE   A N   1 
ATOM   1289  C  CA  . PHE   A  1 166 ? -41.928 8.055   -53.207  1.00 29.65  ? 467  PHE   A CA  1 
ATOM   1290  C  C   . PHE   A  1 166 ? -43.427 8.366   -53.169  1.00 37.10  ? 467  PHE   A C   1 
ATOM   1291  O  O   . PHE   A  1 166 ? -43.857 9.139   -52.312  1.00 48.40  ? 467  PHE   A O   1 
ATOM   1292  C  CB  . PHE   A  1 166 ? -41.638 6.577   -52.985  1.00 24.35  ? 467  PHE   A CB  1 
ATOM   1293  C  CG  . PHE   A  1 166 ? -40.233 6.198   -53.310  1.00 32.24  ? 467  PHE   A CG  1 
ATOM   1294  C  CD1 . PHE   A  1 166 ? -39.765 6.280   -54.609  1.00 35.47  ? 467  PHE   A CD1 1 
ATOM   1295  C  CD2 . PHE   A  1 166 ? -39.374 5.754   -52.321  1.00 44.78  ? 467  PHE   A CD2 1 
ATOM   1296  C  CE1 . PHE   A  1 166 ? -38.459 5.928   -54.923  1.00 45.91  ? 467  PHE   A CE1 1 
ATOM   1297  C  CE2 . PHE   A  1 166 ? -38.067 5.400   -52.620  1.00 48.74  ? 467  PHE   A CE2 1 
ATOM   1298  C  CZ  . PHE   A  1 166 ? -37.603 5.488   -53.920  1.00 45.73  ? 467  PHE   A CZ  1 
ATOM   1299  N  N   . PRO   A  1 167 ? -44.255 7.853   -54.085  1.00 50.29  ? 468  PRO   A N   1 
ATOM   1300  C  CA  . PRO   A  1 167 ? -45.625 8.375   -54.160  1.00 46.91  ? 468  PRO   A CA  1 
ATOM   1301  C  C   . PRO   A  1 167 ? -46.383 8.123   -52.869  1.00 36.98  ? 468  PRO   A C   1 
ATOM   1302  O  O   . PRO   A  1 167 ? -46.320 7.033   -52.295  1.00 31.78  ? 468  PRO   A O   1 
ATOM   1303  C  CB  . PRO   A  1 167 ? -46.245 7.614   -55.338  1.00 40.66  ? 468  PRO   A CB  1 
ATOM   1304  C  CG  . PRO   A  1 167 ? -45.123 7.151   -56.133  1.00 35.55  ? 468  PRO   A CG  1 
ATOM   1305  C  CD  . PRO   A  1 167 ? -44.048 6.838   -55.134  1.00 45.17  ? 468  PRO   A CD  1 
ATOM   1306  N  N   . GLN   A  1 168 ? -47.151 9.131   -52.441  1.00 38.47  ? 469  GLN   A N   1 
ATOM   1307  C  CA  . GLN   A  1 168 ? -47.947 9.025   -51.225  1.00 36.69  ? 469  GLN   A CA  1 
ATOM   1308  C  C   . GLN   A  1 168 ? -48.912 7.856   -51.273  1.00 41.61  ? 469  GLN   A C   1 
ATOM   1309  O  O   . GLN   A  1 168 ? -49.040 7.167   -52.282  1.00 44.71  ? 469  GLN   A O   1 
ATOM   1310  C  CB  . GLN   A  1 168 ? -48.746 10.295  -50.998  1.00 38.84  ? 469  GLN   A CB  1 
ATOM   1311  C  CG  . GLN   A  1 168 ? -49.894 10.445  -51.948  1.00 45.09  ? 469  GLN   A CG  1 
ATOM   1312  C  CD  . GLN   A  1 168 ? -50.109 11.885  -52.329  1.00 47.49  ? 469  GLN   A CD  1 
ATOM   1313  O  OE1 . GLN   A  1 168 ? -49.147 12.625  -52.546  1.00 53.02  ? 469  GLN   A OE1 1 
ATOM   1314  N  NE2 . GLN   A  1 168 ? -51.376 12.303  -52.398  1.00 43.66  ? 469  GLN   A NE2 1 
ATOM   1315  N  N   . ARG   A  1 169 ? -49.618 7.638   -50.181  1.00 54.48  ? 470  ARG   A N   1 
ATOM   1316  C  CA  . ARG   A  1 169 ? -50.593 6.570   -50.147  1.00 53.96  ? 470  ARG   A CA  1 
ATOM   1317  C  C   . ARG   A  1 169 ? -51.813 6.997   -50.946  1.00 46.95  ? 470  ARG   A C   1 
ATOM   1318  O  O   . ARG   A  1 169 ? -52.012 8.185   -51.211  1.00 50.25  ? 470  ARG   A O   1 
ATOM   1319  C  CB  . ARG   A  1 169 ? -50.948 6.247   -48.696  1.00 54.86  ? 470  ARG   A CB  1 
ATOM   1320  C  CG  . ARG   A  1 169 ? -51.742 4.985   -48.523  1.00 64.16  ? 470  ARG   A CG  1 
ATOM   1321  C  CD  . ARG   A  1 169 ? -51.992 4.732   -47.073  1.00 63.25  ? 470  ARG   A CD  1 
ATOM   1322  N  NE  . ARG   A  1 169 ? -50.842 4.118   -46.449  1.00 63.88  ? 470  ARG   A NE  1 
ATOM   1323  C  CZ  . ARG   A  1 169 ? -50.928 3.422   -45.331  1.00 78.22  ? 470  ARG   A CZ  1 
ATOM   1324  N  NH1 . ARG   A  1 169 ? -52.118 3.282   -44.759  1.00 94.11  ? 470  ARG   A NH1 1 
ATOM   1325  N  NH2 . ARG   A  1 169 ? -49.843 2.870   -44.793  1.00 75.24  ? 470  ARG   A NH2 1 
ATOM   1326  N  N   . THR   A  1 170 ? -52.616 6.017   -51.366  1.00 49.83  ? 471  THR   A N   1 
ATOM   1327  C  CA  . THR   A  1 170 ? -53.875 6.337   -52.039  1.00 53.35  ? 471  THR   A CA  1 
ATOM   1328  C  C   . THR   A  1 170 ? -55.044 5.674   -51.323  1.00 55.87  ? 471  THR   A C   1 
ATOM   1329  O  O   . THR   A  1 170 ? -55.690 6.291   -50.473  1.00 60.78  ? 471  THR   A O   1 
ATOM   1330  C  CB  . THR   A  1 170 ? -53.869 5.915   -53.522  1.00 51.53  ? 471  THR   A CB  1 
ATOM   1331  O  OG1 . THR   A  1 170 ? -53.722 4.495   -53.644  1.00 52.59  ? 471  THR   A OG1 1 
ATOM   1332  C  CG2 . THR   A  1 170 ? -52.745 6.584   -54.279  1.00 43.55  ? 471  THR   A CG2 1 
ATOM   1333  N  N   . ASP   A  1 171 ? -55.328 4.419   -51.667  1.00 53.66  ? 472  ASP   A N   1 
ATOM   1334  C  CA  . ASP   A  1 171 ? -56.403 3.652   -51.055  1.00 51.35  ? 472  ASP   A CA  1 
ATOM   1335  C  C   . ASP   A  1 171 ? -55.880 2.598   -50.093  1.00 61.84  ? 472  ASP   A C   1 
ATOM   1336  O  O   . ASP   A  1 171 ? -56.605 1.654   -49.771  1.00 70.05  ? 472  ASP   A O   1 
ATOM   1337  C  CB  . ASP   A  1 171 ? -57.244 2.980   -52.134  1.00 62.83  ? 472  ASP   A CB  1 
ATOM   1338  C  CG  . ASP   A  1 171 ? -56.441 1.987   -52.960  1.00 73.04  ? 472  ASP   A CG  1 
ATOM   1339  O  OD1 . ASP   A  1 171 ? -55.205 2.134   -53.024  1.00 74.46  ? 472  ASP   A OD1 1 
ATOM   1340  O  OD2 . ASP   A  1 171 ? -57.043 1.064   -53.551  1.00 73.25  ? 472  ASP   A OD2 1 
ATOM   1341  N  N   . GLY   A  1 172 ? -54.626 2.725   -49.646  1.00 55.48  ? 473  GLY   A N   1 
ATOM   1342  C  CA  . GLY   A  1 172 ? -53.980 1.713   -48.839  1.00 52.13  ? 473  GLY   A CA  1 
ATOM   1343  C  C   . GLY   A  1 172 ? -53.701 0.407   -49.546  1.00 61.74  ? 473  GLY   A C   1 
ATOM   1344  O  O   . GLY   A  1 172 ? -53.034 -0.460  -48.966  1.00 63.91  ? 473  GLY   A O   1 
ATOM   1345  N  N   . LYS   A  1 173 ? -54.182 0.235   -50.779  1.00 61.12  ? 474  LYS   A N   1 
ATOM   1346  C  CA  . LYS   A  1 173 ? -53.981 -0.982  -51.548  1.00 50.73  ? 474  LYS   A CA  1 
ATOM   1347  C  C   . LYS   A  1 173 ? -52.847 -0.873  -52.560  1.00 54.57  ? 474  LYS   A C   1 
ATOM   1348  O  O   . LYS   A  1 173 ? -52.549 -1.856  -53.243  1.00 54.62  ? 474  LYS   A O   1 
ATOM   1349  C  CB  . LYS   A  1 173 ? -55.285 -1.367  -52.249  1.00 38.08  ? 474  LYS   A CB  1 
ATOM   1350  C  CG  . LYS   A  1 173 ? -56.277 -2.042  -51.311  1.00 49.91  ? 474  LYS   A CG  1 
ATOM   1351  C  CD  . LYS   A  1 173 ? -57.731 -1.790  -51.696  1.00 60.95  ? 474  LYS   A CD  1 
ATOM   1352  C  CE  . LYS   A  1 173 ? -58.708 -2.495  -50.742  1.00 67.50  ? 474  LYS   A CE  1 
ATOM   1353  N  NZ  . LYS   A  1 173 ? -60.130 -2.355  -51.191  1.00 63.41  ? 474  LYS   A NZ  1 
ATOM   1354  N  N   . HIS   A  1 174 ? -52.187 0.279   -52.651  1.00 58.31  ? 475  HIS   A N   1 
ATOM   1355  C  CA  . HIS   A  1 174 ? -51.110 0.481   -53.614  1.00 55.87  ? 475  HIS   A CA  1 
ATOM   1356  C  C   . HIS   A  1 174 ? -49.962 1.227   -52.958  1.00 55.42  ? 475  HIS   A C   1 
ATOM   1357  O  O   . HIS   A  1 174 ? -49.456 2.218   -53.485  1.00 51.73  ? 475  HIS   A O   1 
ATOM   1358  C  CB  . HIS   A  1 174 ? -51.621 1.223   -54.847  1.00 51.71  ? 475  HIS   A CB  1 
ATOM   1359  C  CG  . HIS   A  1 174 ? -52.773 0.545   -55.507  1.00 61.78  ? 475  HIS   A CG  1 
ATOM   1360  N  ND1 . HIS   A  1 174 ? -54.077 0.735   -55.107  1.00 67.25  ? 475  HIS   A ND1 1 
ATOM   1361  C  CD2 . HIS   A  1 174 ? -52.817 -0.358  -56.512  1.00 66.86  ? 475  HIS   A CD2 1 
ATOM   1362  C  CE1 . HIS   A  1 174 ? -54.877 -0.009  -55.849  1.00 71.08  ? 475  HIS   A CE1 1 
ATOM   1363  N  NE2 . HIS   A  1 174 ? -54.138 -0.679  -56.714  1.00 72.32  ? 475  HIS   A NE2 1 
ATOM   1364  N  N   . ASP   A  1 175 ? -49.553 0.750   -51.782  1.00 58.91  ? 476  ASP   A N   1 
ATOM   1365  C  CA  . ASP   A  1 175 ? -48.468 1.383   -51.044  1.00 53.07  ? 476  ASP   A CA  1 
ATOM   1366  C  C   . ASP   A  1 175 ? -47.134 1.123   -51.728  1.00 50.91  ? 476  ASP   A C   1 
ATOM   1367  O  O   . ASP   A  1 175 ? -46.847 0.000   -52.164  1.00 42.38  ? 476  ASP   A O   1 
ATOM   1368  C  CB  . ASP   A  1 175 ? -48.395 0.846   -49.612  1.00 57.02  ? 476  ASP   A CB  1 
ATOM   1369  C  CG  . ASP   A  1 175 ? -49.535 1.321   -48.738  1.00 59.88  ? 476  ASP   A CG  1 
ATOM   1370  O  OD1 . ASP   A  1 175 ? -49.882 2.519   -48.782  1.00 60.84  ? 476  ASP   A OD1 1 
ATOM   1371  O  OD2 . ASP   A  1 175 ? -50.087 0.478   -48.002  1.00 60.47  ? 476  ASP   A OD2 1 
ATOM   1372  N  N   . PHE   A  1 176 ? -46.318 2.172   -51.823  1.00 43.37  ? 477  PHE   A N   1 
ATOM   1373  C  CA  . PHE   A  1 176 ? -44.886 2.004   -52.023  1.00 38.04  ? 477  PHE   A CA  1 
ATOM   1374  C  C   . PHE   A  1 176 ? -44.229 1.749   -50.665  1.00 52.35  ? 477  PHE   A C   1 
ATOM   1375  O  O   . PHE   A  1 176 ? -44.501 2.461   -49.692  1.00 49.85  ? 477  PHE   A O   1 
ATOM   1376  C  CB  . PHE   A  1 176 ? -44.290 3.249   -52.669  1.00 41.05  ? 477  PHE   A CB  1 
ATOM   1377  C  CG  . PHE   A  1 176 ? -44.660 3.432   -54.113  1.00 52.84  ? 477  PHE   A CG  1 
ATOM   1378  C  CD1 . PHE   A  1 176 ? -45.947 3.775   -54.483  1.00 57.13  ? 477  PHE   A CD1 1 
ATOM   1379  C  CD2 . PHE   A  1 176 ? -43.702 3.297   -55.104  1.00 54.85  ? 477  PHE   A CD2 1 
ATOM   1380  C  CE1 . PHE   A  1 176 ? -46.274 3.959   -55.804  1.00 53.41  ? 477  PHE   A CE1 1 
ATOM   1381  C  CE2 . PHE   A  1 176 ? -44.026 3.481   -56.434  1.00 47.62  ? 477  PHE   A CE2 1 
ATOM   1382  C  CZ  . PHE   A  1 176 ? -45.312 3.807   -56.779  1.00 47.09  ? 477  PHE   A CZ  1 
ATOM   1383  N  N   . ARG   A  1 177 ? -43.379 0.732   -50.586  1.00 49.14  ? 478  ARG   A N   1 
ATOM   1384  C  CA  . ARG   A  1 177 ? -42.704 0.435   -49.334  1.00 34.10  ? 478  ARG   A CA  1 
ATOM   1385  C  C   . ARG   A  1 177 ? -41.272 0.030   -49.606  1.00 45.00  ? 478  ARG   A C   1 
ATOM   1386  O  O   . ARG   A  1 177 ? -41.029 -0.807  -50.480  1.00 46.13  ? 478  ARG   A O   1 
ATOM   1387  C  CB  . ARG   A  1 177 ? -43.408 -0.693  -48.585  1.00 40.91  ? 478  ARG   A CB  1 
ATOM   1388  C  CG  . ARG   A  1 177 ? -44.766 -0.314  -48.017  1.00 50.63  ? 478  ARG   A CG  1 
ATOM   1389  C  CD  . ARG   A  1 177 ? -44.646 0.822   -46.997  1.00 48.08  ? 478  ARG   A CD  1 
ATOM   1390  N  NE  . ARG   A  1 177 ? -43.870 0.451   -45.812  1.00 46.83  ? 478  ARG   A NE  1 
ATOM   1391  C  CZ  . ARG   A  1 177 ? -44.405 0.070   -44.649  1.00 50.20  ? 478  ARG   A CZ  1 
ATOM   1392  N  NH1 . ARG   A  1 177 ? -45.725 -0.013  -44.494  1.00 47.74  ? 478  ARG   A NH1 1 
ATOM   1393  N  NH2 . ARG   A  1 177 ? -43.619 -0.221  -43.630  1.00 38.62  ? 478  ARG   A NH2 1 
ATOM   1394  N  N   . VAL   A  1 178 ? -40.333 0.607   -48.856  1.00 44.65  ? 479  VAL   A N   1 
ATOM   1395  C  CA  . VAL   A  1 178 ? -39.011 0.002   -48.719  1.00 42.00  ? 479  VAL   A CA  1 
ATOM   1396  C  C   . VAL   A  1 178 ? -39.113 -1.000  -47.578  1.00 44.33  ? 479  VAL   A C   1 
ATOM   1397  O  O   . VAL   A  1 178 ? -39.251 -0.610  -46.416  1.00 57.28  ? 479  VAL   A O   1 
ATOM   1398  C  CB  . VAL   A  1 178 ? -37.915 1.031   -48.435  1.00 41.20  ? 479  VAL   A CB  1 
ATOM   1399  C  CG1 . VAL   A  1 178 ? -36.561 0.356   -48.555  1.00 41.76  ? 479  VAL   A CG1 1 
ATOM   1400  C  CG2 . VAL   A  1 178 ? -38.019 2.255   -49.362  1.00 35.36  ? 479  VAL   A CG2 1 
ATOM   1401  N  N   . TRP   A  1 179 ? -39.045 -2.291  -47.901  1.00 38.66  ? 480  TRP   A N   1 
ATOM   1402  C  CA  . TRP   A  1 179 ? -39.206 -3.300  -46.861  1.00 47.01  ? 480  TRP   A CA  1 
ATOM   1403  C  C   . TRP   A  1 179 ? -38.033 -3.322  -45.885  1.00 49.27  ? 480  TRP   A C   1 
ATOM   1404  O  O   . TRP   A  1 179 ? -38.228 -3.654  -44.713  1.00 52.10  ? 480  TRP   A O   1 
ATOM   1405  C  CB  . TRP   A  1 179 ? -39.414 -4.674  -47.478  1.00 44.46  ? 480  TRP   A CB  1 
ATOM   1406  C  CG  . TRP   A  1 179 ? -40.792 -4.863  -47.985  1.00 40.38  ? 480  TRP   A CG  1 
ATOM   1407  C  CD1 . TRP   A  1 179 ? -41.598 -3.910  -48.542  1.00 37.15  ? 480  TRP   A CD1 1 
ATOM   1408  C  CD2 . TRP   A  1 179 ? -41.557 -6.077  -47.961  1.00 35.19  ? 480  TRP   A CD2 1 
ATOM   1409  N  NE1 . TRP   A  1 179 ? -42.821 -4.467  -48.885  1.00 40.50  ? 480  TRP   A NE1 1 
ATOM   1410  C  CE2 . TRP   A  1 179 ? -42.813 -5.796  -48.542  1.00 37.91  ? 480  TRP   A CE2 1 
ATOM   1411  C  CE3 . TRP   A  1 179 ? -41.300 -7.371  -47.511  1.00 36.17  ? 480  TRP   A CE3 1 
ATOM   1412  C  CZ2 . TRP   A  1 179 ? -43.813 -6.766  -48.666  1.00 42.17  ? 480  TRP   A CZ2 1 
ATOM   1413  C  CZ3 . TRP   A  1 179 ? -42.283 -8.337  -47.647  1.00 32.24  ? 480  TRP   A CZ3 1 
ATOM   1414  C  CH2 . TRP   A  1 179 ? -43.527 -8.029  -48.214  1.00 41.90  ? 480  TRP   A CH2 1 
ATOM   1415  N  N   . ASN   A  1 180 ? -36.820 -3.008  -46.341  1.00 52.17  ? 481  ASN   A N   1 
ATOM   1416  C  CA  . ASN   A  1 180 ? -35.694 -2.832  -45.427  1.00 44.13  ? 481  ASN   A CA  1 
ATOM   1417  C  C   . ASN   A  1 180 ? -36.003 -1.758  -44.394  1.00 50.39  ? 481  ASN   A C   1 
ATOM   1418  O  O   . ASN   A  1 180 ? -36.576 -0.716  -44.733  1.00 44.50  ? 481  ASN   A O   1 
ATOM   1419  C  CB  . ASN   A  1 180 ? -34.444 -2.406  -46.182  1.00 37.49  ? 481  ASN   A CB  1 
ATOM   1420  C  CG  . ASN   A  1 180 ? -34.161 -3.263  -47.365  1.00 39.76  ? 481  ASN   A CG  1 
ATOM   1421  O  OD1 . ASN   A  1 180 ? -34.863 -3.205  -48.383  1.00 49.56  ? 481  ASN   A OD1 1 
ATOM   1422  N  ND2 . ASN   A  1 180 ? -33.111 -4.057  -47.264  1.00 31.69  ? 481  ASN   A ND2 1 
ATOM   1423  N  N   . SER   A  1 181 ? -35.593 -2.010  -43.132  1.00 38.41  ? 482  SER   A N   1 
ATOM   1424  C  CA  . SER   A  1 181 ? -35.732 -1.008  -42.080  1.00 31.59  ? 482  SER   A CA  1 
ATOM   1425  C  C   . SER   A  1 181 ? -34.741 0.121   -42.290  1.00 41.14  ? 482  SER   A C   1 
ATOM   1426  O  O   . SER   A  1 181 ? -35.091 1.300   -42.170  1.00 48.25  ? 482  SER   A O   1 
ATOM   1427  C  CB  . SER   A  1 181 ? -35.554 -1.630  -40.681  1.00 36.50  ? 482  SER   A CB  1 
ATOM   1428  O  OG  . SER   A  1 181 ? -34.417 -2.479  -40.583  1.00 41.28  ? 482  SER   A OG  1 
ATOM   1429  N  N   . GLN   A  1 182 ? -33.503 -0.218  -42.611  1.00 44.40  ? 483  GLN   A N   1 
ATOM   1430  C  CA  . GLN   A  1 182 ? -32.541 0.751   -43.110  1.00 50.00  ? 483  GLN   A CA  1 
ATOM   1431  C  C   . GLN   A  1 182 ? -32.078 0.334   -44.500  1.00 43.66  ? 483  GLN   A C   1 
ATOM   1432  O  O   . GLN   A  1 182 ? -32.190 -0.835  -44.883  1.00 52.03  ? 483  GLN   A O   1 
ATOM   1433  C  CB  . GLN   A  1 182 ? -31.331 0.870   -42.185  1.00 54.48  ? 483  GLN   A CB  1 
ATOM   1434  C  CG  . GLN   A  1 182 ? -31.611 1.437   -40.806  1.00 57.28  ? 483  GLN   A CG  1 
ATOM   1435  C  CD  . GLN   A  1 182 ? -30.431 1.221   -39.887  1.00 53.83  ? 483  GLN   A CD  1 
ATOM   1436  O  OE1 . GLN   A  1 182 ? -29.300 1.644   -40.194  1.00 37.49  ? 483  GLN   A OE1 1 
ATOM   1437  N  NE2 . GLN   A  1 182 ? -30.666 0.510   -38.779  1.00 47.71  ? 483  GLN   A NE2 1 
ATOM   1438  N  N   . LEU   A  1 183 ? -31.534 1.295   -45.257  1.00 36.25  ? 484  LEU   A N   1 
ATOM   1439  C  CA  . LEU   A  1 183 ? -31.087 0.964   -46.614  1.00 46.96  ? 484  LEU   A CA  1 
ATOM   1440  C  C   . LEU   A  1 183 ? -29.846 0.075   -46.570  1.00 49.81  ? 484  LEU   A C   1 
ATOM   1441  O  O   . LEU   A  1 183 ? -29.775 -0.947  -47.260  1.00 40.85  ? 484  LEU   A O   1 
ATOM   1442  C  CB  . LEU   A  1 183 ? -30.828 2.238   -47.426  1.00 29.34  ? 484  LEU   A CB  1 
ATOM   1443  C  CG  . LEU   A  1 183 ? -31.980 3.246   -47.605  1.00 29.71  ? 484  LEU   A CG  1 
ATOM   1444  C  CD1 . LEU   A  1 183 ? -31.538 4.493   -48.356  1.00 23.93  ? 484  LEU   A CD1 1 
ATOM   1445  C  CD2 . LEU   A  1 183 ? -33.148 2.625   -48.296  1.00 25.98  ? 484  LEU   A CD2 1 
ATOM   1446  N  N   . ILE   A  1 184 ? -28.879 0.414   -45.732  1.00 50.36  ? 485  ILE   A N   1 
ATOM   1447  C  CA  . ILE   A  1 184 ? -27.697 -0.413  -45.539  1.00 48.99  ? 485  ILE   A CA  1 
ATOM   1448  C  C   . ILE   A  1 184 ? -27.784 -1.034  -44.152  1.00 46.44  ? 485  ILE   A C   1 
ATOM   1449  O  O   . ILE   A  1 184 ? -27.852 -0.314  -43.149  1.00 51.95  ? 485  ILE   A O   1 
ATOM   1450  C  CB  . ILE   A  1 184 ? -26.411 0.400   -45.718  1.00 40.38  ? 485  ILE   A CB  1 
ATOM   1451  C  CG1 . ILE   A  1 184 ? -26.477 1.140   -47.055  1.00 51.93  ? 485  ILE   A CG1 1 
ATOM   1452  C  CG2 . ILE   A  1 184 ? -25.217 -0.512  -45.692  1.00 37.36  ? 485  ILE   A CG2 1 
ATOM   1453  C  CD1 . ILE   A  1 184 ? -25.616 2.364   -47.108  1.00 62.84  ? 485  ILE   A CD1 1 
ATOM   1454  N  N   . ARG   A  1 185 ? -27.820 -2.367  -44.112  1.00 36.07  ? 486  ARG   A N   1 
ATOM   1455  C  CA  . ARG   A  1 185 ? -27.856 -3.194  -42.907  1.00 47.04  ? 486  ARG   A CA  1 
ATOM   1456  C  C   . ARG   A  1 185 ? -27.202 -4.527  -43.245  1.00 51.71  ? 486  ARG   A C   1 
ATOM   1457  O  O   . ARG   A  1 185 ? -27.244 -4.982  -44.397  1.00 42.04  ? 486  ARG   A O   1 
ATOM   1458  C  CB  . ARG   A  1 185 ? -29.273 -3.500  -42.383  1.00 53.63  ? 486  ARG   A CB  1 
ATOM   1459  C  CG  . ARG   A  1 185 ? -30.021 -2.376  -41.699  1.00 68.29  ? 486  ARG   A CG  1 
ATOM   1460  C  CD  . ARG   A  1 185 ? -29.386 -1.959  -40.375  1.00 79.06  ? 486  ARG   A CD  1 
ATOM   1461  N  NE  . ARG   A  1 185 ? -29.479 -2.968  -39.328  1.00 79.29  ? 486  ARG   A NE  1 
ATOM   1462  C  CZ  . ARG   A  1 185 ? -30.564 -3.179  -38.591  1.00 76.99  ? 486  ARG   A CZ  1 
ATOM   1463  N  NH1 . ARG   A  1 185 ? -31.668 -2.470  -38.790  1.00 72.31  ? 486  ARG   A NH1 1 
ATOM   1464  N  NH2 . ARG   A  1 185 ? -30.549 -4.115  -37.660  1.00 76.91  ? 486  ARG   A NH2 1 
ATOM   1465  N  N   . TYR   A  1 186 ? -26.612 -5.157  -42.232  1.00 45.47  ? 487  TYR   A N   1 
ATOM   1466  C  CA  . TYR   A  1 186 ? -26.001 -6.461  -42.404  1.00 37.48  ? 487  TYR   A CA  1 
ATOM   1467  C  C   . TYR   A  1 186 ? -27.015 -7.575  -42.146  1.00 41.58  ? 487  TYR   A C   1 
ATOM   1468  O  O   . TYR   A  1 186 ? -28.049 -7.384  -41.507  1.00 47.08  ? 487  TYR   A O   1 
ATOM   1469  C  CB  . TYR   A  1 186 ? -24.797 -6.608  -41.489  1.00 40.50  ? 487  TYR   A CB  1 
ATOM   1470  C  CG  . TYR   A  1 186 ? -23.694 -5.630  -41.797  1.00 40.18  ? 487  TYR   A CG  1 
ATOM   1471  C  CD1 . TYR   A  1 186 ? -23.420 -4.588  -40.938  1.00 46.10  ? 487  TYR   A CD1 1 
ATOM   1472  C  CD2 . TYR   A  1 186 ? -22.922 -5.752  -42.941  1.00 45.43  ? 487  TYR   A CD2 1 
ATOM   1473  C  CE1 . TYR   A  1 186 ? -22.407 -3.683  -41.201  1.00 49.06  ? 487  TYR   A CE1 1 
ATOM   1474  C  CE2 . TYR   A  1 186 ? -21.893 -4.843  -43.223  1.00 50.77  ? 487  TYR   A CE2 1 
ATOM   1475  C  CZ  . TYR   A  1 186 ? -21.646 -3.803  -42.342  1.00 49.53  ? 487  TYR   A CZ  1 
ATOM   1476  O  OH  . TYR   A  1 186 ? -20.637 -2.878  -42.573  1.00 43.16  ? 487  TYR   A OH  1 
ATOM   1477  N  N   . ALA   A  1 187 ? -26.716 -8.739  -42.681  1.00 43.80  ? 488  ALA   A N   1 
ATOM   1478  C  CA  . ALA   A  1 187 ? -27.583 -9.884  -42.532  1.00 47.54  ? 488  ALA   A CA  1 
ATOM   1479  C  C   . ALA   A  1 187 ? -27.258 -10.607 -41.237  1.00 66.11  ? 488  ALA   A C   1 
ATOM   1480  O  O   . ALA   A  1 187 ? -26.203 -10.410 -40.630  1.00 69.67  ? 488  ALA   A O   1 
ATOM   1481  C  CB  . ALA   A  1 187 ? -27.420 -10.834 -43.718  1.00 49.58  ? 488  ALA   A CB  1 
ATOM   1482  N  N   . GLY   A  1 188 ? -28.186 -11.461 -40.824  1.00 73.67  ? 489  GLY   A N   1 
ATOM   1483  C  CA  . GLY   A  1 188 ? -28.007 -12.312 -39.669  1.00 70.12  ? 489  GLY   A CA  1 
ATOM   1484  C  C   . GLY   A  1 188 ? -28.596 -13.675 -39.953  1.00 78.38  ? 489  GLY   A C   1 
ATOM   1485  O  O   . GLY   A  1 188 ? -29.747 -13.782 -40.387  1.00 89.42  ? 489  GLY   A O   1 
ATOM   1486  N  N   . TYR   A  1 189 ? -27.816 -14.727 -39.738  1.00 72.75  ? 490  TYR   A N   1 
ATOM   1487  C  CA  . TYR   A  1 189 ? -28.242 -16.087 -40.021  1.00 64.21  ? 490  TYR   A CA  1 
ATOM   1488  C  C   . TYR   A  1 189 ? -28.161 -16.878 -38.730  1.00 64.88  ? 490  TYR   A C   1 
ATOM   1489  O  O   . TYR   A  1 189 ? -27.086 -16.970 -38.128  1.00 62.26  ? 490  TYR   A O   1 
ATOM   1490  C  CB  . TYR   A  1 189 ? -27.369 -16.736 -41.090  1.00 57.65  ? 490  TYR   A CB  1 
ATOM   1491  C  CG  . TYR   A  1 189 ? -26.976 -15.841 -42.249  1.00 64.98  ? 490  TYR   A CG  1 
ATOM   1492  C  CD1 . TYR   A  1 189 ? -25.875 -14.994 -42.154  1.00 64.76  ? 490  TYR   A CD1 1 
ATOM   1493  C  CD2 . TYR   A  1 189 ? -27.681 -15.867 -43.454  1.00 67.73  ? 490  TYR   A CD2 1 
ATOM   1494  C  CE1 . TYR   A  1 189 ? -25.495 -14.191 -43.209  1.00 65.27  ? 490  TYR   A CE1 1 
ATOM   1495  C  CE2 . TYR   A  1 189 ? -27.304 -15.055 -44.529  1.00 61.72  ? 490  TYR   A CE2 1 
ATOM   1496  C  CZ  . TYR   A  1 189 ? -26.209 -14.227 -44.392  1.00 59.75  ? 490  TYR   A CZ  1 
ATOM   1497  O  OH  . TYR   A  1 189 ? -25.814 -13.420 -45.425  1.00 60.45  ? 490  TYR   A OH  1 
ATOM   1498  N  N   . LYS   A  1 190 ? -29.288 -17.445 -38.309  1.00 58.55  ? 491  LYS   A N   1 
ATOM   1499  C  CA  . LYS   A  1 190 ? -29.285 -18.351 -37.172  1.00 63.24  ? 491  LYS   A CA  1 
ATOM   1500  C  C   . LYS   A  1 190 ? -28.696 -19.694 -37.586  1.00 61.40  ? 491  LYS   A C   1 
ATOM   1501  O  O   . LYS   A  1 190 ? -29.109 -20.275 -38.593  1.00 63.86  ? 491  LYS   A O   1 
ATOM   1502  C  CB  . LYS   A  1 190 ? -30.700 -18.532 -36.627  1.00 75.05  ? 491  LYS   A CB  1 
ATOM   1503  C  CG  . LYS   A  1 190 ? -30.768 -18.933 -35.138  1.00 82.16  ? 491  LYS   A CG  1 
ATOM   1504  C  CD  . LYS   A  1 190 ? -30.881 -17.707 -34.205  1.00 79.70  ? 491  LYS   A CD  1 
ATOM   1505  C  CE  . LYS   A  1 190 ? -31.269 -18.113 -32.779  1.00 80.69  ? 491  LYS   A CE  1 
ATOM   1506  N  NZ  . LYS   A  1 190 ? -32.688 -18.601 -32.656  1.00 79.15  ? 491  LYS   A NZ  1 
ATOM   1507  N  N   . GLN   A  1 191 ? -27.720 -20.178 -36.807  1.00 61.09  ? 492  GLN   A N   1 
ATOM   1508  C  CA  . GLN   A  1 191 ? -27.098 -21.479 -37.024  1.00 63.15  ? 492  GLN   A CA  1 
ATOM   1509  C  C   . GLN   A  1 191 ? -27.945 -22.576 -36.384  1.00 63.05  ? 492  GLN   A C   1 
ATOM   1510  O  O   . GLN   A  1 191 ? -28.731 -22.311 -35.475  1.00 70.06  ? 492  GLN   A O   1 
ATOM   1511  C  CB  . GLN   A  1 191 ? -25.680 -21.490 -36.447  1.00 63.36  ? 492  GLN   A CB  1 
ATOM   1512  C  CG  . GLN   A  1 191 ? -24.716 -20.489 -37.087  1.00 63.36  ? 492  GLN   A CG  1 
ATOM   1513  C  CD  . GLN   A  1 191 ? -24.640 -20.640 -38.590  1.00 69.67  ? 492  GLN   A CD  1 
ATOM   1514  O  OE1 . GLN   A  1 191 ? -25.089 -19.763 -39.337  1.00 64.85  ? 492  GLN   A OE1 1 
ATOM   1515  N  NE2 . GLN   A  1 191 ? -24.079 -21.758 -39.047  1.00 76.63  ? 492  GLN   A NE2 1 
ATOM   1516  N  N   . PRO   A  1 192 ? -27.818 -23.823 -36.850  1.00 56.85  ? 493  PRO   A N   1 
ATOM   1517  C  CA  . PRO   A  1 192 ? -28.624 -24.893 -36.245  1.00 62.13  ? 493  PRO   A CA  1 
ATOM   1518  C  C   . PRO   A  1 192 ? -28.355 -25.053 -34.765  1.00 69.32  ? 493  PRO   A C   1 
ATOM   1519  O  O   . PRO   A  1 192 ? -29.253 -25.450 -34.011  1.00 69.86  ? 493  PRO   A O   1 
ATOM   1520  C  CB  . PRO   A  1 192 ? -28.203 -26.146 -37.026  1.00 61.84  ? 493  PRO   A CB  1 
ATOM   1521  C  CG  . PRO   A  1 192 ? -27.488 -25.659 -38.214  1.00 52.07  ? 493  PRO   A CG  1 
ATOM   1522  C  CD  . PRO   A  1 192 ? -26.905 -24.339 -37.880  1.00 57.15  ? 493  PRO   A CD  1 
ATOM   1523  N  N   . ASP   A  1 193 ? -27.136 -24.742 -34.329  1.00 74.29  ? 494  ASP   A N   1 
ATOM   1524  C  CA  . ASP   A  1 193 ? -26.687 -24.999 -32.968  1.00 71.02  ? 494  ASP   A CA  1 
ATOM   1525  C  C   . ASP   A  1 193 ? -27.141 -23.930 -31.987  1.00 64.51  ? 494  ASP   A C   1 
ATOM   1526  O  O   . ASP   A  1 193 ? -26.745 -23.972 -30.818  1.00 81.17  ? 494  ASP   A O   1 
ATOM   1527  C  CB  . ASP   A  1 193 ? -25.158 -25.135 -32.945  1.00 72.33  ? 494  ASP   A CB  1 
ATOM   1528  C  CG  . ASP   A  1 193 ? -24.442 -23.797 -33.031  1.00 71.84  ? 494  ASP   A CG  1 
ATOM   1529  O  OD1 . ASP   A  1 193 ? -23.336 -23.674 -32.458  1.00 74.32  ? 494  ASP   A OD1 1 
ATOM   1530  O  OD2 . ASP   A  1 193 ? -24.990 -22.863 -33.642  1.00 70.08  ? 494  ASP   A OD2 1 
ATOM   1531  N  N   . GLY   A  1 194 ? -27.970 -22.985 -32.428  1.00 56.98  ? 495  GLY   A N   1 
ATOM   1532  C  CA  . GLY   A  1 194 ? -28.447 -21.910 -31.600  1.00 60.87  ? 495  GLY   A CA  1 
ATOM   1533  C  C   . GLY   A  1 194 ? -27.718 -20.598 -31.802  1.00 58.61  ? 495  GLY   A C   1 
ATOM   1534  O  O   . GLY   A  1 194 ? -28.322 -19.532 -31.624  1.00 54.90  ? 495  GLY   A O   1 
ATOM   1535  N  N   . SER   A  1 195 ? -26.443 -20.651 -32.185  1.00 63.37  ? 496  SER   A N   1 
ATOM   1536  C  CA  . SER   A  1 195 ? -25.646 -19.446 -32.362  1.00 66.86  ? 496  SER   A CA  1 
ATOM   1537  C  C   . SER   A  1 195 ? -26.164 -18.621 -33.541  1.00 68.67  ? 496  SER   A C   1 
ATOM   1538  O  O   . SER   A  1 195 ? -26.998 -19.065 -34.335  1.00 76.82  ? 496  SER   A O   1 
ATOM   1539  C  CB  . SER   A  1 195 ? -24.174 -19.799 -32.560  1.00 69.49  ? 496  SER   A CB  1 
ATOM   1540  O  OG  . SER   A  1 195 ? -23.995 -20.563 -33.731  1.00 80.16  ? 496  SER   A OG  1 
ATOM   1541  N  N   . THR   A  1 196 ? -25.668 -17.389 -33.640  1.00 64.93  ? 497  THR   A N   1 
ATOM   1542  C  CA  . THR   A  1 196 ? -26.147 -16.430 -34.626  1.00 63.85  ? 497  THR   A CA  1 
ATOM   1543  C  C   . THR   A  1 196 ? -24.962 -15.763 -35.316  1.00 72.48  ? 497  THR   A C   1 
ATOM   1544  O  O   . THR   A  1 196 ? -24.057 -15.251 -34.646  1.00 77.71  ? 497  THR   A O   1 
ATOM   1545  C  CB  . THR   A  1 196 ? -27.050 -15.387 -33.965  1.00 63.63  ? 497  THR   A CB  1 
ATOM   1546  O  OG1 . THR   A  1 196 ? -28.134 -16.047 -33.291  1.00 72.51  ? 497  THR   A OG1 1 
ATOM   1547  C  CG2 . THR   A  1 196 ? -27.599 -14.419 -35.004  1.00 60.28  ? 497  THR   A CG2 1 
ATOM   1548  N  N   . LEU   A  1 197 ? -24.969 -15.768 -36.652  1.00 66.92  ? 498  LEU   A N   1 
ATOM   1549  C  CA  . LEU   A  1 197 ? -23.877 -15.236 -37.459  1.00 53.44  ? 498  LEU   A CA  1 
ATOM   1550  C  C   . LEU   A  1 197 ? -24.346 -13.974 -38.158  1.00 49.04  ? 498  LEU   A C   1 
ATOM   1551  O  O   . LEU   A  1 197 ? -25.440 -13.950 -38.725  1.00 57.69  ? 498  LEU   A O   1 
ATOM   1552  C  CB  . LEU   A  1 197 ? -23.398 -16.261 -38.486  1.00 51.47  ? 498  LEU   A CB  1 
ATOM   1553  C  CG  . LEU   A  1 197 ? -22.367 -15.698 -39.455  1.00 57.91  ? 498  LEU   A CG  1 
ATOM   1554  C  CD1 . LEU   A  1 197 ? -21.171 -15.148 -38.690  1.00 44.41  ? 498  LEU   A CD1 1 
ATOM   1555  C  CD2 . LEU   A  1 197 ? -21.952 -16.740 -40.511  1.00 62.09  ? 498  LEU   A CD2 1 
ATOM   1556  N  N   . GLY   A  1 198 ? -23.520 -12.932 -38.109  1.00 48.31  ? 499  GLY   A N   1 
ATOM   1557  C  CA  . GLY   A  1 198 ? -23.968 -11.611 -38.502  1.00 55.51  ? 499  GLY   A CA  1 
ATOM   1558  C  C   . GLY   A  1 198 ? -24.783 -10.915 -37.418  1.00 60.86  ? 499  GLY   A C   1 
ATOM   1559  O  O   . GLY   A  1 198 ? -24.626 -11.149 -36.217  1.00 77.54  ? 499  GLY   A O   1 
ATOM   1560  N  N   . ASP   A  1 199 ? -25.682 -10.051 -37.869  1.00 60.05  ? 500  ASP   A N   1 
ATOM   1561  C  CA  . ASP   A  1 199 ? -26.397 -9.129  -36.998  1.00 56.65  ? 500  ASP   A CA  1 
ATOM   1562  C  C   . ASP   A  1 199 ? -27.724 -9.748  -36.584  1.00 54.60  ? 500  ASP   A C   1 
ATOM   1563  O  O   . ASP   A  1 199 ? -28.632 -9.851  -37.422  1.00 55.21  ? 500  ASP   A O   1 
ATOM   1564  C  CB  . ASP   A  1 199 ? -26.623 -7.820  -37.735  1.00 58.97  ? 500  ASP   A CB  1 
ATOM   1565  C  CG  . ASP   A  1 199 ? -27.170 -6.736  -36.861  1.00 61.65  ? 500  ASP   A CG  1 
ATOM   1566  O  OD1 . ASP   A  1 199 ? -28.320 -6.867  -36.382  1.00 55.42  ? 500  ASP   A OD1 1 
ATOM   1567  O  OD2 . ASP   A  1 199 ? -26.442 -5.734  -36.689  1.00 63.96  ? 500  ASP   A OD2 1 
ATOM   1568  N  N   . PRO   A  1 200 ? -27.894 -10.160 -35.326  1.00 59.06  ? 501  PRO   A N   1 
ATOM   1569  C  CA  . PRO   A  1 200 ? -29.116 -10.894 -34.945  1.00 55.56  ? 501  PRO   A CA  1 
ATOM   1570  C  C   . PRO   A  1 200 ? -30.402 -10.099 -35.106  1.00 56.68  ? 501  PRO   A C   1 
ATOM   1571  O  O   . PRO   A  1 200 ? -31.490 -10.693 -35.023  1.00 52.04  ? 501  PRO   A O   1 
ATOM   1572  C  CB  . PRO   A  1 200 ? -28.863 -11.247 -33.477  1.00 46.81  ? 501  PRO   A CB  1 
ATOM   1573  C  CG  . PRO   A  1 200 ? -27.372 -11.213 -33.352  1.00 46.07  ? 501  PRO   A CG  1 
ATOM   1574  C  CD  . PRO   A  1 200 ? -26.911 -10.116 -34.231  1.00 45.09  ? 501  PRO   A CD  1 
ATOM   1575  N  N   . ALA   A  1 201 ? -30.322 -8.785  -35.335  1.00 59.71  ? 502  ALA   A N   1 
ATOM   1576  C  CA  . ALA   A  1 201 ? -31.540 -7.997  -35.496  1.00 54.49  ? 502  ALA   A CA  1 
ATOM   1577  C  C   . ALA   A  1 201 ? -32.264 -8.379  -36.767  1.00 60.99  ? 502  ALA   A C   1 
ATOM   1578  O  O   . ALA   A  1 201 ? -33.491 -8.514  -36.780  1.00 68.88  ? 502  ALA   A O   1 
ATOM   1579  C  CB  . ALA   A  1 201 ? -31.217 -6.508  -35.531  1.00 48.93  ? 502  ALA   A CB  1 
ATOM   1580  N  N   . ASN   A  1 202 ? -31.508 -8.582  -37.835  1.00 61.48  ? 503  ASN   A N   1 
ATOM   1581  C  CA  . ASN   A  1 202 ? -32.026 -8.698  -39.181  1.00 54.11  ? 503  ASN   A CA  1 
ATOM   1582  C  C   . ASN   A  1 202 ? -32.272 -10.146 -39.596  1.00 56.30  ? 503  ASN   A C   1 
ATOM   1583  O  O   . ASN   A  1 202 ? -32.414 -10.423 -40.791  1.00 65.81  ? 503  ASN   A O   1 
ATOM   1584  C  CB  . ASN   A  1 202 ? -31.052 -8.010  -40.130  1.00 57.59  ? 503  ASN   A CB  1 
ATOM   1585  C  CG  . ASN   A  1 202 ? -30.715 -6.587  -39.691  1.00 59.72  ? 503  ASN   A CG  1 
ATOM   1586  O  OD1 . ASN   A  1 202 ? -31.614 -5.790  -39.413  1.00 63.50  ? 503  ASN   A OD1 1 
ATOM   1587  N  ND2 . ASN   A  1 202 ? -29.418 -6.262  -39.636  1.00 54.57  ? 503  ASN   A ND2 1 
ATOM   1588  N  N   . VAL   A  1 203 ? -32.359 -11.068 -38.634  1.00 54.13  ? 504  VAL   A N   1 
ATOM   1589  C  CA  . VAL   A  1 203 ? -32.455 -12.489 -38.958  1.00 49.93  ? 504  VAL   A CA  1 
ATOM   1590  C  C   . VAL   A  1 203 ? -33.784 -12.822 -39.622  1.00 62.25  ? 504  VAL   A C   1 
ATOM   1591  O  O   . VAL   A  1 203 ? -33.835 -13.632 -40.556  1.00 68.93  ? 504  VAL   A O   1 
ATOM   1592  C  CB  . VAL   A  1 203 ? -32.236 -13.333 -37.700  1.00 51.20  ? 504  VAL   A CB  1 
ATOM   1593  C  CG1 . VAL   A  1 203 ? -32.514 -14.802 -37.998  1.00 55.86  ? 504  VAL   A CG1 1 
ATOM   1594  C  CG2 . VAL   A  1 203 ? -30.822 -13.142 -37.218  1.00 59.37  ? 504  VAL   A CG2 1 
ATOM   1595  N  N   . GLN   A  1 204 ? -34.883 -12.231 -39.155  1.00 60.29  ? 505  GLN   A N   1 
ATOM   1596  C  CA  . GLN   A  1 204 ? -36.147 -12.512 -39.824  1.00 64.02  ? 505  GLN   A CA  1 
ATOM   1597  C  C   . GLN   A  1 204 ? -36.184 -11.898 -41.219  1.00 68.71  ? 505  GLN   A C   1 
ATOM   1598  O  O   . GLN   A  1 204 ? -36.747 -12.498 -42.144  1.00 69.76  ? 505  GLN   A O   1 
ATOM   1599  C  CB  . GLN   A  1 204 ? -37.327 -12.014 -38.999  1.00 63.80  ? 505  GLN   A CB  1 
ATOM   1600  C  CG  . GLN   A  1 204 ? -38.585 -12.851 -39.226  1.00 74.20  ? 505  GLN   A CG  1 
ATOM   1601  C  CD  . GLN   A  1 204 ? -39.826 -12.018 -39.530  1.00 80.87  ? 505  GLN   A CD  1 
ATOM   1602  O  OE1 . GLN   A  1 204 ? -40.213 -11.136 -38.752  1.00 69.11  ? 505  GLN   A OE1 1 
ATOM   1603  N  NE2 . GLN   A  1 204 ? -40.457 -12.296 -40.675  1.00 89.12  ? 505  GLN   A NE2 1 
ATOM   1604  N  N   . PHE   A  1 205 ? -35.587 -10.714 -41.393  1.00 61.01  ? 506  PHE   A N   1 
ATOM   1605  C  CA  . PHE   A  1 205 ? -35.535 -10.107 -42.719  1.00 52.25  ? 506  PHE   A CA  1 
ATOM   1606  C  C   . PHE   A  1 205 ? -34.588 -10.866 -43.639  1.00 61.27  ? 506  PHE   A C   1 
ATOM   1607  O  O   . PHE   A  1 205 ? -34.849 -10.989 -44.841  1.00 66.67  ? 506  PHE   A O   1 
ATOM   1608  C  CB  . PHE   A  1 205 ? -35.105 -8.656  -42.617  1.00 39.54  ? 506  PHE   A CB  1 
ATOM   1609  C  CG  . PHE   A  1 205 ? -35.195 -7.922  -43.907  1.00 50.40  ? 506  PHE   A CG  1 
ATOM   1610  C  CD1 . PHE   A  1 205 ? -36.380 -7.315  -44.280  1.00 55.10  ? 506  PHE   A CD1 1 
ATOM   1611  C  CD2 . PHE   A  1 205 ? -34.100 -7.832  -44.759  1.00 50.93  ? 506  PHE   A CD2 1 
ATOM   1612  C  CE1 . PHE   A  1 205 ? -36.477 -6.620  -45.477  1.00 57.18  ? 506  PHE   A CE1 1 
ATOM   1613  C  CE2 . PHE   A  1 205 ? -34.192 -7.136  -45.951  1.00 53.89  ? 506  PHE   A CE2 1 
ATOM   1614  C  CZ  . PHE   A  1 205 ? -35.383 -6.534  -46.318  1.00 55.58  ? 506  PHE   A CZ  1 
ATOM   1615  N  N   . THR   A  1 206 ? -33.475 -11.370 -43.098  1.00 57.95  ? 507  THR   A N   1 
ATOM   1616  C  CA  . THR   A  1 206 ? -32.593 -12.226 -43.884  1.00 48.18  ? 507  THR   A CA  1 
ATOM   1617  C  C   . THR   A  1 206 ? -33.340 -13.457 -44.394  1.00 63.13  ? 507  THR   A C   1 
ATOM   1618  O  O   . THR   A  1 206 ? -33.182 -13.856 -45.555  1.00 69.23  ? 507  THR   A O   1 
ATOM   1619  C  CB  . THR   A  1 206 ? -31.373 -12.619 -43.050  1.00 37.02  ? 507  THR   A CB  1 
ATOM   1620  O  OG1 . THR   A  1 206 ? -30.726 -11.426 -42.577  1.00 39.45  ? 507  THR   A OG1 1 
ATOM   1621  C  CG2 . THR   A  1 206 ? -30.384 -13.417 -43.875  1.00 37.91  ? 507  THR   A CG2 1 
ATOM   1622  N  N   . GLU   A  1 207 ? -34.187 -14.052 -43.554  1.00 67.74  ? 508  GLU   A N   1 
ATOM   1623  C  CA  . GLU   A  1 207 ? -34.981 -15.187 -44.010  1.00 67.02  ? 508  GLU   A CA  1 
ATOM   1624  C  C   . GLU   A  1 207 ? -35.881 -14.786 -45.171  1.00 57.15  ? 508  GLU   A C   1 
ATOM   1625  O  O   . GLU   A  1 207 ? -35.957 -15.498 -46.179  1.00 55.85  ? 508  GLU   A O   1 
ATOM   1626  C  CB  . GLU   A  1 207 ? -35.799 -15.764 -42.852  1.00 69.92  ? 508  GLU   A CB  1 
ATOM   1627  C  CG  . GLU   A  1 207 ? -35.023 -16.709 -41.954  1.00 76.59  ? 508  GLU   A CG  1 
ATOM   1628  C  CD  . GLU   A  1 207 ? -35.471 -16.637 -40.496  1.00 90.96  ? 508  GLU   A CD  1 
ATOM   1629  O  OE1 . GLU   A  1 207 ? -36.445 -15.905 -40.193  1.00 90.14  ? 508  GLU   A OE1 1 
ATOM   1630  O  OE2 . GLU   A  1 207 ? -34.837 -17.311 -39.651  1.00 92.48  ? 508  GLU   A OE2 1 
ATOM   1631  N  N   . ILE   A  1 208 ? -36.560 -13.639 -45.055  1.00 51.80  ? 509  ILE   A N   1 
ATOM   1632  C  CA  . ILE   A  1 208 ? -37.475 -13.219 -46.114  1.00 54.42  ? 509  ILE   A CA  1 
ATOM   1633  C  C   . ILE   A  1 208 ? -36.719 -13.043 -47.415  1.00 56.21  ? 509  ILE   A C   1 
ATOM   1634  O  O   . ILE   A  1 208 ? -37.088 -13.616 -48.448  1.00 65.97  ? 509  ILE   A O   1 
ATOM   1635  C  CB  . ILE   A  1 208 ? -38.212 -11.926 -45.732  1.00 56.34  ? 509  ILE   A CB  1 
ATOM   1636  C  CG1 . ILE   A  1 208 ? -38.970 -12.094 -44.417  1.00 62.89  ? 509  ILE   A CG1 1 
ATOM   1637  C  CG2 . ILE   A  1 208 ? -39.179 -11.561 -46.833  1.00 41.06  ? 509  ILE   A CG2 1 
ATOM   1638  C  CD1 . ILE   A  1 208 ? -39.660 -10.819 -43.959  1.00 62.04  ? 509  ILE   A CD1 1 
ATOM   1639  N  N   . CYS   A  1 209 ? -35.636 -12.257 -47.372  1.00 51.27  ? 510  CYS   A N   1 
ATOM   1640  C  CA  . CYS   A  1 209 ? -34.757 -12.073 -48.525  1.00 50.68  ? 510  CYS   A CA  1 
ATOM   1641  C  C   . CYS   A  1 209 ? -34.423 -13.401 -49.189  1.00 53.74  ? 510  CYS   A C   1 
ATOM   1642  O  O   . CYS   A  1 209 ? -34.684 -13.602 -50.377  1.00 59.01  ? 510  CYS   A O   1 
ATOM   1643  C  CB  . CYS   A  1 209 ? -33.471 -11.368 -48.096  1.00 48.18  ? 510  CYS   A CB  1 
ATOM   1644  S  SG  . CYS   A  1 209 ? -33.639 -9.596  -47.844  1.00 53.29  ? 510  CYS   A SG  1 
ATOM   1645  N  N   . ILE   A  1 210 ? -33.838 -14.322 -48.425  1.00 52.55  ? 511  ILE   A N   1 
ATOM   1646  C  CA  . ILE   A  1 210 ? -33.461 -15.614 -48.986  1.00 52.63  ? 511  ILE   A CA  1 
ATOM   1647  C  C   . ILE   A  1 210 ? -34.661 -16.294 -49.623  1.00 57.36  ? 511  ILE   A C   1 
ATOM   1648  O  O   . ILE   A  1 210 ? -34.565 -16.866 -50.715  1.00 69.93  ? 511  ILE   A O   1 
ATOM   1649  C  CB  . ILE   A  1 210 ? -32.830 -16.490 -47.895  1.00 50.83  ? 511  ILE   A CB  1 
ATOM   1650  C  CG1 . ILE   A  1 210 ? -31.575 -15.814 -47.359  1.00 44.38  ? 511  ILE   A CG1 1 
ATOM   1651  C  CG2 . ILE   A  1 210 ? -32.533 -17.868 -48.446  1.00 44.63  ? 511  ILE   A CG2 1 
ATOM   1652  C  CD1 . ILE   A  1 210 ? -31.002 -16.524 -46.155  1.00 49.68  ? 511  ILE   A CD1 1 
ATOM   1653  N  N   . GLN   A  1 211 ? -35.820 -16.216 -48.968  1.00 51.49  ? 512  GLN   A N   1 
ATOM   1654  C  CA  . GLN   A  1 211 ? -37.001 -16.900 -49.482  1.00 62.48  ? 512  GLN   A CA  1 
ATOM   1655  C  C   . GLN   A  1 211 ? -37.478 -16.282 -50.789  1.00 71.39  ? 512  GLN   A C   1 
ATOM   1656  O  O   . GLN   A  1 211 ? -38.092 -16.967 -51.616  1.00 73.29  ? 512  GLN   A O   1 
ATOM   1657  C  CB  . GLN   A  1 211 ? -38.115 -16.876 -48.445  1.00 61.97  ? 512  GLN   A CB  1 
ATOM   1658  C  CG  . GLN   A  1 211 ? -39.108 -17.990 -48.595  1.00 70.47  ? 512  GLN   A CG  1 
ATOM   1659  C  CD  . GLN   A  1 211 ? -40.517 -17.492 -48.434  1.00 82.13  ? 512  GLN   A CD  1 
ATOM   1660  O  OE1 . GLN   A  1 211 ? -40.788 -16.607 -47.620  1.00 83.65  ? 512  GLN   A OE1 1 
ATOM   1661  N  NE2 . GLN   A  1 211 ? -41.426 -18.040 -49.227  1.00 89.62  ? 512  GLN   A NE2 1 
ATOM   1662  N  N   . GLN   A  1 212 ? -37.210 -14.998 -50.987  1.00 62.40  ? 513  GLN   A N   1 
ATOM   1663  C  CA  . GLN   A  1 212 ? -37.494 -14.326 -52.239  1.00 59.22  ? 513  GLN   A CA  1 
ATOM   1664  C  C   . GLN   A  1 212 ? -36.402 -14.535 -53.271  1.00 62.18  ? 513  GLN   A C   1 
ATOM   1665  O  O   . GLN   A  1 212 ? -36.521 -14.008 -54.382  1.00 57.66  ? 513  GLN   A O   1 
ATOM   1666  C  CB  . GLN   A  1 212 ? -37.680 -12.824 -52.014  1.00 65.59  ? 513  GLN   A CB  1 
ATOM   1667  C  CG  . GLN   A  1 212 ? -38.710 -12.471 -50.959  1.00 70.63  ? 513  GLN   A CG  1 
ATOM   1668  C  CD  . GLN   A  1 212 ? -40.078 -12.997 -51.295  1.00 75.86  ? 513  GLN   A CD  1 
ATOM   1669  O  OE1 . GLN   A  1 212 ? -40.455 -13.066 -52.464  1.00 86.63  ? 513  GLN   A OE1 1 
ATOM   1670  N  NE2 . GLN   A  1 212 ? -40.834 -13.378 -50.273  1.00 77.03  ? 513  GLN   A NE2 1 
ATOM   1671  N  N   . GLY   A  1 213 ? -35.335 -15.260 -52.932  1.00 60.50  ? 514  GLY   A N   1 
ATOM   1672  C  CA  . GLY   A  1 213 ? -34.374 -15.652 -53.948  1.00 64.55  ? 514  GLY   A CA  1 
ATOM   1673  C  C   . GLY   A  1 213 ? -32.923 -15.356 -53.647  1.00 61.98  ? 514  GLY   A C   1 
ATOM   1674  O  O   . GLY   A  1 213 ? -32.032 -16.038 -54.156  1.00 67.87  ? 514  GLY   A O   1 
ATOM   1675  N  N   . TRP   A  1 214 ? -32.684 -14.346 -52.817  1.00 56.49  ? 515  TRP   A N   1 
ATOM   1676  C  CA  . TRP   A  1 214 ? -31.338 -13.912 -52.478  1.00 51.91  ? 515  TRP   A CA  1 
ATOM   1677  C  C   . TRP   A  1 214 ? -30.430 -15.089 -52.154  1.00 60.89  ? 515  TRP   A C   1 
ATOM   1678  O  O   . TRP   A  1 214 ? -30.776 -15.956 -51.348  1.00 56.84  ? 515  TRP   A O   1 
ATOM   1679  C  CB  . TRP   A  1 214 ? -31.414 -12.965 -51.286  1.00 58.28  ? 515  TRP   A CB  1 
ATOM   1680  C  CG  . TRP   A  1 214 ? -30.143 -12.251 -50.983  1.00 66.48  ? 515  TRP   A CG  1 
ATOM   1681  C  CD1 . TRP   A  1 214 ? -29.423 -11.461 -51.830  1.00 62.69  ? 515  TRP   A CD1 1 
ATOM   1682  C  CD2 . TRP   A  1 214 ? -29.450 -12.230 -49.728  1.00 59.27  ? 515  TRP   A CD2 1 
ATOM   1683  N  NE1 . TRP   A  1 214 ? -28.319 -10.965 -51.186  1.00 61.16  ? 515  TRP   A NE1 1 
ATOM   1684  C  CE2 . TRP   A  1 214 ? -28.311 -11.423 -49.896  1.00 54.43  ? 515  TRP   A CE2 1 
ATOM   1685  C  CE3 . TRP   A  1 214 ? -29.678 -12.824 -48.490  1.00 56.80  ? 515  TRP   A CE3 1 
ATOM   1686  C  CZ2 . TRP   A  1 214 ? -27.405 -11.194 -48.874  1.00 48.77  ? 515  TRP   A CZ2 1 
ATOM   1687  C  CZ3 . TRP   A  1 214 ? -28.783 -12.586 -47.476  1.00 64.26  ? 515  TRP   A CZ3 1 
ATOM   1688  C  CH2 . TRP   A  1 214 ? -27.658 -11.782 -47.673  1.00 56.90  ? 515  TRP   A CH2 1 
ATOM   1689  N  N   . LYS   A  1 215 ? -29.277 -15.130 -52.828  1.00 67.73  ? 516  LYS   A N   1 
ATOM   1690  C  CA  . LYS   A  1 215 ? -28.238 -16.107 -52.543  1.00 57.43  ? 516  LYS   A CA  1 
ATOM   1691  C  C   . LYS   A  1 215 ? -27.306 -15.489 -51.521  1.00 54.24  ? 516  LYS   A C   1 
ATOM   1692  O  O   . LYS   A  1 215 ? -26.568 -14.555 -51.863  1.00 61.02  ? 516  LYS   A O   1 
ATOM   1693  C  CB  . LYS   A  1 215 ? -27.468 -16.460 -53.801  1.00 64.74  ? 516  LYS   A CB  1 
ATOM   1694  C  CG  . LYS   A  1 215 ? -28.339 -16.875 -54.968  1.00 76.12  ? 516  LYS   A CG  1 
ATOM   1695  C  CD  . LYS   A  1 215 ? -28.458 -18.378 -55.064  1.00 75.84  ? 516  LYS   A CD  1 
ATOM   1696  C  CE  . LYS   A  1 215 ? -29.845 -18.762 -55.506  1.00 72.52  ? 516  LYS   A CE  1 
ATOM   1697  N  NZ  . LYS   A  1 215 ? -30.864 -18.294 -54.530  1.00 67.99  ? 516  LYS   A NZ  1 
ATOM   1698  N  N   . PRO   A  1 216 ? -27.309 -15.944 -50.276  1.00 60.71  ? 517  PRO   A N   1 
ATOM   1699  C  CA  . PRO   A  1 216 ? -26.559 -15.247 -49.225  1.00 56.45  ? 517  PRO   A CA  1 
ATOM   1700  C  C   . PRO   A  1 216 ? -25.117 -15.715 -49.179  1.00 57.85  ? 517  PRO   A C   1 
ATOM   1701  O  O   . PRO   A  1 216 ? -24.835 -16.908 -49.361  1.00 64.52  ? 517  PRO   A O   1 
ATOM   1702  C  CB  . PRO   A  1 216 ? -27.312 -15.640 -47.950  1.00 55.42  ? 517  PRO   A CB  1 
ATOM   1703  C  CG  . PRO   A  1 216 ? -27.826 -17.010 -48.250  1.00 58.10  ? 517  PRO   A CG  1 
ATOM   1704  C  CD  . PRO   A  1 216 ? -28.133 -17.039 -49.737  1.00 61.65  ? 517  PRO   A CD  1 
ATOM   1705  N  N   . PRO   A  1 217 ? -24.172 -14.803 -48.950  1.00 55.77  ? 518  PRO   A N   1 
ATOM   1706  C  CA  . PRO   A  1 217 ? -22.775 -15.226 -48.732  1.00 53.86  ? 518  PRO   A CA  1 
ATOM   1707  C  C   . PRO   A  1 217 ? -22.580 -16.042 -47.471  1.00 61.16  ? 518  PRO   A C   1 
ATOM   1708  O  O   . PRO   A  1 217 ? -21.614 -16.812 -47.400  1.00 52.29  ? 518  PRO   A O   1 
ATOM   1709  C  CB  . PRO   A  1 217 ? -22.010 -13.896 -48.643  1.00 49.28  ? 518  PRO   A CB  1 
ATOM   1710  C  CG  . PRO   A  1 217 ? -22.895 -12.902 -49.322  1.00 50.04  ? 518  PRO   A CG  1 
ATOM   1711  C  CD  . PRO   A  1 217 ? -24.304 -13.343 -49.055  1.00 53.27  ? 518  PRO   A CD  1 
ATOM   1712  N  N   . ARG   A  1 218 ? -23.476 -15.908 -46.492  1.00 70.96  ? 519  ARG   A N   1 
ATOM   1713  C  CA  . ARG   A  1 218 ? -23.328 -16.485 -45.156  1.00 70.84  ? 519  ARG   A CA  1 
ATOM   1714  C  C   . ARG   A  1 218 ? -21.960 -16.136 -44.570  1.00 73.84  ? 519  ARG   A C   1 
ATOM   1715  O  O   . ARG   A  1 218 ? -21.120 -16.992 -44.294  1.00 74.26  ? 519  ARG   A O   1 
ATOM   1716  C  CB  . ARG   A  1 218 ? -23.583 -17.994 -45.175  1.00 69.60  ? 519  ARG   A CB  1 
ATOM   1717  C  CG  . ARG   A  1 218 ? -25.010 -18.318 -45.586  1.00 70.30  ? 519  ARG   A CG  1 
ATOM   1718  C  CD  . ARG   A  1 218 ? -25.522 -19.660 -45.076  1.00 68.55  ? 519  ARG   A CD  1 
ATOM   1719  N  NE  . ARG   A  1 218 ? -26.953 -19.564 -44.779  1.00 81.07  ? 519  ARG   A NE  1 
ATOM   1720  C  CZ  . ARG   A  1 218 ? -27.461 -19.499 -43.549  1.00 89.18  ? 519  ARG   A CZ  1 
ATOM   1721  N  NH1 . ARG   A  1 218 ? -28.777 -19.385 -43.365  1.00 83.08  ? 519  ARG   A NH1 1 
ATOM   1722  N  NH2 . ARG   A  1 218 ? -26.647 -19.565 -42.500  1.00 91.44  ? 519  ARG   A NH2 1 
ATOM   1723  N  N   . GLY   A  1 219 ? -21.750 -14.831 -44.415  1.00 72.47  ? 520  GLY   A N   1 
ATOM   1724  C  CA  . GLY   A  1 219 ? -20.629 -14.301 -43.671  1.00 69.66  ? 520  GLY   A CA  1 
ATOM   1725  C  C   . GLY   A  1 219 ? -21.131 -13.441 -42.532  1.00 72.40  ? 520  GLY   A C   1 
ATOM   1726  O  O   . GLY   A  1 219 ? -22.318 -13.481 -42.192  1.00 73.67  ? 520  GLY   A O   1 
ATOM   1727  N  N   . ARG   A  1 220 ? -20.254 -12.642 -41.943  1.00 72.28  ? 521  ARG   A N   1 
ATOM   1728  C  CA  . ARG   A  1 220 ? -20.650 -11.837 -40.800  1.00 69.03  ? 521  ARG   A CA  1 
ATOM   1729  C  C   . ARG   A  1 220 ? -21.119 -10.446 -41.179  1.00 61.75  ? 521  ARG   A C   1 
ATOM   1730  O  O   . ARG   A  1 220 ? -21.827 -9.818  -40.391  1.00 60.36  ? 521  ARG   A O   1 
ATOM   1731  C  CB  . ARG   A  1 220 ? -19.485 -11.719 -39.812  1.00 77.54  ? 521  ARG   A CB  1 
ATOM   1732  C  CG  . ARG   A  1 220 ? -19.866 -11.206 -38.430  1.00 83.98  ? 521  ARG   A CG  1 
ATOM   1733  C  CD  . ARG   A  1 220 ? -19.111 -11.997 -37.380  1.00 88.15  ? 521  ARG   A CD  1 
ATOM   1734  N  NE  . ARG   A  1 220 ? -19.310 -11.487 -36.032  1.00 90.76  ? 521  ARG   A NE  1 
ATOM   1735  C  CZ  . ARG   A  1 220 ? -18.424 -10.745 -35.374  1.00 94.56  ? 521  ARG   A CZ  1 
ATOM   1736  N  NH1 . ARG   A  1 220 ? -17.271 -10.421 -35.950  1.00 87.12  ? 521  ARG   A NH1 1 
ATOM   1737  N  NH2 . ARG   A  1 220 ? -18.688 -10.330 -34.135  1.00 98.67  ? 521  ARG   A NH2 1 
ATOM   1738  N  N   . PHE   A  1 221 ? -20.740 -9.944  -42.348  1.00 64.69  ? 522  PHE   A N   1 
ATOM   1739  C  CA  . PHE   A  1 221 ? -20.997 -8.549  -42.691  1.00 64.01  ? 522  PHE   A CA  1 
ATOM   1740  C  C   . PHE   A  1 221 ? -21.445 -8.430  -44.145  1.00 55.68  ? 522  PHE   A C   1 
ATOM   1741  O  O   . PHE   A  1 221 ? -20.972 -7.588  -44.908  1.00 53.99  ? 522  PHE   A O   1 
ATOM   1742  C  CB  . PHE   A  1 221 ? -19.770 -7.685  -42.397  1.00 62.96  ? 522  PHE   A CB  1 
ATOM   1743  C  CG  . PHE   A  1 221 ? -19.480 -7.529  -40.920  1.00 60.35  ? 522  PHE   A CG  1 
ATOM   1744  C  CD1 . PHE   A  1 221 ? -18.212 -7.757  -40.417  1.00 63.00  ? 522  PHE   A CD1 1 
ATOM   1745  C  CD2 . PHE   A  1 221 ? -20.480 -7.157  -40.040  1.00 63.08  ? 522  PHE   A CD2 1 
ATOM   1746  C  CE1 . PHE   A  1 221 ? -17.946 -7.619  -39.057  1.00 63.47  ? 522  PHE   A CE1 1 
ATOM   1747  C  CE2 . PHE   A  1 221 ? -20.221 -7.019  -38.680  1.00 65.23  ? 522  PHE   A CE2 1 
ATOM   1748  C  CZ  . PHE   A  1 221 ? -18.958 -7.250  -38.192  1.00 61.43  ? 522  PHE   A CZ  1 
ATOM   1749  N  N   . ASP   A  1 222 ? -22.389 -9.281  -44.527  1.00 46.91  ? 523  ASP   A N   1 
ATOM   1750  C  CA  . ASP   A  1 222 ? -23.054 -9.180  -45.813  1.00 48.15  ? 523  ASP   A CA  1 
ATOM   1751  C  C   . ASP   A  1 222 ? -24.023 -8.005  -45.794  1.00 58.63  ? 523  ASP   A C   1 
ATOM   1752  O  O   . ASP   A  1 222 ? -24.854 -7.903  -44.891  1.00 73.62  ? 523  ASP   A O   1 
ATOM   1753  C  CB  . ASP   A  1 222 ? -23.792 -10.484 -46.108  1.00 36.51  ? 523  ASP   A CB  1 
ATOM   1754  C  CG  . ASP   A  1 222 ? -22.924 -11.711 -45.883  1.00 55.39  ? 523  ASP   A CG  1 
ATOM   1755  O  OD1 . ASP   A  1 222 ? -21.720 -11.572 -45.531  1.00 58.40  ? 523  ASP   A OD1 1 
ATOM   1756  O  OD2 . ASP   A  1 222 ? -23.459 -12.826 -46.040  1.00 62.86  ? 523  ASP   A OD2 1 
ATOM   1757  N  N   . VAL   A  1 223 ? -23.900 -7.100  -46.771  1.00 55.92  ? 524  VAL   A N   1 
ATOM   1758  C  CA  . VAL   A  1 223 ? -24.880 -6.026  -46.916  1.00 45.82  ? 524  VAL   A CA  1 
ATOM   1759  C  C   . VAL   A  1 223 ? -26.164 -6.609  -47.480  1.00 46.72  ? 524  VAL   A C   1 
ATOM   1760  O  O   . VAL   A  1 223 ? -26.135 -7.407  -48.427  1.00 53.72  ? 524  VAL   A O   1 
ATOM   1761  C  CB  . VAL   A  1 223 ? -24.334 -4.915  -47.826  1.00 40.09  ? 524  VAL   A CB  1 
ATOM   1762  C  CG1 . VAL   A  1 223 ? -25.247 -3.717  -47.801  1.00 40.25  ? 524  VAL   A CG1 1 
ATOM   1763  C  CG2 . VAL   A  1 223 ? -22.921 -4.544  -47.406  1.00 34.70  ? 524  VAL   A CG2 1 
ATOM   1764  N  N   . LEU   A  1 224 ? -27.292 -6.242  -46.902  1.00 34.27  ? 525  LEU   A N   1 
ATOM   1765  C  CA  . LEU   A  1 224 ? -28.495 -6.925  -47.355  1.00 39.90  ? 525  LEU   A CA  1 
ATOM   1766  C  C   . LEU   A  1 224 ? -29.002 -6.343  -48.673  1.00 47.79  ? 525  LEU   A C   1 
ATOM   1767  O  O   . LEU   A  1 224 ? -28.797 -5.164  -48.963  1.00 58.40  ? 525  LEU   A O   1 
ATOM   1768  C  CB  . LEU   A  1 224 ? -29.591 -6.826  -46.313  1.00 34.03  ? 525  LEU   A CB  1 
ATOM   1769  C  CG  . LEU   A  1 224 ? -29.502 -7.840  -45.180  1.00 42.75  ? 525  LEU   A CG  1 
ATOM   1770  C  CD1 . LEU   A  1 224 ? -30.330 -7.332  -44.026  1.00 43.67  ? 525  LEU   A CD1 1 
ATOM   1771  C  CD2 . LEU   A  1 224 ? -29.986 -9.202  -45.656  1.00 38.84  ? 525  LEU   A CD2 1 
ATOM   1772  N  N   . PRO   A  1 225 ? -29.670 -7.147  -49.488  1.00 37.83  ? 526  PRO   A N   1 
ATOM   1773  C  CA  . PRO   A  1 225 ? -30.262 -6.612  -50.711  1.00 42.27  ? 526  PRO   A CA  1 
ATOM   1774  C  C   . PRO   A  1 225 ? -31.419 -5.715  -50.358  1.00 44.86  ? 526  PRO   A C   1 
ATOM   1775  O  O   . PRO   A  1 225 ? -32.075 -5.914  -49.337  1.00 51.32  ? 526  PRO   A O   1 
ATOM   1776  C  CB  . PRO   A  1 225 ? -30.754 -7.864  -51.435  1.00 41.91  ? 526  PRO   A CB  1 
ATOM   1777  C  CG  . PRO   A  1 225 ? -31.083 -8.791  -50.313  1.00 39.08  ? 526  PRO   A CG  1 
ATOM   1778  C  CD  . PRO   A  1 225 ? -29.964 -8.577  -49.338  1.00 35.01  ? 526  PRO   A CD  1 
ATOM   1779  N  N   . LEU   A  1 226 ? -31.663 -4.716  -51.203  1.00 37.77  ? 527  LEU   A N   1 
ATOM   1780  C  CA  . LEU   A  1 226 ? -32.886 -3.942  -51.087  1.00 34.39  ? 527  LEU   A CA  1 
ATOM   1781  C  C   . LEU   A  1 226 ? -34.079 -4.794  -51.494  1.00 46.77  ? 527  LEU   A C   1 
ATOM   1782  O  O   . LEU   A  1 226 ? -33.987 -5.601  -52.423  1.00 61.58  ? 527  LEU   A O   1 
ATOM   1783  C  CB  . LEU   A  1 226 ? -32.799 -2.695  -51.955  1.00 44.81  ? 527  LEU   A CB  1 
ATOM   1784  C  CG  . LEU   A  1 226 ? -31.858 -1.655  -51.352  1.00 46.95  ? 527  LEU   A CG  1 
ATOM   1785  C  CD1 . LEU   A  1 226 ? -31.631 -0.458  -52.276  1.00 42.62  ? 527  LEU   A CD1 1 
ATOM   1786  C  CD2 . LEU   A  1 226 ? -32.472 -1.201  -50.067  1.00 41.42  ? 527  LEU   A CD2 1 
ATOM   1787  N  N   . LEU   A  1 227 ? -35.194 -4.635  -50.769  1.00 53.70  ? 528  LEU   A N   1 
ATOM   1788  C  CA  . LEU   A  1 227 ? -36.467 -5.316  -51.039  1.00 48.52  ? 528  LEU   A CA  1 
ATOM   1789  C  C   . LEU   A  1 227 ? -37.524 -4.238  -51.235  1.00 51.49  ? 528  LEU   A C   1 
ATOM   1790  O  O   . LEU   A  1 227 ? -38.043 -3.686  -50.262  1.00 48.23  ? 528  LEU   A O   1 
ATOM   1791  C  CB  . LEU   A  1 227 ? -36.866 -6.242  -49.898  1.00 47.18  ? 528  LEU   A CB  1 
ATOM   1792  C  CG  . LEU   A  1 227 ? -37.392 -7.631  -50.253  1.00 51.26  ? 528  LEU   A CG  1 
ATOM   1793  C  CD1 . LEU   A  1 227 ? -38.478 -8.003  -49.283  1.00 49.68  ? 528  LEU   A CD1 1 
ATOM   1794  C  CD2 . LEU   A  1 227 ? -37.902 -7.696  -51.674  1.00 57.69  ? 528  LEU   A CD2 1 
ATOM   1795  N  N   . LEU   A  1 228 ? -37.861 -3.942  -52.481  1.00 53.33  ? 529  LEU   A N   1 
ATOM   1796  C  CA  . LEU   A  1 228 ? -38.646 -2.762  -52.791  1.00 51.97  ? 529  LEU   A CA  1 
ATOM   1797  C  C   . LEU   A  1 228 ? -40.014 -3.149  -53.324  1.00 56.85  ? 529  LEU   A C   1 
ATOM   1798  O  O   . LEU   A  1 228 ? -40.148 -4.102  -54.103  1.00 49.63  ? 529  LEU   A O   1 
ATOM   1799  C  CB  . LEU   A  1 228 ? -37.914 -1.882  -53.797  1.00 43.52  ? 529  LEU   A CB  1 
ATOM   1800  C  CG  . LEU   A  1 228 ? -36.474 -1.662  -53.355  1.00 40.13  ? 529  LEU   A CG  1 
ATOM   1801  C  CD1 . LEU   A  1 228 ? -35.699 -1.002  -54.425  1.00 38.49  ? 529  LEU   A CD1 1 
ATOM   1802  C  CD2 . LEU   A  1 228 ? -36.450 -0.794  -52.114  1.00 42.62  ? 529  LEU   A CD2 1 
ATOM   1803  N  N   . GLN   A  1 229 ? -41.022 -2.388  -52.904  1.00 57.63  ? 530  GLN   A N   1 
ATOM   1804  C  CA  . GLN   A  1 229 ? -42.401 -2.595  -53.314  1.00 54.71  ? 530  GLN   A CA  1 
ATOM   1805  C  C   . GLN   A  1 229 ? -42.953 -1.283  -53.846  1.00 49.44  ? 530  GLN   A C   1 
ATOM   1806  O  O   . GLN   A  1 229 ? -42.831 -0.245  -53.188  1.00 44.45  ? 530  GLN   A O   1 
ATOM   1807  C  CB  . GLN   A  1 229 ? -43.237 -3.110  -52.141  1.00 50.41  ? 530  GLN   A CB  1 
ATOM   1808  C  CG  . GLN   A  1 229 ? -44.706 -2.704  -52.114  1.00 34.77  ? 530  GLN   A CG  1 
ATOM   1809  C  CD  . GLN   A  1 229 ? -45.439 -3.376  -50.978  1.00 49.56  ? 530  GLN   A CD  1 
ATOM   1810  O  OE1 . GLN   A  1 229 ? -45.184 -3.105  -49.792  1.00 59.30  ? 530  GLN   A OE1 1 
ATOM   1811  N  NE2 . GLN   A  1 229 ? -46.343 -4.276  -51.324  1.00 51.05  ? 530  GLN   A NE2 1 
ATOM   1812  N  N   . ALA   A  1 230 ? -43.549 -1.333  -55.034  1.00 53.41  ? 531  ALA   A N   1 
ATOM   1813  C  CA  . ALA   A  1 230 ? -44.201 -0.186  -55.645  1.00 50.43  ? 531  ALA   A CA  1 
ATOM   1814  C  C   . ALA   A  1 230 ? -45.651 -0.524  -55.958  1.00 52.48  ? 531  ALA   A C   1 
ATOM   1815  O  O   . ALA   A  1 230 ? -45.967 -1.656  -56.336  1.00 51.05  ? 531  ALA   A O   1 
ATOM   1816  C  CB  . ALA   A  1 230 ? -43.468 0.241   -56.914  1.00 43.82  ? 531  ALA   A CB  1 
ATOM   1817  N  N   . ASN   A  1 231 ? -46.530 0.456   -55.750  1.00 56.46  ? 532  ASN   A N   1 
ATOM   1818  C  CA  . ASN   A  1 231 ? -47.951 0.354   -56.111  1.00 55.63  ? 532  ASN   A CA  1 
ATOM   1819  C  C   . ASN   A  1 231 ? -48.607 -0.928  -55.600  1.00 56.49  ? 532  ASN   A C   1 
ATOM   1820  O  O   . ASN   A  1 231 ? -49.425 -1.540  -56.289  1.00 60.30  ? 532  ASN   A O   1 
ATOM   1821  C  CB  . ASN   A  1 231 ? -48.135 0.477   -57.626  1.00 47.89  ? 532  ASN   A CB  1 
ATOM   1822  C  CG  . ASN   A  1 231 ? -49.046 1.633   -58.007  1.00 58.42  ? 532  ASN   A CG  1 
ATOM   1823  O  OD1 . ASN   A  1 231 ? -48.851 2.768   -57.564  1.00 61.82  ? 532  ASN   A OD1 1 
ATOM   1824  N  ND2 . ASN   A  1 231 ? -50.061 1.346   -58.815  1.00 64.97  ? 532  ASN   A ND2 1 
ATOM   1825  N  N   . GLY   A  1 232 ? -48.266 -1.326  -54.373  1.00 52.77  ? 533  GLY   A N   1 
ATOM   1826  C  CA  . GLY   A  1 232 ? -48.862 -2.499  -53.745  1.00 41.79  ? 533  GLY   A CA  1 
ATOM   1827  C  C   . GLY   A  1 232 ? -48.524 -3.820  -54.396  1.00 45.70  ? 533  GLY   A C   1 
ATOM   1828  O  O   . GLY   A  1 232 ? -49.185 -4.823  -54.114  1.00 52.17  ? 533  GLY   A O   1 
ATOM   1829  N  N   . ASN   A  1 233 ? -47.531 -3.851  -55.280  1.00 49.73  ? 534  ASN   A N   1 
ATOM   1830  C  CA  . ASN   A  1 233 ? -47.123 -5.107  -55.883  1.00 47.46  ? 534  ASN   A CA  1 
ATOM   1831  C  C   . ASN   A  1 233 ? -46.140 -5.847  -54.988  1.00 43.61  ? 534  ASN   A C   1 
ATOM   1832  O  O   . ASN   A  1 233 ? -45.574 -5.287  -54.049  1.00 41.72  ? 534  ASN   A O   1 
ATOM   1833  C  CB  . ASN   A  1 233 ? -46.502 -4.861  -57.247  1.00 54.13  ? 534  ASN   A CB  1 
ATOM   1834  C  CG  . ASN   A  1 233 ? -47.528 -4.442  -58.265  1.00 63.67  ? 534  ASN   A CG  1 
ATOM   1835  O  OD1 . ASN   A  1 233 ? -48.632 -4.990  -58.295  1.00 70.95  ? 534  ASN   A OD1 1 
ATOM   1836  N  ND2 . ASN   A  1 233 ? -47.196 -3.437  -59.078  1.00 58.48  ? 534  ASN   A ND2 1 
ATOM   1837  N  N   . ASP   A  1 234 ? -45.945 -7.136  -55.289  1.00 43.84  ? 535  ASP   A N   1 
ATOM   1838  C  CA  . ASP   A  1 234 ? -45.012 -7.949  -54.512  1.00 48.86  ? 535  ASP   A CA  1 
ATOM   1839  C  C   . ASP   A  1 234 ? -43.669 -7.239  -54.504  1.00 49.53  ? 535  ASP   A C   1 
ATOM   1840  O  O   . ASP   A  1 234 ? -43.349 -6.519  -55.454  1.00 54.58  ? 535  ASP   A O   1 
ATOM   1841  C  CB  . ASP   A  1 234 ? -44.866 -9.366  -55.082  1.00 53.24  ? 535  ASP   A CB  1 
ATOM   1842  C  CG  . ASP   A  1 234 ? -46.134 -10.205 -54.917  1.00 54.46  ? 535  ASP   A CG  1 
ATOM   1843  O  OD1 . ASP   A  1 234 ? -46.166 -11.349 -55.433  1.00 54.51  ? 535  ASP   A OD1 1 
ATOM   1844  O  OD2 . ASP   A  1 234 ? -47.092 -9.719  -54.267  1.00 55.94  ? 535  ASP   A OD2 1 
ATOM   1845  N  N   . PRO   A  1 235 ? -42.883 -7.353  -53.447  1.00 50.89  ? 536  PRO   A N   1 
ATOM   1846  C  CA  . PRO   A  1 235 ? -41.593 -6.666  -53.425  1.00 50.60  ? 536  PRO   A CA  1 
ATOM   1847  C  C   . PRO   A  1 235 ? -40.570 -7.379  -54.301  1.00 47.69  ? 536  PRO   A C   1 
ATOM   1848  O  O   . PRO   A  1 235 ? -40.679 -8.572  -54.589  1.00 41.83  ? 536  PRO   A O   1 
ATOM   1849  C  CB  . PRO   A  1 235 ? -41.195 -6.702  -51.946  1.00 49.41  ? 536  PRO   A CB  1 
ATOM   1850  C  CG  . PRO   A  1 235 ? -41.892 -7.916  -51.404  1.00 53.62  ? 536  PRO   A CG  1 
ATOM   1851  C  CD  . PRO   A  1 235 ? -43.202 -7.983  -52.156  1.00 60.11  ? 536  PRO   A CD  1 
ATOM   1852  N  N   . GLU   A  1 236 ? -39.552 -6.618  -54.724  1.00 43.70  ? 537  GLU   A N   1 
ATOM   1853  C  CA  . GLU   A  1 236 ? -38.515 -7.128  -55.612  1.00 46.51  ? 537  GLU   A CA  1 
ATOM   1854  C  C   . GLU   A  1 236 ? -37.126 -6.877  -55.031  1.00 50.38  ? 537  GLU   A C   1 
ATOM   1855  O  O   . GLU   A  1 236 ? -36.894 -5.885  -54.333  1.00 49.18  ? 537  GLU   A O   1 
ATOM   1856  C  CB  . GLU   A  1 236 ? -38.638 -6.491  -57.017  1.00 44.46  ? 537  GLU   A CB  1 
ATOM   1857  C  CG  . GLU   A  1 236 ? -39.953 -6.855  -57.700  1.00 39.62  ? 537  GLU   A CG  1 
ATOM   1858  C  CD  . GLU   A  1 236 ? -40.191 -6.099  -58.985  1.00 54.70  ? 537  GLU   A CD  1 
ATOM   1859  O  OE1 . GLU   A  1 236 ? -39.361 -6.218  -59.917  1.00 61.62  ? 537  GLU   A OE1 1 
ATOM   1860  O  OE2 . GLU   A  1 236 ? -41.209 -5.377  -59.057  1.00 60.56  ? 537  GLU   A OE2 1 
ATOM   1861  N  N   . LEU   A  1 237 ? -36.202 -7.792  -55.332  1.00 48.58  ? 538  LEU   A N   1 
ATOM   1862  C  CA  . LEU   A  1 237 ? -34.839 -7.732  -54.824  1.00 51.50  ? 538  LEU   A CA  1 
ATOM   1863  C  C   . LEU   A  1 237 ? -33.936 -6.899  -55.727  1.00 57.40  ? 538  LEU   A C   1 
ATOM   1864  O  O   . LEU   A  1 237 ? -34.113 -6.852  -56.941  1.00 59.19  ? 538  LEU   A O   1 
ATOM   1865  C  CB  . LEU   A  1 237 ? -34.261 -9.139  -54.684  1.00 47.97  ? 538  LEU   A CB  1 
ATOM   1866  C  CG  . LEU   A  1 237 ? -34.868 -9.954  -53.549  1.00 48.60  ? 538  LEU   A CG  1 
ATOM   1867  C  CD1 . LEU   A  1 237 ? -34.245 -11.339 -53.452  1.00 43.76  ? 538  LEU   A CD1 1 
ATOM   1868  C  CD2 . LEU   A  1 237 ? -34.702 -9.190  -52.244  1.00 54.67  ? 538  LEU   A CD2 1 
ATOM   1869  N  N   . PHE   A  1 238 ? -32.963 -6.231  -55.112  1.00 62.80  ? 539  PHE   A N   1 
ATOM   1870  C  CA  . PHE   A  1 238 ? -31.913 -5.529  -55.836  1.00 53.70  ? 539  PHE   A CA  1 
ATOM   1871  C  C   . PHE   A  1 238 ? -30.653 -5.535  -54.985  1.00 58.19  ? 539  PHE   A C   1 
ATOM   1872  O  O   . PHE   A  1 238 ? -30.729 -5.474  -53.755  1.00 61.37  ? 539  PHE   A O   1 
ATOM   1873  C  CB  . PHE   A  1 238 ? -32.319 -4.091  -56.156  1.00 42.15  ? 539  PHE   A CB  1 
ATOM   1874  C  CG  . PHE   A  1 238 ? -33.569 -3.992  -56.943  1.00 43.95  ? 539  PHE   A CG  1 
ATOM   1875  C  CD1 . PHE   A  1 238 ? -34.778 -3.797  -56.315  1.00 42.78  ? 539  PHE   A CD1 1 
ATOM   1876  C  CD2 . PHE   A  1 238 ? -33.542 -4.143  -58.320  1.00 50.58  ? 539  PHE   A CD2 1 
ATOM   1877  C  CE1 . PHE   A  1 238 ? -35.953 -3.712  -57.032  1.00 51.28  ? 539  PHE   A CE1 1 
ATOM   1878  C  CE2 . PHE   A  1 238 ? -34.705 -4.073  -59.046  1.00 50.28  ? 539  PHE   A CE2 1 
ATOM   1879  C  CZ  . PHE   A  1 238 ? -35.922 -3.850  -58.399  1.00 54.12  ? 539  PHE   A CZ  1 
ATOM   1880  N  N   . GLN   A  1 239 ? -29.496 -5.613  -55.640  1.00 50.80  ? 540  GLN   A N   1 
ATOM   1881  C  CA  . GLN   A  1 239 ? -28.208 -5.535  -54.960  1.00 53.11  ? 540  GLN   A CA  1 
ATOM   1882  C  C   . GLN   A  1 239 ? -27.645 -4.130  -55.162  1.00 55.25  ? 540  GLN   A C   1 
ATOM   1883  O  O   . GLN   A  1 239 ? -27.268 -3.771  -56.283  1.00 60.25  ? 540  GLN   A O   1 
ATOM   1884  C  CB  . GLN   A  1 239 ? -27.246 -6.593  -55.501  1.00 54.80  ? 540  GLN   A CB  1 
ATOM   1885  C  CG  . GLN   A  1 239 ? -25.854 -6.616  -54.834  1.00 63.64  ? 540  GLN   A CG  1 
ATOM   1886  C  CD  . GLN   A  1 239 ? -24.704 -6.753  -55.840  1.00 71.31  ? 540  GLN   A CD  1 
ATOM   1887  O  OE1 . GLN   A  1 239 ? -24.519 -5.894  -56.712  1.00 87.60  ? 540  GLN   A OE1 1 
ATOM   1888  N  NE2 . GLN   A  1 239 ? -23.940 -7.836  -55.731  1.00 53.68  ? 540  GLN   A NE2 1 
ATOM   1889  N  N   . ILE   A  1 240 ? -27.612 -3.330  -54.093  1.00 45.50  ? 541  ILE   A N   1 
ATOM   1890  C  CA  . ILE   A  1 240 ? -26.928 -2.032  -54.109  1.00 41.86  ? 541  ILE   A CA  1 
ATOM   1891  C  C   . ILE   A  1 240 ? -25.510 -2.281  -54.592  1.00 51.00  ? 541  ILE   A C   1 
ATOM   1892  O  O   . ILE   A  1 240 ? -24.827 -3.149  -54.026  1.00 54.91  ? 541  ILE   A O   1 
ATOM   1893  C  CB  . ILE   A  1 240 ? -26.876 -1.365  -52.725  1.00 40.93  ? 541  ILE   A CB  1 
ATOM   1894  C  CG1 . ILE   A  1 240 ? -28.248 -1.336  -52.069  1.00 42.26  ? 541  ILE   A CG1 1 
ATOM   1895  C  CG2 . ILE   A  1 240 ? -26.337 0.046   -52.857  1.00 33.14  ? 541  ILE   A CG2 1 
ATOM   1896  C  CD1 . ILE   A  1 240 ? -28.201 -0.938  -50.633  1.00 44.01  ? 541  ILE   A CD1 1 
ATOM   1897  N  N   . PRO   A  1 241 ? -25.022 -1.581  -55.608  1.00 53.58  ? 542  PRO   A N   1 
ATOM   1898  C  CA  . PRO   A  1 241 ? -23.711 -1.914  -56.141  1.00 52.63  ? 542  PRO   A CA  1 
ATOM   1899  C  C   . PRO   A  1 241 ? -22.654 -1.675  -55.079  1.00 45.56  ? 542  PRO   A C   1 
ATOM   1900  O  O   . PRO   A  1 241 ? -22.615 -0.604  -54.454  1.00 41.98  ? 542  PRO   A O   1 
ATOM   1901  C  CB  . PRO   A  1 241 ? -23.554 -0.959  -57.337  1.00 37.52  ? 542  PRO   A CB  1 
ATOM   1902  C  CG  . PRO   A  1 241 ? -24.943 -0.526  -57.659  1.00 34.96  ? 542  PRO   A CG  1 
ATOM   1903  C  CD  . PRO   A  1 241 ? -25.601 -0.428  -56.309  1.00 41.87  ? 542  PRO   A CD  1 
ATOM   1904  N  N   . PRO   A  1 242 ? -21.798 -2.663  -54.830  1.00 36.91  ? 543  PRO   A N   1 
ATOM   1905  C  CA  . PRO   A  1 242 ? -20.894 -2.572  -53.674  1.00 46.98  ? 543  PRO   A CA  1 
ATOM   1906  C  C   . PRO   A  1 242 ? -20.058 -1.301  -53.664  1.00 56.91  ? 543  PRO   A C   1 
ATOM   1907  O  O   . PRO   A  1 242 ? -19.660 -0.833  -52.585  1.00 64.33  ? 543  PRO   A O   1 
ATOM   1908  C  CB  . PRO   A  1 242 ? -20.014 -3.823  -53.819  1.00 48.37  ? 543  PRO   A CB  1 
ATOM   1909  C  CG  . PRO   A  1 242 ? -20.750 -4.714  -54.764  1.00 49.96  ? 543  PRO   A CG  1 
ATOM   1910  C  CD  . PRO   A  1 242 ? -21.513 -3.826  -55.678  1.00 42.97  ? 543  PRO   A CD  1 
ATOM   1911  N  N   . GLU   A  1 243 ? -19.788 -0.720  -54.838  1.00 45.46  ? 544  GLU   A N   1 
ATOM   1912  C  CA  . GLU   A  1 243 ? -18.995 0.500   -54.893  1.00 45.14  ? 544  GLU   A CA  1 
ATOM   1913  C  C   . GLU   A  1 243 ? -19.726 1.700   -54.293  1.00 46.52  ? 544  GLU   A C   1 
ATOM   1914  O  O   . GLU   A  1 243 ? -19.109 2.756   -54.110  1.00 41.18  ? 544  GLU   A O   1 
ATOM   1915  C  CB  . GLU   A  1 243 ? -18.573 0.781   -56.347  1.00 43.22  ? 544  GLU   A CB  1 
ATOM   1916  C  CG  . GLU   A  1 243 ? -19.694 1.229   -57.290  1.00 42.60  ? 544  GLU   A CG  1 
ATOM   1917  C  CD  . GLU   A  1 243 ? -20.196 0.133   -58.201  1.00 51.08  ? 544  GLU   A CD  1 
ATOM   1918  O  OE1 . GLU   A  1 243 ? -19.976 -1.046  -57.879  1.00 52.49  ? 544  GLU   A OE1 1 
ATOM   1919  O  OE2 . GLU   A  1 243 ? -20.804 0.455   -59.255  1.00 64.69  ? 544  GLU   A OE2 1 
ATOM   1920  N  N   . LEU   A  1 244 ? -21.013 1.562   -53.972  1.00 44.91  ? 545  LEU   A N   1 
ATOM   1921  C  CA  . LEU   A  1 244 ? -21.797 2.641   -53.381  1.00 39.29  ? 545  LEU   A CA  1 
ATOM   1922  C  C   . LEU   A  1 244 ? -21.990 2.510   -51.869  1.00 37.40  ? 545  LEU   A C   1 
ATOM   1923  O  O   . LEU   A  1 244 ? -22.510 3.446   -51.261  1.00 37.16  ? 545  LEU   A O   1 
ATOM   1924  C  CB  . LEU   A  1 244 ? -23.189 2.716   -54.033  1.00 36.50  ? 545  LEU   A CB  1 
ATOM   1925  C  CG  . LEU   A  1 244 ? -23.446 3.187   -55.464  1.00 38.10  ? 545  LEU   A CG  1 
ATOM   1926  C  CD1 . LEU   A  1 244 ? -24.940 3.301   -55.646  1.00 33.84  ? 545  LEU   A CD1 1 
ATOM   1927  C  CD2 . LEU   A  1 244 ? -22.787 4.521   -55.712  1.00 47.28  ? 545  LEU   A CD2 1 
ATOM   1928  N  N   . VAL   A  1 245 ? -21.633 1.373   -51.263  1.00 30.47  ? 546  VAL   A N   1 
ATOM   1929  C  CA  . VAL   A  1 245 ? -21.780 1.134   -49.829  1.00 36.17  ? 546  VAL   A CA  1 
ATOM   1930  C  C   . VAL   A  1 245 ? -20.447 1.462   -49.164  1.00 41.34  ? 546  VAL   A C   1 
ATOM   1931  O  O   . VAL   A  1 245 ? -19.529 0.632   -49.146  1.00 35.94  ? 546  VAL   A O   1 
ATOM   1932  C  CB  . VAL   A  1 245 ? -22.179 -0.314  -49.543  1.00 43.36  ? 546  VAL   A CB  1 
ATOM   1933  C  CG1 . VAL   A  1 245 ? -22.405 -0.516  -48.047  1.00 46.02  ? 546  VAL   A CG1 1 
ATOM   1934  C  CG2 . VAL   A  1 245 ? -23.415 -0.689  -50.337  1.00 38.90  ? 546  VAL   A CG2 1 
ATOM   1935  N  N   . LEU   A  1 246 ? -20.315 2.661   -48.607  1.00 31.71  ? 547  LEU   A N   1 
ATOM   1936  C  CA  . LEU   A  1 246 ? -19.074 2.982   -47.910  1.00 37.68  ? 547  LEU   A CA  1 
ATOM   1937  C  C   . LEU   A  1 246 ? -19.048 2.275   -46.561  1.00 48.95  ? 547  LEU   A C   1 
ATOM   1938  O  O   . LEU   A  1 246 ? -20.067 2.191   -45.865  1.00 55.73  ? 547  LEU   A O   1 
ATOM   1939  C  CB  . LEU   A  1 246 ? -18.943 4.486   -47.721  1.00 40.98  ? 547  LEU   A CB  1 
ATOM   1940  C  CG  . LEU   A  1 246 ? -17.762 5.035   -46.936  1.00 38.35  ? 547  LEU   A CG  1 
ATOM   1941  C  CD1 . LEU   A  1 246 ? -16.491 4.462   -47.482  1.00 42.21  ? 547  LEU   A CD1 1 
ATOM   1942  C  CD2 . LEU   A  1 246 ? -17.722 6.538   -47.060  1.00 37.87  ? 547  LEU   A CD2 1 
ATOM   1943  N  N   . GLU   A  1 247 ? -17.877 1.747   -46.201  1.00 44.75  ? 548  GLU   A N   1 
ATOM   1944  C  CA  . GLU   A  1 247 ? -17.713 0.978   -44.974  1.00 43.38  ? 548  GLU   A CA  1 
ATOM   1945  C  C   . GLU   A  1 247 ? -16.409 1.379   -44.291  1.00 50.24  ? 548  GLU   A C   1 
ATOM   1946  O  O   . GLU   A  1 247 ? -15.444 1.793   -44.939  1.00 55.16  ? 548  GLU   A O   1 
ATOM   1947  C  CB  . GLU   A  1 247 ? -17.721 -0.538  -45.257  1.00 41.14  ? 548  GLU   A CB  1 
ATOM   1948  C  CG  . GLU   A  1 247 ? -19.077 -1.158  -45.593  1.00 27.56  ? 548  GLU   A CG  1 
ATOM   1949  C  CD  . GLU   A  1 247 ? -18.987 -2.683  -45.752  1.00 45.81  ? 548  GLU   A CD  1 
ATOM   1950  O  OE1 . GLU   A  1 247 ? -18.075 -3.168  -46.465  1.00 43.32  ? 548  GLU   A OE1 1 
ATOM   1951  O  OE2 . GLU   A  1 247 ? -19.816 -3.405  -45.150  1.00 49.68  ? 548  GLU   A OE2 1 
ATOM   1952  N  N   . VAL   A  1 248 ? -16.371 1.245   -42.968  1.00 51.46  ? 549  VAL   A N   1 
ATOM   1953  C  CA  . VAL   A  1 248 ? -15.216 1.648   -42.182  1.00 40.84  ? 549  VAL   A CA  1 
ATOM   1954  C  C   . VAL   A  1 248 ? -14.733 0.461   -41.361  1.00 43.13  ? 549  VAL   A C   1 
ATOM   1955  O  O   . VAL   A  1 248 ? -15.472 -0.040  -40.510  1.00 41.60  ? 549  VAL   A O   1 
ATOM   1956  C  CB  . VAL   A  1 248 ? -15.534 2.832   -41.256  1.00 39.43  ? 549  VAL   A CB  1 
ATOM   1957  C  CG1 . VAL   A  1 248 ? -14.308 3.226   -40.505  1.00 42.59  ? 549  VAL   A CG1 1 
ATOM   1958  C  CG2 . VAL   A  1 248 ? -16.087 4.002   -42.054  1.00 38.41  ? 549  VAL   A CG2 1 
ATOM   1959  N  N   . PRO   A  1 249 ? -13.506 -0.021  -41.565  1.00 38.56  ? 550  PRO   A N   1 
ATOM   1960  C  CA  . PRO   A  1 249 ? -12.976 -1.089  -40.705  1.00 43.30  ? 550  PRO   A CA  1 
ATOM   1961  C  C   . PRO   A  1 249 ? -12.606 -0.504  -39.347  1.00 54.95  ? 550  PRO   A C   1 
ATOM   1962  O  O   . PRO   A  1 249 ? -11.968 0.550   -39.275  1.00 57.95  ? 550  PRO   A O   1 
ATOM   1963  C  CB  . PRO   A  1 249 ? -11.735 -1.575  -41.466  1.00 42.73  ? 550  PRO   A CB  1 
ATOM   1964  C  CG  . PRO   A  1 249 ? -11.277 -0.354  -42.198  1.00 41.58  ? 550  PRO   A CG  1 
ATOM   1965  C  CD  . PRO   A  1 249 ? -12.527 0.433   -42.564  1.00 35.02  ? 550  PRO   A CD  1 
ATOM   1966  N  N   . ILE   A  1 250 ? -13.015 -1.179  -38.271  1.00 50.55  ? 551  ILE   A N   1 
ATOM   1967  C  CA  . ILE   A  1 250 ? -12.891 -0.628  -36.919  1.00 48.25  ? 551  ILE   A CA  1 
ATOM   1968  C  C   . ILE   A  1 250 ? -11.571 -1.086  -36.313  1.00 44.10  ? 551  ILE   A C   1 
ATOM   1969  O  O   . ILE   A  1 250 ? -11.376 -2.277  -36.039  1.00 40.92  ? 551  ILE   A O   1 
ATOM   1970  C  CB  . ILE   A  1 250 ? -14.079 -1.013  -36.028  1.00 42.46  ? 551  ILE   A CB  1 
ATOM   1971  C  CG1 . ILE   A  1 250 ? -15.384 -0.568  -36.682  1.00 41.85  ? 551  ILE   A CG1 1 
ATOM   1972  C  CG2 . ILE   A  1 250 ? -13.968 -0.343  -34.697  1.00 41.04  ? 551  ILE   A CG2 1 
ATOM   1973  C  CD1 . ILE   A  1 250 ? -15.345 0.838   -37.262  1.00 38.74  ? 551  ILE   A CD1 1 
ATOM   1974  N  N   . ARG   A  1 251 ? -10.652 -0.136  -36.133  1.00 40.57  ? 552  ARG   A N   1 
ATOM   1975  C  CA  . ARG   A  1 251 ? -9.410  -0.375  -35.419  1.00 53.47  ? 552  ARG   A CA  1 
ATOM   1976  C  C   . ARG   A  1 251 ? -9.315  0.575   -34.221  1.00 55.05  ? 552  ARG   A C   1 
ATOM   1977  O  O   . ARG   A  1 251 ? -10.062 1.552   -34.113  1.00 56.05  ? 552  ARG   A O   1 
ATOM   1978  C  CB  . ARG   A  1 251 ? -8.200  -0.233  -36.356  1.00 45.83  ? 552  ARG   A CB  1 
ATOM   1979  C  CG  . ARG   A  1 251 ? -7.991  1.153   -36.936  1.00 57.31  ? 552  ARG   A CG  1 
ATOM   1980  C  CD  . ARG   A  1 251 ? -8.757  1.334   -38.243  1.00 55.81  ? 552  ARG   A CD  1 
ATOM   1981  N  NE  . ARG   A  1 251 ? -8.360  2.538   -38.964  1.00 53.31  ? 552  ARG   A NE  1 
ATOM   1982  C  CZ  . ARG   A  1 251 ? -9.044  3.052   -39.984  1.00 62.76  ? 552  ARG   A CZ  1 
ATOM   1983  N  NH1 . ARG   A  1 251 ? -8.614  4.143   -40.592  1.00 65.52  ? 552  ARG   A NH1 1 
ATOM   1984  N  NH2 . ARG   A  1 251 ? -10.162 2.474   -40.401  1.00 54.04  ? 552  ARG   A NH2 1 
ATOM   1985  N  N   . HIS   A  1 252 ? -8.399  0.264   -33.288  1.00 55.55  ? 553  HIS   A N   1 
ATOM   1986  C  CA  . HIS   A  1 252 ? -8.264  1.051   -32.056  1.00 58.14  ? 553  HIS   A CA  1 
ATOM   1987  C  C   . HIS   A  1 252 ? -6.912  1.755   -32.021  1.00 61.92  ? 553  HIS   A C   1 
ATOM   1988  O  O   . HIS   A  1 252 ? -5.911  1.178   -32.458  1.00 68.11  ? 553  HIS   A O   1 
ATOM   1989  C  CB  . HIS   A  1 252 ? -8.408  0.161   -30.811  1.00 50.79  ? 553  HIS   A CB  1 
ATOM   1990  C  CG  . HIS   A  1 252 ? -8.546  0.918   -29.525  1.00 49.74  ? 553  HIS   A CG  1 
ATOM   1991  N  ND1 . HIS   A  1 252 ? -7.464  1.395   -28.816  1.00 46.95  ? 553  HIS   A ND1 1 
ATOM   1992  C  CD2 . HIS   A  1 252 ? -9.641  1.253   -28.805  1.00 48.72  ? 553  HIS   A CD2 1 
ATOM   1993  C  CE1 . HIS   A  1 252 ? -7.889  2.021   -27.734  1.00 41.40  ? 553  HIS   A CE1 1 
ATOM   1994  N  NE2 . HIS   A  1 252 ? -9.207  1.951   -27.704  1.00 45.10  ? 553  HIS   A NE2 1 
ATOM   1995  N  N   . PRO   A  1 253 ? -6.845  2.996   -31.523  1.00 58.97  ? 554  PRO   A N   1 
ATOM   1996  C  CA  . PRO   A  1 253 ? -5.586  3.757   -31.600  1.00 51.84  ? 554  PRO   A CA  1 
ATOM   1997  C  C   . PRO   A  1 253 ? -4.538  3.316   -30.612  1.00 63.81  ? 554  PRO   A C   1 
ATOM   1998  O  O   . PRO   A  1 253 ? -3.378  3.725   -30.741  1.00 70.99  ? 554  PRO   A O   1 
ATOM   1999  C  CB  . PRO   A  1 253 ? -6.023  5.190   -31.296  1.00 45.45  ? 554  PRO   A CB  1 
ATOM   2000  C  CG  . PRO   A  1 253 ? -7.235  5.013   -30.423  1.00 50.10  ? 554  PRO   A CG  1 
ATOM   2001  C  CD  . PRO   A  1 253 ? -7.943  3.792   -30.943  1.00 50.14  ? 554  PRO   A CD  1 
ATOM   2002  N  N   . LYS   A  1 254 ? -4.902  2.515   -29.628  1.00 68.37  ? 555  LYS   A N   1 
ATOM   2003  C  CA  . LYS   A  1 254 ? -3.957  2.030   -28.644  1.00 72.06  ? 555  LYS   A CA  1 
ATOM   2004  C  C   . LYS   A  1 254 ? -3.795  0.525   -28.662  1.00 67.74  ? 555  LYS   A C   1 
ATOM   2005  O  O   . LYS   A  1 254 ? -2.708  0.036   -28.355  1.00 73.89  ? 555  LYS   A O   1 
ATOM   2006  C  CB  . LYS   A  1 254 ? -4.381  2.469   -27.231  1.00 79.89  ? 555  LYS   A CB  1 
ATOM   2007  C  CG  . LYS   A  1 254 ? -3.980  3.891   -26.865  1.00 88.03  ? 555  LYS   A CG  1 
ATOM   2008  C  CD  . LYS   A  1 254 ? -2.914  3.884   -25.769  1.00 105.47 ? 555  LYS   A CD  1 
ATOM   2009  C  CE  . LYS   A  1 254 ? -1.540  3.428   -26.278  1.00 112.15 ? 555  LYS   A CE  1 
ATOM   2010  N  NZ  . LYS   A  1 254 ? -0.918  4.442   -27.176  1.00 113.49 ? 555  LYS   A NZ  1 
ATOM   2011  N  N   . PHE   A  1 255 ? -4.832  -0.222  -29.017  1.00 62.23  ? 556  PHE   A N   1 
ATOM   2012  C  CA  . PHE   A  1 255 ? -4.804  -1.678  -28.911  1.00 65.92  ? 556  PHE   A CA  1 
ATOM   2013  C  C   . PHE   A  1 255 ? -4.517  -2.257  -30.293  1.00 64.75  ? 556  PHE   A C   1 
ATOM   2014  O  O   . PHE   A  1 255 ? -5.402  -2.333  -31.150  1.00 63.37  ? 556  PHE   A O   1 
ATOM   2015  C  CB  . PHE   A  1 255 ? -6.109  -2.208  -28.321  1.00 67.91  ? 556  PHE   A CB  1 
ATOM   2016  C  CG  . PHE   A  1 255 ? -6.331  -1.815  -26.880  1.00 69.55  ? 556  PHE   A CG  1 
ATOM   2017  C  CD1 . PHE   A  1 255 ? -7.581  -1.908  -26.305  1.00 62.74  ? 556  PHE   A CD1 1 
ATOM   2018  C  CD2 . PHE   A  1 255 ? -5.290  -1.340  -26.110  1.00 74.13  ? 556  PHE   A CD2 1 
ATOM   2019  C  CE1 . PHE   A  1 255 ? -7.784  -1.539  -25.007  1.00 64.67  ? 556  PHE   A CE1 1 
ATOM   2020  C  CE2 . PHE   A  1 255 ? -5.494  -0.970  -24.805  1.00 70.79  ? 556  PHE   A CE2 1 
ATOM   2021  C  CZ  . PHE   A  1 255 ? -6.738  -1.076  -24.255  1.00 69.14  ? 556  PHE   A CZ  1 
ATOM   2022  N  N   . GLU   A  1 256 ? -3.263  -2.660  -30.497  1.00 70.19  ? 557  GLU   A N   1 
ATOM   2023  C  CA  . GLU   A  1 256 ? -2.869  -3.340  -31.725  1.00 69.34  ? 557  GLU   A CA  1 
ATOM   2024  C  C   . GLU   A  1 256 ? -3.803  -4.493  -32.051  1.00 66.03  ? 557  GLU   A C   1 
ATOM   2025  O  O   . GLU   A  1 256 ? -4.075  -4.771  -33.218  1.00 75.35  ? 557  GLU   A O   1 
ATOM   2026  C  CB  . GLU   A  1 256 ? -1.444  -3.863  -31.580  1.00 82.48  ? 557  GLU   A CB  1 
ATOM   2027  C  CG  . GLU   A  1 256 ? -0.371  -2.910  -32.008  1.00 96.47  ? 557  GLU   A CG  1 
ATOM   2028  C  CD  . GLU   A  1 256 ? 0.064   -3.179  -33.430  1.00 118.46 ? 557  GLU   A CD  1 
ATOM   2029  O  OE1 . GLU   A  1 256 ? -0.741  -2.935  -34.365  1.00 124.11 ? 557  GLU   A OE1 1 
ATOM   2030  O  OE2 . GLU   A  1 256 ? 1.204   -3.663  -33.609  1.00 125.79 ? 557  GLU   A OE2 1 
ATOM   2031  N  N   . TRP   A  1 257 ? -4.292  -5.187  -31.028  1.00 71.11  ? 558  TRP   A N   1 
ATOM   2032  C  CA  . TRP   A  1 257 ? -5.087  -6.390  -31.229  1.00 66.28  ? 558  TRP   A CA  1 
ATOM   2033  C  C   . TRP   A  1 257 ? -6.492  -6.102  -31.724  1.00 60.69  ? 558  TRP   A C   1 
ATOM   2034  O  O   . TRP   A  1 257 ? -7.182  -7.046  -32.118  1.00 58.47  ? 558  TRP   A O   1 
ATOM   2035  C  CB  . TRP   A  1 257 ? -5.169  -7.192  -29.917  1.00 71.00  ? 558  TRP   A CB  1 
ATOM   2036  C  CG  . TRP   A  1 257 ? -5.676  -6.415  -28.724  1.00 68.86  ? 558  TRP   A CG  1 
ATOM   2037  C  CD1 . TRP   A  1 257 ? -4.921  -5.737  -27.803  1.00 79.73  ? 558  TRP   A CD1 1 
ATOM   2038  C  CD2 . TRP   A  1 257 ? -7.043  -6.248  -28.318  1.00 74.29  ? 558  TRP   A CD2 1 
ATOM   2039  N  NE1 . TRP   A  1 257 ? -5.735  -5.154  -26.854  1.00 88.29  ? 558  TRP   A NE1 1 
ATOM   2040  C  CE2 . TRP   A  1 257 ? -7.041  -5.450  -27.147  1.00 80.82  ? 558  TRP   A CE2 1 
ATOM   2041  C  CE3 . TRP   A  1 257 ? -8.270  -6.688  -28.833  1.00 70.20  ? 558  TRP   A CE3 1 
ATOM   2042  C  CZ2 . TRP   A  1 257 ? -8.215  -5.091  -26.479  1.00 70.67  ? 558  TRP   A CZ2 1 
ATOM   2043  C  CZ3 . TRP   A  1 257 ? -9.437  -6.318  -28.177  1.00 70.16  ? 558  TRP   A CZ3 1 
ATOM   2044  C  CH2 . TRP   A  1 257 ? -9.400  -5.531  -27.006  1.00 70.30  ? 558  TRP   A CH2 1 
ATOM   2045  N  N   . PHE   A  1 258 ? -6.938  -4.841  -31.705  1.00 59.83  ? 559  PHE   A N   1 
ATOM   2046  C  CA  . PHE   A  1 258 ? -8.359  -4.564  -31.909  1.00 57.71  ? 559  PHE   A CA  1 
ATOM   2047  C  C   . PHE   A  1 258 ? -8.791  -4.888  -33.333  1.00 58.34  ? 559  PHE   A C   1 
ATOM   2048  O  O   . PHE   A  1 258 ? -9.859  -5.481  -33.537  1.00 55.46  ? 559  PHE   A O   1 
ATOM   2049  C  CB  . PHE   A  1 258 ? -8.675  -3.110  -31.575  1.00 56.16  ? 559  PHE   A CB  1 
ATOM   2050  C  CG  . PHE   A  1 258 ? -10.125 -2.862  -31.246  1.00 57.55  ? 559  PHE   A CG  1 
ATOM   2051  C  CD1 . PHE   A  1 258 ? -10.526 -2.581  -29.946  1.00 59.54  ? 559  PHE   A CD1 1 
ATOM   2052  C  CD2 . PHE   A  1 258 ? -11.090 -2.900  -32.235  1.00 56.72  ? 559  PHE   A CD2 1 
ATOM   2053  C  CE1 . PHE   A  1 258 ? -11.860 -2.352  -29.651  1.00 54.09  ? 559  PHE   A CE1 1 
ATOM   2054  C  CE2 . PHE   A  1 258 ? -12.411 -2.674  -31.942  1.00 50.71  ? 559  PHE   A CE2 1 
ATOM   2055  C  CZ  . PHE   A  1 258 ? -12.798 -2.408  -30.660  1.00 52.73  ? 559  PHE   A CZ  1 
ATOM   2056  N  N   . LYS   A  1 259 ? -7.971  -4.504  -34.321  1.00 51.86  ? 560  LYS   A N   1 
ATOM   2057  C  CA  . LYS   A  1 259 ? -8.260  -4.789  -35.726  1.00 55.95  ? 560  LYS   A CA  1 
ATOM   2058  C  C   . LYS   A  1 259 ? -8.498  -6.273  -35.978  1.00 60.84  ? 560  LYS   A C   1 
ATOM   2059  O  O   . LYS   A  1 259 ? -9.200  -6.639  -36.931  1.00 59.40  ? 560  LYS   A O   1 
ATOM   2060  C  CB  . LYS   A  1 259 ? -7.115  -4.291  -36.616  1.00 58.41  ? 560  LYS   A CB  1 
ATOM   2061  C  CG  . LYS   A  1 259 ? -5.736  -4.830  -36.233  1.00 60.38  ? 560  LYS   A CG  1 
ATOM   2062  C  CD  . LYS   A  1 259 ? -4.682  -4.595  -37.328  1.00 68.73  ? 560  LYS   A CD  1 
ATOM   2063  C  CE  . LYS   A  1 259 ? -3.310  -5.188  -36.944  1.00 66.14  ? 560  LYS   A CE  1 
ATOM   2064  N  NZ  . LYS   A  1 259 ? -2.673  -4.514  -35.761  1.00 63.69  ? 560  LYS   A NZ  1 
ATOM   2065  N  N   . ASP   A  1 260 ? -7.916  -7.140  -35.147  1.00 58.40  ? 561  ASP   A N   1 
ATOM   2066  C  CA  . ASP   A  1 260 ? -8.103  -8.581  -35.274  1.00 66.97  ? 561  ASP   A CA  1 
ATOM   2067  C  C   . ASP   A  1 260 ? -9.476  -9.036  -34.802  1.00 65.25  ? 561  ASP   A C   1 
ATOM   2068  O  O   . ASP   A  1 260 ? -9.804  -10.223 -34.935  1.00 61.52  ? 561  ASP   A O   1 
ATOM   2069  C  CB  . ASP   A  1 260 ? -7.014  -9.326  -34.492  1.00 73.15  ? 561  ASP   A CB  1 
ATOM   2070  C  CG  . ASP   A  1 260 ? -5.616  -8.822  -34.818  1.00 86.29  ? 561  ASP   A CG  1 
ATOM   2071  O  OD1 . ASP   A  1 260 ? -5.397  -8.374  -35.971  1.00 94.00  ? 561  ASP   A OD1 1 
ATOM   2072  O  OD2 . ASP   A  1 260 ? -4.741  -8.866  -33.922  1.00 86.14  ? 561  ASP   A OD2 1 
ATOM   2073  N  N   . LEU   A  1 261 ? -10.282 -8.137  -34.238  1.00 58.41  ? 562  LEU   A N   1 
ATOM   2074  C  CA  . LEU   A  1 261 ? -11.656 -8.516  -33.965  1.00 56.55  ? 562  LEU   A CA  1 
ATOM   2075  C  C   . LEU   A  1 261 ? -12.445 -8.693  -35.263  1.00 69.05  ? 562  LEU   A C   1 
ATOM   2076  O  O   . LEU   A  1 261 ? -13.452 -9.410  -35.268  1.00 78.47  ? 562  LEU   A O   1 
ATOM   2077  C  CB  . LEU   A  1 261 ? -12.296 -7.485  -33.032  1.00 39.55  ? 562  LEU   A CB  1 
ATOM   2078  C  CG  . LEU   A  1 261 ? -11.628 -7.444  -31.657  1.00 54.19  ? 562  LEU   A CG  1 
ATOM   2079  C  CD1 . LEU   A  1 261 ? -11.946 -6.150  -30.937  1.00 57.61  ? 562  LEU   A CD1 1 
ATOM   2080  C  CD2 . LEU   A  1 261 ? -12.076 -8.619  -30.805  1.00 57.09  ? 562  LEU   A CD2 1 
ATOM   2081  N  N   . GLY   A  1 262 ? -11.988 -8.088  -36.366  1.00 65.39  ? 563  GLY   A N   1 
ATOM   2082  C  CA  . GLY   A  1 262 ? -12.609 -8.267  -37.666  1.00 50.50  ? 563  GLY   A CA  1 
ATOM   2083  C  C   . GLY   A  1 262 ? -13.813 -7.388  -37.932  1.00 60.63  ? 563  GLY   A C   1 
ATOM   2084  O  O   . GLY   A  1 262 ? -14.595 -7.667  -38.848  1.00 61.88  ? 563  GLY   A O   1 
ATOM   2085  N  N   . LEU   A  1 263 ? -13.991 -6.329  -37.166  1.00 60.89  ? 564  LEU   A N   1 
ATOM   2086  C  CA  . LEU   A  1 263 ? -15.228 -5.578  -37.222  1.00 56.77  ? 564  LEU   A CA  1 
ATOM   2087  C  C   . LEU   A  1 263 ? -15.119 -4.425  -38.205  1.00 60.04  ? 564  LEU   A C   1 
ATOM   2088  O  O   . LEU   A  1 263 ? -14.047 -3.841  -38.400  1.00 54.29  ? 564  LEU   A O   1 
ATOM   2089  C  CB  . LEU   A  1 263 ? -15.603 -5.047  -35.838  1.00 49.40  ? 564  LEU   A CB  1 
ATOM   2090  C  CG  . LEU   A  1 263 ? -15.481 -6.039  -34.678  1.00 54.09  ? 564  LEU   A CG  1 
ATOM   2091  C  CD1 . LEU   A  1 263 ? -15.488 -5.263  -33.388  1.00 52.47  ? 564  LEU   A CD1 1 
ATOM   2092  C  CD2 . LEU   A  1 263 ? -16.582 -7.094  -34.668  1.00 51.44  ? 564  LEU   A CD2 1 
ATOM   2093  N  N   . LYS   A  1 264 ? -16.260 -4.118  -38.824  1.00 65.18  ? 565  LYS   A N   1 
ATOM   2094  C  CA  . LYS   A  1 264 ? -16.468 -2.951  -39.669  1.00 55.46  ? 565  LYS   A CA  1 
ATOM   2095  C  C   . LYS   A  1 264 ? -17.914 -2.507  -39.501  1.00 54.47  ? 565  LYS   A C   1 
ATOM   2096  O  O   . LYS   A  1 264 ? -18.755 -3.247  -38.981  1.00 59.00  ? 565  LYS   A O   1 
ATOM   2097  C  CB  . LYS   A  1 264 ? -16.170 -3.249  -41.140  1.00 57.21  ? 565  LYS   A CB  1 
ATOM   2098  C  CG  . LYS   A  1 264 ? -16.944 -4.450  -41.719  1.00 55.29  ? 565  LYS   A CG  1 
ATOM   2099  C  CD  . LYS   A  1 264 ? -16.720 -4.599  -43.217  1.00 47.56  ? 565  LYS   A CD  1 
ATOM   2100  C  CE  . LYS   A  1 264 ? -16.953 -6.036  -43.697  1.00 57.18  ? 565  LYS   A CE  1 
ATOM   2101  N  NZ  . LYS   A  1 264 ? -17.671 -6.083  -45.023  1.00 66.00  ? 565  LYS   A NZ  1 
ATOM   2102  N  N   . TRP   A  1 265 ? -18.201 -1.282  -39.922  1.00 48.55  ? 566  TRP   A N   1 
ATOM   2103  C  CA  . TRP   A  1 265 ? -19.586 -0.838  -39.970  1.00 51.37  ? 566  TRP   A CA  1 
ATOM   2104  C  C   . TRP   A  1 265 ? -19.810 -0.072  -41.269  1.00 54.26  ? 566  TRP   A C   1 
ATOM   2105  O  O   . TRP   A  1 265 ? -18.864 0.401   -41.909  1.00 57.37  ? 566  TRP   A O   1 
ATOM   2106  C  CB  . TRP   A  1 265 ? -19.965 0.022   -38.751  1.00 33.22  ? 566  TRP   A CB  1 
ATOM   2107  C  CG  . TRP   A  1 265 ? -21.419 -0.038  -38.443  1.00 34.77  ? 566  TRP   A CG  1 
ATOM   2108  C  CD1 . TRP   A  1 265 ? -22.318 1.001   -38.469  1.00 37.64  ? 566  TRP   A CD1 1 
ATOM   2109  C  CD2 . TRP   A  1 265 ? -22.166 -1.203  -38.082  1.00 34.70  ? 566  TRP   A CD2 1 
ATOM   2110  N  NE1 . TRP   A  1 265 ? -23.591 0.546   -38.144  1.00 29.82  ? 566  TRP   A NE1 1 
ATOM   2111  C  CE2 . TRP   A  1 265 ? -23.519 -0.802  -37.898  1.00 32.59  ? 566  TRP   A CE2 1 
ATOM   2112  C  CE3 . TRP   A  1 265 ? -21.825 -2.544  -37.880  1.00 41.62  ? 566  TRP   A CE3 1 
ATOM   2113  C  CZ2 . TRP   A  1 265 ? -24.520 -1.697  -37.532  1.00 33.77  ? 566  TRP   A CZ2 1 
ATOM   2114  C  CZ3 . TRP   A  1 265 ? -22.820 -3.433  -37.505  1.00 48.28  ? 566  TRP   A CZ3 1 
ATOM   2115  C  CH2 . TRP   A  1 265 ? -24.155 -3.005  -37.336  1.00 50.59  ? 566  TRP   A CH2 1 
ATOM   2116  N  N   . TYR   A  1 266 ? -21.076 0.024   -41.668  1.00 43.27  ? 567  TYR   A N   1 
ATOM   2117  C  CA  . TYR   A  1 266 ? -21.409 0.906   -42.771  1.00 39.58  ? 567  TYR   A CA  1 
ATOM   2118  C  C   . TYR   A  1 266 ? -21.377 2.361   -42.321  1.00 43.36  ? 567  TYR   A C   1 
ATOM   2119  O  O   . TYR   A  1 266 ? -21.480 2.671   -41.135  1.00 50.92  ? 567  TYR   A O   1 
ATOM   2120  C  CB  . TYR   A  1 266 ? -22.778 0.575   -43.344  1.00 31.74  ? 567  TYR   A CB  1 
ATOM   2121  C  CG  . TYR   A  1 266 ? -23.859 0.329   -42.337  1.00 41.82  ? 567  TYR   A CG  1 
ATOM   2122  C  CD1 . TYR   A  1 266 ? -24.751 1.328   -41.993  1.00 48.77  ? 567  TYR   A CD1 1 
ATOM   2123  C  CD2 . TYR   A  1 266 ? -24.005 -0.911  -41.745  1.00 46.25  ? 567  TYR   A CD2 1 
ATOM   2124  C  CE1 . TYR   A  1 266 ? -25.750 1.094   -41.080  1.00 51.07  ? 567  TYR   A CE1 1 
ATOM   2125  C  CE2 . TYR   A  1 266 ? -25.002 -1.157  -40.845  1.00 46.58  ? 567  TYR   A CE2 1 
ATOM   2126  C  CZ  . TYR   A  1 266 ? -25.872 -0.150  -40.505  1.00 55.30  ? 567  TYR   A CZ  1 
ATOM   2127  O  OH  . TYR   A  1 266 ? -26.875 -0.393  -39.588  1.00 61.47  ? 567  TYR   A OH  1 
ATOM   2128  N  N   . GLY   A  1 267 ? -21.226 3.262   -43.285  1.00 43.14  ? 568  GLY   A N   1 
ATOM   2129  C  CA  . GLY   A  1 267 ? -21.002 4.658   -42.975  1.00 36.39  ? 568  GLY   A CA  1 
ATOM   2130  C  C   . GLY   A  1 267 ? -22.235 5.522   -42.986  1.00 37.46  ? 568  GLY   A C   1 
ATOM   2131  O  O   . GLY   A  1 267 ? -22.175 6.677   -42.553  1.00 43.12  ? 568  GLY   A O   1 
ATOM   2132  N  N   . LEU   A  1 268 ? -23.361 5.003   -43.453  1.00 36.20  ? 569  LEU   A N   1 
ATOM   2133  C  CA  . LEU   A  1 268 ? -24.512 5.831   -43.797  1.00 42.65  ? 569  LEU   A CA  1 
ATOM   2134  C  C   . LEU   A  1 268 ? -25.734 5.286   -43.085  1.00 44.87  ? 569  LEU   A C   1 
ATOM   2135  O  O   . LEU   A  1 268 ? -26.261 4.225   -43.483  1.00 41.27  ? 569  LEU   A O   1 
ATOM   2136  C  CB  . LEU   A  1 268 ? -24.753 5.868   -45.309  1.00 39.21  ? 569  LEU   A CB  1 
ATOM   2137  C  CG  . LEU   A  1 268 ? -25.958 6.701   -45.776  1.00 38.43  ? 569  LEU   A CG  1 
ATOM   2138  C  CD1 . LEU   A  1 268 ? -25.625 8.186   -45.857  1.00 36.75  ? 569  LEU   A CD1 1 
ATOM   2139  C  CD2 . LEU   A  1 268 ? -26.504 6.198   -47.113  1.00 24.66  ? 569  LEU   A CD2 1 
ATOM   2140  N  N   . PRO   A  1 269 ? -26.206 5.950   -42.030  1.00 45.43  ? 570  PRO   A N   1 
ATOM   2141  C  CA  . PRO   A  1 269 ? -27.471 5.545   -41.409  1.00 38.02  ? 570  PRO   A CA  1 
ATOM   2142  C  C   . PRO   A  1 269 ? -28.603 6.092   -42.256  1.00 39.84  ? 570  PRO   A C   1 
ATOM   2143  O  O   . PRO   A  1 269 ? -28.673 7.296   -42.499  1.00 38.17  ? 570  PRO   A O   1 
ATOM   2144  C  CB  . PRO   A  1 269 ? -27.423 6.215   -40.036  1.00 20.74  ? 570  PRO   A CB  1 
ATOM   2145  C  CG  . PRO   A  1 269 ? -26.552 7.428   -40.239  1.00 27.47  ? 570  PRO   A CG  1 
ATOM   2146  C  CD  . PRO   A  1 269 ? -25.554 7.069   -41.324  1.00 39.02  ? 570  PRO   A CD  1 
ATOM   2147  N  N   . ALA   A  1 270 ? -29.478 5.212   -42.723  1.00 40.66  ? 571  ALA   A N   1 
ATOM   2148  C  CA  . ALA   A  1 270 ? -30.548 5.640   -43.617  1.00 42.71  ? 571  ALA   A CA  1 
ATOM   2149  C  C   . ALA   A  1 270 ? -31.798 4.848   -43.264  1.00 42.87  ? 571  ALA   A C   1 
ATOM   2150  O  O   . ALA   A  1 270 ? -31.905 3.666   -43.597  1.00 47.34  ? 571  ALA   A O   1 
ATOM   2151  C  CB  . ALA   A  1 270 ? -30.145 5.448   -45.070  1.00 38.51  ? 571  ALA   A CB  1 
ATOM   2152  N  N   . VAL   A  1 271 ? -32.737 5.498   -42.598  1.00 37.26  ? 572  VAL   A N   1 
ATOM   2153  C  CA  . VAL   A  1 271 ? -33.931 4.819   -42.114  1.00 37.57  ? 572  VAL   A CA  1 
ATOM   2154  C  C   . VAL   A  1 271 ? -34.985 4.850   -43.208  1.00 36.54  ? 572  VAL   A C   1 
ATOM   2155  O  O   . VAL   A  1 271 ? -35.272 5.913   -43.777  1.00 40.64  ? 572  VAL   A O   1 
ATOM   2156  C  CB  . VAL   A  1 271 ? -34.442 5.469   -40.820  1.00 42.56  ? 572  VAL   A CB  1 
ATOM   2157  C  CG1 . VAL   A  1 271 ? -35.960 5.361   -40.712  1.00 36.92  ? 572  VAL   A CG1 1 
ATOM   2158  C  CG2 . VAL   A  1 271 ? -33.800 4.792   -39.656  1.00 41.87  ? 572  VAL   A CG2 1 
ATOM   2159  N  N   . SER   A  1 272 ? -35.580 3.684   -43.484  1.00 29.18  ? 573  SER   A N   1 
ATOM   2160  C  CA  . SER   A  1 272 ? -36.483 3.497   -44.609  1.00 35.43  ? 573  SER   A CA  1 
ATOM   2161  C  C   . SER   A  1 272 ? -37.813 2.833   -44.264  1.00 51.19  ? 573  SER   A C   1 
ATOM   2162  O  O   . SER   A  1 272 ? -38.565 2.486   -45.187  1.00 59.69  ? 573  SER   A O   1 
ATOM   2163  C  CB  . SER   A  1 272 ? -35.791 2.673   -45.704  1.00 37.64  ? 573  SER   A CB  1 
ATOM   2164  O  OG  . SER   A  1 272 ? -35.237 1.476   -45.183  1.00 31.40  ? 573  SER   A OG  1 
ATOM   2165  N  N   . ASN   A  1 273 ? -38.142 2.646   -42.982  1.00 47.30  ? 574  ASN   A N   1 
ATOM   2166  C  CA  . ASN   A  1 273 ? -39.342 1.896   -42.628  1.00 31.31  ? 574  ASN   A CA  1 
ATOM   2167  C  C   . ASN   A  1 273 ? -40.386 2.745   -41.921  1.00 37.68  ? 574  ASN   A C   1 
ATOM   2168  O  O   . ASN   A  1 273 ? -41.346 2.190   -41.372  1.00 43.14  ? 574  ASN   A O   1 
ATOM   2169  C  CB  . ASN   A  1 273 ? -38.987 0.687   -41.763  1.00 29.12  ? 574  ASN   A CB  1 
ATOM   2170  C  CG  . ASN   A  1 273 ? -38.373 1.088   -40.432  1.00 44.68  ? 574  ASN   A CG  1 
ATOM   2171  O  OD1 . ASN   A  1 273 ? -38.193 2.276   -40.144  1.00 49.38  ? 574  ASN   A OD1 1 
ATOM   2172  N  ND2 . ASN   A  1 273 ? -38.044 0.092   -39.608  1.00 40.29  ? 574  ASN   A ND2 1 
ATOM   2173  N  N   . MET   A  1 274 ? -40.226 4.063   -41.923  1.00 33.66  ? 575  MET   A N   1 
ATOM   2174  C  CA  . MET   A  1 274 ? -41.149 4.989   -41.290  1.00 36.39  ? 575  MET   A CA  1 
ATOM   2175  C  C   . MET   A  1 274 ? -42.000 5.702   -42.332  1.00 47.32  ? 575  MET   A C   1 
ATOM   2176  O  O   . MET   A  1 274 ? -41.741 5.648   -43.535  1.00 62.85  ? 575  MET   A O   1 
ATOM   2177  C  CB  . MET   A  1 274 ? -40.382 6.003   -40.441  1.00 34.66  ? 575  MET   A CB  1 
ATOM   2178  C  CG  . MET   A  1 274 ? -39.803 5.376   -39.156  1.00 43.96  ? 575  MET   A CG  1 
ATOM   2179  S  SD  . MET   A  1 274 ? -38.941 6.568   -38.128  1.00 46.65  ? 575  MET   A SD  1 
ATOM   2180  C  CE  . MET   A  1 274 ? -40.307 7.510   -37.481  1.00 43.93  ? 575  MET   A CE  1 
ATOM   2181  N  N   . LEU   A  1 275 ? -43.018 6.405   -41.849  1.00 43.64  ? 576  LEU   A N   1 
ATOM   2182  C  CA  . LEU   A  1 275 ? -44.028 6.996   -42.706  1.00 38.25  ? 576  LEU   A CA  1 
ATOM   2183  C  C   . LEU   A  1 275 ? -43.970 8.501   -42.551  1.00 43.22  ? 576  LEU   A C   1 
ATOM   2184  O  O   . LEU   A  1 275 ? -44.075 9.004   -41.436  1.00 43.15  ? 576  LEU   A O   1 
ATOM   2185  C  CB  . LEU   A  1 275 ? -45.422 6.464   -42.344  1.00 38.23  ? 576  LEU   A CB  1 
ATOM   2186  C  CG  . LEU   A  1 275 ? -46.592 6.814   -43.279  1.00 37.77  ? 576  LEU   A CG  1 
ATOM   2187  C  CD1 . LEU   A  1 275 ? -47.571 5.668   -43.419  1.00 35.95  ? 576  LEU   A CD1 1 
ATOM   2188  C  CD2 . LEU   A  1 275 ? -47.319 8.042   -42.800  1.00 29.69  ? 576  LEU   A CD2 1 
ATOM   2189  N  N   . LEU   A  1 276 ? -43.812 9.223   -43.664  1.00 48.86  ? 577  LEU   A N   1 
ATOM   2190  C  CA  . LEU   A  1 276 ? -43.798 10.685  -43.633  1.00 39.39  ? 577  LEU   A CA  1 
ATOM   2191  C  C   . LEU   A  1 276 ? -45.215 11.201  -43.839  1.00 48.54  ? 577  LEU   A C   1 
ATOM   2192  O  O   . LEU   A  1 276 ? -45.904 10.773  -44.767  1.00 47.00  ? 577  LEU   A O   1 
ATOM   2193  C  CB  . LEU   A  1 276 ? -42.862 11.253  -44.696  1.00 37.13  ? 577  LEU   A CB  1 
ATOM   2194  C  CG  . LEU   A  1 276 ? -43.003 12.764  -44.914  1.00 37.57  ? 577  LEU   A CG  1 
ATOM   2195  C  CD1 . LEU   A  1 276 ? -42.450 13.485  -43.732  1.00 28.73  ? 577  LEU   A CD1 1 
ATOM   2196  C  CD2 . LEU   A  1 276 ? -42.290 13.233  -46.210  1.00 22.88  ? 577  LEU   A CD2 1 
ATOM   2197  N  N   . GLU   A  1 277 ? -45.669 12.085  -42.952  1.00 51.57  ? 578  GLU   A N   1 
ATOM   2198  C  CA  . GLU   A  1 277 ? -47.041 12.575  -43.008  1.00 45.45  ? 578  GLU   A CA  1 
ATOM   2199  C  C   . GLU   A  1 277 ? -47.050 14.095  -43.078  1.00 43.69  ? 578  GLU   A C   1 
ATOM   2200  O  O   . GLU   A  1 277 ? -46.672 14.767  -42.118  1.00 45.87  ? 578  GLU   A O   1 
ATOM   2201  C  CB  . GLU   A  1 277 ? -47.845 12.081  -41.812  1.00 43.37  ? 578  GLU   A CB  1 
ATOM   2202  C  CG  . GLU   A  1 277 ? -49.285 12.501  -41.870  1.00 45.86  ? 578  GLU   A CG  1 
ATOM   2203  C  CD  . GLU   A  1 277 ? -49.593 13.598  -40.889  1.00 61.45  ? 578  GLU   A CD  1 
ATOM   2204  O  OE1 . GLU   A  1 277 ? -50.035 14.693  -41.316  1.00 59.12  ? 578  GLU   A OE1 1 
ATOM   2205  O  OE2 . GLU   A  1 277 ? -49.378 13.358  -39.681  1.00 69.54  ? 578  GLU   A OE2 1 
ATOM   2206  N  N   . ILE   A  1 278 ? -47.500 14.630  -44.214  1.00 47.59  ? 579  ILE   A N   1 
ATOM   2207  C  CA  . ILE   A  1 278 ? -47.589 16.066  -44.465  1.00 38.50  ? 579  ILE   A CA  1 
ATOM   2208  C  C   . ILE   A  1 278 ? -49.011 16.376  -44.907  1.00 43.76  ? 579  ILE   A C   1 
ATOM   2209  O  O   . ILE   A  1 278 ? -49.542 15.702  -45.796  1.00 48.48  ? 579  ILE   A O   1 
ATOM   2210  C  CB  . ILE   A  1 278 ? -46.588 16.516  -45.546  1.00 39.32  ? 579  ILE   A CB  1 
ATOM   2211  C  CG1 . ILE   A  1 278 ? -45.156 16.130  -45.174  1.00 47.57  ? 579  ILE   A CG1 1 
ATOM   2212  C  CG2 . ILE   A  1 278 ? -46.685 18.006  -45.763  1.00 41.76  ? 579  ILE   A CG2 1 
ATOM   2213  C  CD1 . ILE   A  1 278 ? -44.164 16.260  -46.312  1.00 53.25  ? 579  ILE   A CD1 1 
ATOM   2214  N  N   . GLY   A  1 279 ? -49.631 17.377  -44.276  1.00 39.72  ? 580  GLY   A N   1 
ATOM   2215  C  CA  . GLY   A  1 279 ? -50.970 17.816  -44.625  1.00 34.91  ? 580  GLY   A CA  1 
ATOM   2216  C  C   . GLY   A  1 279 ? -52.019 16.723  -44.696  1.00 45.10  ? 580  GLY   A C   1 
ATOM   2217  O  O   . GLY   A  1 279 ? -52.965 16.813  -45.490  1.00 49.53  ? 580  GLY   A O   1 
ATOM   2218  N  N   . GLY   A  1 280 ? -51.891 15.699  -43.856  1.00 49.66  ? 581  GLY   A N   1 
ATOM   2219  C  CA  . GLY   A  1 280 ? -52.795 14.569  -43.893  1.00 48.04  ? 581  GLY   A CA  1 
ATOM   2220  C  C   . GLY   A  1 280 ? -52.478 13.563  -44.968  1.00 49.86  ? 581  GLY   A C   1 
ATOM   2221  O  O   . GLY   A  1 280 ? -53.142 12.526  -45.041  1.00 54.27  ? 581  GLY   A O   1 
ATOM   2222  N  N   . LEU   A  1 281 ? -51.492 13.837  -45.809  1.00 45.95  ? 582  LEU   A N   1 
ATOM   2223  C  CA  . LEU   A  1 281 ? -51.021 12.868  -46.780  1.00 48.82  ? 582  LEU   A CA  1 
ATOM   2224  C  C   . LEU   A  1 281 ? -49.993 11.955  -46.121  1.00 46.82  ? 582  LEU   A C   1 
ATOM   2225  O  O   . LEU   A  1 281 ? -49.220 12.386  -45.263  1.00 47.08  ? 582  LEU   A O   1 
ATOM   2226  C  CB  . LEU   A  1 281 ? -50.423 13.592  -47.997  1.00 43.84  ? 582  LEU   A CB  1 
ATOM   2227  C  CG  . LEU   A  1 281 ? -51.388 14.634  -48.575  1.00 42.54  ? 582  LEU   A CG  1 
ATOM   2228  C  CD1 . LEU   A  1 281 ? -50.746 15.469  -49.647  1.00 43.99  ? 582  LEU   A CD1 1 
ATOM   2229  C  CD2 . LEU   A  1 281 ? -52.612 13.942  -49.127  1.00 46.72  ? 582  LEU   A CD2 1 
ATOM   2230  N  N   . GLU   A  1 282 ? -49.988 10.684  -46.520  1.00 41.40  ? 583  GLU   A N   1 
ATOM   2231  C  CA  . GLU   A  1 282 ? -49.095 9.684   -45.937  1.00 41.22  ? 583  GLU   A CA  1 
ATOM   2232  C  C   . GLU   A  1 282 ? -48.162 9.140   -47.018  1.00 41.00  ? 583  GLU   A C   1 
ATOM   2233  O  O   . GLU   A  1 282 ? -48.610 8.427   -47.922  1.00 37.44  ? 583  GLU   A O   1 
ATOM   2234  C  CB  . GLU   A  1 282 ? -49.893 8.540   -45.303  1.00 38.47  ? 583  GLU   A CB  1 
ATOM   2235  C  CG  . GLU   A  1 282 ? -50.929 8.917   -44.247  1.00 35.80  ? 583  GLU   A CG  1 
ATOM   2236  C  CD  . GLU   A  1 282 ? -51.713 7.702   -43.778  1.00 43.67  ? 583  GLU   A CD  1 
ATOM   2237  O  OE1 . GLU   A  1 282 ? -52.116 6.864   -44.623  1.00 46.72  ? 583  GLU   A OE1 1 
ATOM   2238  O  OE2 . GLU   A  1 282 ? -51.902 7.562   -42.554  1.00 52.96  ? 583  GLU   A OE2 1 
ATOM   2239  N  N   . PHE   A  1 283 ? -46.869 9.438   -46.902  1.00 30.99  ? 584  PHE   A N   1 
ATOM   2240  C  CA  . PHE   A  1 283 ? -45.833 8.906   -47.785  1.00 26.59  ? 584  PHE   A CA  1 
ATOM   2241  C  C   . PHE   A  1 283 ? -45.198 7.683   -47.123  1.00 29.53  ? 584  PHE   A C   1 
ATOM   2242  O  O   . PHE   A  1 283 ? -44.205 7.792   -46.414  1.00 40.00  ? 584  PHE   A O   1 
ATOM   2243  C  CB  . PHE   A  1 283 ? -44.790 9.978   -48.084  1.00 34.90  ? 584  PHE   A CB  1 
ATOM   2244  C  CG  . PHE   A  1 283 ? -45.349 11.178  -48.800  1.00 35.71  ? 584  PHE   A CG  1 
ATOM   2245  C  CD1 . PHE   A  1 283 ? -45.816 12.276  -48.087  1.00 32.13  ? 584  PHE   A CD1 1 
ATOM   2246  C  CD2 . PHE   A  1 283 ? -45.446 11.184  -50.184  1.00 32.07  ? 584  PHE   A CD2 1 
ATOM   2247  C  CE1 . PHE   A  1 283 ? -46.355 13.373  -48.734  1.00 32.86  ? 584  PHE   A CE1 1 
ATOM   2248  C  CE2 . PHE   A  1 283 ? -45.993 12.282  -50.848  1.00 32.66  ? 584  PHE   A CE2 1 
ATOM   2249  C  CZ  . PHE   A  1 283 ? -46.446 13.377  -50.131  1.00 32.74  ? 584  PHE   A CZ  1 
ATOM   2250  N  N   . SER   A  1 284 ? -45.758 6.500   -47.390  1.00 25.48  ? 585  SER   A N   1 
ATOM   2251  C  CA  . SER   A  1 284 ? -45.341 5.258   -46.739  1.00 36.51  ? 585  SER   A CA  1 
ATOM   2252  C  C   . SER   A  1 284 ? -43.922 4.818   -47.074  1.00 36.37  ? 585  SER   A C   1 
ATOM   2253  O  O   . SER   A  1 284 ? -43.457 3.810   -46.514  1.00 42.40  ? 585  SER   A O   1 
ATOM   2254  C  CB  . SER   A  1 284 ? -46.306 4.133   -47.113  1.00 36.46  ? 585  SER   A CB  1 
ATOM   2255  O  OG  . SER   A  1 284 ? -46.395 4.019   -48.525  1.00 41.24  ? 585  SER   A OG  1 
ATOM   2256  N  N   . ALA   A  1 285 ? -43.229 5.497   -47.981  1.00 40.49  ? 586  ALA   A N   1 
ATOM   2257  C  CA  . ALA   A  1 285 ? -41.881 5.089   -48.377  1.00 40.00  ? 586  ALA   A CA  1 
ATOM   2258  C  C   . ALA   A  1 285 ? -41.086 6.359   -48.618  1.00 41.55  ? 586  ALA   A C   1 
ATOM   2259  O  O   . ALA   A  1 285 ? -41.302 7.045   -49.626  1.00 57.37  ? 586  ALA   A O   1 
ATOM   2260  C  CB  . ALA   A  1 285 ? -41.906 4.201   -49.617  1.00 46.28  ? 586  ALA   A CB  1 
ATOM   2261  N  N   . CYS   A  1 286 ? -40.169 6.664   -47.700  1.00 36.31  ? 587  CYS   A N   1 
ATOM   2262  C  CA  . CYS   A  1 286 ? -39.530 7.969   -47.619  1.00 38.62  ? 587  CYS   A CA  1 
ATOM   2263  C  C   . CYS   A  1 286 ? -38.138 7.899   -47.013  1.00 47.86  ? 587  CYS   A C   1 
ATOM   2264  O  O   . CYS   A  1 286 ? -37.845 8.672   -46.093  1.00 50.32  ? 587  CYS   A O   1 
ATOM   2265  C  CB  . CYS   A  1 286 ? -40.382 8.912   -46.769  1.00 39.16  ? 587  CYS   A CB  1 
ATOM   2266  S  SG  . CYS   A  1 286 ? -40.683 8.318   -45.067  1.00 42.22  ? 587  CYS   A SG  1 
ATOM   2267  N  N   . PRO   A  1 287 ? -37.247 7.037   -47.509  1.00 44.90  ? 588  PRO   A N   1 
ATOM   2268  C  CA  . PRO   A  1 287 ? -35.973 6.824   -46.813  1.00 25.51  ? 588  PRO   A CA  1 
ATOM   2269  C  C   . PRO   A  1 287 ? -35.224 8.130   -46.597  1.00 34.64  ? 588  PRO   A C   1 
ATOM   2270  O  O   . PRO   A  1 287 ? -35.191 8.990   -47.478  1.00 43.23  ? 588  PRO   A O   1 
ATOM   2271  C  CB  . PRO   A  1 287 ? -35.207 5.881   -47.743  1.00 29.88  ? 588  PRO   A CB  1 
ATOM   2272  C  CG  . PRO   A  1 287 ? -35.912 5.911   -49.028  1.00 43.83  ? 588  PRO   A CG  1 
ATOM   2273  C  CD  . PRO   A  1 287 ? -37.336 6.252   -48.751  1.00 44.29  ? 588  PRO   A CD  1 
ATOM   2274  N  N   . PHE   A  1 288 ? -34.638 8.283   -45.398  1.00 38.49  ? 589  PHE   A N   1 
ATOM   2275  C  CA  . PHE   A  1 288 ? -33.851 9.466   -45.042  1.00 30.71  ? 589  PHE   A CA  1 
ATOM   2276  C  C   . PHE   A  1 288 ? -32.591 9.047   -44.308  1.00 33.56  ? 589  PHE   A C   1 
ATOM   2277  O  O   . PHE   A  1 288 ? -32.510 7.958   -43.736  1.00 36.71  ? 589  PHE   A O   1 
ATOM   2278  C  CB  . PHE   A  1 288 ? -34.627 10.463  -44.175  1.00 36.61  ? 589  PHE   A CB  1 
ATOM   2279  C  CG  . PHE   A  1 288 ? -35.257 9.850   -42.947  1.00 48.54  ? 589  PHE   A CG  1 
ATOM   2280  C  CD1 . PHE   A  1 288 ? -34.560 9.786   -41.745  1.00 41.09  ? 589  PHE   A CD1 1 
ATOM   2281  C  CD2 . PHE   A  1 288 ? -36.546 9.340   -42.992  1.00 43.55  ? 589  PHE   A CD2 1 
ATOM   2282  C  CE1 . PHE   A  1 288 ? -35.135 9.237   -40.627  1.00 32.44  ? 589  PHE   A CE1 1 
ATOM   2283  C  CE2 . PHE   A  1 288 ? -37.119 8.783   -41.862  1.00 38.33  ? 589  PHE   A CE2 1 
ATOM   2284  C  CZ  . PHE   A  1 288 ? -36.403 8.738   -40.681  1.00 36.21  ? 589  PHE   A CZ  1 
ATOM   2285  N  N   . SER   A  1 289 ? -31.607 9.944   -44.327  1.00 31.47  ? 590  SER   A N   1 
ATOM   2286  C  CA  . SER   A  1 289 ? -30.249 9.605   -43.933  1.00 35.75  ? 590  SER   A CA  1 
ATOM   2287  C  C   . SER   A  1 289 ? -29.537 10.860  -43.434  1.00 42.91  ? 590  SER   A C   1 
ATOM   2288  O  O   . SER   A  1 289 ? -29.828 11.972  -43.879  1.00 30.01  ? 590  SER   A O   1 
ATOM   2289  C  CB  . SER   A  1 289 ? -29.481 9.008   -45.111  1.00 39.94  ? 590  SER   A CB  1 
ATOM   2290  O  OG  . SER   A  1 289 ? -29.271 10.026  -46.065  1.00 42.90  ? 590  SER   A OG  1 
ATOM   2291  N  N   . GLY   A  1 290 ? -28.607 10.671  -42.497  1.00 42.75  ? 591  GLY   A N   1 
ATOM   2292  C  CA  . GLY   A  1 290 ? -27.749 11.753  -42.057  1.00 38.07  ? 591  GLY   A CA  1 
ATOM   2293  C  C   . GLY   A  1 290 ? -26.330 11.264  -41.870  1.00 44.52  ? 591  GLY   A C   1 
ATOM   2294  O  O   . GLY   A  1 290 ? -25.690 10.856  -42.845  1.00 59.49  ? 591  GLY   A O   1 
ATOM   2295  N  N   . TRP   A  1 291 ? -25.827 11.295  -40.632  1.00 35.75  ? 592  TRP   A N   1 
ATOM   2296  C  CA  . TRP   A  1 291 ? -24.590 10.606  -40.266  1.00 37.07  ? 592  TRP   A CA  1 
ATOM   2297  C  C   . TRP   A  1 291 ? -24.720 10.100  -38.836  1.00 45.15  ? 592  TRP   A C   1 
ATOM   2298  O  O   . TRP   A  1 291 ? -25.610 10.506  -38.084  1.00 43.45  ? 592  TRP   A O   1 
ATOM   2299  C  CB  . TRP   A  1 291 ? -23.344 11.498  -40.397  1.00 33.24  ? 592  TRP   A CB  1 
ATOM   2300  C  CG  . TRP   A  1 291 ? -23.505 12.803  -39.719  1.00 43.69  ? 592  TRP   A CG  1 
ATOM   2301  C  CD1 . TRP   A  1 291 ? -23.287 13.084  -38.398  1.00 46.24  ? 592  TRP   A CD1 1 
ATOM   2302  C  CD2 . TRP   A  1 291 ? -23.972 14.006  -40.316  1.00 43.96  ? 592  TRP   A CD2 1 
ATOM   2303  N  NE1 . TRP   A  1 291 ? -23.580 14.403  -38.142  1.00 48.83  ? 592  TRP   A NE1 1 
ATOM   2304  C  CE2 . TRP   A  1 291 ? -24.004 14.989  -39.306  1.00 49.49  ? 592  TRP   A CE2 1 
ATOM   2305  C  CE3 . TRP   A  1 291 ? -24.383 14.347  -41.605  1.00 41.77  ? 592  TRP   A CE3 1 
ATOM   2306  C  CZ2 . TRP   A  1 291 ? -24.420 16.293  -39.551  1.00 53.27  ? 592  TRP   A CZ2 1 
ATOM   2307  C  CZ3 . TRP   A  1 291 ? -24.780 15.642  -41.851  1.00 45.61  ? 592  TRP   A CZ3 1 
ATOM   2308  C  CH2 . TRP   A  1 291 ? -24.795 16.601  -40.829  1.00 56.27  ? 592  TRP   A CH2 1 
ATOM   2309  N  N   . TYR   A  1 292 ? -23.795 9.218   -38.468  1.00 46.58  ? 593  TYR   A N   1 
ATOM   2310  C  CA  . TYR   A  1 292 ? -23.832 8.511   -37.196  1.00 40.13  ? 593  TYR   A CA  1 
ATOM   2311  C  C   . TYR   A  1 292 ? -23.307 9.344   -36.032  1.00 35.49  ? 593  TYR   A C   1 
ATOM   2312  O  O   . TYR   A  1 292 ? -22.299 10.057  -36.144  1.00 46.97  ? 593  TYR   A O   1 
ATOM   2313  C  CB  . TYR   A  1 292 ? -22.989 7.240   -37.300  1.00 40.17  ? 593  TYR   A CB  1 
ATOM   2314  C  CG  . TYR   A  1 292 ? -23.755 6.002   -37.674  1.00 51.78  ? 593  TYR   A CG  1 
ATOM   2315  C  CD1 . TYR   A  1 292 ? -23.309 5.159   -38.694  1.00 59.03  ? 593  TYR   A CD1 1 
ATOM   2316  C  CD2 . TYR   A  1 292 ? -24.908 5.655   -36.995  1.00 50.80  ? 593  TYR   A CD2 1 
ATOM   2317  C  CE1 . TYR   A  1 292 ? -24.000 4.003   -39.019  1.00 53.33  ? 593  TYR   A CE1 1 
ATOM   2318  C  CE2 . TYR   A  1 292 ? -25.604 4.514   -37.318  1.00 53.62  ? 593  TYR   A CE2 1 
ATOM   2319  C  CZ  . TYR   A  1 292 ? -25.146 3.692   -38.320  1.00 55.36  ? 593  TYR   A CZ  1 
ATOM   2320  O  OH  . TYR   A  1 292 ? -25.849 2.555   -38.611  1.00 64.52  ? 593  TYR   A OH  1 
ATOM   2321  N  N   . MET   A  1 293 ? -23.994 9.233   -34.903  1.00 32.90  ? 594  MET   A N   1 
ATOM   2322  C  CA  . MET   A  1 293 ? -23.377 9.444   -33.607  1.00 28.18  ? 594  MET   A CA  1 
ATOM   2323  C  C   . MET   A  1 293 ? -22.696 8.147   -33.181  1.00 36.24  ? 594  MET   A C   1 
ATOM   2324  O  O   . MET   A  1 293 ? -23.214 7.057   -33.425  1.00 42.84  ? 594  MET   A O   1 
ATOM   2325  C  CB  . MET   A  1 293 ? -24.419 9.871   -32.581  1.00 37.04  ? 594  MET   A CB  1 
ATOM   2326  C  CG  . MET   A  1 293 ? -23.871 10.265  -31.226  1.00 44.61  ? 594  MET   A CG  1 
ATOM   2327  S  SD  . MET   A  1 293 ? -25.208 11.011  -30.287  1.00 45.25  ? 594  MET   A SD  1 
ATOM   2328  C  CE  . MET   A  1 293 ? -26.173 9.553   -29.904  1.00 39.05  ? 594  MET   A CE  1 
ATOM   2329  N  N   . GLY   A  1 294 ? -21.529 8.265   -32.553  1.00 33.68  ? 595  GLY   A N   1 
ATOM   2330  C  CA  . GLY   A  1 294 ? -20.697 7.090   -32.328  1.00 40.44  ? 595  GLY   A CA  1 
ATOM   2331  C  C   . GLY   A  1 294 ? -21.381 5.999   -31.527  1.00 50.79  ? 595  GLY   A C   1 
ATOM   2332  O  O   . GLY   A  1 294 ? -21.209 4.812   -31.817  1.00 52.13  ? 595  GLY   A O   1 
ATOM   2333  N  N   . THR   A  1 295 ? -22.183 6.388   -30.520  1.00 47.38  ? 596  THR   A N   1 
ATOM   2334  C  CA  . THR   A  1 295 ? -22.755 5.420   -29.584  1.00 44.37  ? 596  THR   A CA  1 
ATOM   2335  C  C   . THR   A  1 295 ? -23.706 4.444   -30.261  1.00 41.34  ? 596  THR   A C   1 
ATOM   2336  O  O   . THR   A  1 295 ? -23.908 3.335   -29.747  1.00 44.08  ? 596  THR   A O   1 
ATOM   2337  C  CB  . THR   A  1 295 ? -23.512 6.112   -28.447  1.00 44.75  ? 596  THR   A CB  1 
ATOM   2338  O  OG1 . THR   A  1 295 ? -24.418 7.091   -28.995  1.00 48.85  ? 596  THR   A OG1 1 
ATOM   2339  C  CG2 . THR   A  1 295 ? -22.543 6.738   -27.433  1.00 35.67  ? 596  THR   A CG2 1 
ATOM   2340  N  N   . GLU   A  1 296 ? -24.334 4.843   -31.377  1.00 42.00  ? 597  GLU   A N   1 
ATOM   2341  C  CA  . GLU   A  1 296 ? -25.274 3.955   -32.060  1.00 33.66  ? 597  GLU   A CA  1 
ATOM   2342  C  C   . GLU   A  1 296 ? -24.579 2.677   -32.512  1.00 43.18  ? 597  GLU   A C   1 
ATOM   2343  O  O   . GLU   A  1 296 ? -25.139 1.580   -32.391  1.00 45.04  ? 597  GLU   A O   1 
ATOM   2344  C  CB  . GLU   A  1 296 ? -25.905 4.653   -33.260  1.00 42.61  ? 597  GLU   A CB  1 
ATOM   2345  C  CG  . GLU   A  1 296 ? -26.632 5.957   -32.980  1.00 41.48  ? 597  GLU   A CG  1 
ATOM   2346  C  CD  . GLU   A  1 296 ? -27.189 6.609   -34.264  1.00 49.12  ? 597  GLU   A CD  1 
ATOM   2347  O  OE1 . GLU   A  1 296 ? -28.173 6.076   -34.834  1.00 46.59  ? 597  GLU   A OE1 1 
ATOM   2348  O  OE2 . GLU   A  1 296 ? -26.637 7.648   -34.703  1.00 43.48  ? 597  GLU   A OE2 1 
ATOM   2349  N  N   . ILE   A  1 297 ? -23.353 2.801   -33.024  1.00 45.89  ? 598  ILE   A N   1 
ATOM   2350  C  CA  . ILE   A  1 297 ? -22.567 1.634   -33.407  1.00 49.11  ? 598  ILE   A CA  1 
ATOM   2351  C  C   . ILE   A  1 297 ? -21.874 1.030   -32.187  1.00 52.28  ? 598  ILE   A C   1 
ATOM   2352  O  O   . ILE   A  1 297 ? -21.836 -0.195  -32.033  1.00 51.97  ? 598  ILE   A O   1 
ATOM   2353  C  CB  . ILE   A  1 297 ? -21.528 2.010   -34.491  1.00 48.28  ? 598  ILE   A CB  1 
ATOM   2354  C  CG1 . ILE   A  1 297 ? -22.144 2.875   -35.578  1.00 40.89  ? 598  ILE   A CG1 1 
ATOM   2355  C  CG2 . ILE   A  1 297 ? -20.888 0.778   -35.121  1.00 36.28  ? 598  ILE   A CG2 1 
ATOM   2356  C  CD1 . ILE   A  1 297 ? -21.154 3.835   -36.186  1.00 42.40  ? 598  ILE   A CD1 1 
ATOM   2357  N  N   . GLY   A  1 298 ? -21.311 1.897   -31.332  1.00 57.65  ? 599  GLY   A N   1 
ATOM   2358  C  CA  . GLY   A  1 298 ? -20.429 1.456   -30.250  1.00 64.75  ? 599  GLY   A CA  1 
ATOM   2359  C  C   . GLY   A  1 298 ? -21.159 0.838   -29.073  1.00 66.30  ? 599  GLY   A C   1 
ATOM   2360  O  O   . GLY   A  1 298 ? -20.768 -0.226  -28.575  1.00 57.20  ? 599  GLY   A O   1 
ATOM   2361  N  N   . VAL   A  1 299 ? -22.226 1.490   -28.618  1.00 65.66  ? 600  VAL   A N   1 
ATOM   2362  C  CA  . VAL   A  1 299 ? -23.008 0.989   -27.493  1.00 56.40  ? 600  VAL   A CA  1 
ATOM   2363  C  C   . VAL   A  1 299 ? -24.086 0.014   -27.955  1.00 60.79  ? 600  VAL   A C   1 
ATOM   2364  O  O   . VAL   A  1 299 ? -24.150 -1.126  -27.475  1.00 46.09  ? 600  VAL   A O   1 
ATOM   2365  C  CB  . VAL   A  1 299 ? -23.616 2.164   -26.717  1.00 54.74  ? 600  VAL   A CB  1 
ATOM   2366  C  CG1 . VAL   A  1 299 ? -24.415 1.657   -25.554  1.00 45.45  ? 600  VAL   A CG1 1 
ATOM   2367  C  CG2 . VAL   A  1 299 ? -22.524 3.099   -26.260  1.00 58.45  ? 600  VAL   A CG2 1 
ATOM   2368  N  N   . ARG   A  1 300 ? -24.918 0.437   -28.923  1.00 60.39  ? 601  ARG   A N   1 
ATOM   2369  C  CA  . ARG   A  1 300 ? -26.110 -0.325  -29.304  1.00 61.77  ? 601  ARG   A CA  1 
ATOM   2370  C  C   . ARG   A  1 300 ? -25.800 -1.476  -30.268  1.00 58.28  ? 601  ARG   A C   1 
ATOM   2371  O  O   . ARG   A  1 300 ? -26.131 -2.634  -29.988  1.00 50.55  ? 601  ARG   A O   1 
ATOM   2372  C  CB  . ARG   A  1 300 ? -27.171 0.604   -29.916  1.00 60.86  ? 601  ARG   A CB  1 
ATOM   2373  C  CG  . ARG   A  1 300 ? -27.533 1.859   -29.088  1.00 54.31  ? 601  ARG   A CG  1 
ATOM   2374  C  CD  . ARG   A  1 300 ? -27.973 1.546   -27.665  1.00 51.45  ? 601  ARG   A CD  1 
ATOM   2375  N  NE  . ARG   A  1 300 ? -28.866 0.393   -27.574  1.00 47.11  ? 601  ARG   A NE  1 
ATOM   2376  C  CZ  . ARG   A  1 300 ? -30.182 0.445   -27.743  1.00 36.38  ? 601  ARG   A CZ  1 
ATOM   2377  N  NH1 . ARG   A  1 300 ? -30.785 1.597   -28.025  1.00 28.08  ? 601  ARG   A NH1 1 
ATOM   2378  N  NH2 . ARG   A  1 300 ? -30.891 -0.665  -27.638  1.00 33.75  ? 601  ARG   A NH2 1 
ATOM   2379  N  N   . ASP   A  1 301 ? -25.187 -1.172  -31.422  1.00 64.69  ? 602  ASP   A N   1 
ATOM   2380  C  CA  . ASP   A  1 301 ? -24.976 -2.186  -32.458  1.00 62.05  ? 602  ASP   A CA  1 
ATOM   2381  C  C   . ASP   A  1 301 ? -24.041 -3.295  -31.997  1.00 65.65  ? 602  ASP   A C   1 
ATOM   2382  O  O   . ASP   A  1 301 ? -24.317 -4.481  -32.227  1.00 67.86  ? 602  ASP   A O   1 
ATOM   2383  C  CB  . ASP   A  1 301 ? -24.428 -1.540  -33.727  1.00 55.49  ? 602  ASP   A CB  1 
ATOM   2384  C  CG  . ASP   A  1 301 ? -25.464 -0.723  -34.431  1.00 51.21  ? 602  ASP   A CG  1 
ATOM   2385  O  OD1 . ASP   A  1 301 ? -26.618 -1.187  -34.462  1.00 49.22  ? 602  ASP   A OD1 1 
ATOM   2386  O  OD2 . ASP   A  1 301 ? -25.138 0.385   -34.915  1.00 47.65  ? 602  ASP   A OD2 1 
ATOM   2387  N  N   . TYR   A  1 302 ? -22.932 -2.936  -31.352  1.00 63.81  ? 603  TYR   A N   1 
ATOM   2388  C  CA  . TYR   A  1 302 ? -21.931 -3.920  -30.957  1.00 66.77  ? 603  TYR   A CA  1 
ATOM   2389  C  C   . TYR   A  1 302 ? -22.188 -4.574  -29.608  1.00 59.75  ? 603  TYR   A C   1 
ATOM   2390  O  O   . TYR   A  1 302 ? -21.687 -5.687  -29.383  1.00 48.11  ? 603  TYR   A O   1 
ATOM   2391  C  CB  . TYR   A  1 302 ? -20.552 -3.277  -30.913  1.00 66.47  ? 603  TYR   A CB  1 
ATOM   2392  C  CG  . TYR   A  1 302 ? -20.016 -2.961  -32.268  1.00 62.19  ? 603  TYR   A CG  1 
ATOM   2393  C  CD1 . TYR   A  1 302 ? -18.887 -2.174  -32.413  1.00 58.63  ? 603  TYR   A CD1 1 
ATOM   2394  C  CD2 . TYR   A  1 302 ? -20.637 -3.446  -33.408  1.00 57.72  ? 603  TYR   A CD2 1 
ATOM   2395  C  CE1 . TYR   A  1 302 ? -18.381 -1.883  -33.646  1.00 57.84  ? 603  TYR   A CE1 1 
ATOM   2396  C  CE2 . TYR   A  1 302 ? -20.140 -3.156  -34.653  1.00 57.60  ? 603  TYR   A CE2 1 
ATOM   2397  C  CZ  . TYR   A  1 302 ? -19.008 -2.372  -34.764  1.00 57.95  ? 603  TYR   A CZ  1 
ATOM   2398  O  OH  . TYR   A  1 302 ? -18.483 -2.077  -35.992  1.00 62.86  ? 603  TYR   A OH  1 
ATOM   2399  N  N   . CYS   A  1 303 ? -22.951 -3.924  -28.709  1.00 61.11  ? 604  CYS   A N   1 
ATOM   2400  C  CA  . CYS   A  1 303 ? -22.922 -4.302  -27.297  1.00 67.18  ? 604  CYS   A CA  1 
ATOM   2401  C  C   . CYS   A  1 303 ? -24.252 -4.739  -26.689  1.00 59.50  ? 604  CYS   A C   1 
ATOM   2402  O  O   . CYS   A  1 303 ? -24.223 -5.520  -25.737  1.00 54.35  ? 604  CYS   A O   1 
ATOM   2403  C  CB  . CYS   A  1 303 ? -22.332 -3.160  -26.467  1.00 60.31  ? 604  CYS   A CB  1 
ATOM   2404  S  SG  . CYS   A  1 303 ? -20.584 -2.924  -26.797  1.00 58.51  ? 604  CYS   A SG  1 
ATOM   2405  N  N   . ASP   A  1 304 ? -25.401 -4.288  -27.200  1.00 58.89  ? 605  ASP   A N   1 
ATOM   2406  C  CA  . ASP   A  1 304 ? -26.666 -4.894  -26.791  1.00 53.22  ? 605  ASP   A CA  1 
ATOM   2407  C  C   . ASP   A  1 304 ? -26.587 -6.415  -26.911  1.00 57.71  ? 605  ASP   A C   1 
ATOM   2408  O  O   . ASP   A  1 304 ? -25.998 -6.954  -27.854  1.00 60.52  ? 605  ASP   A O   1 
ATOM   2409  C  CB  . ASP   A  1 304 ? -27.830 -4.361  -27.632  1.00 54.77  ? 605  ASP   A CB  1 
ATOM   2410  C  CG  . ASP   A  1 304 ? -28.219 -2.939  -27.268  1.00 59.73  ? 605  ASP   A CG  1 
ATOM   2411  O  OD1 . ASP   A  1 304 ? -27.459 -2.275  -26.521  1.00 67.75  ? 605  ASP   A OD1 1 
ATOM   2412  O  OD2 . ASP   A  1 304 ? -29.293 -2.491  -27.727  1.00 51.42  ? 605  ASP   A OD2 1 
ATOM   2413  N  N   . ASN   A  1 305 ? -27.150 -7.113  -25.923  1.00 58.56  ? 606  ASN   A N   1 
ATOM   2414  C  CA  . ASN   A  1 305 ? -27.059 -8.567  -25.927  1.00 64.42  ? 606  ASN   A CA  1 
ATOM   2415  C  C   . ASN   A  1 305 ? -27.818 -9.176  -27.098  1.00 70.64  ? 606  ASN   A C   1 
ATOM   2416  O  O   . ASN   A  1 305 ? -27.422 -10.229 -27.610  1.00 71.50  ? 606  ASN   A O   1 
ATOM   2417  C  CB  . ASN   A  1 305 ? -27.559 -9.128  -24.596  1.00 78.49  ? 606  ASN   A CB  1 
ATOM   2418  C  CG  . ASN   A  1 305 ? -26.580 -8.870  -23.449  1.00 86.10  ? 606  ASN   A CG  1 
ATOM   2419  O  OD1 . ASN   A  1 305 ? -25.565 -9.570  -23.297  1.00 87.02  ? 606  ASN   A OD1 1 
ATOM   2420  N  ND2 . ASN   A  1 305 ? -26.881 -7.858  -22.640  1.00 81.70  ? 606  ASN   A ND2 1 
ATOM   2421  N  N   . SER   A  1 306 ? -28.891 -8.524  -27.549  1.00 76.32  ? 607  SER   A N   1 
ATOM   2422  C  CA  . SER   A  1 306 ? -29.651 -8.977  -28.713  1.00 86.07  ? 607  SER   A CA  1 
ATOM   2423  C  C   . SER   A  1 306 ? -29.030 -8.557  -30.043  1.00 83.08  ? 607  SER   A C   1 
ATOM   2424  O  O   . SER   A  1 306 ? -29.573 -8.905  -31.089  1.00 83.36  ? 607  SER   A O   1 
ATOM   2425  C  CB  . SER   A  1 306 ? -31.086 -8.448  -28.652  1.00 93.72  ? 607  SER   A CB  1 
ATOM   2426  O  OG  . SER   A  1 306 ? -31.670 -8.683  -27.378  1.00 98.21  ? 607  SER   A OG  1 
ATOM   2427  N  N   . ARG   A  1 307 ? -27.925 -7.827  -30.018  1.00 82.45  ? 608  ARG   A N   1 
ATOM   2428  C  CA  . ARG   A  1 307 ? -27.241 -7.354  -31.216  1.00 70.30  ? 608  ARG   A CA  1 
ATOM   2429  C  C   . ARG   A  1 307 ? -25.893 -8.080  -31.347  1.00 67.97  ? 608  ARG   A C   1 
ATOM   2430  O  O   . ARG   A  1 307 ? -25.860 -9.295  -31.124  1.00 67.90  ? 608  ARG   A O   1 
ATOM   2431  C  CB  . ARG   A  1 307 ? -27.167 -5.842  -31.158  1.00 60.56  ? 608  ARG   A CB  1 
ATOM   2432  C  CG  . ARG   A  1 307 ? -28.538 -5.148  -30.993  1.00 60.77  ? 608  ARG   A CG  1 
ATOM   2433  C  CD  . ARG   A  1 307 ? -29.406 -5.208  -32.269  1.00 64.72  ? 608  ARG   A CD  1 
ATOM   2434  N  NE  . ARG   A  1 307 ? -28.621 -5.041  -33.496  1.00 59.34  ? 608  ARG   A NE  1 
ATOM   2435  C  CZ  . ARG   A  1 307 ? -28.158 -3.878  -33.959  1.00 50.46  ? 608  ARG   A CZ  1 
ATOM   2436  N  NH1 . ARG   A  1 307 ? -28.373 -2.739  -33.312  1.00 39.15  ? 608  ARG   A NH1 1 
ATOM   2437  N  NH2 . ARG   A  1 307 ? -27.452 -3.854  -35.074  1.00 56.51  ? 608  ARG   A NH2 1 
ATOM   2438  N  N   . TYR   A  1 308 ? -24.801 -7.403  -31.719  1.00 58.08  ? 609  TYR   A N   1 
ATOM   2439  C  CA  . TYR   A  1 308 ? -23.551 -8.109  -31.995  1.00 60.09  ? 609  TYR   A CA  1 
ATOM   2440  C  C   . TYR   A  1 308 ? -22.838 -8.603  -30.748  1.00 66.74  ? 609  TYR   A C   1 
ATOM   2441  O  O   . TYR   A  1 308 ? -22.022 -9.518  -30.869  1.00 83.80  ? 609  TYR   A O   1 
ATOM   2442  C  CB  . TYR   A  1 308 ? -22.596 -7.231  -32.814  1.00 62.76  ? 609  TYR   A CB  1 
ATOM   2443  C  CG  . TYR   A  1 308 ? -22.718 -7.483  -34.303  1.00 60.76  ? 609  TYR   A CG  1 
ATOM   2444  C  CD1 . TYR   A  1 308 ? -23.616 -6.753  -35.090  1.00 60.24  ? 609  TYR   A CD1 1 
ATOM   2445  C  CD2 . TYR   A  1 308 ? -21.949 -8.460  -34.924  1.00 55.03  ? 609  TYR   A CD2 1 
ATOM   2446  C  CE1 . TYR   A  1 308 ? -23.729 -6.984  -36.452  1.00 51.31  ? 609  TYR   A CE1 1 
ATOM   2447  C  CE2 . TYR   A  1 308 ? -22.053 -8.695  -36.278  1.00 47.49  ? 609  TYR   A CE2 1 
ATOM   2448  C  CZ  . TYR   A  1 308 ? -22.954 -7.962  -37.034  1.00 58.08  ? 609  TYR   A CZ  1 
ATOM   2449  O  OH  . TYR   A  1 308 ? -23.072 -8.201  -38.384  1.00 62.43  ? 609  TYR   A OH  1 
ATOM   2450  N  N   . ASN   A  1 309 ? -23.075 -7.993  -29.581  1.00 64.62  ? 610  ASN   A N   1 
ATOM   2451  C  CA  . ASN   A  1 309 ? -22.739 -8.570  -28.266  1.00 63.03  ? 610  ASN   A CA  1 
ATOM   2452  C  C   . ASN   A  1 309 ? -21.259 -8.982  -28.158  1.00 60.42  ? 610  ASN   A C   1 
ATOM   2453  O  O   . ASN   A  1 309 ? -20.915 -10.148 -27.916  1.00 51.59  ? 610  ASN   A O   1 
ATOM   2454  C  CB  . ASN   A  1 309 ? -23.679 -9.748  -27.957  1.00 58.74  ? 610  ASN   A CB  1 
ATOM   2455  C  CG  . ASN   A  1 309 ? -23.574 -10.235 -26.515  1.00 65.00  ? 610  ASN   A CG  1 
ATOM   2456  O  OD1 . ASN   A  1 309 ? -23.172 -9.488  -25.614  1.00 72.80  ? 610  ASN   A OD1 1 
ATOM   2457  N  ND2 . ASN   A  1 309 ? -23.931 -11.493 -26.293  1.00 64.10  ? 610  ASN   A ND2 1 
ATOM   2458  N  N   . ILE   A  1 310 ? -20.372 -7.994  -28.300  1.00 59.20  ? 611  ILE   A N   1 
ATOM   2459  C  CA  . ILE   A  1 310 ? -18.934 -8.254  -28.321  1.00 68.43  ? 611  ILE   A CA  1 
ATOM   2460  C  C   . ILE   A  1 310 ? -18.246 -7.806  -27.040  1.00 69.83  ? 611  ILE   A C   1 
ATOM   2461  O  O   . ILE   A  1 310 ? -17.012 -7.787  -26.988  1.00 73.65  ? 611  ILE   A O   1 
ATOM   2462  C  CB  . ILE   A  1 310 ? -18.253 -7.603  -29.536  1.00 70.23  ? 611  ILE   A CB  1 
ATOM   2463  C  CG1 . ILE   A  1 310 ? -18.515 -6.099  -29.550  1.00 68.28  ? 611  ILE   A CG1 1 
ATOM   2464  C  CG2 . ILE   A  1 310 ? -18.707 -8.256  -30.824  1.00 71.85  ? 611  ILE   A CG2 1 
ATOM   2465  C  CD1 . ILE   A  1 310 ? -17.526 -5.336  -30.394  1.00 65.44  ? 611  ILE   A CD1 1 
ATOM   2466  N  N   . LEU   A  1 311 ? -19.005 -7.427  -26.007  1.00 69.40  ? 612  LEU   A N   1 
ATOM   2467  C  CA  . LEU   A  1 311 ? -18.387 -7.034  -24.739  1.00 63.41  ? 612  LEU   A CA  1 
ATOM   2468  C  C   . LEU   A  1 311 ? -17.557 -8.171  -24.155  1.00 71.67  ? 612  LEU   A C   1 
ATOM   2469  O  O   . LEU   A  1 311 ? -16.429 -7.964  -23.691  1.00 73.59  ? 612  LEU   A O   1 
ATOM   2470  C  CB  . LEU   A  1 311 ? -19.454 -6.598  -23.737  1.00 47.33  ? 612  LEU   A CB  1 
ATOM   2471  C  CG  . LEU   A  1 311 ? -20.102 -5.235  -23.923  1.00 39.92  ? 612  LEU   A CG  1 
ATOM   2472  C  CD1 . LEU   A  1 311 ? -21.222 -5.097  -22.941  1.00 32.79  ? 612  LEU   A CD1 1 
ATOM   2473  C  CD2 . LEU   A  1 311 ? -19.096 -4.126  -23.725  1.00 36.55  ? 612  LEU   A CD2 1 
ATOM   2474  N  N   . GLU   A  1 312 ? -18.114 -9.382  -24.147  1.00 72.12  ? 613  GLU   A N   1 
ATOM   2475  C  CA  . GLU   A  1 312 ? -17.372 -10.528 -23.639  1.00 75.31  ? 613  GLU   A CA  1 
ATOM   2476  C  C   . GLU   A  1 312 ? -16.073 -10.713 -24.418  1.00 74.04  ? 613  GLU   A C   1 
ATOM   2477  O  O   . GLU   A  1 312 ? -15.005 -10.905 -23.829  1.00 72.28  ? 613  GLU   A O   1 
ATOM   2478  C  CB  . GLU   A  1 312 ? -18.258 -11.774 -23.721  1.00 85.27  ? 613  GLU   A CB  1 
ATOM   2479  C  CG  . GLU   A  1 312 ? -17.938 -12.883 -22.731  1.00 90.82  ? 613  GLU   A CG  1 
ATOM   2480  C  CD  . GLU   A  1 312 ? -19.036 -13.939 -22.663  1.00 92.21  ? 613  GLU   A CD  1 
ATOM   2481  O  OE1 . GLU   A  1 312 ? -20.230 -13.557 -22.593  1.00 90.13  ? 613  GLU   A OE1 1 
ATOM   2482  O  OE2 . GLU   A  1 312 ? -18.702 -15.148 -22.691  1.00 89.64  ? 613  GLU   A OE2 1 
ATOM   2483  N  N   . GLU   A  1 313 ? -16.141 -10.599 -25.746  1.00 70.86  ? 614  GLU   A N   1 
ATOM   2484  C  CA  . GLU   A  1 313 ? -14.969 -10.838 -26.582  1.00 71.96  ? 614  GLU   A CA  1 
ATOM   2485  C  C   . GLU   A  1 313 ? -13.905 -9.767  -26.374  1.00 59.21  ? 614  GLU   A C   1 
ATOM   2486  O  O   . GLU   A  1 313 ? -12.704 -10.060 -26.409  1.00 53.35  ? 614  GLU   A O   1 
ATOM   2487  C  CB  . GLU   A  1 313 ? -15.394 -10.897 -28.052  1.00 70.11  ? 614  GLU   A CB  1 
ATOM   2488  C  CG  . GLU   A  1 313 ? -14.917 -12.120 -28.799  1.00 76.39  ? 614  GLU   A CG  1 
ATOM   2489  C  CD  . GLU   A  1 313 ? -13.718 -11.827 -29.672  1.00 88.18  ? 614  GLU   A CD  1 
ATOM   2490  O  OE1 . GLU   A  1 313 ? -12.650 -11.476 -29.118  1.00 95.57  ? 614  GLU   A OE1 1 
ATOM   2491  O  OE2 . GLU   A  1 313 ? -13.852 -11.938 -30.915  1.00 89.31  ? 614  GLU   A OE2 1 
ATOM   2492  N  N   . VAL   A  1 314 ? -14.328 -8.517  -26.182  1.00 54.40  ? 615  VAL   A N   1 
ATOM   2493  C  CA  . VAL   A  1 314 ? -13.375 -7.425  -26.007  1.00 57.29  ? 615  VAL   A CA  1 
ATOM   2494  C  C   . VAL   A  1 314 ? -12.734 -7.495  -24.626  1.00 69.62  ? 615  VAL   A C   1 
ATOM   2495  O  O   . VAL   A  1 314 ? -11.504 -7.507  -24.495  1.00 75.72  ? 615  VAL   A O   1 
ATOM   2496  C  CB  . VAL   A  1 314 ? -14.069 -6.071  -26.236  1.00 56.73  ? 615  VAL   A CB  1 
ATOM   2497  C  CG1 . VAL   A  1 314 ? -13.140 -4.932  -25.841  1.00 47.41  ? 615  VAL   A CG1 1 
ATOM   2498  C  CG2 . VAL   A  1 314 ? -14.504 -5.931  -27.695  1.00 64.35  ? 615  VAL   A CG2 1 
ATOM   2499  N  N   . ALA   A  1 315 ? -13.564 -7.534  -23.576  1.00 65.52  ? 616  ALA   A N   1 
ATOM   2500  C  CA  . ALA   A  1 315 ? -13.061 -7.617  -22.211  1.00 54.85  ? 616  ALA   A CA  1 
ATOM   2501  C  C   . ALA   A  1 315 ? -12.000 -8.697  -22.084  1.00 56.54  ? 616  ALA   A C   1 
ATOM   2502  O  O   . ALA   A  1 315 ? -10.962 -8.477  -21.459  1.00 49.67  ? 616  ALA   A O   1 
ATOM   2503  C  CB  . ALA   A  1 315 ? -14.215 -7.884  -21.247  1.00 56.31  ? 616  ALA   A CB  1 
ATOM   2504  N  N   . LYS   A  1 316 ? -12.217 -9.854  -22.719  1.00 67.28  ? 617  LYS   A N   1 
ATOM   2505  C  CA  . LYS   A  1 316 ? -11.226 -10.924 -22.656  1.00 66.46  ? 617  LYS   A CA  1 
ATOM   2506  C  C   . LYS   A  1 316 ? -9.880  -10.430 -23.155  1.00 63.92  ? 617  LYS   A C   1 
ATOM   2507  O  O   . LYS   A  1 316 ? -8.909  -10.390 -22.400  1.00 69.96  ? 617  LYS   A O   1 
ATOM   2508  C  CB  . LYS   A  1 316 ? -11.690 -12.147 -23.449  1.00 67.50  ? 617  LYS   A CB  1 
ATOM   2509  C  CG  . LYS   A  1 316 ? -12.702 -12.995 -22.703  1.00 74.50  ? 617  LYS   A CG  1 
ATOM   2510  C  CD  . LYS   A  1 316 ? -12.765 -14.418 -23.232  1.00 79.19  ? 617  LYS   A CD  1 
ATOM   2511  C  CE  . LYS   A  1 316 ? -13.688 -15.270 -22.367  1.00 74.35  ? 617  LYS   A CE  1 
ATOM   2512  N  NZ  . LYS   A  1 316 ? -15.063 -14.681 -22.314  1.00 65.71  ? 617  LYS   A NZ  1 
ATOM   2513  N  N   . LYS   A  1 317 ? -9.819  -9.980  -24.409  1.00 69.22  ? 618  LYS   A N   1 
ATOM   2514  C  CA  . LYS   A  1 317 ? -8.569  -9.434  -24.924  1.00 70.33  ? 618  LYS   A CA  1 
ATOM   2515  C  C   . LYS   A  1 317 ? -8.043  -8.284  -24.070  1.00 69.19  ? 618  LYS   A C   1 
ATOM   2516  O  O   . LYS   A  1 317 ? -6.844  -7.992  -24.120  1.00 71.72  ? 618  LYS   A O   1 
ATOM   2517  C  CB  . LYS   A  1 317 ? -8.740  -8.955  -26.365  1.00 70.31  ? 618  LYS   A CB  1 
ATOM   2518  C  CG  . LYS   A  1 317 ? -9.597  -9.838  -27.284  1.00 74.21  ? 618  LYS   A CG  1 
ATOM   2519  C  CD  . LYS   A  1 317 ? -8.829  -10.336 -28.513  1.00 58.75  ? 618  LYS   A CD  1 
ATOM   2520  C  CE  . LYS   A  1 317 ? -8.413  -11.793 -28.315  1.00 68.41  ? 618  LYS   A CE  1 
ATOM   2521  N  NZ  . LYS   A  1 317 ? -7.680  -12.429 -29.458  1.00 74.40  ? 618  LYS   A NZ  1 
ATOM   2522  N  N   . MET   A  1 318 ? -8.902  -7.628  -23.288  1.00 60.42  ? 619  MET   A N   1 
ATOM   2523  C  CA  . MET   A  1 318 ? -8.447  -6.574  -22.391  1.00 61.06  ? 619  MET   A CA  1 
ATOM   2524  C  C   . MET   A  1 318 ? -7.956  -7.115  -21.065  1.00 62.14  ? 619  MET   A C   1 
ATOM   2525  O  O   . MET   A  1 318 ? -7.429  -6.335  -20.269  1.00 67.92  ? 619  MET   A O   1 
ATOM   2526  C  CB  . MET   A  1 318 ? -9.554  -5.544  -22.119  1.00 56.79  ? 619  MET   A CB  1 
ATOM   2527  C  CG  . MET   A  1 318 ? -9.945  -4.690  -23.317  1.00 57.69  ? 619  MET   A CG  1 
ATOM   2528  S  SD  . MET   A  1 318 ? -11.124 -3.360  -22.939  1.00 56.22  ? 619  MET   A SD  1 
ATOM   2529  C  CE  . MET   A  1 318 ? -10.128 -2.367  -21.825  1.00 53.27  ? 619  MET   A CE  1 
ATOM   2530  N  N   . ASN   A  1 319 ? -8.114  -8.422  -20.827  1.00 64.66  ? 620  ASN   A N   1 
ATOM   2531  C  CA  . ASN   A  1 319 ? -7.698  -9.105  -19.598  1.00 72.19  ? 620  ASN   A CA  1 
ATOM   2532  C  C   . ASN   A  1 319 ? -8.492  -8.673  -18.367  1.00 70.11  ? 620  ASN   A C   1 
ATOM   2533  O  O   . ASN   A  1 319 ? -7.965  -8.665  -17.256  1.00 68.21  ? 620  ASN   A O   1 
ATOM   2534  C  CB  . ASN   A  1 319 ? -6.211  -8.924  -19.332  1.00 73.45  ? 620  ASN   A CB  1 
ATOM   2535  C  CG  . ASN   A  1 319 ? -5.419  -10.059 -19.851  1.00 76.12  ? 620  ASN   A CG  1 
ATOM   2536  O  OD1 . ASN   A  1 319 ? -5.590  -11.197 -19.408  1.00 84.47  ? 620  ASN   A OD1 1 
ATOM   2537  N  ND2 . ASN   A  1 319 ? -4.536  -9.775  -20.799  1.00 67.67  ? 620  ASN   A ND2 1 
ATOM   2538  N  N   . LEU   A  1 320 ? -9.761  -8.342  -18.536  1.00 71.01  ? 621  LEU   A N   1 
ATOM   2539  C  CA  . LEU   A  1 320 ? -10.537 -7.855  -17.417  1.00 73.79  ? 621  LEU   A CA  1 
ATOM   2540  C  C   . LEU   A  1 320 ? -10.971 -9.017  -16.529  1.00 74.44  ? 621  LEU   A C   1 
ATOM   2541  O  O   . LEU   A  1 320 ? -11.060 -10.168 -16.970  1.00 73.12  ? 621  LEU   A O   1 
ATOM   2542  C  CB  . LEU   A  1 320 ? -11.733 -7.065  -17.938  1.00 71.23  ? 621  LEU   A CB  1 
ATOM   2543  C  CG  . LEU   A  1 320 ? -11.269 -5.859  -18.752  1.00 69.14  ? 621  LEU   A CG  1 
ATOM   2544  C  CD1 . LEU   A  1 320 ? -12.454 -5.016  -19.199  1.00 63.28  ? 621  LEU   A CD1 1 
ATOM   2545  C  CD2 . LEU   A  1 320 ? -10.285 -5.030  -17.918  1.00 71.51  ? 621  LEU   A CD2 1 
ATOM   2546  N  N   . ASP   A  1 321 ? -11.203 -8.709  -15.248  1.00 73.96  ? 622  ASP   A N   1 
ATOM   2547  C  CA  . ASP   A  1 321 ? -11.815 -9.668  -14.331  1.00 65.72  ? 622  ASP   A CA  1 
ATOM   2548  C  C   . ASP   A  1 321 ? -13.299 -9.688  -14.630  1.00 63.80  ? 622  ASP   A C   1 
ATOM   2549  O  O   . ASP   A  1 321 ? -14.020 -8.750  -14.288  1.00 65.97  ? 622  ASP   A O   1 
ATOM   2550  C  CB  . ASP   A  1 321 ? -11.561 -9.295  -12.876  1.00 79.94  ? 622  ASP   A CB  1 
ATOM   2551  C  CG  . ASP   A  1 321 ? -12.487 -10.034 -11.923  1.00 84.06  ? 622  ASP   A CG  1 
ATOM   2552  O  OD1 . ASP   A  1 321 ? -13.037 -9.402  -10.989  1.00 88.57  ? 622  ASP   A OD1 1 
ATOM   2553  O  OD2 . ASP   A  1 321 ? -12.686 -11.249 -12.137  1.00 80.64  ? 622  ASP   A OD2 1 
ATOM   2554  N  N   . MET   A  1 322 ? -13.761 -10.745 -15.296  1.00 73.63  ? 623  MET   A N   1 
ATOM   2555  C  CA  . MET   A  1 322 ? -15.166 -10.880 -15.657  1.00 78.11  ? 623  MET   A CA  1 
ATOM   2556  C  C   . MET   A  1 322 ? -15.904 -11.855 -14.754  1.00 82.11  ? 623  MET   A C   1 
ATOM   2557  O  O   . MET   A  1 322 ? -16.930 -12.412 -15.160  1.00 85.35  ? 623  MET   A O   1 
ATOM   2558  C  CB  . MET   A  1 322 ? -15.300 -11.306 -17.110  1.00 75.37  ? 623  MET   A CB  1 
ATOM   2559  C  CG  . MET   A  1 322 ? -14.839 -10.251 -18.088  1.00 76.68  ? 623  MET   A CG  1 
ATOM   2560  S  SD  . MET   A  1 322 ? -14.448 -10.967 -19.684  1.00 75.81  ? 623  MET   A SD  1 
ATOM   2561  C  CE  . MET   A  1 322 ? -15.908 -11.953 -19.986  1.00 76.00  ? 623  MET   A CE  1 
ATOM   2562  N  N   . ARG   A  1 323 ? -15.395 -12.066 -13.538  1.00 81.88  ? 624  ARG   A N   1 
ATOM   2563  C  CA  . ARG   A  1 323 ? -16.046 -12.947 -12.577  1.00 86.32  ? 624  ARG   A CA  1 
ATOM   2564  C  C   . ARG   A  1 323 ? -17.147 -12.240 -11.797  1.00 85.49  ? 624  ARG   A C   1 
ATOM   2565  O  O   . ARG   A  1 323 ? -18.138 -12.878 -11.427  1.00 96.75  ? 624  ARG   A O   1 
ATOM   2566  C  CB  . ARG   A  1 323 ? -15.019 -13.525 -11.603  1.00 84.87  ? 624  ARG   A CB  1 
ATOM   2567  C  CG  . ARG   A  1 323 ? -13.972 -14.446 -12.224  1.00 89.40  ? 624  ARG   A CG  1 
ATOM   2568  C  CD  . ARG   A  1 323 ? -12.847 -14.673 -11.236  1.00 99.18  ? 624  ARG   A CD  1 
ATOM   2569  N  NE  . ARG   A  1 323 ? -12.599 -13.443 -10.487  1.00 108.59 ? 624  ARG   A NE  1 
ATOM   2570  C  CZ  . ARG   A  1 323 ? -11.737 -13.323 -9.485   1.00 111.13 ? 624  ARG   A CZ  1 
ATOM   2571  N  NH1 . ARG   A  1 323 ? -11.017 -14.372 -9.094   1.00 109.69 ? 624  ARG   A NH1 1 
ATOM   2572  N  NH2 . ARG   A  1 323 ? -11.603 -12.148 -8.876   1.00 111.44 ? 624  ARG   A NH2 1 
ATOM   2573  N  N   . LYS   A  1 324 ? -17.005 -10.940 -11.532  1.00 74.15  ? 625  LYS   A N   1 
ATOM   2574  C  CA  . LYS   A  1 324 ? -18.011 -10.202 -10.777  1.00 77.80  ? 625  LYS   A CA  1 
ATOM   2575  C  C   . LYS   A  1 324 ? -18.329 -8.883  -11.468  1.00 72.46  ? 625  LYS   A C   1 
ATOM   2576  O  O   . LYS   A  1 324 ? -17.432 -8.186  -11.947  1.00 71.85  ? 625  LYS   A O   1 
ATOM   2577  C  CB  . LYS   A  1 324 ? -17.560 -9.951  -9.317   1.00 68.29  ? 625  LYS   A CB  1 
ATOM   2578  C  CG  . LYS   A  1 324 ? -16.114 -9.498  -9.187   1.00 74.04  ? 625  LYS   A CG  1 
ATOM   2579  C  CD  . LYS   A  1 324 ? -15.636 -9.502  -7.740   1.00 84.43  ? 625  LYS   A CD  1 
ATOM   2580  C  CE  . LYS   A  1 324 ? -14.147 -9.173  -7.648   1.00 83.11  ? 625  LYS   A CE  1 
ATOM   2581  N  NZ  . LYS   A  1 324 ? -13.834 -7.828  -8.215   1.00 67.30  ? 625  LYS   A NZ  1 
ATOM   2582  N  N   . THR   A  1 325 ? -19.622 -8.543  -11.486  1.00 68.60  ? 626  THR   A N   1 
ATOM   2583  C  CA  . THR   A  1 325 ? -20.092 -7.358  -12.196  1.00 67.61  ? 626  THR   A CA  1 
ATOM   2584  C  C   . THR   A  1 325 ? -19.467 -6.079  -11.651  1.00 65.53  ? 626  THR   A C   1 
ATOM   2585  O  O   . THR   A  1 325 ? -19.214 -5.135  -12.410  1.00 53.15  ? 626  THR   A O   1 
ATOM   2586  C  CB  . THR   A  1 325 ? -21.620 -7.272  -12.098  1.00 67.15  ? 626  THR   A CB  1 
ATOM   2587  O  OG1 . THR   A  1 325 ? -21.990 -6.735  -10.823  1.00 64.10  ? 626  THR   A OG1 1 
ATOM   2588  C  CG2 . THR   A  1 325 ? -22.237 -8.651  -12.228  1.00 70.42  ? 626  THR   A CG2 1 
ATOM   2589  N  N   . SER   A  1 326 ? -19.222 -6.029  -10.342  1.00 66.42  ? 627  SER   A N   1 
ATOM   2590  C  CA  . SER   A  1 326 ? -18.719 -4.826  -9.690   1.00 63.04  ? 627  SER   A CA  1 
ATOM   2591  C  C   . SER   A  1 326 ? -17.327 -4.427  -10.165  1.00 60.63  ? 627  SER   A C   1 
ATOM   2592  O  O   . SER   A  1 326 ? -16.904 -3.299  -9.884   1.00 64.28  ? 627  SER   A O   1 
ATOM   2593  C  CB  . SER   A  1 326 ? -18.729 -5.008  -8.159   1.00 58.88  ? 627  SER   A CB  1 
ATOM   2594  O  OG  . SER   A  1 326 ? -18.625 -6.372  -7.783   1.00 52.69  ? 627  SER   A OG  1 
ATOM   2595  N  N   . SER   A  1 327 ? -16.605 -5.304  -10.870  1.00 52.06  ? 628  SER   A N   1 
ATOM   2596  C  CA  . SER   A  1 327 ? -15.367 -4.867  -11.503  1.00 55.89  ? 628  SER   A CA  1 
ATOM   2597  C  C   . SER   A  1 327 ? -15.623 -3.840  -12.593  1.00 48.73  ? 628  SER   A C   1 
ATOM   2598  O  O   . SER   A  1 327 ? -14.686 -3.151  -13.003  1.00 52.65  ? 628  SER   A O   1 
ATOM   2599  C  CB  . SER   A  1 327 ? -14.606 -6.054  -12.093  1.00 56.00  ? 628  SER   A CB  1 
ATOM   2600  O  OG  . SER   A  1 327 ? -15.107 -6.381  -13.373  1.00 63.25  ? 628  SER   A OG  1 
ATOM   2601  N  N   . LEU   A  1 328 ? -16.872 -3.694  -13.028  1.00 40.89  ? 629  LEU   A N   1 
ATOM   2602  C  CA  . LEU   A  1 328 ? -17.232 -2.784  -14.108  1.00 54.62  ? 629  LEU   A CA  1 
ATOM   2603  C  C   . LEU   A  1 328 ? -16.435 -3.072  -15.375  1.00 58.60  ? 629  LEU   A C   1 
ATOM   2604  O  O   . LEU   A  1 328 ? -16.044 -2.159  -16.096  1.00 67.59  ? 629  LEU   A O   1 
ATOM   2605  C  CB  . LEU   A  1 328 ? -17.057 -1.330  -13.684  1.00 57.49  ? 629  LEU   A CB  1 
ATOM   2606  C  CG  . LEU   A  1 328 ? -17.866 -0.844  -12.486  1.00 47.49  ? 629  LEU   A CG  1 
ATOM   2607  C  CD1 . LEU   A  1 328 ? -17.878 0.665   -12.476  1.00 45.18  ? 629  LEU   A CD1 1 
ATOM   2608  C  CD2 . LEU   A  1 328 ? -19.292 -1.386  -12.489  1.00 46.94  ? 629  LEU   A CD2 1 
ATOM   2609  N  N   . TRP   A  1 329 ? -16.191 -4.357  -15.656  1.00 55.51  ? 630  TRP   A N   1 
ATOM   2610  C  CA  . TRP   A  1 329 ? -15.551 -4.702  -16.922  1.00 58.60  ? 630  TRP   A CA  1 
ATOM   2611  C  C   . TRP   A  1 329 ? -16.414 -4.273  -18.106  1.00 58.12  ? 630  TRP   A C   1 
ATOM   2612  O  O   . TRP   A  1 329 ? -15.925 -3.626  -19.037  1.00 63.23  ? 630  TRP   A O   1 
ATOM   2613  C  CB  . TRP   A  1 329 ? -15.222 -6.200  -16.983  1.00 57.24  ? 630  TRP   A CB  1 
ATOM   2614  C  CG  . TRP   A  1 329 ? -16.368 -7.177  -16.868  1.00 56.31  ? 630  TRP   A CG  1 
ATOM   2615  C  CD1 . TRP   A  1 329 ? -16.829 -7.760  -15.728  1.00 60.02  ? 630  TRP   A CD1 1 
ATOM   2616  C  CD2 . TRP   A  1 329 ? -17.151 -7.725  -17.942  1.00 60.66  ? 630  TRP   A CD2 1 
ATOM   2617  N  NE1 . TRP   A  1 329 ? -17.865 -8.621  -16.015  1.00 63.07  ? 630  TRP   A NE1 1 
ATOM   2618  C  CE2 . TRP   A  1 329 ? -18.080 -8.616  -17.369  1.00 65.38  ? 630  TRP   A CE2 1 
ATOM   2619  C  CE3 . TRP   A  1 329 ? -17.166 -7.538  -19.328  1.00 61.39  ? 630  TRP   A CE3 1 
ATOM   2620  C  CZ2 . TRP   A  1 329 ? -19.018 -9.314  -18.137  1.00 57.44  ? 630  TRP   A CZ2 1 
ATOM   2621  C  CZ3 . TRP   A  1 329 ? -18.090 -8.237  -20.080  1.00 50.22  ? 630  TRP   A CZ3 1 
ATOM   2622  C  CH2 . TRP   A  1 329 ? -19.006 -9.108  -19.486  1.00 53.88  ? 630  TRP   A CH2 1 
ATOM   2623  N  N   . LYS   A  1 330 ? -17.709 -4.604  -18.075  1.00 55.97  ? 631  LYS   A N   1 
ATOM   2624  C  CA  . LYS   A  1 330 ? -18.630 -4.172  -19.123  1.00 50.74  ? 631  LYS   A CA  1 
ATOM   2625  C  C   . LYS   A  1 330 ? -18.485 -2.687  -19.415  1.00 54.50  ? 631  LYS   A C   1 
ATOM   2626  O  O   . LYS   A  1 330 ? -18.288 -2.285  -20.566  1.00 63.83  ? 631  LYS   A O   1 
ATOM   2627  C  CB  . LYS   A  1 330 ? -20.070 -4.485  -18.722  1.00 47.30  ? 631  LYS   A CB  1 
ATOM   2628  C  CG  . LYS   A  1 330 ? -20.478 -5.891  -19.052  1.00 60.34  ? 631  LYS   A CG  1 
ATOM   2629  C  CD  . LYS   A  1 330 ? -21.964 -6.044  -18.934  1.00 61.55  ? 631  LYS   A CD  1 
ATOM   2630  C  CE  . LYS   A  1 330 ? -22.350 -7.498  -19.026  1.00 63.93  ? 631  LYS   A CE  1 
ATOM   2631  N  NZ  . LYS   A  1 330 ? -23.818 -7.636  -18.888  1.00 63.93  ? 631  LYS   A NZ  1 
ATOM   2632  N  N   . ASP   A  1 331 ? -18.568 -1.859  -18.374  1.00 56.19  ? 632  ASP   A N   1 
ATOM   2633  C  CA  . ASP   A  1 331 ? -18.428 -0.415  -18.548  1.00 56.89  ? 632  ASP   A CA  1 
ATOM   2634  C  C   . ASP   A  1 331 ? -17.090 -0.059  -19.187  1.00 53.74  ? 632  ASP   A C   1 
ATOM   2635  O  O   . ASP   A  1 331 ? -17.023 0.793   -20.083  1.00 58.81  ? 632  ASP   A O   1 
ATOM   2636  C  CB  . ASP   A  1 331 ? -18.573 0.290   -17.193  1.00 55.97  ? 632  ASP   A CB  1 
ATOM   2637  C  CG  . ASP   A  1 331 ? -19.840 -0.116  -16.442  1.00 47.77  ? 632  ASP   A CG  1 
ATOM   2638  O  OD1 . ASP   A  1 331 ? -19.909 -1.245  -15.910  1.00 47.51  ? 632  ASP   A OD1 1 
ATOM   2639  O  OD2 . ASP   A  1 331 ? -20.771 0.706   -16.367  1.00 45.97  ? 632  ASP   A OD2 1 
ATOM   2640  N  N   . GLN   A  1 332 ? -16.009 -0.705  -18.731  1.00 48.31  ? 633  GLN   A N   1 
ATOM   2641  C  CA  . GLN   A  1 332 ? -14.672 -0.381  -19.217  1.00 47.25  ? 633  GLN   A CA  1 
ATOM   2642  C  C   . GLN   A  1 332 ? -14.511 -0.783  -20.675  1.00 54.52  ? 633  GLN   A C   1 
ATOM   2643  O  O   . GLN   A  1 332 ? -14.033 0.004   -21.502  1.00 50.30  ? 633  GLN   A O   1 
ATOM   2644  C  CB  . GLN   A  1 332 ? -13.635 -1.092  -18.374  1.00 43.49  ? 633  GLN   A CB  1 
ATOM   2645  C  CG  . GLN   A  1 332 ? -12.470 -0.254  -17.947  1.00 60.14  ? 633  GLN   A CG  1 
ATOM   2646  C  CD  . GLN   A  1 332 ? -11.725 -0.925  -16.806  1.00 70.42  ? 633  GLN   A CD  1 
ATOM   2647  O  OE1 . GLN   A  1 332 ? -11.762 -2.151  -16.667  1.00 68.87  ? 633  GLN   A OE1 1 
ATOM   2648  N  NE2 . GLN   A  1 332 ? -11.065 -0.128  -15.971  1.00 80.58  ? 633  GLN   A NE2 1 
ATOM   2649  N  N   . ALA   A  1 333 ? -14.906 -2.015  -21.001  1.00 49.49  ? 634  ALA   A N   1 
ATOM   2650  C  CA  . ALA   A  1 333 ? -14.802 -2.496  -22.365  1.00 51.25  ? 634  ALA   A CA  1 
ATOM   2651  C  C   . ALA   A  1 333 ? -15.695 -1.698  -23.304  1.00 59.17  ? 634  ALA   A C   1 
ATOM   2652  O  O   . ALA   A  1 333 ? -15.333 -1.495  -24.466  1.00 53.27  ? 634  ALA   A O   1 
ATOM   2653  C  CB  . ALA   A  1 333 ? -15.146 -3.986  -22.406  1.00 49.85  ? 634  ALA   A CB  1 
ATOM   2654  N  N   . LEU   A  1 334 ? -16.846 -1.220  -22.816  1.00 64.55  ? 635  LEU   A N   1 
ATOM   2655  C  CA  . LEU   A  1 334 ? -17.738 -0.437  -23.663  1.00 56.77  ? 635  LEU   A CA  1 
ATOM   2656  C  C   . LEU   A  1 334 ? -17.086 0.867   -24.106  1.00 56.47  ? 635  LEU   A C   1 
ATOM   2657  O  O   . LEU   A  1 334 ? -17.259 1.283   -25.256  1.00 53.56  ? 635  LEU   A O   1 
ATOM   2658  C  CB  . LEU   A  1 334 ? -19.057 -0.149  -22.941  1.00 51.36  ? 635  LEU   A CB  1 
ATOM   2659  C  CG  . LEU   A  1 334 ? -20.025 0.812   -23.655  1.00 44.54  ? 635  LEU   A CG  1 
ATOM   2660  C  CD1 . LEU   A  1 334 ? -20.501 0.216   -24.922  1.00 46.25  ? 635  LEU   A CD1 1 
ATOM   2661  C  CD2 . LEU   A  1 334 ? -21.219 1.125   -22.775  1.00 58.53  ? 635  LEU   A CD2 1 
ATOM   2662  N  N   . VAL   A  1 335 ? -16.342 1.537   -23.213  1.00 57.90  ? 636  VAL   A N   1 
ATOM   2663  C  CA  . VAL   A  1 335 ? -15.751 2.820   -23.596  1.00 52.23  ? 636  VAL   A CA  1 
ATOM   2664  C  C   . VAL   A  1 335 ? -14.731 2.625   -24.708  1.00 54.31  ? 636  VAL   A C   1 
ATOM   2665  O  O   . VAL   A  1 335 ? -14.734 3.356   -25.703  1.00 52.60  ? 636  VAL   A O   1 
ATOM   2666  C  CB  . VAL   A  1 335 ? -15.110 3.534   -22.398  1.00 47.19  ? 636  VAL   A CB  1 
ATOM   2667  C  CG1 . VAL   A  1 335 ? -14.100 4.560   -22.923  1.00 32.18  ? 636  VAL   A CG1 1 
ATOM   2668  C  CG2 . VAL   A  1 335 ? -16.165 4.220   -21.536  1.00 37.15  ? 636  VAL   A CG2 1 
ATOM   2669  N  N   . GLU   A  1 336 ? -13.837 1.642   -24.552  1.00 49.63  ? 637  GLU   A N   1 
ATOM   2670  C  CA  . GLU   A  1 336 ? -12.784 1.449   -25.545  1.00 50.36  ? 637  GLU   A CA  1 
ATOM   2671  C  C   . GLU   A  1 336 ? -13.360 1.199   -26.945  1.00 59.42  ? 637  GLU   A C   1 
ATOM   2672  O  O   . GLU   A  1 336 ? -12.811 1.675   -27.946  1.00 53.16  ? 637  GLU   A O   1 
ATOM   2673  C  CB  . GLU   A  1 336 ? -11.866 0.303   -25.121  1.00 46.30  ? 637  GLU   A CB  1 
ATOM   2674  C  CG  . GLU   A  1 336 ? -11.015 0.577   -23.869  1.00 52.44  ? 637  GLU   A CG  1 
ATOM   2675  C  CD  . GLU   A  1 336 ? -9.934  1.651   -24.060  1.00 55.85  ? 637  GLU   A CD  1 
ATOM   2676  O  OE1 . GLU   A  1 336 ? -10.040 2.497   -24.956  1.00 60.23  ? 637  GLU   A OE1 1 
ATOM   2677  O  OE2 . GLU   A  1 336 ? -8.965  1.664   -23.289  1.00 65.44  ? 637  GLU   A OE2 1 
ATOM   2678  N  N   . ILE   A  1 337 ? -14.465 0.458   -27.031  1.00 57.27  ? 638  ILE   A N   1 
ATOM   2679  C  CA  . ILE   A  1 337 ? -15.106 0.224   -28.320  1.00 45.70  ? 638  ILE   A CA  1 
ATOM   2680  C  C   . ILE   A  1 337 ? -15.557 1.544   -28.932  1.00 50.19  ? 638  ILE   A C   1 
ATOM   2681  O  O   . ILE   A  1 337 ? -15.338 1.809   -30.121  1.00 55.44  ? 638  ILE   A O   1 
ATOM   2682  C  CB  . ILE   A  1 337 ? -16.285 -0.756  -28.159  1.00 44.81  ? 638  ILE   A CB  1 
ATOM   2683  C  CG1 . ILE   A  1 337 ? -15.775 -2.168  -27.846  1.00 48.10  ? 638  ILE   A CG1 1 
ATOM   2684  C  CG2 . ILE   A  1 337 ? -17.165 -0.757  -29.412  1.00 36.12  ? 638  ILE   A CG2 1 
ATOM   2685  C  CD1 . ILE   A  1 337 ? -16.788 -3.023  -27.123  1.00 47.26  ? 638  ILE   A CD1 1 
ATOM   2686  N  N   . ASN   A  1 338 ? -16.199 2.393   -28.130  1.00 50.77  ? 639  ASN   A N   1 
ATOM   2687  C  CA  . ASN   A  1 338 ? -16.685 3.665   -28.655  1.00 57.09  ? 639  ASN   A CA  1 
ATOM   2688  C  C   . ASN   A  1 338 ? -15.537 4.597   -29.024  1.00 55.31  ? 639  ASN   A C   1 
ATOM   2689  O  O   . ASN   A  1 338 ? -15.695 5.455   -29.903  1.00 37.43  ? 639  ASN   A O   1 
ATOM   2690  C  CB  . ASN   A  1 338 ? -17.630 4.313   -27.643  1.00 47.22  ? 639  ASN   A CB  1 
ATOM   2691  C  CG  . ASN   A  1 338 ? -19.014 3.705   -27.690  1.00 51.69  ? 639  ASN   A CG  1 
ATOM   2692  O  OD1 . ASN   A  1 338 ? -19.877 4.141   -28.457  1.00 59.60  ? 639  ASN   A OD1 1 
ATOM   2693  N  ND2 . ASN   A  1 338 ? -19.224 2.667   -26.897  1.00 49.98  ? 639  ASN   A ND2 1 
ATOM   2694  N  N   . ILE   A  1 339 ? -14.388 4.449   -28.356  1.00 52.57  ? 640  ILE   A N   1 
ATOM   2695  C  CA  . ILE   A  1 339 ? -13.185 5.154   -28.778  1.00 50.04  ? 640  ILE   A CA  1 
ATOM   2696  C  C   . ILE   A  1 339 ? -12.745 4.635   -30.129  1.00 46.66  ? 640  ILE   A C   1 
ATOM   2697  O  O   . ILE   A  1 339 ? -12.350 5.407   -31.009  1.00 50.93  ? 640  ILE   A O   1 
ATOM   2698  C  CB  . ILE   A  1 339 ? -12.068 5.009   -27.718  1.00 46.56  ? 640  ILE   A CB  1 
ATOM   2699  C  CG1 . ILE   A  1 339 ? -12.281 6.000   -26.567  1.00 42.58  ? 640  ILE   A CG1 1 
ATOM   2700  C  CG2 . ILE   A  1 339 ? -10.679 5.210   -28.334  1.00 44.08  ? 640  ILE   A CG2 1 
ATOM   2701  C  CD1 . ILE   A  1 339 ? -11.484 5.689   -25.340  1.00 50.30  ? 640  ILE   A CD1 1 
ATOM   2702  N  N   . ALA   A  1 340 ? -12.838 3.313   -30.315  1.00 43.10  ? 641  ALA   A N   1 
ATOM   2703  C  CA  . ALA   A  1 340 ? -12.418 2.676   -31.555  1.00 55.77  ? 641  ALA   A CA  1 
ATOM   2704  C  C   . ALA   A  1 340 ? -13.320 3.074   -32.718  1.00 53.98  ? 641  ALA   A C   1 
ATOM   2705  O  O   . ALA   A  1 340 ? -12.832 3.370   -33.814  1.00 54.68  ? 641  ALA   A O   1 
ATOM   2706  C  CB  . ALA   A  1 340 ? -12.405 1.158   -31.375  1.00 56.57  ? 641  ALA   A CB  1 
ATOM   2707  N  N   . VAL   A  1 341 ? -14.635 3.074   -32.500  1.00 51.25  ? 642  VAL   A N   1 
ATOM   2708  C  CA  . VAL   A  1 341 ? -15.553 3.528   -33.536  1.00 44.67  ? 642  VAL   A CA  1 
ATOM   2709  C  C   . VAL   A  1 341 ? -15.225 4.953   -33.943  1.00 46.74  ? 642  VAL   A C   1 
ATOM   2710  O  O   . VAL   A  1 341 ? -15.164 5.271   -35.131  1.00 43.10  ? 642  VAL   A O   1 
ATOM   2711  C  CB  . VAL   A  1 341 ? -17.011 3.403   -33.069  1.00 36.24  ? 642  VAL   A CB  1 
ATOM   2712  C  CG1 . VAL   A  1 341 ? -17.903 4.115   -34.051  1.00 44.36  ? 642  VAL   A CG1 1 
ATOM   2713  C  CG2 . VAL   A  1 341 ? -17.410 1.941   -32.992  1.00 37.46  ? 642  VAL   A CG2 1 
ATOM   2714  N  N   . LEU   A  1 342 ? -15.009 5.839   -32.974  1.00 45.09  ? 643  LEU   A N   1 
ATOM   2715  C  CA  . LEU   A  1 342 ? -14.805 7.231   -33.360  1.00 45.84  ? 643  LEU   A CA  1 
ATOM   2716  C  C   . LEU   A  1 342 ? -13.453 7.415   -34.032  1.00 52.79  ? 643  LEU   A C   1 
ATOM   2717  O  O   . LEU   A  1 342 ? -13.324 8.201   -34.972  1.00 44.45  ? 643  LEU   A O   1 
ATOM   2718  C  CB  . LEU   A  1 342 ? -14.951 8.164   -32.158  1.00 36.91  ? 643  LEU   A CB  1 
ATOM   2719  C  CG  . LEU   A  1 342 ? -16.381 8.246   -31.618  1.00 35.65  ? 643  LEU   A CG  1 
ATOM   2720  C  CD1 . LEU   A  1 342 ? -16.468 8.829   -30.228  1.00 34.89  ? 643  LEU   A CD1 1 
ATOM   2721  C  CD2 . LEU   A  1 342 ? -17.276 9.006   -32.578  1.00 33.72  ? 643  LEU   A CD2 1 
ATOM   2722  N  N   . TYR   A  1 343 ? -12.432 6.693   -33.582  1.00 53.10  ? 644  TYR   A N   1 
ATOM   2723  C  CA  . TYR   A  1 343 ? -11.125 6.855   -34.200  1.00 44.13  ? 644  TYR   A CA  1 
ATOM   2724  C  C   . TYR   A  1 343 ? -11.114 6.319   -35.615  1.00 54.57  ? 644  TYR   A C   1 
ATOM   2725  O  O   . TYR   A  1 343 ? -10.401 6.841   -36.482  1.00 55.11  ? 644  TYR   A O   1 
ATOM   2726  C  CB  . TYR   A  1 343 ? -10.085 6.123   -33.372  1.00 42.57  ? 644  TYR   A CB  1 
ATOM   2727  C  CG  . TYR   A  1 343 ? -8.729  5.942   -34.016  1.00 39.56  ? 644  TYR   A CG  1 
ATOM   2728  C  CD1 . TYR   A  1 343 ? -7.899  7.023   -34.244  1.00 46.94  ? 644  TYR   A CD1 1 
ATOM   2729  C  CD2 . TYR   A  1 343 ? -8.251  4.679   -34.329  1.00 36.64  ? 644  TYR   A CD2 1 
ATOM   2730  C  CE1 . TYR   A  1 343 ? -6.640  6.855   -34.790  1.00 48.33  ? 644  TYR   A CE1 1 
ATOM   2731  C  CE2 . TYR   A  1 343 ? -6.988  4.502   -34.870  1.00 44.57  ? 644  TYR   A CE2 1 
ATOM   2732  C  CZ  . TYR   A  1 343 ? -6.190  5.596   -35.101  1.00 54.36  ? 644  TYR   A CZ  1 
ATOM   2733  O  OH  . TYR   A  1 343 ? -4.931  5.430   -35.649  1.00 69.63  ? 644  TYR   A OH  1 
ATOM   2734  N  N   . SER   A  1 344 ? -11.887 5.268   -35.856  1.00 53.05  ? 645  SER   A N   1 
ATOM   2735  C  CA  . SER   A  1 344 ? -11.836 4.605   -37.141  1.00 46.60  ? 645  SER   A CA  1 
ATOM   2736  C  C   . SER   A  1 344 ? -12.498 5.459   -38.211  1.00 47.29  ? 645  SER   A C   1 
ATOM   2737  O  O   . SER   A  1 344 ? -11.941 5.645   -39.297  1.00 55.01  ? 645  SER   A O   1 
ATOM   2738  C  CB  . SER   A  1 344 ? -12.485 3.234   -37.020  1.00 45.06  ? 645  SER   A CB  1 
ATOM   2739  O  OG  . SER   A  1 344 ? -11.600 2.350   -36.355  1.00 43.97  ? 645  SER   A OG  1 
ATOM   2740  N  N   . PHE   A  1 345 ? -13.677 6.008   -37.910  1.00 46.20  ? 646  PHE   A N   1 
ATOM   2741  C  CA  . PHE   A  1 345 ? -14.356 6.897   -38.847  1.00 37.97  ? 646  PHE   A CA  1 
ATOM   2742  C  C   . PHE   A  1 345 ? -13.519 8.135   -39.135  1.00 53.14  ? 646  PHE   A C   1 
ATOM   2743  O  O   . PHE   A  1 345 ? -13.342 8.519   -40.293  1.00 64.10  ? 646  PHE   A O   1 
ATOM   2744  C  CB  . PHE   A  1 345 ? -15.720 7.298   -38.289  1.00 29.08  ? 646  PHE   A CB  1 
ATOM   2745  C  CG  . PHE   A  1 345 ? -16.799 6.298   -38.550  1.00 38.30  ? 646  PHE   A CG  1 
ATOM   2746  C  CD1 . PHE   A  1 345 ? -16.659 4.988   -38.136  1.00 30.12  ? 646  PHE   A CD1 1 
ATOM   2747  C  CD2 . PHE   A  1 345 ? -17.961 6.674   -39.204  1.00 42.90  ? 646  PHE   A CD2 1 
ATOM   2748  C  CE1 . PHE   A  1 345 ? -17.664 4.063   -38.368  1.00 35.27  ? 646  PHE   A CE1 1 
ATOM   2749  C  CE2 . PHE   A  1 345 ? -18.964 5.754   -39.454  1.00 38.65  ? 646  PHE   A CE2 1 
ATOM   2750  C  CZ  . PHE   A  1 345 ? -18.818 4.446   -39.040  1.00 37.78  ? 646  PHE   A CZ  1 
ATOM   2751  N  N   . GLN   A  1 346 ? -12.996 8.780   -38.089  1.00 49.38  ? 647  GLN   A N   1 
ATOM   2752  C  CA  . GLN   A  1 346 ? -12.236 10.006  -38.305  1.00 48.83  ? 647  GLN   A CA  1 
ATOM   2753  C  C   . GLN   A  1 346 ? -11.011 9.740   -39.168  1.00 53.71  ? 647  GLN   A C   1 
ATOM   2754  O  O   . GLN   A  1 346 ? -10.646 10.571  -40.003  1.00 64.43  ? 647  GLN   A O   1 
ATOM   2755  C  CB  . GLN   A  1 346 ? -11.823 10.620  -36.965  1.00 47.97  ? 647  GLN   A CB  1 
ATOM   2756  C  CG  . GLN   A  1 346 ? -12.978 11.133  -36.106  1.00 58.40  ? 647  GLN   A CG  1 
ATOM   2757  C  CD  . GLN   A  1 346 ? -12.553 11.401  -34.672  1.00 59.78  ? 647  GLN   A CD  1 
ATOM   2758  O  OE1 . GLN   A  1 346 ? -13.143 12.229  -33.984  1.00 63.77  ? 647  GLN   A OE1 1 
ATOM   2759  N  NE2 . GLN   A  1 346 ? -11.516 10.700  -34.219  1.00 58.51  ? 647  GLN   A NE2 1 
ATOM   2760  N  N   . SER   A  1 347 ? -10.366 8.583   -38.977  1.00 42.96  ? 648  SER   A N   1 
ATOM   2761  C  CA  . SER   A  1 347 ? -9.173  8.249   -39.745  1.00 39.56  ? 648  SER   A CA  1 
ATOM   2762  C  C   . SER   A  1 347 ? -9.497  8.118   -41.232  1.00 55.68  ? 648  SER   A C   1 
ATOM   2763  O  O   . SER   A  1 347 ? -8.722  8.552   -42.095  1.00 57.47  ? 648  SER   A O   1 
ATOM   2764  C  CB  . SER   A  1 347 ? -8.561  6.953   -39.211  1.00 38.56  ? 648  SER   A CB  1 
ATOM   2765  O  OG  . SER   A  1 347 ? -8.036  7.126   -37.896  1.00 50.30  ? 648  SER   A OG  1 
ATOM   2766  N  N   . ASP   A  1 348 ? -10.643 7.528   -41.551  1.00 50.99  ? 649  ASP   A N   1 
ATOM   2767  C  CA  . ASP   A  1 348 ? -11.072 7.385   -42.927  1.00 46.10  ? 649  ASP   A CA  1 
ATOM   2768  C  C   . ASP   A  1 348 ? -11.903 8.569   -43.398  1.00 55.47  ? 649  ASP   A C   1 
ATOM   2769  O  O   . ASP   A  1 348 ? -12.634 8.444   -44.382  1.00 53.21  ? 649  ASP   A O   1 
ATOM   2770  C  CB  . ASP   A  1 348 ? -11.844 6.080   -43.093  1.00 36.11  ? 649  ASP   A CB  1 
ATOM   2771  C  CG  . ASP   A  1 348 ? -11.001 4.865   -42.754  1.00 49.94  ? 649  ASP   A CG  1 
ATOM   2772  O  OD1 . ASP   A  1 348 ? -9.796  5.038   -42.437  1.00 48.39  ? 649  ASP   A OD1 1 
ATOM   2773  O  OD2 . ASP   A  1 348 ? -11.550 3.741   -42.797  1.00 54.54  ? 649  ASP   A OD2 1 
ATOM   2774  N  N   . LYS   A  1 349 ? -11.811 9.709   -42.709  1.00 58.83  ? 650  LYS   A N   1 
ATOM   2775  C  CA  . LYS   A  1 349 ? -12.492 10.944  -43.093  1.00 53.16  ? 650  LYS   A CA  1 
ATOM   2776  C  C   . LYS   A  1 349 ? -13.935 10.681  -43.524  1.00 51.37  ? 650  LYS   A C   1 
ATOM   2777  O  O   . LYS   A  1 349 ? -14.433 11.233  -44.512  1.00 52.70  ? 650  LYS   A O   1 
ATOM   2778  C  CB  . LYS   A  1 349 ? -11.659 11.656  -44.159  1.00 47.84  ? 650  LYS   A CB  1 
ATOM   2779  C  CG  . LYS   A  1 349 ? -10.307 12.135  -43.562  1.00 48.24  ? 650  LYS   A CG  1 
ATOM   2780  C  CD  . LYS   A  1 349 ? -9.209  12.217  -44.593  1.00 69.15  ? 650  LYS   A CD  1 
ATOM   2781  C  CE  . LYS   A  1 349 ? -9.242  13.535  -45.351  1.00 86.39  ? 650  LYS   A CE  1 
ATOM   2782  N  NZ  . LYS   A  1 349 ? -8.381  14.587  -44.731  1.00 95.73  ? 650  LYS   A NZ  1 
ATOM   2783  N  N   . VAL   A  1 350 ? -14.597 9.816   -42.764  1.00 44.48  ? 651  VAL   A N   1 
ATOM   2784  C  CA  . VAL   A  1 350 ? -16.028 9.565   -42.849  1.00 41.07  ? 651  VAL   A CA  1 
ATOM   2785  C  C   . VAL   A  1 350 ? -16.702 10.273  -41.677  1.00 45.47  ? 651  VAL   A C   1 
ATOM   2786  O  O   . VAL   A  1 350 ? -16.365 10.021  -40.510  1.00 41.37  ? 651  VAL   A O   1 
ATOM   2787  C  CB  . VAL   A  1 350 ? -16.315 8.057   -42.826  1.00 36.40  ? 651  VAL   A CB  1 
ATOM   2788  C  CG1 . VAL   A  1 350 ? -17.809 7.782   -42.859  1.00 38.97  ? 651  VAL   A CG1 1 
ATOM   2789  C  CG2 . VAL   A  1 350 ? -15.576 7.357   -43.964  1.00 37.54  ? 651  VAL   A CG2 1 
ATOM   2790  N  N   . THR   A  1 351 ? -17.656 11.151  -41.992  1.00 41.87  ? 652  THR   A N   1 
ATOM   2791  C  CA  . THR   A  1 351 ? -18.344 11.939  -40.979  1.00 35.42  ? 652  THR   A CA  1 
ATOM   2792  C  C   . THR   A  1 351 ? -18.831 11.058  -39.845  1.00 44.72  ? 652  THR   A C   1 
ATOM   2793  O  O   . THR   A  1 351 ? -19.302 9.938   -40.066  1.00 44.99  ? 652  THR   A O   1 
ATOM   2794  C  CB  . THR   A  1 351 ? -19.541 12.676  -41.585  1.00 42.31  ? 652  THR   A CB  1 
ATOM   2795  O  OG1 . THR   A  1 351 ? -19.121 13.450  -42.717  1.00 52.04  ? 652  THR   A OG1 1 
ATOM   2796  C  CG2 . THR   A  1 351 ? -20.183 13.596  -40.543  1.00 38.08  ? 652  THR   A CG2 1 
ATOM   2797  N  N   . ILE   A  1 352 ? -18.678 11.574  -38.623  1.00 45.13  ? 653  ILE   A N   1 
ATOM   2798  C  CA  . ILE   A  1 352 ? -19.295 11.003  -37.432  1.00 38.53  ? 653  ILE   A CA  1 
ATOM   2799  C  C   . ILE   A  1 352 ? -19.266 12.091  -36.379  1.00 43.83  ? 653  ILE   A C   1 
ATOM   2800  O  O   . ILE   A  1 352 ? -18.479 13.042  -36.475  1.00 45.91  ? 653  ILE   A O   1 
ATOM   2801  C  CB  . ILE   A  1 352 ? -18.520 9.747   -36.971  1.00 40.52  ? 653  ILE   A CB  1 
ATOM   2802  C  CG1 . ILE   A  1 352 ? -19.342 8.889   -36.002  1.00 29.55  ? 653  ILE   A CG1 1 
ATOM   2803  C  CG2 . ILE   A  1 352 ? -17.175 10.165  -36.389  1.00 31.19  ? 653  ILE   A CG2 1 
ATOM   2804  C  CD1 . ILE   A  1 352 ? -18.720 7.484   -35.800  1.00 24.94  ? 653  ILE   A CD1 1 
ATOM   2805  N  N   . VAL   A  1 353 ? -20.120 11.954  -35.360  1.00 47.68  ? 654  VAL   A N   1 
ATOM   2806  C  CA  . VAL   A  1 353 ? -20.143 12.866  -34.214  1.00 44.97  ? 654  VAL   A CA  1 
ATOM   2807  C  C   . VAL   A  1 353 ? -20.226 12.049  -32.924  1.00 43.47  ? 654  VAL   A C   1 
ATOM   2808  O  O   . VAL   A  1 353 ? -20.993 11.085  -32.846  1.00 43.59  ? 654  VAL   A O   1 
ATOM   2809  C  CB  . VAL   A  1 353 ? -21.304 13.884  -34.323  1.00 40.88  ? 654  VAL   A CB  1 
ATOM   2810  C  CG1 . VAL   A  1 353 ? -22.635 13.293  -33.884  1.00 32.38  ? 654  VAL   A CG1 1 
ATOM   2811  C  CG2 . VAL   A  1 353 ? -20.993 15.152  -33.562  1.00 45.27  ? 654  VAL   A CG2 1 
ATOM   2812  N  N   . ASP   A  1 354 ? -19.396 12.396  -31.936  1.00 48.29  ? 655  ASP   A N   1 
ATOM   2813  C  CA  . ASP   A  1 354 ? -19.419 11.706  -30.647  1.00 50.65  ? 655  ASP   A CA  1 
ATOM   2814  C  C   . ASP   A  1 354 ? -20.602 12.179  -29.816  1.00 43.06  ? 655  ASP   A C   1 
ATOM   2815  O  O   . ASP   A  1 354 ? -21.182 13.243  -30.066  1.00 44.56  ? 655  ASP   A O   1 
ATOM   2816  C  CB  . ASP   A  1 354 ? -18.123 11.939  -29.853  1.00 52.32  ? 655  ASP   A CB  1 
ATOM   2817  C  CG  . ASP   A  1 354 ? -17.902 13.405  -29.513  1.00 53.40  ? 655  ASP   A CG  1 
ATOM   2818  O  OD1 . ASP   A  1 354 ? -16.963 14.016  -30.063  1.00 66.26  ? 655  ASP   A OD1 1 
ATOM   2819  O  OD2 . ASP   A  1 354 ? -18.680 13.962  -28.719  1.00 56.34  ? 655  ASP   A OD2 1 
ATOM   2820  N  N   . HIS   A  1 355 ? -20.927 11.412  -28.771  1.00 44.32  ? 656  HIS   A N   1 
ATOM   2821  C  CA  . HIS   A  1 355 ? -22.128 11.771  -28.019  1.00 39.08  ? 656  HIS   A CA  1 
ATOM   2822  C  C   . HIS   A  1 355 ? -21.984 13.093  -27.284  1.00 35.55  ? 656  HIS   A C   1 
ATOM   2823  O  O   . HIS   A  1 355 ? -22.996 13.736  -26.991  1.00 40.91  ? 656  HIS   A O   1 
ATOM   2824  C  CB  . HIS   A  1 355 ? -22.539 10.663  -27.050  1.00 34.83  ? 656  HIS   A CB  1 
ATOM   2825  C  CG  . HIS   A  1 355 ? -21.428 10.101  -26.221  1.00 46.19  ? 656  HIS   A CG  1 
ATOM   2826  N  ND1 . HIS   A  1 355 ? -20.502 9.206   -26.718  1.00 48.67  ? 656  HIS   A ND1 1 
ATOM   2827  C  CD2 . HIS   A  1 355 ? -21.136 10.254  -24.909  1.00 39.57  ? 656  HIS   A CD2 1 
ATOM   2828  C  CE1 . HIS   A  1 355 ? -19.669 8.857   -25.752  1.00 44.70  ? 656  HIS   A CE1 1 
ATOM   2829  N  NE2 . HIS   A  1 355 ? -20.031 9.481   -24.647  1.00 46.11  ? 656  HIS   A NE2 1 
ATOM   2830  N  N   . HIS   A  1 356 ? -20.764 13.547  -27.032  1.00 35.48  ? 657  HIS   A N   1 
ATOM   2831  C  CA  . HIS   A  1 356 ? -20.623 14.803  -26.313  1.00 38.87  ? 657  HIS   A CA  1 
ATOM   2832  C  C   . HIS   A  1 356 ? -20.907 15.987  -27.215  1.00 46.37  ? 657  HIS   A C   1 
ATOM   2833  O  O   . HIS   A  1 356 ? -21.723 16.851  -26.872  1.00 53.77  ? 657  HIS   A O   1 
ATOM   2834  C  CB  . HIS   A  1 356 ? -19.233 14.908  -25.709  1.00 40.59  ? 657  HIS   A CB  1 
ATOM   2835  C  CG  . HIS   A  1 356 ? -18.958 13.856  -24.691  1.00 42.47  ? 657  HIS   A CG  1 
ATOM   2836  N  ND1 . HIS   A  1 356 ? -19.532 13.869  -23.442  1.00 45.39  ? 657  HIS   A ND1 1 
ATOM   2837  C  CD2 . HIS   A  1 356 ? -18.189 12.744  -24.748  1.00 43.83  ? 657  HIS   A CD2 1 
ATOM   2838  C  CE1 . HIS   A  1 356 ? -19.115 12.813  -22.767  1.00 48.91  ? 657  HIS   A CE1 1 
ATOM   2839  N  NE2 . HIS   A  1 356 ? -18.298 12.115  -23.539  1.00 44.20  ? 657  HIS   A NE2 1 
ATOM   2840  N  N   . SER   A  1 357 ? -20.239 16.050  -28.369  1.00 53.67  ? 658  SER   A N   1 
ATOM   2841  C  CA  A SER   A  1 357 ? -20.506 17.134  -29.308  0.72 53.86  ? 658  SER   A CA  1 
ATOM   2842  C  CA  B SER   A  1 357 ? -20.504 17.127  -29.315  0.28 53.01  ? 658  SER   A CA  1 
ATOM   2843  C  C   . SER   A  1 357 ? -21.969 17.135  -29.728  1.00 48.02  ? 658  SER   A C   1 
ATOM   2844  O  O   . SER   A  1 357 ? -22.622 18.188  -29.733  1.00 47.53  ? 658  SER   A O   1 
ATOM   2845  C  CB  A SER   A  1 357 ? -19.594 17.026  -30.532  0.72 53.28  ? 658  SER   A CB  1 
ATOM   2846  C  CB  B SER   A  1 357 ? -19.598 16.978  -30.537  0.28 53.03  ? 658  SER   A CB  1 
ATOM   2847  O  OG  A SER   A  1 357 ? -19.871 18.060  -31.471  0.72 53.18  ? 658  SER   A OG  1 
ATOM   2848  O  OG  B SER   A  1 357 ? -18.258 16.739  -30.143  0.28 51.90  ? 658  SER   A OG  1 
ATOM   2849  N  N   . ALA   A  1 358 ? -22.504 15.953  -30.061  1.00 38.83  ? 659  ALA   A N   1 
ATOM   2850  C  CA  . ALA   A  1 358 ? -23.901 15.840  -30.472  1.00 37.09  ? 659  ALA   A CA  1 
ATOM   2851  C  C   . ALA   A  1 358 ? -24.830 16.485  -29.455  1.00 44.77  ? 659  ALA   A C   1 
ATOM   2852  O  O   . ALA   A  1 358 ? -25.623 17.375  -29.799  1.00 50.22  ? 659  ALA   A O   1 
ATOM   2853  C  CB  . ALA   A  1 358 ? -24.275 14.368  -30.676  1.00 29.34  ? 659  ALA   A CB  1 
ATOM   2854  N  N   . THR   A  1 359 ? -24.736 16.052  -28.182  1.00 42.50  ? 660  THR   A N   1 
ATOM   2855  C  CA  . THR   A  1 359 ? -25.674 16.537  -27.173  1.00 34.38  ? 660  THR   A CA  1 
ATOM   2856  C  C   . THR   A  1 359 ? -25.511 18.033  -26.957  1.00 31.35  ? 660  THR   A C   1 
ATOM   2857  O  O   . THR   A  1 359 ? -26.497 18.738  -26.717  1.00 36.10  ? 660  THR   A O   1 
ATOM   2858  C  CB  . THR   A  1 359 ? -25.510 15.791  -25.843  1.00 41.97  ? 660  THR   A CB  1 
ATOM   2859  O  OG1 . THR   A  1 359 ? -24.154 15.877  -25.381  1.00 43.74  ? 660  THR   A OG1 1 
ATOM   2860  C  CG2 . THR   A  1 359 ? -25.913 14.338  -25.982  1.00 37.48  ? 660  THR   A CG2 1 
ATOM   2861  N  N   . GLU   A  1 360 ? -24.278 18.539  -27.036  1.00 36.84  ? 661  GLU   A N   1 
ATOM   2862  C  CA  . GLU   A  1 360 ? -24.085 19.970  -26.834  1.00 46.52  ? 661  GLU   A CA  1 
ATOM   2863  C  C   . GLU   A  1 360 ? -24.748 20.757  -27.952  1.00 50.45  ? 661  GLU   A C   1 
ATOM   2864  O  O   . GLU   A  1 360 ? -25.417 21.768  -27.700  1.00 48.27  ? 661  GLU   A O   1 
ATOM   2865  C  CB  . GLU   A  1 360 ? -22.597 20.308  -26.745  1.00 43.91  ? 661  GLU   A CB  1 
ATOM   2866  C  CG  . GLU   A  1 360 ? -22.327 21.790  -26.450  1.00 57.99  ? 661  GLU   A CG  1 
ATOM   2867  C  CD  . GLU   A  1 360 ? -20.840 22.169  -26.527  1.00 81.20  ? 661  GLU   A CD  1 
ATOM   2868  O  OE1 . GLU   A  1 360 ? -19.978 21.277  -26.367  1.00 87.32  ? 661  GLU   A OE1 1 
ATOM   2869  O  OE2 . GLU   A  1 360 ? -20.528 23.364  -26.751  1.00 88.02  ? 661  GLU   A OE2 1 
ATOM   2870  N  N   . SER   A  1 361 ? -24.577 20.301  -29.196  1.00 50.96  ? 662  SER   A N   1 
ATOM   2871  C  CA  . SER   A  1 361 ? -25.258 20.938  -30.315  1.00 41.82  ? 662  SER   A CA  1 
ATOM   2872  C  C   . SER   A  1 361 ? -26.747 21.001  -30.057  1.00 39.10  ? 662  SER   A C   1 
ATOM   2873  O  O   . SER   A  1 361 ? -27.381 22.045  -30.253  1.00 45.82  ? 662  SER   A O   1 
ATOM   2874  C  CB  . SER   A  1 361 ? -24.965 20.184  -31.608  1.00 40.89  ? 662  SER   A CB  1 
ATOM   2875  O  OG  . SER   A  1 361 ? -23.623 20.397  -32.004  1.00 45.85  ? 662  SER   A OG  1 
ATOM   2876  N  N   . PHE   A  1 362 ? -27.314 19.901  -29.556  1.00 41.52  ? 663  PHE   A N   1 
ATOM   2877  C  CA  . PHE   A  1 362 ? -28.756 19.855  -29.344  1.00 45.64  ? 663  PHE   A CA  1 
ATOM   2878  C  C   . PHE   A  1 362 ? -29.211 20.850  -28.278  1.00 53.35  ? 663  PHE   A C   1 
ATOM   2879  O  O   . PHE   A  1 362 ? -30.274 21.468  -28.416  1.00 58.91  ? 663  PHE   A O   1 
ATOM   2880  C  CB  . PHE   A  1 362 ? -29.202 18.448  -28.976  1.00 41.38  ? 663  PHE   A CB  1 
ATOM   2881  C  CG  . PHE   A  1 362 ? -30.679 18.333  -28.820  1.00 49.28  ? 663  PHE   A CG  1 
ATOM   2882  C  CD1 . PHE   A  1 362 ? -31.505 18.321  -29.938  1.00 43.29  ? 663  PHE   A CD1 1 
ATOM   2883  C  CD2 . PHE   A  1 362 ? -31.252 18.270  -27.561  1.00 43.97  ? 663  PHE   A CD2 1 
ATOM   2884  C  CE1 . PHE   A  1 362 ? -32.880 18.237  -29.805  1.00 43.81  ? 663  PHE   A CE1 1 
ATOM   2885  C  CE2 . PHE   A  1 362 ? -32.630 18.181  -27.420  1.00 53.74  ? 663  PHE   A CE2 1 
ATOM   2886  C  CZ  . PHE   A  1 362 ? -33.445 18.171  -28.544  1.00 50.28  ? 663  PHE   A CZ  1 
ATOM   2887  N  N   . ILE   A  1 363 ? -28.437 21.018  -27.204  1.00 45.25  ? 664  ILE   A N   1 
ATOM   2888  C  CA  . ILE   A  1 363 ? -28.777 22.058  -26.232  1.00 41.36  ? 664  ILE   A CA  1 
ATOM   2889  C  C   . ILE   A  1 363 ? -28.752 23.431  -26.903  1.00 46.90  ? 664  ILE   A C   1 
ATOM   2890  O  O   . ILE   A  1 363 ? -29.668 24.249  -26.729  1.00 47.53  ? 664  ILE   A O   1 
ATOM   2891  C  CB  . ILE   A  1 363 ? -27.838 21.996  -25.014  1.00 37.56  ? 664  ILE   A CB  1 
ATOM   2892  C  CG1 . ILE   A  1 363 ? -28.090 20.715  -24.233  1.00 36.00  ? 664  ILE   A CG1 1 
ATOM   2893  C  CG2 . ILE   A  1 363 ? -28.084 23.190  -24.090  1.00 26.74  ? 664  ILE   A CG2 1 
ATOM   2894  C  CD1 . ILE   A  1 363 ? -29.496 20.661  -23.711  1.00 42.48  ? 664  ILE   A CD1 1 
ATOM   2895  N  N   . LYS   A  1 364 ? -27.720 23.687  -27.713  1.00 47.60  ? 665  LYS   A N   1 
ATOM   2896  C  CA  . LYS   A  1 364 ? -27.655 24.946  -28.451  1.00 50.68  ? 665  LYS   A CA  1 
ATOM   2897  C  C   . LYS   A  1 364 ? -28.826 25.084  -29.418  1.00 50.15  ? 665  LYS   A C   1 
ATOM   2898  O  O   . LYS   A  1 364 ? -29.402 26.171  -29.556  1.00 43.05  ? 665  LYS   A O   1 
ATOM   2899  C  CB  . LYS   A  1 364 ? -26.326 25.047  -29.195  1.00 47.06  ? 665  LYS   A CB  1 
ATOM   2900  C  CG  . LYS   A  1 364 ? -25.246 25.784  -28.436  1.00 54.94  ? 665  LYS   A CG  1 
ATOM   2901  C  CD  . LYS   A  1 364 ? -23.876 25.507  -29.025  1.00 63.36  ? 665  LYS   A CD  1 
ATOM   2902  C  CE  . LYS   A  1 364 ? -22.836 26.503  -28.520  1.00 73.48  ? 665  LYS   A CE  1 
ATOM   2903  N  NZ  . LYS   A  1 364 ? -21.450 26.047  -28.844  1.00 75.88  ? 665  LYS   A NZ  1 
ATOM   2904  N  N   . HIS   A  1 365 ? -29.201 23.987  -30.085  1.00 49.67  ? 666  HIS   A N   1 
ATOM   2905  C  CA  . HIS   A  1 365 ? -30.354 24.003  -30.985  1.00 44.12  ? 666  HIS   A CA  1 
ATOM   2906  C  C   . HIS   A  1 365 ? -31.655 24.228  -30.229  1.00 52.99  ? 666  HIS   A C   1 
ATOM   2907  O  O   . HIS   A  1 365 ? -32.551 24.930  -30.721  1.00 54.54  ? 666  HIS   A O   1 
ATOM   2908  C  CB  . HIS   A  1 365 ? -30.427 22.689  -31.756  1.00 42.36  ? 666  HIS   A CB  1 
ATOM   2909  C  CG  . HIS   A  1 365 ? -31.718 22.482  -32.489  1.00 47.62  ? 666  HIS   A CG  1 
ATOM   2910  N  ND1 . HIS   A  1 365 ? -32.012 23.120  -33.675  1.00 48.94  ? 666  HIS   A ND1 1 
ATOM   2911  C  CD2 . HIS   A  1 365 ? -32.776 21.681  -32.222  1.00 50.00  ? 666  HIS   A CD2 1 
ATOM   2912  C  CE1 . HIS   A  1 365 ? -33.203 22.734  -34.095  1.00 50.90  ? 666  HIS   A CE1 1 
ATOM   2913  N  NE2 . HIS   A  1 365 ? -33.691 21.863  -33.231  1.00 42.72  ? 666  HIS   A NE2 1 
ATOM   2914  N  N   . MET   A  1 366 ? -31.784 23.618  -29.047  1.00 49.65  ? 667  MET   A N   1 
ATOM   2915  C  CA  . MET   A  1 366 ? -33.014 23.735  -28.278  1.00 49.38  ? 667  MET   A CA  1 
ATOM   2916  C  C   . MET   A  1 366 ? -33.259 25.175  -27.876  1.00 50.59  ? 667  MET   A C   1 
ATOM   2917  O  O   . MET   A  1 366 ? -34.344 25.726  -28.107  1.00 43.64  ? 667  MET   A O   1 
ATOM   2918  C  CB  . MET   A  1 366 ? -32.942 22.850  -27.044  1.00 55.92  ? 667  MET   A CB  1 
ATOM   2919  C  CG  . MET   A  1 366 ? -34.236 22.725  -26.282  1.00 59.02  ? 667  MET   A CG  1 
ATOM   2920  S  SD  . MET   A  1 366 ? -34.045 21.482  -24.997  1.00 54.86  ? 667  MET   A SD  1 
ATOM   2921  C  CE  . MET   A  1 366 ? -35.714 20.863  -24.862  1.00 51.08  ? 667  MET   A CE  1 
ATOM   2922  N  N   . GLU   A  1 367 ? -32.251 25.807  -27.276  1.00 51.32  ? 668  GLU   A N   1 
ATOM   2923  C  CA  . GLU   A  1 367 ? -32.404 27.199  -26.881  1.00 57.11  ? 668  GLU   A CA  1 
ATOM   2924  C  C   . GLU   A  1 367 ? -32.784 28.069  -28.084  1.00 50.68  ? 668  GLU   A C   1 
ATOM   2925  O  O   . GLU   A  1 367 ? -33.744 28.842  -28.026  1.00 47.59  ? 668  GLU   A O   1 
ATOM   2926  C  CB  . GLU   A  1 367 ? -31.125 27.669  -26.178  1.00 60.49  ? 668  GLU   A CB  1 
ATOM   2927  C  CG  . GLU   A  1 367 ? -30.943 26.959  -24.824  1.00 61.08  ? 668  GLU   A CG  1 
ATOM   2928  C  CD  . GLU   A  1 367 ? -29.532 27.030  -24.230  1.00 66.65  ? 668  GLU   A CD  1 
ATOM   2929  O  OE1 . GLU   A  1 367 ? -28.534 27.195  -24.977  1.00 61.52  ? 668  GLU   A OE1 1 
ATOM   2930  O  OE2 . GLU   A  1 367 ? -29.432 26.901  -22.988  1.00 68.72  ? 668  GLU   A OE2 1 
ATOM   2931  N  N   . ASN   A  1 368 ? -32.101 27.885  -29.215  1.00 62.53  ? 669  ASN   A N   1 
ATOM   2932  C  CA  . ASN   A  1 368 ? -32.416 28.674  -30.409  1.00 59.81  ? 669  ASN   A CA  1 
ATOM   2933  C  C   . ASN   A  1 368 ? -33.857 28.459  -30.867  1.00 53.08  ? 669  ASN   A C   1 
ATOM   2934  O  O   . ASN   A  1 368 ? -34.551 29.421  -31.236  1.00 46.34  ? 669  ASN   A O   1 
ATOM   2935  C  CB  . ASN   A  1 368 ? -31.442 28.328  -31.533  1.00 61.29  ? 669  ASN   A CB  1 
ATOM   2936  C  CG  . ASN   A  1 368 ? -31.635 29.199  -32.761  1.00 55.89  ? 669  ASN   A CG  1 
ATOM   2937  O  OD1 . ASN   A  1 368 ? -31.371 30.410  -32.722  1.00 53.16  ? 669  ASN   A OD1 1 
ATOM   2938  N  ND2 . ASN   A  1 368 ? -32.100 28.585  -33.866  1.00 43.43  ? 669  ASN   A ND2 1 
ATOM   2939  N  N   . GLU   A  1 369 ? -34.318 27.199  -30.853  1.00 47.14  ? 670  GLU   A N   1 
ATOM   2940  C  CA  . GLU   A  1 369 ? -35.712 26.885  -31.173  1.00 38.18  ? 670  GLU   A CA  1 
ATOM   2941  C  C   . GLU   A  1 369 ? -36.710 27.503  -30.192  1.00 50.27  ? 670  GLU   A C   1 
ATOM   2942  O  O   . GLU   A  1 369 ? -37.846 27.787  -30.582  1.00 54.82  ? 670  GLU   A O   1 
ATOM   2943  C  CB  . GLU   A  1 369 ? -35.908 25.377  -31.215  1.00 34.40  ? 670  GLU   A CB  1 
ATOM   2944  C  CG  . GLU   A  1 369 ? -35.223 24.746  -32.390  1.00 47.97  ? 670  GLU   A CG  1 
ATOM   2945  C  CD  . GLU   A  1 369 ? -36.067 24.879  -33.631  1.00 48.98  ? 670  GLU   A CD  1 
ATOM   2946  O  OE1 . GLU   A  1 369 ? -36.845 23.931  -33.903  1.00 45.25  ? 670  GLU   A OE1 1 
ATOM   2947  O  OE2 . GLU   A  1 369 ? -35.985 25.951  -34.281  1.00 45.56  ? 670  GLU   A OE2 1 
ATOM   2948  N  N   . TYR   A  1 370 ? -36.345 27.680  -28.913  1.00 47.02  ? 671  TYR   A N   1 
ATOM   2949  C  CA  . TYR   A  1 370 ? -37.250 28.417  -28.032  1.00 51.19  ? 671  TYR   A CA  1 
ATOM   2950  C  C   . TYR   A  1 370 ? -37.213 29.905  -28.353  1.00 51.77  ? 671  TYR   A C   1 
ATOM   2951  O  O   . TYR   A  1 370 ? -38.252 30.574  -28.340  1.00 53.66  ? 671  TYR   A O   1 
ATOM   2952  C  CB  . TYR   A  1 370 ? -36.913 28.162  -26.554  1.00 53.58  ? 671  TYR   A CB  1 
ATOM   2953  C  CG  . TYR   A  1 370 ? -37.486 26.864  -26.003  1.00 51.95  ? 671  TYR   A CG  1 
ATOM   2954  C  CD1 . TYR   A  1 370 ? -36.804 25.667  -26.144  1.00 50.67  ? 671  TYR   A CD1 1 
ATOM   2955  C  CD2 . TYR   A  1 370 ? -38.708 26.841  -25.340  1.00 60.26  ? 671  TYR   A CD2 1 
ATOM   2956  C  CE1 . TYR   A  1 370 ? -37.329 24.477  -25.656  1.00 55.19  ? 671  TYR   A CE1 1 
ATOM   2957  C  CE2 . TYR   A  1 370 ? -39.236 25.654  -24.837  1.00 57.99  ? 671  TYR   A CE2 1 
ATOM   2958  C  CZ  . TYR   A  1 370 ? -38.543 24.475  -25.004  1.00 55.38  ? 671  TYR   A CZ  1 
ATOM   2959  O  OH  . TYR   A  1 370 ? -39.052 23.288  -24.522  1.00 46.77  ? 671  TYR   A OH  1 
ATOM   2960  N  N   . ARG   A  1 371 ? -36.024 30.434  -28.655  1.00 59.52  ? 672  ARG   A N   1 
ATOM   2961  C  CA  . ARG   A  1 371 ? -35.878 31.831  -29.054  1.00 71.01  ? 672  ARG   A CA  1 
ATOM   2962  C  C   . ARG   A  1 371 ? -36.857 32.202  -30.167  1.00 68.51  ? 672  ARG   A C   1 
ATOM   2963  O  O   . ARG   A  1 371 ? -37.657 33.132  -30.027  1.00 70.55  ? 672  ARG   A O   1 
ATOM   2964  C  CB  . ARG   A  1 371 ? -34.432 32.101  -29.502  1.00 86.65  ? 672  ARG   A CB  1 
ATOM   2965  C  CG  . ARG   A  1 371 ? -33.570 32.956  -28.551  1.00 97.12  ? 672  ARG   A CG  1 
ATOM   2966  C  CD  . ARG   A  1 371 ? -33.063 32.188  -27.324  1.00 105.48 ? 672  ARG   A CD  1 
ATOM   2967  N  NE  . ARG   A  1 371 ? -34.105 32.017  -26.309  1.00 112.72 ? 672  ARG   A NE  1 
ATOM   2968  C  CZ  . ARG   A  1 371 ? -33.928 31.429  -25.126  1.00 110.17 ? 672  ARG   A CZ  1 
ATOM   2969  N  NH1 . ARG   A  1 371 ? -32.737 30.944  -24.786  1.00 107.18 ? 672  ARG   A NH1 1 
ATOM   2970  N  NH2 . ARG   A  1 371 ? -34.948 31.330  -24.281  1.00 106.40 ? 672  ARG   A NH2 1 
ATOM   2971  N  N   . CYS   A  1 372 ? -36.822 31.464  -31.279  1.00 67.94  ? 673  CYS   A N   1 
ATOM   2972  C  CA  . CYS   A  1 372 ? -37.458 31.902  -32.518  1.00 71.61  ? 673  CYS   A CA  1 
ATOM   2973  C  C   . CYS   A  1 372 ? -38.720 31.137  -32.897  1.00 62.10  ? 673  CYS   A C   1 
ATOM   2974  O  O   . CYS   A  1 372 ? -39.420 31.556  -33.820  1.00 56.02  ? 673  CYS   A O   1 
ATOM   2975  C  CB  . CYS   A  1 372 ? -36.463 31.786  -33.681  1.00 68.48  ? 673  CYS   A CB  1 
ATOM   2976  S  SG  . CYS   A  1 372 ? -36.237 30.079  -34.232  1.00 69.75  ? 673  CYS   A SG  1 
ATOM   2977  N  N   . ARG   A  1 373 ? -39.017 30.023  -32.240  1.00 62.75  ? 674  ARG   A N   1 
ATOM   2978  C  CA  . ARG   A  1 373 ? -40.162 29.197  -32.586  1.00 51.53  ? 674  ARG   A CA  1 
ATOM   2979  C  C   . ARG   A  1 373 ? -41.147 29.024  -31.441  1.00 54.68  ? 674  ARG   A C   1 
ATOM   2980  O  O   . ARG   A  1 373 ? -42.308 28.675  -31.691  1.00 51.89  ? 674  ARG   A O   1 
ATOM   2981  C  CB  . ARG   A  1 373 ? -39.694 27.808  -33.067  1.00 43.92  ? 674  ARG   A CB  1 
ATOM   2982  C  CG  . ARG   A  1 373 ? -40.728 27.025  -33.890  1.00 41.03  ? 674  ARG   A CG  1 
ATOM   2983  C  CD  . ARG   A  1 373 ? -40.345 25.561  -34.085  1.00 34.92  ? 674  ARG   A CD  1 
ATOM   2984  N  NE  . ARG   A  1 373 ? -41.291 24.907  -34.983  1.00 39.76  ? 674  ARG   A NE  1 
ATOM   2985  C  CZ  . ARG   A  1 373 ? -41.401 23.590  -35.128  1.00 43.69  ? 674  ARG   A CZ  1 
ATOM   2986  N  NH1 . ARG   A  1 373 ? -40.631 22.780  -34.421  1.00 51.38  ? 674  ARG   A NH1 1 
ATOM   2987  N  NH2 . ARG   A  1 373 ? -42.287 23.079  -35.975  1.00 32.49  ? 674  ARG   A NH2 1 
ATOM   2988  N  N   . GLY   A  1 374 ? -40.731 29.262  -30.202  1.00 50.33  ? 675  GLY   A N   1 
ATOM   2989  C  CA  . GLY   A  1 374 ? -41.634 29.126  -29.085  1.00 57.95  ? 675  GLY   A CA  1 
ATOM   2990  C  C   . GLY   A  1 374 ? -41.607 27.770  -28.439  1.00 62.79  ? 675  GLY   A C   1 
ATOM   2991  O  O   . GLY   A  1 374 ? -42.458 27.491  -27.586  1.00 67.14  ? 675  GLY   A O   1 
ATOM   2992  N  N   . GLY   A  1 375 ? -40.664 26.922  -28.819  1.00 56.61  ? 676  GLY   A N   1 
ATOM   2993  C  CA  . GLY   A  1 375 ? -40.530 25.627  -28.195  1.00 57.57  ? 676  GLY   A CA  1 
ATOM   2994  C  C   . GLY   A  1 375 ? -39.734 24.694  -29.086  1.00 50.65  ? 676  GLY   A C   1 
ATOM   2995  O  O   . GLY   A  1 375 ? -39.241 25.079  -30.146  1.00 53.03  ? 676  GLY   A O   1 
ATOM   2996  N  N   . CYS   A  1 376 ? -39.627 23.456  -28.620  1.00 42.91  ? 677  CYS   A N   1 
ATOM   2997  C  CA  . CYS   A  1 376 ? -38.930 22.409  -29.341  1.00 41.80  ? 677  CYS   A CA  1 
ATOM   2998  C  C   . CYS   A  1 376 ? -39.209 21.066  -28.675  1.00 49.68  ? 677  CYS   A C   1 
ATOM   2999  O  O   . CYS   A  1 376 ? -38.613 20.740  -27.643  1.00 61.05  ? 677  CYS   A O   1 
ATOM   3000  C  CB  . CYS   A  1 376 ? -37.435 22.695  -29.392  1.00 39.17  ? 677  CYS   A CB  1 
ATOM   3001  S  SG  . CYS   A  1 376 ? -36.462 21.265  -29.840  1.00 45.06  ? 677  CYS   A SG  1 
ATOM   3002  N  N   . PRO   A  1 377 ? -40.109 20.261  -29.226  1.00 46.87  ? 678  PRO   A N   1 
ATOM   3003  C  CA  . PRO   A  1 377 ? -40.454 18.996  -28.570  1.00 45.94  ? 678  PRO   A CA  1 
ATOM   3004  C  C   . PRO   A  1 377 ? -39.281 18.021  -28.561  1.00 47.47  ? 678  PRO   A C   1 
ATOM   3005  O  O   . PRO   A  1 377 ? -38.604 17.831  -29.572  1.00 50.91  ? 678  PRO   A O   1 
ATOM   3006  C  CB  . PRO   A  1 377 ? -41.630 18.480  -29.407  1.00 53.56  ? 678  PRO   A CB  1 
ATOM   3007  C  CG  . PRO   A  1 377 ? -41.479 19.166  -30.746  1.00 48.96  ? 678  PRO   A CG  1 
ATOM   3008  C  CD  . PRO   A  1 377 ? -40.907 20.509  -30.444  1.00 48.03  ? 678  PRO   A CD  1 
ATOM   3009  N  N   . ALA   A  1 378 ? -39.043 17.398  -27.405  1.00 52.52  ? 679  ALA   A N   1 
ATOM   3010  C  CA  . ALA   A  1 378 ? -37.927 16.467  -27.241  1.00 45.46  ? 679  ALA   A CA  1 
ATOM   3011  C  C   . ALA   A  1 378 ? -38.329 15.316  -26.326  1.00 45.77  ? 679  ALA   A C   1 
ATOM   3012  O  O   . ALA   A  1 378 ? -39.249 15.427  -25.512  1.00 41.95  ? 679  ALA   A O   1 
ATOM   3013  C  CB  . ALA   A  1 378 ? -36.678 17.162  -26.681  1.00 40.06  ? 679  ALA   A CB  1 
ATOM   3014  N  N   . ASP   A  1 379 ? -37.617 14.202  -26.470  1.00 40.37  ? 680  ASP   A N   1 
ATOM   3015  C  CA  . ASP   A  1 379 ? -37.913 12.955  -25.768  1.00 38.06  ? 680  ASP   A CA  1 
ATOM   3016  C  C   . ASP   A  1 379 ? -36.629 12.577  -25.038  1.00 47.00  ? 680  ASP   A C   1 
ATOM   3017  O  O   . ASP   A  1 379 ? -35.717 11.985  -25.635  1.00 40.25  ? 680  ASP   A O   1 
ATOM   3018  C  CB  . ASP   A  1 379 ? -38.369 11.875  -26.756  1.00 43.96  ? 680  ASP   A CB  1 
ATOM   3019  C  CG  . ASP   A  1 379 ? -38.773 10.573  -26.085  1.00 46.56  ? 680  ASP   A CG  1 
ATOM   3020  O  OD1 . ASP   A  1 379 ? -39.537 9.809   -26.700  1.00 46.91  ? 680  ASP   A OD1 1 
ATOM   3021  O  OD2 . ASP   A  1 379 ? -38.346 10.303  -24.948  1.00 56.52  ? 680  ASP   A OD2 1 
ATOM   3022  N  N   . TRP   A  1 380 ? -36.572 12.966  -23.757  1.00 51.09  ? 681  TRP   A N   1 
ATOM   3023  C  CA  . TRP   A  1 380 ? -35.418 12.707  -22.902  1.00 32.47  ? 681  TRP   A CA  1 
ATOM   3024  C  C   . TRP   A  1 380 ? -34.975 11.251  -22.986  1.00 31.92  ? 681  TRP   A C   1 
ATOM   3025  O  O   . TRP   A  1 380 ? -33.785 10.955  -23.112  1.00 32.54  ? 681  TRP   A O   1 
ATOM   3026  C  CB  . TRP   A  1 380 ? -35.784 13.075  -21.458  1.00 43.59  ? 681  TRP   A CB  1 
ATOM   3027  C  CG  . TRP   A  1 380 ? -34.637 13.256  -20.527  1.00 29.22  ? 681  TRP   A CG  1 
ATOM   3028  C  CD1 . TRP   A  1 380 ? -34.053 14.439  -20.161  1.00 26.25  ? 681  TRP   A CD1 1 
ATOM   3029  C  CD2 . TRP   A  1 380 ? -33.923 12.226  -19.844  1.00 33.82  ? 681  TRP   A CD2 1 
ATOM   3030  N  NE1 . TRP   A  1 380 ? -33.025 14.200  -19.274  1.00 40.46  ? 681  TRP   A NE1 1 
ATOM   3031  C  CE2 . TRP   A  1 380 ? -32.934 12.850  -19.058  1.00 38.70  ? 681  TRP   A CE2 1 
ATOM   3032  C  CE3 . TRP   A  1 380 ? -34.045 10.837  -19.791  1.00 37.17  ? 681  TRP   A CE3 1 
ATOM   3033  C  CZ2 . TRP   A  1 380 ? -32.057 12.132  -18.262  1.00 43.57  ? 681  TRP   A CZ2 1 
ATOM   3034  C  CZ3 . TRP   A  1 380 ? -33.175 10.122  -18.993  1.00 34.59  ? 681  TRP   A CZ3 1 
ATOM   3035  C  CH2 . TRP   A  1 380 ? -32.186 10.767  -18.250  1.00 40.23  ? 681  TRP   A CH2 1 
ATOM   3036  N  N   . VAL   A  1 381 ? -35.932 10.324  -22.886  1.00 28.46  ? 682  VAL   A N   1 
ATOM   3037  C  CA  . VAL   A  1 381 ? -35.648 8.894   -22.961  1.00 24.40  ? 682  VAL   A CA  1 
ATOM   3038  C  C   . VAL   A  1 381 ? -34.850 8.535   -24.207  1.00 39.67  ? 682  VAL   A C   1 
ATOM   3039  O  O   . VAL   A  1 381 ? -34.126 7.527   -24.227  1.00 44.05  ? 682  VAL   A O   1 
ATOM   3040  C  CB  . VAL   A  1 381 ? -36.987 8.130   -22.895  1.00 29.10  ? 682  VAL   A CB  1 
ATOM   3041  C  CG1 . VAL   A  1 381 ? -36.794 6.658   -23.142  1.00 37.72  ? 682  VAL   A CG1 1 
ATOM   3042  C  CG2 . VAL   A  1 381 ? -37.653 8.383   -21.556  1.00 32.91  ? 682  VAL   A CG2 1 
ATOM   3043  N  N   . TRP   A  1 382 ? -34.958 9.341   -25.268  1.00 38.82  ? 683  TRP   A N   1 
ATOM   3044  C  CA  . TRP   A  1 382 ? -34.229 9.086   -26.499  1.00 40.45  ? 683  TRP   A CA  1 
ATOM   3045  C  C   . TRP   A  1 382 ? -33.075 10.045  -26.740  1.00 47.91  ? 683  TRP   A C   1 
ATOM   3046  O  O   . TRP   A  1 382 ? -32.061 9.635   -27.326  1.00 47.30  ? 683  TRP   A O   1 
ATOM   3047  C  CB  . TRP   A  1 382 ? -35.180 9.134   -27.708  1.00 41.35  ? 683  TRP   A CB  1 
ATOM   3048  C  CG  . TRP   A  1 382 ? -35.989 7.870   -27.911  1.00 40.95  ? 683  TRP   A CG  1 
ATOM   3049  C  CD1 . TRP   A  1 382 ? -36.952 7.376   -27.091  1.00 33.60  ? 683  TRP   A CD1 1 
ATOM   3050  C  CD2 . TRP   A  1 382 ? -35.891 6.953   -29.009  1.00 49.53  ? 683  TRP   A CD2 1 
ATOM   3051  N  NE1 . TRP   A  1 382 ? -37.456 6.202   -27.597  1.00 44.57  ? 683  TRP   A NE1 1 
ATOM   3052  C  CE2 . TRP   A  1 382 ? -36.826 5.925   -28.780  1.00 50.64  ? 683  TRP   A CE2 1 
ATOM   3053  C  CE3 . TRP   A  1 382 ? -35.101 6.902   -30.159  1.00 52.00  ? 683  TRP   A CE3 1 
ATOM   3054  C  CZ2 . TRP   A  1 382 ? -36.991 4.857   -29.657  1.00 46.98  ? 683  TRP   A CZ2 1 
ATOM   3055  C  CZ3 . TRP   A  1 382 ? -35.272 5.843   -31.035  1.00 57.82  ? 683  TRP   A CZ3 1 
ATOM   3056  C  CH2 . TRP   A  1 382 ? -36.206 4.836   -30.778  1.00 53.73  ? 683  TRP   A CH2 1 
ATOM   3057  N  N   . ILE   A  1 383 ? -33.198 11.311  -26.312  1.00 25.31  ? 684  ILE   A N   1 
ATOM   3058  C  CA  . ILE   A  1 383 ? -32.104 12.261  -26.537  1.00 27.19  ? 684  ILE   A CA  1 
ATOM   3059  C  C   . ILE   A  1 383 ? -30.852 11.851  -25.767  1.00 30.85  ? 684  ILE   A C   1 
ATOM   3060  O  O   . ILE   A  1 383 ? -29.735 11.956  -26.278  1.00 43.65  ? 684  ILE   A O   1 
ATOM   3061  C  CB  . ILE   A  1 383 ? -32.545 13.689  -26.177  1.00 23.06  ? 684  ILE   A CB  1 
ATOM   3062  C  CG1 . ILE   A  1 383 ? -33.680 14.106  -27.097  1.00 38.91  ? 684  ILE   A CG1 1 
ATOM   3063  C  CG2 . ILE   A  1 383 ? -31.386 14.663  -26.315  1.00 21.75  ? 684  ILE   A CG2 1 
ATOM   3064  C  CD1 . ILE   A  1 383 ? -33.352 13.919  -28.576  1.00 51.34  ? 684  ILE   A CD1 1 
ATOM   3065  N  N   . VAL   A  1 384 ? -31.010 11.357  -24.544  1.00 38.29  ? 685  VAL   A N   1 
ATOM   3066  C  CA  . VAL   A  1 384 ? -29.839 11.064  -23.714  1.00 37.72  ? 685  VAL   A CA  1 
ATOM   3067  C  C   . VAL   A  1 384 ? -29.065 9.891   -24.311  1.00 38.24  ? 685  VAL   A C   1 
ATOM   3068  O  O   . VAL   A  1 384 ? -29.665 8.850   -24.625  1.00 37.48  ? 685  VAL   A O   1 
ATOM   3069  C  CB  . VAL   A  1 384 ? -30.267 10.789  -22.268  1.00 40.70  ? 685  VAL   A CB  1 
ATOM   3070  C  CG1 . VAL   A  1 384 ? -29.063 10.424  -21.401  1.00 23.78  ? 685  VAL   A CG1 1 
ATOM   3071  C  CG2 . VAL   A  1 384 ? -30.906 12.035  -21.715  1.00 37.43  ? 685  VAL   A CG2 1 
ATOM   3072  N  N   . PRO   A  1 385 ? -27.755 10.028  -24.520  1.00 41.83  ? 686  PRO   A N   1 
ATOM   3073  C  CA  . PRO   A  1 385 ? -26.975 8.919   -25.076  1.00 46.08  ? 686  PRO   A CA  1 
ATOM   3074  C  C   . PRO   A  1 385 ? -27.087 7.679   -24.212  1.00 56.77  ? 686  PRO   A C   1 
ATOM   3075  O  O   . PRO   A  1 385 ? -27.269 7.769   -22.986  1.00 63.47  ? 686  PRO   A O   1 
ATOM   3076  C  CB  . PRO   A  1 385 ? -25.538 9.462   -25.078  1.00 41.60  ? 686  PRO   A CB  1 
ATOM   3077  C  CG  . PRO   A  1 385 ? -25.702 10.921  -25.162  1.00 45.04  ? 686  PRO   A CG  1 
ATOM   3078  C  CD  . PRO   A  1 385 ? -27.016 11.296  -24.565  1.00 39.55  ? 686  PRO   A CD  1 
ATOM   3079  N  N   . PRO   A  1 386 ? -26.934 6.496   -24.807  1.00 53.64  ? 687  PRO   A N   1 
ATOM   3080  C  CA  . PRO   A  1 386 ? -27.066 5.237   -24.056  1.00 50.10  ? 687  PRO   A CA  1 
ATOM   3081  C  C   . PRO   A  1 386 ? -25.875 4.876   -23.177  1.00 52.15  ? 687  PRO   A C   1 
ATOM   3082  O  O   . PRO   A  1 386 ? -25.806 3.744   -22.687  1.00 49.03  ? 687  PRO   A O   1 
ATOM   3083  C  CB  . PRO   A  1 386 ? -27.233 4.205   -25.180  1.00 46.93  ? 687  PRO   A CB  1 
ATOM   3084  C  CG  . PRO   A  1 386 ? -26.453 4.797   -26.313  1.00 49.38  ? 687  PRO   A CG  1 
ATOM   3085  C  CD  . PRO   A  1 386 ? -26.659 6.278   -26.236  1.00 41.43  ? 687  PRO   A CD  1 
ATOM   3086  N  N   . MET   A  1 387 ? -24.929 5.785   -22.983  1.00 39.70  ? 688  MET   A N   1 
ATOM   3087  C  CA  . MET   A  1 387 ? -23.774 5.545   -22.140  1.00 38.74  ? 688  MET   A CA  1 
ATOM   3088  C  C   . MET   A  1 387 ? -23.307 6.907   -21.674  1.00 54.04  ? 688  MET   A C   1 
ATOM   3089  O  O   . MET   A  1 387 ? -23.508 7.900   -22.376  1.00 53.09  ? 688  MET   A O   1 
ATOM   3090  C  CB  . MET   A  1 387 ? -22.635 4.816   -22.865  1.00 43.60  ? 688  MET   A CB  1 
ATOM   3091  C  CG  . MET   A  1 387 ? -21.922 5.655   -23.920  1.00 51.86  ? 688  MET   A CG  1 
ATOM   3092  S  SD  . MET   A  1 387 ? -20.325 4.970   -24.418  1.00 51.49  ? 688  MET   A SD  1 
ATOM   3093  C  CE  . MET   A  1 387 ? -19.212 5.821   -23.303  1.00 55.88  ? 688  MET   A CE  1 
ATOM   3094  N  N   . SER   A  1 388 ? -22.710 6.954   -20.477  1.00 51.35  ? 689  SER   A N   1 
ATOM   3095  C  CA  . SER   A  1 388 ? -22.180 8.207   -19.926  1.00 42.38  ? 689  SER   A CA  1 
ATOM   3096  C  C   . SER   A  1 388 ? -23.238 9.309   -19.905  1.00 39.81  ? 689  SER   A C   1 
ATOM   3097  O  O   . SER   A  1 388 ? -22.934 10.480  -20.158  1.00 42.65  ? 689  SER   A O   1 
ATOM   3098  C  CB  . SER   A  1 388 ? -20.948 8.693   -20.710  1.00 36.15  ? 689  SER   A CB  1 
ATOM   3099  O  OG  . SER   A  1 388 ? -19.918 7.721   -20.745  1.00 48.33  ? 689  SER   A OG  1 
ATOM   3100  N  N   . GLY   A  1 389 ? -24.487 8.943   -19.625  1.00 38.86  ? 690  GLY   A N   1 
ATOM   3101  C  CA  . GLY   A  1 389 ? -25.591 9.893   -19.617  1.00 38.35  ? 690  GLY   A CA  1 
ATOM   3102  C  C   . GLY   A  1 389 ? -25.390 11.228  -18.917  1.00 51.69  ? 690  GLY   A C   1 
ATOM   3103  O  O   . GLY   A  1 389 ? -25.428 12.270  -19.584  1.00 55.52  ? 690  GLY   A O   1 
ATOM   3104  N  N   . SER   A  1 390 ? -25.153 11.220  -17.590  1.00 47.34  ? 691  SER   A N   1 
ATOM   3105  C  CA  . SER   A  1 390 ? -25.180 12.443  -16.784  1.00 45.80  ? 691  SER   A CA  1 
ATOM   3106  C  C   . SER   A  1 390 ? -23.985 13.367  -17.016  1.00 44.76  ? 691  SER   A C   1 
ATOM   3107  O  O   . SER   A  1 390 ? -24.001 14.497  -16.509  1.00 44.66  ? 691  SER   A O   1 
ATOM   3108  C  CB  . SER   A  1 390 ? -25.284 12.111  -15.280  1.00 54.31  ? 691  SER   A CB  1 
ATOM   3109  O  OG  . SER   A  1 390 ? -24.021 11.966  -14.629  1.00 49.91  ? 691  SER   A OG  1 
ATOM   3110  N  N   . ILE   A  1 391 ? -22.952 12.935  -17.753  1.00 39.85  ? 692  ILE   A N   1 
ATOM   3111  C  CA  . ILE   A  1 391 ? -21.885 13.854  -18.135  1.00 47.48  ? 692  ILE   A CA  1 
ATOM   3112  C  C   . ILE   A  1 391 ? -22.141 14.498  -19.492  1.00 49.86  ? 692  ILE   A C   1 
ATOM   3113  O  O   . ILE   A  1 391 ? -21.340 15.331  -19.942  1.00 54.96  ? 692  ILE   A O   1 
ATOM   3114  C  CB  . ILE   A  1 391 ? -20.516 13.154  -18.116  1.00 49.54  ? 692  ILE   A CB  1 
ATOM   3115  C  CG1 . ILE   A  1 391 ? -20.382 12.194  -19.281  1.00 43.75  ? 692  ILE   A CG1 1 
ATOM   3116  C  CG2 . ILE   A  1 391 ? -20.313 12.438  -16.781  1.00 47.39  ? 692  ILE   A CG2 1 
ATOM   3117  C  CD1 . ILE   A  1 391 ? -19.046 11.485  -19.259  1.00 38.61  ? 692  ILE   A CD1 1 
ATOM   3118  N  N   . THR   A  1 392 ? -23.223 14.159  -20.138  1.00 50.26  ? 693  THR   A N   1 
ATOM   3119  C  CA  . THR   A  1 392 ? -23.628 14.941  -21.286  1.00 47.15  ? 693  THR   A CA  1 
ATOM   3120  C  C   . THR   A  1 392 ? -24.659 15.962  -20.855  1.00 46.20  ? 693  THR   A C   1 
ATOM   3121  O  O   . THR   A  1 392 ? -25.505 15.655  -20.019  1.00 52.49  ? 693  THR   A O   1 
ATOM   3122  C  CB  . THR   A  1 392 ? -24.241 14.052  -22.351  1.00 48.14  ? 693  THR   A CB  1 
ATOM   3123  O  OG1 . THR   A  1 392 ? -25.474 13.530  -21.845  1.00 51.63  ? 693  THR   A OG1 1 
ATOM   3124  C  CG2 . THR   A  1 392 ? -23.304 12.905  -22.674  1.00 47.69  ? 693  THR   A CG2 1 
ATOM   3125  N  N   . PRO   A  1 393 ? -24.651 17.169  -21.432  1.00 44.60  ? 694  PRO   A N   1 
ATOM   3126  C  CA  . PRO   A  1 393 ? -25.476 18.258  -20.873  1.00 46.79  ? 694  PRO   A CA  1 
ATOM   3127  C  C   . PRO   A  1 393 ? -26.978 18.080  -21.042  1.00 51.49  ? 694  PRO   A C   1 
ATOM   3128  O  O   . PRO   A  1 393 ? -27.723 18.799  -20.376  1.00 52.67  ? 694  PRO   A O   1 
ATOM   3129  C  CB  . PRO   A  1 393 ? -24.986 19.494  -21.635  1.00 38.23  ? 694  PRO   A CB  1 
ATOM   3130  C  CG  . PRO   A  1 393 ? -24.513 18.939  -22.916  1.00 50.41  ? 694  PRO   A CG  1 
ATOM   3131  C  CD  . PRO   A  1 393 ? -23.865 17.622  -22.585  1.00 43.44  ? 694  PRO   A CD  1 
ATOM   3132  N  N   . VAL   A  1 394 ? -27.454 17.183  -21.918  1.00 58.94  ? 695  VAL   A N   1 
ATOM   3133  C  CA  . VAL   A  1 394 ? -28.900 17.036  -22.108  1.00 51.53  ? 695  VAL   A CA  1 
ATOM   3134  C  C   . VAL   A  1 394 ? -29.537 16.284  -20.955  1.00 45.67  ? 695  VAL   A C   1 
ATOM   3135  O  O   . VAL   A  1 394 ? -30.749 16.414  -20.731  1.00 35.31  ? 695  VAL   A O   1 
ATOM   3136  C  CB  . VAL   A  1 394 ? -29.284 16.309  -23.421  1.00 47.45  ? 695  VAL   A CB  1 
ATOM   3137  C  CG1 . VAL   A  1 394 ? -29.228 17.243  -24.622  1.00 39.54  ? 695  VAL   A CG1 1 
ATOM   3138  C  CG2 . VAL   A  1 394 ? -28.444 15.071  -23.623  1.00 30.16  ? 695  VAL   A CG2 1 
ATOM   3139  N  N   . PHE   A  1 395 ? -28.746 15.488  -20.229  1.00 44.29  ? 696  PHE   A N   1 
ATOM   3140  C  CA  . PHE   A  1 395 ? -29.244 14.781  -19.051  1.00 42.26  ? 696  PHE   A CA  1 
ATOM   3141  C  C   . PHE   A  1 395 ? -29.938 15.734  -18.090  1.00 43.21  ? 696  PHE   A C   1 
ATOM   3142  O  O   . PHE   A  1 395 ? -31.053 15.467  -17.618  1.00 38.93  ? 696  PHE   A O   1 
ATOM   3143  C  CB  . PHE   A  1 395 ? -28.086 14.070  -18.358  1.00 45.06  ? 696  PHE   A CB  1 
ATOM   3144  C  CG  . PHE   A  1 395 ? -28.493 13.251  -17.180  1.00 50.27  ? 696  PHE   A CG  1 
ATOM   3145  C  CD1 . PHE   A  1 395 ? -28.813 11.919  -17.334  1.00 46.92  ? 696  PHE   A CD1 1 
ATOM   3146  C  CD2 . PHE   A  1 395 ? -28.539 13.810  -15.906  1.00 50.19  ? 696  PHE   A CD2 1 
ATOM   3147  C  CE1 . PHE   A  1 395 ? -29.191 11.164  -16.246  1.00 47.19  ? 696  PHE   A CE1 1 
ATOM   3148  C  CE2 . PHE   A  1 395 ? -28.918 13.064  -14.819  1.00 38.60  ? 696  PHE   A CE2 1 
ATOM   3149  C  CZ  . PHE   A  1 395 ? -29.240 11.742  -14.979  1.00 42.18  ? 696  PHE   A CZ  1 
ATOM   3150  N  N   . HIS   A  1 396 ? -29.304 16.870  -17.817  1.00 40.66  ? 697  HIS   A N   1 
ATOM   3151  C  CA  . HIS   A  1 396 ? -29.795 17.834  -16.847  1.00 48.59  ? 697  HIS   A CA  1 
ATOM   3152  C  C   . HIS   A  1 396 ? -30.767 18.826  -17.452  1.00 52.31  ? 697  HIS   A C   1 
ATOM   3153  O  O   . HIS   A  1 396 ? -31.082 19.835  -16.811  1.00 55.26  ? 697  HIS   A O   1 
ATOM   3154  C  CB  . HIS   A  1 396 ? -28.615 18.569  -16.224  1.00 52.69  ? 697  HIS   A CB  1 
ATOM   3155  C  CG  . HIS   A  1 396 ? -27.477 17.663  -15.910  1.00 53.94  ? 697  HIS   A CG  1 
ATOM   3156  N  ND1 . HIS   A  1 396 ? -27.338 17.046  -14.684  1.00 49.62  ? 697  HIS   A ND1 1 
ATOM   3157  C  CD2 . HIS   A  1 396 ? -26.460 17.213  -16.683  1.00 54.57  ? 697  HIS   A CD2 1 
ATOM   3158  C  CE1 . HIS   A  1 396 ? -26.261 16.280  -14.705  1.00 55.17  ? 697  HIS   A CE1 1 
ATOM   3159  N  NE2 . HIS   A  1 396 ? -25.709 16.366  -15.905  1.00 58.26  ? 697  HIS   A NE2 1 
ATOM   3160  N  N   . GLN   A  1 397 ? -31.237 18.564  -18.666  1.00 51.46  ? 698  GLN   A N   1 
ATOM   3161  C  CA  . GLN   A  1 397 ? -32.121 19.462  -19.389  1.00 43.97  ? 698  GLN   A CA  1 
ATOM   3162  C  C   . GLN   A  1 397 ? -33.539 18.905  -19.322  1.00 47.01  ? 698  GLN   A C   1 
ATOM   3163  O  O   . GLN   A  1 397 ? -33.810 17.820  -19.850  1.00 50.20  ? 698  GLN   A O   1 
ATOM   3164  C  CB  . GLN   A  1 397 ? -31.657 19.606  -20.842  1.00 33.98  ? 698  GLN   A CB  1 
ATOM   3165  C  CG  . GLN   A  1 397 ? -32.564 20.470  -21.687  1.00 36.90  ? 698  GLN   A CG  1 
ATOM   3166  C  CD  . GLN   A  1 397 ? -32.610 21.886  -21.179  1.00 45.80  ? 698  GLN   A CD  1 
ATOM   3167  O  OE1 . GLN   A  1 397 ? -31.571 22.557  -21.086  1.00 44.93  ? 698  GLN   A OE1 1 
ATOM   3168  N  NE2 . GLN   A  1 397 ? -33.810 22.353  -20.829  1.00 37.56  ? 698  GLN   A NE2 1 
ATOM   3169  N  N   . GLU   A  1 398 ? -34.437 19.629  -18.664  1.00 38.93  ? 699  GLU   A N   1 
ATOM   3170  C  CA  . GLU   A  1 398 ? -35.845 19.278  -18.764  1.00 42.88  ? 699  GLU   A CA  1 
ATOM   3171  C  C   . GLU   A  1 398 ? -36.319 19.454  -20.213  1.00 49.05  ? 699  GLU   A C   1 
ATOM   3172  O  O   . GLU   A  1 398 ? -35.821 20.313  -20.954  1.00 43.72  ? 699  GLU   A O   1 
ATOM   3173  C  CB  . GLU   A  1 398 ? -36.678 20.132  -17.807  1.00 40.41  ? 699  GLU   A CB  1 
ATOM   3174  C  CG  . GLU   A  1 398 ? -36.672 19.627  -16.378  1.00 42.93  ? 699  GLU   A CG  1 
ATOM   3175  C  CD  . GLU   A  1 398 ? -37.323 20.596  -15.414  1.00 51.92  ? 699  GLU   A CD  1 
ATOM   3176  O  OE1 . GLU   A  1 398 ? -37.273 20.341  -14.180  1.00 56.65  ? 699  GLU   A OE1 1 
ATOM   3177  O  OE2 . GLU   A  1 398 ? -37.885 21.609  -15.885  1.00 54.28  ? 699  GLU   A OE2 1 
ATOM   3178  N  N   . MET   A  1 399 ? -37.270 18.603  -20.623  1.00 42.31  ? 700  MET   A N   1 
ATOM   3179  C  CA  . MET   A  1 399 ? -37.733 18.536  -22.009  1.00 46.57  ? 700  MET   A CA  1 
ATOM   3180  C  C   . MET   A  1 399 ? -39.226 18.241  -22.043  1.00 51.71  ? 700  MET   A C   1 
ATOM   3181  O  O   . MET   A  1 399 ? -39.682 17.219  -21.512  1.00 58.81  ? 700  MET   A O   1 
ATOM   3182  C  CB  . MET   A  1 399 ? -36.976 17.465  -22.811  1.00 43.11  ? 700  MET   A CB  1 
ATOM   3183  C  CG  . MET   A  1 399 ? -35.492 17.739  -23.057  1.00 42.59  ? 700  MET   A CG  1 
ATOM   3184  S  SD  . MET   A  1 399 ? -34.646 16.250  -23.650  1.00 50.07  ? 700  MET   A SD  1 
ATOM   3185  C  CE  . MET   A  1 399 ? -32.920 16.781  -23.676  1.00 27.79  ? 700  MET   A CE  1 
ATOM   3186  N  N   . LEU   A  1 400 ? -39.982 19.131  -22.679  1.00 47.55  ? 701  LEU   A N   1 
ATOM   3187  C  CA  . LEU   A  1 400 ? -41.400 18.914  -22.933  1.00 54.13  ? 701  LEU   A CA  1 
ATOM   3188  C  C   . LEU   A  1 400 ? -41.585 18.138  -24.235  1.00 54.93  ? 701  LEU   A C   1 
ATOM   3189  O  O   . LEU   A  1 400 ? -40.931 18.437  -25.242  1.00 46.47  ? 701  LEU   A O   1 
ATOM   3190  C  CB  . LEU   A  1 400 ? -42.135 20.252  -23.004  1.00 50.27  ? 701  LEU   A CB  1 
ATOM   3191  C  CG  . LEU   A  1 400 ? -42.266 20.947  -21.663  1.00 50.74  ? 701  LEU   A CG  1 
ATOM   3192  C  CD1 . LEU   A  1 400 ? -42.715 22.358  -21.887  1.00 52.78  ? 701  LEU   A CD1 1 
ATOM   3193  C  CD2 . LEU   A  1 400 ? -43.238 20.172  -20.785  1.00 53.46  ? 701  LEU   A CD2 1 
ATOM   3194  N  N   . ASN   A  1 401 ? -42.469 17.142  -24.220  1.00 53.80  ? 702  ASN   A N   1 
ATOM   3195  C  CA  . ASN   A  1 401 ? -42.608 16.215  -25.340  1.00 53.90  ? 702  ASN   A CA  1 
ATOM   3196  C  C   . ASN   A  1 401 ? -44.022 16.276  -25.895  1.00 52.31  ? 702  ASN   A C   1 
ATOM   3197  O  O   . ASN   A  1 401 ? -44.983 15.989  -25.180  1.00 58.53  ? 702  ASN   A O   1 
ATOM   3198  C  CB  . ASN   A  1 401 ? -42.278 14.789  -24.912  1.00 51.72  ? 702  ASN   A CB  1 
ATOM   3199  C  CG  . ASN   A  1 401 ? -42.212 13.844  -26.076  1.00 43.86  ? 702  ASN   A CG  1 
ATOM   3200  O  OD1 . ASN   A  1 401 ? -41.946 14.255  -27.199  1.00 51.95  ? 702  ASN   A OD1 1 
ATOM   3201  N  ND2 . ASN   A  1 401 ? -42.454 12.563  -25.819  1.00 48.53  ? 702  ASN   A ND2 1 
ATOM   3202  N  N   . TYR   A  1 402 ? -44.145 16.630  -27.170  1.00 53.48  ? 703  TYR   A N   1 
ATOM   3203  C  CA  . TYR   A  1 402 ? -45.448 16.705  -27.811  1.00 55.49  ? 703  TYR   A CA  1 
ATOM   3204  C  C   . TYR   A  1 402 ? -45.254 16.488  -29.310  1.00 57.77  ? 703  TYR   A C   1 
ATOM   3205  O  O   . TYR   A  1 402 ? -44.132 16.550  -29.822  1.00 58.44  ? 703  TYR   A O   1 
ATOM   3206  C  CB  . TYR   A  1 402 ? -46.154 18.034  -27.478  1.00 44.12  ? 703  TYR   A CB  1 
ATOM   3207  C  CG  . TYR   A  1 402 ? -45.284 19.265  -27.625  1.00 48.51  ? 703  TYR   A CG  1 
ATOM   3208  C  CD1 . TYR   A  1 402 ? -45.155 19.915  -28.843  1.00 53.14  ? 703  TYR   A CD1 1 
ATOM   3209  C  CD2 . TYR   A  1 402 ? -44.581 19.772  -26.550  1.00 49.20  ? 703  TYR   A CD2 1 
ATOM   3210  C  CE1 . TYR   A  1 402 ? -44.350 21.044  -28.975  1.00 51.05  ? 703  TYR   A CE1 1 
ATOM   3211  C  CE2 . TYR   A  1 402 ? -43.776 20.900  -26.673  1.00 44.00  ? 703  TYR   A CE2 1 
ATOM   3212  C  CZ  . TYR   A  1 402 ? -43.671 21.527  -27.883  1.00 49.17  ? 703  TYR   A CZ  1 
ATOM   3213  O  OH  . TYR   A  1 402 ? -42.872 22.633  -27.998  1.00 53.87  ? 703  TYR   A OH  1 
ATOM   3214  N  N   . ARG   A  1 403 ? -46.356 16.187  -30.004  1.00 52.32  ? 704  ARG   A N   1 
ATOM   3215  C  CA  . ARG   A  1 403 ? -46.327 15.734  -31.392  1.00 52.37  ? 704  ARG   A CA  1 
ATOM   3216  C  C   . ARG   A  1 403 ? -46.843 16.841  -32.301  1.00 55.51  ? 704  ARG   A C   1 
ATOM   3217  O  O   . ARG   A  1 403 ? -48.048 17.101  -32.345  1.00 53.73  ? 704  ARG   A O   1 
ATOM   3218  C  CB  . ARG   A  1 403 ? -47.169 14.474  -31.578  1.00 59.24  ? 704  ARG   A CB  1 
ATOM   3219  C  CG  . ARG   A  1 403 ? -46.696 13.266  -30.784  1.00 69.85  ? 704  ARG   A CG  1 
ATOM   3220  C  CD  . ARG   A  1 403 ? -46.250 12.118  -31.697  1.00 79.24  ? 704  ARG   A CD  1 
ATOM   3221  N  NE  . ARG   A  1 403 ? -46.858 12.195  -33.026  1.00 86.70  ? 704  ARG   A NE  1 
ATOM   3222  C  CZ  . ARG   A  1 403 ? -48.087 11.777  -33.328  1.00 89.46  ? 704  ARG   A CZ  1 
ATOM   3223  N  NH1 . ARG   A  1 403 ? -48.873 11.246  -32.402  1.00 85.75  ? 704  ARG   A NH1 1 
ATOM   3224  N  NH2 . ARG   A  1 403 ? -48.534 11.896  -34.568  1.00 95.13  ? 704  ARG   A NH2 1 
ATOM   3225  N  N   . LEU   A  1 404 ? -45.937 17.473  -33.033  1.00 46.69  ? 705  LEU   A N   1 
ATOM   3226  C  CA  . LEU   A  1 404 ? -46.329 18.373  -34.102  1.00 47.16  ? 705  LEU   A CA  1 
ATOM   3227  C  C   . LEU   A  1 404 ? -46.393 17.611  -35.423  1.00 42.73  ? 705  LEU   A C   1 
ATOM   3228  O  O   . LEU   A  1 404 ? -45.760 16.563  -35.591  1.00 44.64  ? 705  LEU   A O   1 
ATOM   3229  C  CB  . LEU   A  1 404 ? -45.336 19.525  -34.223  1.00 41.49  ? 705  LEU   A CB  1 
ATOM   3230  C  CG  . LEU   A  1 404 ? -45.152 20.310  -32.937  1.00 41.67  ? 705  LEU   A CG  1 
ATOM   3231  C  CD1 . LEU   A  1 404 ? -44.139 21.439  -33.141  1.00 41.07  ? 705  LEU   A CD1 1 
ATOM   3232  C  CD2 . LEU   A  1 404 ? -46.482 20.850  -32.534  1.00 46.14  ? 705  LEU   A CD2 1 
ATOM   3233  N  N   . THR   A  1 405 ? -47.181 18.154  -36.372  1.00 45.21  ? 706  THR   A N   1 
ATOM   3234  C  CA  A THR   A  1 405 ? -47.132 17.680  -37.745  0.50 41.56  ? 706  THR   A CA  1 
ATOM   3235  C  CA  B THR   A  1 405 ? -47.178 17.693  -37.765  0.50 41.51  ? 706  THR   A CA  1 
ATOM   3236  C  C   . THR   A  1 405 ? -46.665 18.798  -38.685  1.00 43.41  ? 706  THR   A C   1 
ATOM   3237  O  O   . THR   A  1 405 ? -46.875 19.984  -38.410  1.00 45.84  ? 706  THR   A O   1 
ATOM   3238  C  CB  A THR   A  1 405 ? -48.498 17.135  -38.185  0.50 37.90  ? 706  THR   A CB  1 
ATOM   3239  C  CB  B THR   A  1 405 ? -48.568 17.268  -38.254  0.50 37.85  ? 706  THR   A CB  1 
ATOM   3240  O  OG1 A THR   A  1 405 ? -48.307 16.119  -39.175  0.50 41.36  ? 706  THR   A OG1 1 
ATOM   3241  O  OG1 B THR   A  1 405 ? -49.473 18.376  -38.172  0.50 29.68  ? 706  THR   A OG1 1 
ATOM   3242  C  CG2 A THR   A  1 405 ? -49.390 18.241  -38.733  0.50 35.51  ? 706  THR   A CG2 1 
ATOM   3243  C  CG2 B THR   A  1 405 ? -49.096 16.114  -37.439  0.50 41.19  ? 706  THR   A CG2 1 
ATOM   3244  N  N   . PRO   A  1 406 ? -45.994 18.462  -39.806  1.00 47.35  ? 707  PRO   A N   1 
ATOM   3245  C  CA  . PRO   A  1 406 ? -45.625 17.163  -40.381  1.00 43.60  ? 707  PRO   A CA  1 
ATOM   3246  C  C   . PRO   A  1 406 ? -44.798 16.364  -39.416  1.00 50.19  ? 707  PRO   A C   1 
ATOM   3247  O  O   . PRO   A  1 406 ? -44.088 16.965  -38.617  1.00 58.15  ? 707  PRO   A O   1 
ATOM   3248  C  CB  . PRO   A  1 406 ? -44.794 17.536  -41.617  1.00 40.24  ? 707  PRO   A CB  1 
ATOM   3249  C  CG  . PRO   A  1 406 ? -45.148 18.960  -41.923  1.00 41.17  ? 707  PRO   A CG  1 
ATOM   3250  C  CD  . PRO   A  1 406 ? -45.460 19.586  -40.606  1.00 47.55  ? 707  PRO   A CD  1 
ATOM   3251  N  N   . SER   A  1 407 ? -44.927 15.045  -39.436  1.00 51.48  ? 708  SER   A N   1 
ATOM   3252  C  CA  . SER   A  1 407 ? -44.123 14.226  -38.549  1.00 52.89  ? 708  SER   A CA  1 
ATOM   3253  C  C   . SER   A  1 407 ? -43.720 12.945  -39.258  1.00 44.82  ? 708  SER   A C   1 
ATOM   3254  O  O   . SER   A  1 407 ? -44.282 12.571  -40.288  1.00 53.18  ? 708  SER   A O   1 
ATOM   3255  C  CB  . SER   A  1 407 ? -44.859 13.897  -37.250  1.00 45.80  ? 708  SER   A CB  1 
ATOM   3256  O  OG  . SER   A  1 407 ? -45.929 13.008  -37.497  1.00 48.06  ? 708  SER   A OG  1 
ATOM   3257  N  N   . PHE   A  1 408 ? -42.698 12.308  -38.705  1.00 38.44  ? 709  PHE   A N   1 
ATOM   3258  C  CA  . PHE   A  1 408 ? -42.370 10.939  -39.044  1.00 34.74  ? 709  PHE   A CA  1 
ATOM   3259  C  C   . PHE   A  1 408 ? -43.099 10.026  -38.082  1.00 43.87  ? 709  PHE   A C   1 
ATOM   3260  O  O   . PHE   A  1 408 ? -43.286 10.363  -36.910  1.00 56.42  ? 709  PHE   A O   1 
ATOM   3261  C  CB  . PHE   A  1 408 ? -40.861 10.704  -39.003  1.00 28.30  ? 709  PHE   A CB  1 
ATOM   3262  C  CG  . PHE   A  1 408 ? -40.130 11.391  -40.125  1.00 32.53  ? 709  PHE   A CG  1 
ATOM   3263  C  CD1 . PHE   A  1 408 ? -39.379 12.535  -39.886  1.00 36.95  ? 709  PHE   A CD1 1 
ATOM   3264  C  CD2 . PHE   A  1 408 ? -40.240 10.924  -41.432  1.00 32.79  ? 709  PHE   A CD2 1 
ATOM   3265  C  CE1 . PHE   A  1 408 ? -38.714 13.172  -40.904  1.00 38.62  ? 709  PHE   A CE1 1 
ATOM   3266  C  CE2 . PHE   A  1 408 ? -39.580 11.574  -42.475  1.00 26.55  ? 709  PHE   A CE2 1 
ATOM   3267  C  CZ  . PHE   A  1 408 ? -38.818 12.689  -42.215  1.00 40.29  ? 709  PHE   A CZ  1 
ATOM   3268  N  N   . GLU   A  1 409 ? -43.562 8.904   -38.602  1.00 40.53  ? 710  GLU   A N   1 
ATOM   3269  C  CA  . GLU   A  1 409 ? -44.424 7.999   -37.878  1.00 45.52  ? 710  GLU   A CA  1 
ATOM   3270  C  C   . GLU   A  1 409 ? -43.931 6.590   -38.114  1.00 46.76  ? 710  GLU   A C   1 
ATOM   3271  O  O   . GLU   A  1 409 ? -43.398 6.277   -39.178  1.00 50.07  ? 710  GLU   A O   1 
ATOM   3272  C  CB  . GLU   A  1 409 ? -45.882 8.092   -38.346  1.00 53.38  ? 710  GLU   A CB  1 
ATOM   3273  C  CG  . GLU   A  1 409 ? -46.498 9.463   -38.272  1.00 60.91  ? 710  GLU   A CG  1 
ATOM   3274  C  CD  . GLU   A  1 409 ? -46.865 9.863   -36.857  1.00 71.32  ? 710  GLU   A CD  1 
ATOM   3275  O  OE1 . GLU   A  1 409 ? -46.827 8.996   -35.954  1.00 75.26  ? 710  GLU   A OE1 1 
ATOM   3276  O  OE2 . GLU   A  1 409 ? -47.192 11.052  -36.648  1.00 73.59  ? 710  GLU   A OE2 1 
ATOM   3277  N  N   . TYR   A  1 410 ? -44.125 5.742   -37.116  1.00 44.88  ? 711  TYR   A N   1 
ATOM   3278  C  CA  . TYR   A  1 410 ? -43.942 4.325   -37.333  1.00 45.38  ? 711  TYR   A CA  1 
ATOM   3279  C  C   . TYR   A  1 410 ? -45.099 3.767   -38.142  1.00 47.06  ? 711  TYR   A C   1 
ATOM   3280  O  O   . TYR   A  1 410 ? -46.212 4.295   -38.133  1.00 49.31  ? 711  TYR   A O   1 
ATOM   3281  C  CB  . TYR   A  1 410 ? -43.855 3.585   -36.007  1.00 49.32  ? 711  TYR   A CB  1 
ATOM   3282  C  CG  . TYR   A  1 410 ? -42.688 3.996   -35.179  1.00 54.22  ? 711  TYR   A CG  1 
ATOM   3283  C  CD1 . TYR   A  1 410 ? -42.852 4.825   -34.087  1.00 64.53  ? 711  TYR   A CD1 1 
ATOM   3284  C  CD2 . TYR   A  1 410 ? -41.412 3.578   -35.505  1.00 58.96  ? 711  TYR   A CD2 1 
ATOM   3285  C  CE1 . TYR   A  1 410 ? -41.778 5.208   -33.326  1.00 71.91  ? 711  TYR   A CE1 1 
ATOM   3286  C  CE2 . TYR   A  1 410 ? -40.332 3.962   -34.761  1.00 69.22  ? 711  TYR   A CE2 1 
ATOM   3287  C  CZ  . TYR   A  1 410 ? -40.520 4.771   -33.669  1.00 73.97  ? 711  TYR   A CZ  1 
ATOM   3288  O  OH  . TYR   A  1 410 ? -39.438 5.145   -32.922  1.00 79.50  ? 711  TYR   A OH  1 
ATOM   3289  N  N   . GLN   A  1 411 ? -44.829 2.674   -38.836  1.00 46.69  ? 712  GLN   A N   1 
ATOM   3290  C  CA  . GLN   A  1 411 ? -45.890 1.940   -39.492  1.00 53.11  ? 712  GLN   A CA  1 
ATOM   3291  C  C   . GLN   A  1 411 ? -45.582 0.461   -39.354  1.00 47.35  ? 712  GLN   A C   1 
ATOM   3292  O  O   . GLN   A  1 411 ? -44.421 0.084   -39.154  1.00 58.27  ? 712  GLN   A O   1 
ATOM   3293  C  CB  . GLN   A  1 411 ? -46.023 2.327   -40.973  1.00 56.11  ? 712  GLN   A CB  1 
ATOM   3294  C  CG  . GLN   A  1 411 ? -44.729 2.379   -41.706  1.00 59.98  ? 712  GLN   A CG  1 
ATOM   3295  C  CD  . GLN   A  1 411 ? -44.914 2.821   -43.138  1.00 56.47  ? 712  GLN   A CD  1 
ATOM   3296  O  OE1 . GLN   A  1 411 ? -46.040 3.005   -43.616  1.00 47.74  ? 712  GLN   A OE1 1 
ATOM   3297  N  NE2 . GLN   A  1 411 ? -43.807 2.989   -43.835  1.00 54.16  ? 712  GLN   A NE2 1 
ATOM   3298  N  N   . PRO   A  1 412 ? -46.593 -0.393  -39.419  1.00 43.12  ? 713  PRO   A N   1 
ATOM   3299  C  CA  . PRO   A  1 412 ? -46.345 -1.825  -39.240  1.00 54.05  ? 713  PRO   A CA  1 
ATOM   3300  C  C   . PRO   A  1 412 ? -45.449 -2.382  -40.343  1.00 62.27  ? 713  PRO   A C   1 
ATOM   3301  O  O   . PRO   A  1 412 ? -45.364 -1.835  -41.447  1.00 56.62  ? 713  PRO   A O   1 
ATOM   3302  C  CB  . PRO   A  1 412 ? -47.749 -2.431  -39.286  1.00 48.86  ? 713  PRO   A CB  1 
ATOM   3303  C  CG  . PRO   A  1 412 ? -48.555 -1.426  -40.055  1.00 43.13  ? 713  PRO   A CG  1 
ATOM   3304  C  CD  . PRO   A  1 412 ? -48.021 -0.104  -39.616  1.00 37.98  ? 713  PRO   A CD  1 
ATOM   3305  N  N   . ASP   A  1 413 ? -44.767 -3.477  -40.017  1.00 64.26  ? 714  ASP   A N   1 
ATOM   3306  C  CA  . ASP   A  1 413 ? -43.852 -4.095  -40.959  1.00 63.42  ? 714  ASP   A CA  1 
ATOM   3307  C  C   . ASP   A  1 413 ? -44.600 -4.580  -42.197  1.00 68.11  ? 714  ASP   A C   1 
ATOM   3308  O  O   . ASP   A  1 413 ? -45.703 -5.127  -42.085  1.00 74.16  ? 714  ASP   A O   1 
ATOM   3309  C  CB  . ASP   A  1 413 ? -43.125 -5.263  -40.300  1.00 69.59  ? 714  ASP   A CB  1 
ATOM   3310  C  CG  . ASP   A  1 413 ? -42.165 -4.814  -39.236  1.00 75.80  ? 714  ASP   A CG  1 
ATOM   3311  O  OD1 . ASP   A  1 413 ? -41.624 -3.696  -39.362  1.00 72.92  ? 714  ASP   A OD1 1 
ATOM   3312  O  OD2 . ASP   A  1 413 ? -41.951 -5.576  -38.274  1.00 83.18  ? 714  ASP   A OD2 1 
ATOM   3313  N  N   . PRO   A  1 414 ? -44.020 -4.416  -43.385  1.00 60.99  ? 715  PRO   A N   1 
ATOM   3314  C  CA  . PRO   A  1 414 ? -44.754 -4.750  -44.615  1.00 56.80  ? 715  PRO   A CA  1 
ATOM   3315  C  C   . PRO   A  1 414 ? -45.187 -6.198  -44.713  1.00 65.79  ? 715  PRO   A C   1 
ATOM   3316  O  O   . PRO   A  1 414 ? -46.270 -6.473  -45.243  1.00 67.04  ? 715  PRO   A O   1 
ATOM   3317  C  CB  . PRO   A  1 414 ? -43.748 -4.395  -45.711  1.00 51.16  ? 715  PRO   A CB  1 
ATOM   3318  C  CG  . PRO   A  1 414 ? -42.897 -3.324  -45.093  1.00 59.68  ? 715  PRO   A CG  1 
ATOM   3319  C  CD  . PRO   A  1 414 ? -42.748 -3.730  -43.658  1.00 60.86  ? 715  PRO   A CD  1 
ATOM   3320  N  N   . TRP   A  1 415 ? -44.380 -7.141  -44.224  1.00 68.71  ? 716  TRP   A N   1 
ATOM   3321  C  CA  . TRP   A  1 415 ? -44.737 -8.547  -44.358  1.00 66.88  ? 716  TRP   A CA  1 
ATOM   3322  C  C   . TRP   A  1 415 ? -45.850 -8.976  -43.416  1.00 73.05  ? 716  TRP   A C   1 
ATOM   3323  O  O   . TRP   A  1 415 ? -46.377 -10.079 -43.577  1.00 77.21  ? 716  TRP   A O   1 
ATOM   3324  C  CB  . TRP   A  1 415 ? -43.512 -9.431  -44.130  1.00 68.93  ? 716  TRP   A CB  1 
ATOM   3325  C  CG  . TRP   A  1 415 ? -42.804 -9.158  -42.847  1.00 73.02  ? 716  TRP   A CG  1 
ATOM   3326  C  CD1 . TRP   A  1 415 ? -43.033 -9.753  -41.643  1.00 73.05  ? 716  TRP   A CD1 1 
ATOM   3327  C  CD2 . TRP   A  1 415 ? -41.740 -8.219  -42.634  1.00 66.94  ? 716  TRP   A CD2 1 
ATOM   3328  N  NE1 . TRP   A  1 415 ? -42.177 -9.246  -40.691  1.00 61.03  ? 716  TRP   A NE1 1 
ATOM   3329  C  CE2 . TRP   A  1 415 ? -41.377 -8.300  -41.273  1.00 58.40  ? 716  TRP   A CE2 1 
ATOM   3330  C  CE3 . TRP   A  1 415 ? -41.064 -7.317  -43.458  1.00 63.20  ? 716  TRP   A CE3 1 
ATOM   3331  C  CZ2 . TRP   A  1 415 ? -40.371 -7.518  -40.722  1.00 52.99  ? 716  TRP   A CZ2 1 
ATOM   3332  C  CZ3 . TRP   A  1 415 ? -40.065 -6.542  -42.907  1.00 63.71  ? 716  TRP   A CZ3 1 
ATOM   3333  C  CH2 . TRP   A  1 415 ? -39.727 -6.648  -41.550  1.00 59.01  ? 716  TRP   A CH2 1 
ATOM   3334  N  N   . ASN   A  1 416 ? -46.218 -8.145  -42.437  1.00 72.82  ? 717  ASN   A N   1 
ATOM   3335  C  CA  . ASN   A  1 416 ? -47.359 -8.467  -41.587  1.00 62.33  ? 717  ASN   A CA  1 
ATOM   3336  C  C   . ASN   A  1 416 ? -48.684 -8.190  -42.277  1.00 61.18  ? 717  ASN   A C   1 
ATOM   3337  O  O   . ASN   A  1 416 ? -49.656 -8.920  -42.065  1.00 63.54  ? 717  ASN   A O   1 
ATOM   3338  C  CB  . ASN   A  1 416 ? -47.278 -7.684  -40.283  1.00 61.04  ? 717  ASN   A CB  1 
ATOM   3339  C  CG  . ASN   A  1 416 ? -46.124 -8.136  -39.415  1.00 63.58  ? 717  ASN   A CG  1 
ATOM   3340  O  OD1 . ASN   A  1 416 ? -45.751 -9.312  -39.426  1.00 65.51  ? 717  ASN   A OD1 1 
ATOM   3341  N  ND2 . ASN   A  1 416 ? -45.539 -7.201  -38.664  1.00 60.08  ? 717  ASN   A ND2 1 
ATOM   3342  N  N   . THR   A  1 417 ? -48.742 -7.167  -43.123  1.00 60.17  ? 718  THR   A N   1 
ATOM   3343  C  CA  . THR   A  1 417 ? -50.001 -6.746  -43.709  1.00 62.04  ? 718  THR   A CA  1 
ATOM   3344  C  C   . THR   A  1 417 ? -50.114 -6.982  -45.211  1.00 63.27  ? 718  THR   A C   1 
ATOM   3345  O  O   . THR   A  1 417 ? -51.240 -6.989  -45.724  1.00 51.11  ? 718  THR   A O   1 
ATOM   3346  C  CB  . THR   A  1 417 ? -50.228 -5.258  -43.428  1.00 55.80  ? 718  THR   A CB  1 
ATOM   3347  O  OG1 . THR   A  1 417 ? -49.221 -4.502  -44.113  1.00 60.18  ? 718  THR   A OG1 1 
ATOM   3348  C  CG2 . THR   A  1 417 ? -50.120 -5.000  -41.938  1.00 52.57  ? 718  THR   A CG2 1 
ATOM   3349  N  N   . HIS   A  1 418 ? -48.999 -7.182  -45.921  1.00 63.10  ? 719  HIS   A N   1 
ATOM   3350  C  CA  . HIS   A  1 418 ? -49.050 -7.316  -47.373  1.00 64.84  ? 719  HIS   A CA  1 
ATOM   3351  C  C   . HIS   A  1 418 ? -49.728 -8.617  -47.796  1.00 64.86  ? 719  HIS   A C   1 
ATOM   3352  O  O   . HIS   A  1 418 ? -49.502 -9.678  -47.209  1.00 69.14  ? 719  HIS   A O   1 
ATOM   3353  C  CB  . HIS   A  1 418 ? -47.647 -7.252  -47.975  1.00 65.13  ? 719  HIS   A CB  1 
ATOM   3354  C  CG  . HIS   A  1 418 ? -47.608 -7.563  -49.440  1.00 64.45  ? 719  HIS   A CG  1 
ATOM   3355  N  ND1 . HIS   A  1 418 ? -48.180 -6.745  -50.391  1.00 63.59  ? 719  HIS   A ND1 1 
ATOM   3356  C  CD2 . HIS   A  1 418 ? -47.077 -8.610  -50.116  1.00 64.19  ? 719  HIS   A CD2 1 
ATOM   3357  C  CE1 . HIS   A  1 418 ? -47.999 -7.273  -51.588  1.00 67.15  ? 719  HIS   A CE1 1 
ATOM   3358  N  NE2 . HIS   A  1 418 ? -47.333 -8.405  -51.449  1.00 65.41  ? 719  HIS   A NE2 1 
ATOM   3359  N  N   . VAL   A  1 419 ? -50.559 -8.523  -48.831  1.00 69.14  ? 720  VAL   A N   1 
ATOM   3360  C  CA  . VAL   A  1 419 ? -51.249 -9.668  -49.417  1.00 77.65  ? 720  VAL   A CA  1 
ATOM   3361  C  C   . VAL   A  1 419 ? -50.611 -9.957  -50.772  1.00 78.13  ? 720  VAL   A C   1 
ATOM   3362  O  O   . VAL   A  1 419 ? -50.586 -9.089  -51.656  1.00 80.29  ? 720  VAL   A O   1 
ATOM   3363  C  CB  . VAL   A  1 419 ? -52.760 -9.412  -49.534  1.00 81.59  ? 720  VAL   A CB  1 
ATOM   3364  C  CG1 . VAL   A  1 419 ? -53.373 -10.255 -50.640  1.00 82.69  ? 720  VAL   A CG1 1 
ATOM   3365  C  CG2 . VAL   A  1 419 ? -53.433 -9.718  -48.207  1.00 85.82  ? 720  VAL   A CG2 1 
ATOM   3366  N  N   . TRP   A  1 420 ? -50.109 -11.182 -50.933  1.00 75.14  ? 721  TRP   A N   1 
ATOM   3367  C  CA  . TRP   A  1 420 ? -49.205 -11.521 -52.027  1.00 79.95  ? 721  TRP   A CA  1 
ATOM   3368  C  C   . TRP   A  1 420 ? -49.949 -11.734 -53.346  1.00 87.89  ? 721  TRP   A C   1 
ATOM   3369  O  O   . TRP   A  1 420 ? -50.947 -12.461 -53.396  1.00 92.24  ? 721  TRP   A O   1 
ATOM   3370  C  CB  . TRP   A  1 420 ? -48.395 -12.764 -51.653  1.00 73.48  ? 721  TRP   A CB  1 
ATOM   3371  C  CG  . TRP   A  1 420 ? -47.307 -12.450 -50.662  1.00 70.33  ? 721  TRP   A CG  1 
ATOM   3372  C  CD1 . TRP   A  1 420 ? -47.417 -12.423 -49.296  1.00 68.42  ? 721  TRP   A CD1 1 
ATOM   3373  C  CD2 . TRP   A  1 420 ? -45.950 -12.090 -50.959  1.00 67.32  ? 721  TRP   A CD2 1 
ATOM   3374  N  NE1 . TRP   A  1 420 ? -46.211 -12.074 -48.729  1.00 57.83  ? 721  TRP   A NE1 1 
ATOM   3375  C  CE2 . TRP   A  1 420 ? -45.296 -11.865 -49.728  1.00 67.39  ? 721  TRP   A CE2 1 
ATOM   3376  C  CE3 . TRP   A  1 420 ? -45.223 -11.946 -52.144  1.00 61.97  ? 721  TRP   A CE3 1 
ATOM   3377  C  CZ2 . TRP   A  1 420 ? -43.956 -11.499 -49.654  1.00 69.52  ? 721  TRP   A CZ2 1 
ATOM   3378  C  CZ3 . TRP   A  1 420 ? -43.900 -11.582 -52.068  1.00 62.11  ? 721  TRP   A CZ3 1 
ATOM   3379  C  CH2 . TRP   A  1 420 ? -43.276 -11.362 -50.833  1.00 65.38  ? 721  TRP   A CH2 1 
ATOM   3380  N  N   . LYS   A  1 421 ? -49.435 -11.106 -54.414  1.00 87.78  ? 722  LYS   A N   1 
ATOM   3381  C  CA  . LYS   A  1 421 ? -49.997 -11.159 -55.776  1.00 86.38  ? 722  LYS   A CA  1 
ATOM   3382  C  C   . LYS   A  1 421 ? -50.006 -12.564 -56.396  1.00 91.78  ? 722  LYS   A C   1 
ATOM   3383  O  O   . LYS   A  1 421 ? -51.034 -13.012 -56.917  1.00 92.84  ? 722  LYS   A O   1 
ATOM   3384  C  CB  . LYS   A  1 421 ? -49.218 -10.222 -56.716  1.00 82.98  ? 722  LYS   A CB  1 
ATOM   3385  C  CG  . LYS   A  1 421 ? -49.267 -8.739  -56.378  1.00 86.59  ? 722  LYS   A CG  1 
ATOM   3386  C  CD  . LYS   A  1 421 ? -50.668 -8.175  -56.476  1.00 85.76  ? 722  LYS   A CD  1 
ATOM   3387  C  CE  . LYS   A  1 421 ? -50.983 -7.316  -55.269  1.00 78.24  ? 722  LYS   A CE  1 
ATOM   3388  N  NZ  . LYS   A  1 421 ? -52.416 -6.937  -55.264  1.00 75.47  ? 722  LYS   A NZ  1 
ATOM   3389  N  N   . ARG   B  1 3   ? -58.160 1.795   -19.734  1.00 93.67  ? 304  ARG   B N   1 
ATOM   3390  C  CA  . ARG   B  1 3   ? -58.448 0.366   -19.676  1.00 103.05 ? 304  ARG   B CA  1 
ATOM   3391  C  C   . ARG   B  1 3   ? -57.372 -0.375  -18.865  1.00 111.53 ? 304  ARG   B C   1 
ATOM   3392  O  O   . ARG   B  1 3   ? -57.245 -0.156  -17.660  1.00 120.25 ? 304  ARG   B O   1 
ATOM   3393  C  CB  . ARG   B  1 3   ? -58.567 -0.199  -21.094  1.00 106.22 ? 304  ARG   B CB  1 
ATOM   3394  C  CG  . ARG   B  1 3   ? -59.644 0.500   -21.927  1.00 113.92 ? 304  ARG   B CG  1 
ATOM   3395  C  CD  . ARG   B  1 3   ? -59.422 0.364   -23.430  1.00 118.49 ? 304  ARG   B CD  1 
ATOM   3396  N  NE  . ARG   B  1 3   ? -59.727 -0.974  -23.937  1.00 127.78 ? 304  ARG   B NE  1 
ATOM   3397  C  CZ  . ARG   B  1 3   ? -58.835 -1.953  -24.073  1.00 135.50 ? 304  ARG   B CZ  1 
ATOM   3398  N  NH1 . ARG   B  1 3   ? -57.566 -1.754  -23.732  1.00 139.12 ? 304  ARG   B NH1 1 
ATOM   3399  N  NH2 . ARG   B  1 3   ? -59.213 -3.136  -24.549  1.00 135.63 ? 304  ARG   B NH2 1 
ATOM   3400  N  N   . PHE   B  1 4   ? -56.601 -1.245  -19.524  1.00 105.20 ? 305  PHE   B N   1 
ATOM   3401  C  CA  . PHE   B  1 4   ? -55.541 -2.028  -18.894  1.00 84.87  ? 305  PHE   B CA  1 
ATOM   3402  C  C   . PHE   B  1 4   ? -54.321 -1.982  -19.799  1.00 75.94  ? 305  PHE   B C   1 
ATOM   3403  O  O   . PHE   B  1 4   ? -54.457 -2.064  -21.021  1.00 91.78  ? 305  PHE   B O   1 
ATOM   3404  C  CB  . PHE   B  1 4   ? -55.978 -3.474  -18.663  1.00 85.71  ? 305  PHE   B CB  1 
ATOM   3405  C  CG  . PHE   B  1 4   ? -57.428 -3.609  -18.294  1.00 92.43  ? 305  PHE   B CG  1 
ATOM   3406  C  CD1 . PHE   B  1 4   ? -58.407 -3.674  -19.284  1.00 102.62 ? 305  PHE   B CD1 1 
ATOM   3407  C  CD2 . PHE   B  1 4   ? -57.819 -3.657  -16.963  1.00 88.30  ? 305  PHE   B CD2 1 
ATOM   3408  C  CE1 . PHE   B  1 4   ? -59.746 -3.788  -18.956  1.00 109.34 ? 305  PHE   B CE1 1 
ATOM   3409  C  CE2 . PHE   B  1 4   ? -59.155 -3.772  -16.618  1.00 94.80  ? 305  PHE   B CE2 1 
ATOM   3410  C  CZ  . PHE   B  1 4   ? -60.122 -3.841  -17.616  1.00 109.48 ? 305  PHE   B CZ  1 
ATOM   3411  N  N   . LEU   B  1 5   ? -53.135 -1.842  -19.209  1.00 56.62  ? 306  LEU   B N   1 
ATOM   3412  C  CA  . LEU   B  1 5   ? -51.947 -1.424  -19.942  1.00 48.00  ? 306  LEU   B CA  1 
ATOM   3413  C  C   . LEU   B  1 5   ? -50.820 -2.442  -19.822  1.00 50.42  ? 306  LEU   B C   1 
ATOM   3414  O  O   . LEU   B  1 5   ? -50.506 -2.910  -18.726  1.00 56.77  ? 306  LEU   B O   1 
ATOM   3415  C  CB  . LEU   B  1 5   ? -51.465 -0.063  -19.448  1.00 44.59  ? 306  LEU   B CB  1 
ATOM   3416  C  CG  . LEU   B  1 5   ? -52.518 1.040   -19.420  1.00 40.36  ? 306  LEU   B CG  1 
ATOM   3417  C  CD1 . LEU   B  1 5   ? -51.874 2.318   -18.986  1.00 41.78  ? 306  LEU   B CD1 1 
ATOM   3418  C  CD2 . LEU   B  1 5   ? -53.126 1.211   -20.791  1.00 45.77  ? 306  LEU   B CD2 1 
ATOM   3419  N  N   . LYS   B  1 6   ? -50.201 -2.756  -20.956  1.00 50.22  ? 307  LYS   B N   1 
ATOM   3420  C  CA  . LYS   B  1 6   ? -49.094 -3.695  -21.038  1.00 53.90  ? 307  LYS   B CA  1 
ATOM   3421  C  C   . LYS   B  1 6   ? -47.781 -2.931  -21.098  1.00 55.30  ? 307  LYS   B C   1 
ATOM   3422  O  O   . LYS   B  1 6   ? -47.714 -1.843  -21.672  1.00 59.39  ? 307  LYS   B O   1 
ATOM   3423  C  CB  . LYS   B  1 6   ? -49.207 -4.573  -22.287  1.00 66.89  ? 307  LYS   B CB  1 
ATOM   3424  C  CG  . LYS   B  1 6   ? -50.598 -5.079  -22.624  1.00 73.59  ? 307  LYS   B CG  1 
ATOM   3425  C  CD  . LYS   B  1 6   ? -50.648 -6.606  -22.591  1.00 71.67  ? 307  LYS   B CD  1 
ATOM   3426  C  CE  . LYS   B  1 6   ? -52.039 -7.119  -22.899  1.00 72.65  ? 307  LYS   B CE  1 
ATOM   3427  N  NZ  . LYS   B  1 6   ? -52.229 -8.519  -22.429  1.00 76.25  ? 307  LYS   B NZ  1 
ATOM   3428  N  N   . VAL   B  1 7   ? -46.740 -3.495  -20.508  1.00 54.87  ? 308  VAL   B N   1 
ATOM   3429  C  CA  . VAL   B  1 7   ? -45.390 -2.995  -20.709  1.00 51.59  ? 308  VAL   B CA  1 
ATOM   3430  C  C   . VAL   B  1 7   ? -44.568 -4.156  -21.247  1.00 51.93  ? 308  VAL   B C   1 
ATOM   3431  O  O   . VAL   B  1 7   ? -44.887 -5.324  -21.006  1.00 63.03  ? 308  VAL   B O   1 
ATOM   3432  C  CB  . VAL   B  1 7   ? -44.776 -2.410  -19.414  1.00 55.92  ? 308  VAL   B CB  1 
ATOM   3433  C  CG1 . VAL   B  1 7   ? -45.793 -1.553  -18.682  1.00 57.46  ? 308  VAL   B CG1 1 
ATOM   3434  C  CG2 . VAL   B  1 7   ? -44.235 -3.504  -18.509  1.00 54.82  ? 308  VAL   B CG2 1 
ATOM   3435  N  N   . LYS   B  1 8   ? -43.529 -3.837  -22.008  1.00 38.88  ? 309  LYS   B N   1 
ATOM   3436  C  CA  . LYS   B  1 8   ? -42.741 -4.853  -22.691  1.00 34.15  ? 309  LYS   B CA  1 
ATOM   3437  C  C   . LYS   B  1 8   ? -41.267 -4.574  -22.490  1.00 40.56  ? 309  LYS   B C   1 
ATOM   3438  O  O   . LYS   B  1 8   ? -40.847 -3.411  -22.441  1.00 45.22  ? 309  LYS   B O   1 
ATOM   3439  C  CB  . LYS   B  1 8   ? -43.057 -4.896  -24.208  1.00 50.98  ? 309  LYS   B CB  1 
ATOM   3440  C  CG  . LYS   B  1 8   ? -42.179 -5.845  -25.028  1.00 58.55  ? 309  LYS   B CG  1 
ATOM   3441  C  CD  . LYS   B  1 8   ? -42.418 -5.696  -26.535  1.00 69.96  ? 309  LYS   B CD  1 
ATOM   3442  C  CE  . LYS   B  1 8   ? -41.530 -6.649  -27.338  1.00 70.85  ? 309  LYS   B CE  1 
ATOM   3443  N  NZ  . LYS   B  1 8   ? -41.608 -6.405  -28.804  1.00 71.42  ? 309  LYS   B NZ  1 
ATOM   3444  N  N   . ASN   B  1 9   ? -40.489 -5.653  -22.376  1.00 45.12  ? 310  ASN   B N   1 
ATOM   3445  C  CA  . ASN   B  1 9   ? -39.036 -5.586  -22.270  1.00 44.81  ? 310  ASN   B CA  1 
ATOM   3446  C  C   . ASN   B  1 9   ? -38.457 -5.946  -23.628  1.00 53.90  ? 310  ASN   B C   1 
ATOM   3447  O  O   . ASN   B  1 9   ? -38.567 -7.093  -24.071  1.00 57.11  ? 310  ASN   B O   1 
ATOM   3448  C  CB  . ASN   B  1 9   ? -38.526 -6.530  -21.186  1.00 50.85  ? 310  ASN   B CB  1 
ATOM   3449  C  CG  . ASN   B  1 9   ? -37.054 -6.334  -20.891  1.00 68.18  ? 310  ASN   B CG  1 
ATOM   3450  O  OD1 . ASN   B  1 9   ? -36.211 -6.615  -21.738  1.00 78.52  ? 310  ASN   B OD1 1 
ATOM   3451  N  ND2 . ASN   B  1 9   ? -36.733 -5.859  -19.681  1.00 67.13  ? 310  ASN   B ND2 1 
ATOM   3452  N  N   . TRP   B  1 10  ? -37.837 -4.972  -24.289  1.00 50.78  ? 311  TRP   B N   1 
ATOM   3453  C  CA  . TRP   B  1 10  ? -37.399 -5.199  -25.658  1.00 54.98  ? 311  TRP   B CA  1 
ATOM   3454  C  C   . TRP   B  1 10  ? -36.156 -6.067  -25.741  1.00 57.04  ? 311  TRP   B C   1 
ATOM   3455  O  O   . TRP   B  1 10  ? -35.663 -6.308  -26.845  1.00 57.05  ? 311  TRP   B O   1 
ATOM   3456  C  CB  . TRP   B  1 10  ? -37.175 -3.863  -26.363  1.00 50.41  ? 311  TRP   B CB  1 
ATOM   3457  C  CG  . TRP   B  1 10  ? -38.450 -3.169  -26.605  1.00 45.38  ? 311  TRP   B CG  1 
ATOM   3458  C  CD1 . TRP   B  1 10  ? -39.094 -2.336  -25.750  1.00 48.04  ? 311  TRP   B CD1 1 
ATOM   3459  C  CD2 . TRP   B  1 10  ? -39.273 -3.269  -27.770  1.00 55.64  ? 311  TRP   B CD2 1 
ATOM   3460  N  NE1 . TRP   B  1 10  ? -40.267 -1.895  -26.309  1.00 52.36  ? 311  TRP   B NE1 1 
ATOM   3461  C  CE2 . TRP   B  1 10  ? -40.401 -2.453  -27.553  1.00 56.53  ? 311  TRP   B CE2 1 
ATOM   3462  C  CE3 . TRP   B  1 10  ? -39.157 -3.953  -28.984  1.00 57.25  ? 311  TRP   B CE3 1 
ATOM   3463  C  CZ2 . TRP   B  1 10  ? -41.417 -2.312  -28.499  1.00 56.07  ? 311  TRP   B CZ2 1 
ATOM   3464  C  CZ3 . TRP   B  1 10  ? -40.164 -3.813  -29.923  1.00 61.63  ? 311  TRP   B CZ3 1 
ATOM   3465  C  CH2 . TRP   B  1 10  ? -41.279 -2.996  -29.677  1.00 62.63  ? 311  TRP   B CH2 1 
ATOM   3466  N  N   . GLU   B  1 11  ? -35.641 -6.546  -24.611  1.00 54.21  ? 312  GLU   B N   1 
ATOM   3467  C  CA  . GLU   B  1 11  ? -34.520 -7.472  -24.627  1.00 54.40  ? 312  GLU   B CA  1 
ATOM   3468  C  C   . GLU   B  1 11  ? -34.956 -8.911  -24.399  1.00 66.63  ? 312  GLU   B C   1 
ATOM   3469  O  O   . GLU   B  1 11  ? -34.261 -9.828  -24.844  1.00 80.18  ? 312  GLU   B O   1 
ATOM   3470  C  CB  . GLU   B  1 11  ? -33.487 -7.067  -23.567  1.00 53.17  ? 312  GLU   B CB  1 
ATOM   3471  C  CG  . GLU   B  1 11  ? -32.041 -7.381  -23.920  1.00 73.41  ? 312  GLU   B CG  1 
ATOM   3472  C  CD  . GLU   B  1 11  ? -31.041 -7.034  -22.795  1.00 83.57  ? 312  GLU   B CD  1 
ATOM   3473  O  OE1 . GLU   B  1 11  ? -31.471 -6.750  -21.643  1.00 64.76  ? 312  GLU   B OE1 1 
ATOM   3474  O  OE2 . GLU   B  1 11  ? -29.815 -7.053  -23.080  1.00 98.22  ? 312  GLU   B OE2 1 
ATOM   3475  N  N   . THR   B  1 12  ? -36.096 -9.127  -23.736  1.00 68.92  ? 313  THR   B N   1 
ATOM   3476  C  CA  . THR   B  1 12  ? -36.619 -10.456 -23.454  1.00 63.05  ? 313  THR   B CA  1 
ATOM   3477  C  C   . THR   B  1 12  ? -37.992 -10.697 -24.056  1.00 69.86  ? 313  THR   B C   1 
ATOM   3478  O  O   . THR   B  1 12  ? -38.452 -11.845 -24.063  1.00 75.57  ? 313  THR   B O   1 
ATOM   3479  C  CB  . THR   B  1 12  ? -36.708 -10.684 -21.940  1.00 58.80  ? 313  THR   B CB  1 
ATOM   3480  O  OG1 . THR   B  1 12  ? -37.827 -9.957  -21.421  1.00 62.66  ? 313  THR   B OG1 1 
ATOM   3481  C  CG2 . THR   B  1 12  ? -35.457 -10.182 -21.254  1.00 54.96  ? 313  THR   B CG2 1 
ATOM   3482  N  N   . GLU   B  1 13  ? -38.653 -9.651  -24.555  1.00 72.92  ? 314  GLU   B N   1 
ATOM   3483  C  CA  . GLU   B  1 13  ? -40.029 -9.653  -25.053  1.00 73.94  ? 314  GLU   B CA  1 
ATOM   3484  C  C   . GLU   B  1 13  ? -41.044 -10.013 -23.975  1.00 71.23  ? 314  GLU   B C   1 
ATOM   3485  O  O   . GLU   B  1 13  ? -42.200 -10.310 -24.286  1.00 71.70  ? 314  GLU   B O   1 
ATOM   3486  C  CB  . GLU   B  1 13  ? -40.183 -10.564 -26.271  1.00 77.49  ? 314  GLU   B CB  1 
ATOM   3487  C  CG  . GLU   B  1 13  ? -39.534 -9.974  -27.515  1.00 78.76  ? 314  GLU   B CG  1 
ATOM   3488  C  CD  . GLU   B  1 13  ? -39.510 -10.939 -28.672  1.00 78.12  ? 314  GLU   B CD  1 
ATOM   3489  O  OE1 . GLU   B  1 13  ? -40.597 -11.297 -29.161  1.00 81.65  ? 314  GLU   B OE1 1 
ATOM   3490  O  OE2 . GLU   B  1 13  ? -38.404 -11.344 -29.083  1.00 80.74  ? 314  GLU   B OE2 1 
ATOM   3491  N  N   . VAL   B  1 14  ? -40.644 -9.968  -22.708  1.00 68.18  ? 315  VAL   B N   1 
ATOM   3492  C  CA  . VAL   B  1 14  ? -41.583 -10.185 -21.619  1.00 61.97  ? 315  VAL   B CA  1 
ATOM   3493  C  C   . VAL   B  1 14  ? -42.584 -9.037  -21.576  1.00 61.17  ? 315  VAL   B C   1 
ATOM   3494  O  O   . VAL   B  1 14  ? -42.211 -7.856  -21.631  1.00 61.27  ? 315  VAL   B O   1 
ATOM   3495  C  CB  . VAL   B  1 14  ? -40.822 -10.341 -20.294  1.00 62.43  ? 315  VAL   B CB  1 
ATOM   3496  C  CG1 . VAL   B  1 14  ? -41.718 -10.021 -19.091  1.00 62.13  ? 315  VAL   B CG1 1 
ATOM   3497  C  CG2 . VAL   B  1 14  ? -40.250 -11.743 -20.197  1.00 61.51  ? 315  VAL   B CG2 1 
ATOM   3498  N  N   . VAL   B  1 15  ? -43.866 -9.382  -21.486  1.00 57.13  ? 316  VAL   B N   1 
ATOM   3499  C  CA  . VAL   B  1 15  ? -44.941 -8.409  -21.351  1.00 54.80  ? 316  VAL   B CA  1 
ATOM   3500  C  C   . VAL   B  1 15  ? -45.580 -8.583  -19.981  1.00 68.38  ? 316  VAL   B C   1 
ATOM   3501  O  O   . VAL   B  1 15  ? -45.866 -9.709  -19.556  1.00 75.79  ? 316  VAL   B O   1 
ATOM   3502  C  CB  . VAL   B  1 15  ? -45.986 -8.557  -22.470  1.00 49.20  ? 316  VAL   B CB  1 
ATOM   3503  C  CG1 . VAL   B  1 15  ? -47.130 -7.569  -22.286  1.00 44.95  ? 316  VAL   B CG1 1 
ATOM   3504  C  CG2 . VAL   B  1 15  ? -45.336 -8.315  -23.770  1.00 38.01  ? 316  VAL   B CG2 1 
ATOM   3505  N  N   . LEU   B  1 16  ? -45.775 -7.467  -19.284  1.00 63.30  ? 317  LEU   B N   1 
ATOM   3506  C  CA  . LEU   B  1 16  ? -46.481 -7.431  -18.015  1.00 63.07  ? 317  LEU   B CA  1 
ATOM   3507  C  C   . LEU   B  1 16  ? -47.735 -6.595  -18.206  1.00 66.62  ? 317  LEU   B C   1 
ATOM   3508  O  O   . LEU   B  1 16  ? -47.751 -5.666  -19.016  1.00 73.47  ? 317  LEU   B O   1 
ATOM   3509  C  CB  . LEU   B  1 16  ? -45.597 -6.849  -16.894  1.00 50.94  ? 317  LEU   B CB  1 
ATOM   3510  C  CG  . LEU   B  1 16  ? -44.192 -7.467  -16.772  1.00 44.65  ? 317  LEU   B CG  1 
ATOM   3511  C  CD1 . LEU   B  1 16  ? -43.260 -6.673  -15.857  1.00 31.54  ? 317  LEU   B CD1 1 
ATOM   3512  C  CD2 . LEU   B  1 16  ? -44.288 -8.919  -16.341  1.00 45.42  ? 317  LEU   B CD2 1 
ATOM   3513  N  N   . THR   B  1 17  ? -48.795 -6.950  -17.488  1.00 67.88  ? 318  THR   B N   1 
ATOM   3514  C  CA  . THR   B  1 17  ? -50.075 -6.269  -17.602  1.00 65.47  ? 318  THR   B CA  1 
ATOM   3515  C  C   . THR   B  1 17  ? -50.323 -5.490  -16.323  1.00 59.05  ? 318  THR   B C   1 
ATOM   3516  O  O   . THR   B  1 17  ? -50.210 -6.041  -15.229  1.00 72.73  ? 318  THR   B O   1 
ATOM   3517  C  CB  . THR   B  1 17  ? -51.211 -7.256  -17.865  1.00 70.44  ? 318  THR   B CB  1 
ATOM   3518  O  OG1 . THR   B  1 17  ? -50.747 -8.268  -18.769  1.00 72.85  ? 318  THR   B OG1 1 
ATOM   3519  C  CG2 . THR   B  1 17  ? -52.395 -6.533  -18.502  1.00 66.55  ? 318  THR   B CG2 1 
ATOM   3520  N  N   . ASP   B  1 18  ? -50.651 -4.215  -16.467  1.00 52.95  ? 319  ASP   B N   1 
ATOM   3521  C  CA  . ASP   B  1 18  ? -50.744 -3.283  -15.351  1.00 55.10  ? 319  ASP   B CA  1 
ATOM   3522  C  C   . ASP   B  1 18  ? -52.203 -2.913  -15.138  1.00 61.62  ? 319  ASP   B C   1 
ATOM   3523  O  O   . ASP   B  1 18  ? -52.822 -2.283  -16.008  1.00 54.03  ? 319  ASP   B O   1 
ATOM   3524  C  CB  . ASP   B  1 18  ? -49.908 -2.040  -15.633  1.00 58.98  ? 319  ASP   B CB  1 
ATOM   3525  C  CG  . ASP   B  1 18  ? -49.713 -1.167  -14.411  1.00 54.18  ? 319  ASP   B CG  1 
ATOM   3526  O  OD1 . ASP   B  1 18  ? -50.722 -0.795  -13.772  1.00 48.00  ? 319  ASP   B OD1 1 
ATOM   3527  O  OD2 . ASP   B  1 18  ? -48.539 -0.853  -14.100  1.00 49.66  ? 319  ASP   B OD2 1 
ATOM   3528  N  N   . THR   B  1 19  ? -52.747 -3.306  -13.980  1.00 59.30  ? 320  THR   B N   1 
ATOM   3529  C  CA  . THR   B  1 19  ? -54.032 -2.807  -13.510  1.00 50.31  ? 320  THR   B CA  1 
ATOM   3530  C  C   . THR   B  1 19  ? -53.914 -1.886  -12.308  1.00 48.41  ? 320  THR   B C   1 
ATOM   3531  O  O   . THR   B  1 19  ? -54.870 -1.160  -12.019  1.00 47.69  ? 320  THR   B O   1 
ATOM   3532  C  CB  . THR   B  1 19  ? -54.968 -3.961  -13.134  1.00 52.61  ? 320  THR   B CB  1 
ATOM   3533  O  OG1 . THR   B  1 19  ? -54.296 -4.870  -12.242  1.00 58.95  ? 320  THR   B OG1 1 
ATOM   3534  C  CG2 . THR   B  1 19  ? -55.431 -4.680  -14.371  1.00 52.54  ? 320  THR   B CG2 1 
ATOM   3535  N  N   . LEU   B  1 20  ? -52.775 -1.895  -11.606  1.00 50.00  ? 321  LEU   B N   1 
ATOM   3536  C  CA  . LEU   B  1 20  ? -52.646 -1.083  -10.394  1.00 53.43  ? 321  LEU   B CA  1 
ATOM   3537  C  C   . LEU   B  1 20  ? -52.817 0.400   -10.702  1.00 52.41  ? 321  LEU   B C   1 
ATOM   3538  O  O   . LEU   B  1 20  ? -53.269 1.163   -9.846   1.00 42.42  ? 321  LEU   B O   1 
ATOM   3539  C  CB  . LEU   B  1 20  ? -51.297 -1.352  -9.719   1.00 41.53  ? 321  LEU   B CB  1 
ATOM   3540  C  CG  . LEU   B  1 20  ? -50.914 -0.688  -8.382   1.00 51.19  ? 321  LEU   B CG  1 
ATOM   3541  C  CD1 . LEU   B  1 20  ? -51.923 -0.967  -7.264   1.00 40.97  ? 321  LEU   B CD1 1 
ATOM   3542  C  CD2 . LEU   B  1 20  ? -49.495 -1.090  -7.947   1.00 49.84  ? 321  LEU   B CD2 1 
ATOM   3543  N  N   . HIS   B  1 21  ? -52.517 0.818   -11.933  1.00 53.67  ? 322  HIS   B N   1 
ATOM   3544  C  CA  . HIS   B  1 21  ? -52.611 2.230   -12.273  1.00 52.94  ? 322  HIS   B CA  1 
ATOM   3545  C  C   . HIS   B  1 21  ? -54.022 2.775   -12.111  1.00 49.20  ? 322  HIS   B C   1 
ATOM   3546  O  O   . HIS   B  1 21  ? -54.189 3.994   -12.070  1.00 57.80  ? 322  HIS   B O   1 
ATOM   3547  C  CB  . HIS   B  1 21  ? -52.149 2.464   -13.707  1.00 63.72  ? 322  HIS   B CB  1 
ATOM   3548  C  CG  . HIS   B  1 21  ? -53.147 2.016   -14.727  1.00 54.68  ? 322  HIS   B CG  1 
ATOM   3549  N  ND1 . HIS   B  1 21  ? -53.199 0.720   -15.195  1.00 53.13  ? 322  HIS   B ND1 1 
ATOM   3550  C  CD2 . HIS   B  1 21  ? -54.154 2.682   -15.339  1.00 56.09  ? 322  HIS   B CD2 1 
ATOM   3551  C  CE1 . HIS   B  1 21  ? -54.189 0.611   -16.064  1.00 61.17  ? 322  HIS   B CE1 1 
ATOM   3552  N  NE2 . HIS   B  1 21  ? -54.785 1.786   -16.167  1.00 61.43  ? 322  HIS   B NE2 1 
ATOM   3553  N  N   . LEU   B  1 22  ? -55.041 1.912   -12.038  1.00 48.97  ? 323  LEU   B N   1 
ATOM   3554  C  CA  . LEU   B  1 22  ? -56.403 2.406   -11.849  1.00 48.17  ? 323  LEU   B CA  1 
ATOM   3555  C  C   . LEU   B  1 22  ? -56.623 2.934   -10.433  1.00 53.75  ? 323  LEU   B C   1 
ATOM   3556  O  O   . LEU   B  1 22  ? -57.494 3.785   -10.232  1.00 61.67  ? 323  LEU   B O   1 
ATOM   3557  C  CB  . LEU   B  1 22  ? -57.426 1.312   -12.179  1.00 48.09  ? 323  LEU   B CB  1 
ATOM   3558  C  CG  . LEU   B  1 22  ? -57.483 0.727   -13.599  1.00 57.34  ? 323  LEU   B CG  1 
ATOM   3559  C  CD1 . LEU   B  1 22  ? -58.321 -0.552  -13.663  1.00 48.25  ? 323  LEU   B CD1 1 
ATOM   3560  C  CD2 . LEU   B  1 22  ? -58.021 1.747   -14.598  1.00 67.24  ? 323  LEU   B CD2 1 
ATOM   3561  N  N   . LYS   B  1 23  ? -55.830 2.482   -9.454   1.00 55.65  ? 324  LYS   B N   1 
ATOM   3562  C  CA  . LYS   B  1 23  ? -55.873 3.013   -8.091   1.00 60.18  ? 324  LYS   B CA  1 
ATOM   3563  C  C   . LYS   B  1 23  ? -55.068 4.301   -7.916   1.00 66.73  ? 324  LYS   B C   1 
ATOM   3564  O  O   . LYS   B  1 23  ? -54.696 4.632   -6.783   1.00 77.96  ? 324  LYS   B O   1 
ATOM   3565  C  CB  . LYS   B  1 23  ? -55.372 1.967   -7.083   1.00 61.97  ? 324  LYS   B CB  1 
ATOM   3566  C  CG  . LYS   B  1 23  ? -56.474 1.350   -6.220   1.00 69.13  ? 324  LYS   B CG  1 
ATOM   3567  C  CD  . LYS   B  1 23  ? -57.460 0.556   -7.087   1.00 83.36  ? 324  LYS   B CD  1 
ATOM   3568  C  CE  . LYS   B  1 23  ? -58.844 0.442   -6.442   1.00 89.14  ? 324  LYS   B CE  1 
ATOM   3569  N  NZ  . LYS   B  1 23  ? -58.762 0.174   -4.965   1.00 83.39  ? 324  LYS   B NZ  1 
ATOM   3570  N  N   . SER   B  1 24  ? -54.781 5.029   -8.987   1.00 64.94  ? 325  SER   B N   1 
ATOM   3571  C  CA  . SER   B  1 24  ? -53.992 6.250   -8.901   1.00 67.26  ? 325  SER   B CA  1 
ATOM   3572  C  C   . SER   B  1 24  ? -54.916 7.439   -8.692   1.00 72.04  ? 325  SER   B C   1 
ATOM   3573  O  O   . SER   B  1 24  ? -56.031 7.467   -9.221   1.00 80.53  ? 325  SER   B O   1 
ATOM   3574  C  CB  . SER   B  1 24  ? -53.162 6.432   -10.171  1.00 76.06  ? 325  SER   B CB  1 
ATOM   3575  O  OG  . SER   B  1 24  ? -52.468 7.667   -10.186  1.00 86.09  ? 325  SER   B OG  1 
ATOM   3576  N  N   . THR   B  1 25  ? -54.452 8.423   -7.917   1.00 75.41  ? 326  THR   B N   1 
ATOM   3577  C  CA  . THR   B  1 25  ? -55.315 9.531   -7.515   1.00 87.96  ? 326  THR   B CA  1 
ATOM   3578  C  C   . THR   B  1 25  ? -54.854 10.907  -7.978   1.00 89.79  ? 326  THR   B C   1 
ATOM   3579  O  O   . THR   B  1 25  ? -55.706 11.755  -8.255   1.00 104.21 ? 326  THR   B O   1 
ATOM   3580  C  CB  . THR   B  1 25  ? -55.484 9.570   -5.982   1.00 89.36  ? 326  THR   B CB  1 
ATOM   3581  O  OG1 . THR   B  1 25  ? -54.558 8.661   -5.350   1.00 81.61  ? 326  THR   B OG1 1 
ATOM   3582  C  CG2 . THR   B  1 25  ? -56.930 9.223   -5.607   1.00 89.73  ? 326  THR   B CG2 1 
ATOM   3583  N  N   . LEU   B  1 26  ? -53.554 11.160  -8.071   1.00 73.55  ? 327  LEU   B N   1 
ATOM   3584  C  CA  . LEU   B  1 26  ? -53.049 12.486  -8.395   1.00 68.86  ? 327  LEU   B CA  1 
ATOM   3585  C  C   . LEU   B  1 26  ? -52.527 12.565  -9.831   1.00 72.39  ? 327  LEU   B C   1 
ATOM   3586  O  O   . LEU   B  1 26  ? -52.107 11.563  -10.423  1.00 73.57  ? 327  LEU   B O   1 
ATOM   3587  C  CB  . LEU   B  1 26  ? -51.943 12.891  -7.423   1.00 69.81  ? 327  LEU   B CB  1 
ATOM   3588  C  CG  . LEU   B  1 26  ? -52.325 12.834  -5.943   1.00 73.00  ? 327  LEU   B CG  1 
ATOM   3589  C  CD1 . LEU   B  1 26  ? -52.006 11.460  -5.316   1.00 71.10  ? 327  LEU   B CD1 1 
ATOM   3590  C  CD2 . LEU   B  1 26  ? -51.641 13.968  -5.197   1.00 69.25  ? 327  LEU   B CD2 1 
ATOM   3591  N  N   . GLU   B  1 27  ? -52.547 13.781  -10.380  1.00 59.40  ? 328  GLU   B N   1 
ATOM   3592  C  CA  . GLU   B  1 27  ? -52.045 14.014  -11.727  1.00 61.37  ? 328  GLU   B CA  1 
ATOM   3593  C  C   . GLU   B  1 27  ? -50.531 13.808  -11.784  1.00 60.83  ? 328  GLU   B C   1 
ATOM   3594  O  O   . GLU   B  1 27  ? -49.817 13.990  -10.794  1.00 51.17  ? 328  GLU   B O   1 
ATOM   3595  C  CB  . GLU   B  1 27  ? -52.419 15.429  -12.200  1.00 56.07  ? 328  GLU   B CB  1 
ATOM   3596  C  CG  . GLU   B  1 27  ? -53.908 15.595  -12.530  1.00 52.92  ? 328  GLU   B CG  1 
ATOM   3597  C  CD  . GLU   B  1 27  ? -54.353 17.045  -12.684  1.00 61.32  ? 328  GLU   B CD  1 
ATOM   3598  O  OE1 . GLU   B  1 27  ? -55.583 17.287  -12.764  1.00 67.78  ? 328  GLU   B OE1 1 
ATOM   3599  O  OE2 . GLU   B  1 27  ? -53.480 17.938  -12.725  1.00 58.95  ? 328  GLU   B OE2 1 
ATOM   3600  N  N   . THR   B  1 28  ? -50.044 13.398  -12.962  1.00 55.92  ? 329  THR   B N   1 
ATOM   3601  C  CA  . THR   B  1 28  ? -48.610 13.264  -13.188  1.00 45.35  ? 329  THR   B CA  1 
ATOM   3602  C  C   . THR   B  1 28  ? -47.997 14.510  -13.782  1.00 45.80  ? 329  THR   B C   1 
ATOM   3603  O  O   . THR   B  1 28  ? -46.775 14.662  -13.735  1.00 54.50  ? 329  THR   B O   1 
ATOM   3604  C  CB  . THR   B  1 28  ? -48.317 12.114  -14.147  1.00 49.12  ? 329  THR   B CB  1 
ATOM   3605  O  OG1 . THR   B  1 28  ? -49.100 12.291  -15.358  1.00 48.06  ? 329  THR   B OG1 1 
ATOM   3606  C  CG2 . THR   B  1 28  ? -48.618 10.791  -13.482  1.00 30.95  ? 329  THR   B CG2 1 
ATOM   3607  N  N   . GLY   B  1 29  ? -48.822 15.383  -14.351  1.00 49.65  ? 330  GLY   B N   1 
ATOM   3608  C  CA  . GLY   B  1 29  ? -48.381 16.507  -15.143  1.00 51.86  ? 330  GLY   B CA  1 
ATOM   3609  C  C   . GLY   B  1 29  ? -48.662 16.338  -16.619  1.00 57.92  ? 330  GLY   B C   1 
ATOM   3610  O  O   . GLY   B  1 29  ? -48.740 17.339  -17.348  1.00 52.51  ? 330  GLY   B O   1 
ATOM   3611  N  N   . CYS   B  1 30  ? -48.836 15.101  -17.070  1.00 54.07  ? 331  CYS   B N   1 
ATOM   3612  C  CA  . CYS   B  1 30  ? -48.999 14.809  -18.481  1.00 42.68  ? 331  CYS   B CA  1 
ATOM   3613  C  C   . CYS   B  1 30  ? -50.449 14.993  -18.915  1.00 54.33  ? 331  CYS   B C   1 
ATOM   3614  O  O   . CYS   B  1 30  ? -51.382 14.907  -18.114  1.00 59.66  ? 331  CYS   B O   1 
ATOM   3615  C  CB  . CYS   B  1 30  ? -48.559 13.374  -18.776  1.00 34.93  ? 331  CYS   B CB  1 
ATOM   3616  S  SG  . CYS   B  1 30  ? -46.828 13.023  -18.474  1.00 49.86  ? 331  CYS   B SG  1 
ATOM   3617  N  N   . THR   B  1 31  ? -50.633 15.272  -20.199  1.00 41.67  ? 332  THR   B N   1 
ATOM   3618  C  CA  . THR   B  1 31  ? -51.937 15.163  -20.823  1.00 51.52  ? 332  THR   B CA  1 
ATOM   3619  C  C   . THR   B  1 31  ? -51.800 14.299  -22.070  1.00 56.86  ? 332  THR   B C   1 
ATOM   3620  O  O   . THR   B  1 31  ? -50.699 13.896  -22.457  1.00 64.75  ? 332  THR   B O   1 
ATOM   3621  C  CB  . THR   B  1 31  ? -52.523 16.541  -21.157  1.00 55.14  ? 332  THR   B CB  1 
ATOM   3622  O  OG1 . THR   B  1 31  ? -51.829 17.125  -22.274  1.00 52.17  ? 332  THR   B OG1 1 
ATOM   3623  C  CG2 . THR   B  1 31  ? -52.441 17.453  -19.953  1.00 44.16  ? 332  THR   B CG2 1 
ATOM   3624  N  N   . GLU   B  1 32  ? -52.936 14.008  -22.706  1.00 59.78  ? 333  GLU   B N   1 
ATOM   3625  C  CA  . GLU   B  1 32  ? -52.894 13.352  -24.004  1.00 58.37  ? 333  GLU   B CA  1 
ATOM   3626  C  C   . GLU   B  1 32  ? -52.009 14.106  -24.985  1.00 52.17  ? 333  GLU   B C   1 
ATOM   3627  O  O   . GLU   B  1 32  ? -51.507 13.497  -25.934  1.00 57.04  ? 333  GLU   B O   1 
ATOM   3628  C  CB  . GLU   B  1 32  ? -54.308 13.200  -24.575  1.00 74.32  ? 333  GLU   B CB  1 
ATOM   3629  C  CG  . GLU   B  1 32  ? -55.087 12.009  -24.034  1.00 83.09  ? 333  GLU   B CG  1 
ATOM   3630  C  CD  . GLU   B  1 32  ? -55.811 12.302  -22.730  1.00 97.24  ? 333  GLU   B CD  1 
ATOM   3631  O  OE1 . GLU   B  1 32  ? -55.450 13.276  -22.022  1.00 92.35  ? 333  GLU   B OE1 1 
ATOM   3632  O  OE2 . GLU   B  1 32  ? -56.755 11.545  -22.415  1.00 108.17 ? 333  GLU   B OE2 1 
ATOM   3633  N  N   . TYR   B  1 33  ? -51.761 15.401  -24.745  1.00 47.97  ? 334  TYR   B N   1 
ATOM   3634  C  CA  . TYR   B  1 33  ? -51.063 16.265  -25.686  1.00 52.82  ? 334  TYR   B CA  1 
ATOM   3635  C  C   . TYR   B  1 33  ? -49.660 16.708  -25.274  1.00 49.82  ? 334  TYR   B C   1 
ATOM   3636  O  O   . TYR   B  1 33  ? -48.914 17.195  -26.128  1.00 51.83  ? 334  TYR   B O   1 
ATOM   3637  C  CB  . TYR   B  1 33  ? -51.918 17.506  -25.959  1.00 68.82  ? 334  TYR   B CB  1 
ATOM   3638  C  CG  . TYR   B  1 33  ? -53.205 17.132  -26.626  1.00 74.22  ? 334  TYR   B CG  1 
ATOM   3639  C  CD1 . TYR   B  1 33  ? -53.220 16.770  -27.962  1.00 79.35  ? 334  TYR   B CD1 1 
ATOM   3640  C  CD2 . TYR   B  1 33  ? -54.396 17.086  -25.917  1.00 75.43  ? 334  TYR   B CD2 1 
ATOM   3641  C  CE1 . TYR   B  1 33  ? -54.384 16.404  -28.585  1.00 84.27  ? 334  TYR   B CE1 1 
ATOM   3642  C  CE2 . TYR   B  1 33  ? -55.571 16.724  -26.531  1.00 79.53  ? 334  TYR   B CE2 1 
ATOM   3643  C  CZ  . TYR   B  1 33  ? -55.553 16.388  -27.870  1.00 81.79  ? 334  TYR   B CZ  1 
ATOM   3644  O  OH  . TYR   B  1 33  ? -56.701 16.024  -28.510  1.00 84.64  ? 334  TYR   B OH  1 
ATOM   3645  N  N   . ILE   B  1 34  ? -49.280 16.600  -24.005  1.00 59.50  ? 335  ILE   B N   1 
ATOM   3646  C  CA  . ILE   B  1 34  ? -47.934 16.978  -23.591  1.00 54.15  ? 335  ILE   B CA  1 
ATOM   3647  C  C   . ILE   B  1 34  ? -47.489 15.985  -22.534  1.00 54.05  ? 335  ILE   B C   1 
ATOM   3648  O  O   . ILE   B  1 34  ? -48.239 15.703  -21.597  1.00 61.64  ? 335  ILE   B O   1 
ATOM   3649  C  CB  . ILE   B  1 34  ? -47.844 18.421  -23.052  1.00 49.59  ? 335  ILE   B CB  1 
ATOM   3650  C  CG1 . ILE   B  1 34  ? -48.647 19.401  -23.915  1.00 73.61  ? 335  ILE   B CG1 1 
ATOM   3651  C  CG2 . ILE   B  1 34  ? -46.419 18.898  -23.117  1.00 41.09  ? 335  ILE   B CG2 1 
ATOM   3652  C  CD1 . ILE   B  1 34  ? -49.814 20.060  -23.215  1.00 84.07  ? 335  ILE   B CD1 1 
ATOM   3653  N  N   . CYS   B  1 35  ? -46.285 15.439  -22.693  1.00 53.05  ? 336  CYS   B N   1 
ATOM   3654  C  CA  . CYS   B  1 35  ? -45.697 14.521  -21.722  1.00 47.01  ? 336  CYS   B CA  1 
ATOM   3655  C  C   . CYS   B  1 35  ? -44.585 15.211  -20.950  1.00 51.09  ? 336  CYS   B C   1 
ATOM   3656  O  O   . CYS   B  1 35  ? -43.671 15.788  -21.554  1.00 44.94  ? 336  CYS   B O   1 
ATOM   3657  C  CB  . CYS   B  1 35  ? -45.126 13.276  -22.388  1.00 34.14  ? 336  CYS   B CB  1 
ATOM   3658  S  SG  . CYS   B  1 35  ? -44.027 12.407  -21.249  1.00 47.57  ? 336  CYS   B SG  1 
ATOM   3659  N  N   . MET   B  1 36  ? -44.636 15.102  -19.617  1.00 46.16  ? 337  MET   B N   1 
ATOM   3660  C  CA  . MET   B  1 36  ? -43.712 15.809  -18.737  1.00 36.30  ? 337  MET   B CA  1 
ATOM   3661  C  C   . MET   B  1 36  ? -42.797 14.869  -17.958  1.00 38.54  ? 337  MET   B C   1 
ATOM   3662  O  O   . MET   B  1 36  ? -42.215 15.275  -16.944  1.00 36.25  ? 337  MET   B O   1 
ATOM   3663  C  CB  . MET   B  1 36  ? -44.494 16.702  -17.772  1.00 38.44  ? 337  MET   B CB  1 
ATOM   3664  C  CG  . MET   B  1 36  ? -45.366 17.731  -18.443  1.00 52.46  ? 337  MET   B CG  1 
ATOM   3665  S  SD  . MET   B  1 36  ? -45.763 19.020  -17.265  1.00 59.79  ? 337  MET   B SD  1 
ATOM   3666  C  CE  . MET   B  1 36  ? -46.575 20.198  -18.330  1.00 63.20  ? 337  MET   B CE  1 
ATOM   3667  N  N   . GLY   B  1 37  ? -42.636 13.628  -18.414  1.00 46.20  ? 338  GLY   B N   1 
ATOM   3668  C  CA  . GLY   B  1 37  ? -41.878 12.646  -17.651  1.00 47.69  ? 338  GLY   B CA  1 
ATOM   3669  C  C   . GLY   B  1 37  ? -40.406 12.957  -17.420  1.00 44.39  ? 338  GLY   B C   1 
ATOM   3670  O  O   . GLY   B  1 37  ? -39.708 12.132  -16.819  1.00 45.99  ? 338  GLY   B O   1 
ATOM   3671  N  N   . SER   B  1 38  ? -39.916 14.096  -17.899  1.00 46.25  ? 339  SER   B N   1 
ATOM   3672  C  CA  . SER   B  1 38  ? -38.558 14.561  -17.662  1.00 43.96  ? 339  SER   B CA  1 
ATOM   3673  C  C   . SER   B  1 38  ? -38.525 15.890  -16.924  1.00 45.27  ? 339  SER   B C   1 
ATOM   3674  O  O   . SER   B  1 38  ? -37.446 16.487  -16.785  1.00 41.89  ? 339  SER   B O   1 
ATOM   3675  C  CB  . SER   B  1 38  ? -37.808 14.722  -18.989  1.00 51.39  ? 339  SER   B CB  1 
ATOM   3676  O  OG  . SER   B  1 38  ? -38.320 15.827  -19.719  1.00 54.11  ? 339  SER   B OG  1 
ATOM   3677  N  N   . ILE   B  1 39  ? -39.681 16.396  -16.513  1.00 44.42  ? 340  ILE   B N   1 
ATOM   3678  C  CA  . ILE   B  1 39  ? -39.775 17.557  -15.639  1.00 46.98  ? 340  ILE   B CA  1 
ATOM   3679  C  C   . ILE   B  1 39  ? -39.580 17.108  -14.192  1.00 52.90  ? 340  ILE   B C   1 
ATOM   3680  O  O   . ILE   B  1 39  ? -40.125 16.076  -13.768  1.00 56.12  ? 340  ILE   B O   1 
ATOM   3681  C  CB  . ILE   B  1 39  ? -41.130 18.244  -15.842  1.00 46.17  ? 340  ILE   B CB  1 
ATOM   3682  C  CG1 . ILE   B  1 39  ? -41.267 18.719  -17.283  1.00 52.35  ? 340  ILE   B CG1 1 
ATOM   3683  C  CG2 . ILE   B  1 39  ? -41.275 19.404  -14.876  1.00 56.30  ? 340  ILE   B CG2 1 
ATOM   3684  C  CD1 . ILE   B  1 39  ? -40.416 19.937  -17.580  1.00 60.76  ? 340  ILE   B CD1 1 
ATOM   3685  N  N   . MET   B  1 40  ? -38.790 17.874  -13.430  1.00 46.73  ? 341  MET   B N   1 
ATOM   3686  C  CA  . MET   B  1 40  ? -38.399 17.440  -12.091  1.00 50.83  ? 341  MET   B CA  1 
ATOM   3687  C  C   . MET   B  1 40  ? -39.592 17.439  -11.134  1.00 56.76  ? 341  MET   B C   1 
ATOM   3688  O  O   . MET   B  1 40  ? -39.794 16.475  -10.384  1.00 50.54  ? 341  MET   B O   1 
ATOM   3689  C  CB  . MET   B  1 40  ? -37.270 18.329  -11.568  1.00 53.92  ? 341  MET   B CB  1 
ATOM   3690  C  CG  . MET   B  1 40  ? -36.963 18.136  -10.079  1.00 68.40  ? 341  MET   B CG  1 
ATOM   3691  S  SD  . MET   B  1 40  ? -35.930 16.715  -9.648   1.00 74.62  ? 341  MET   B SD  1 
ATOM   3692  C  CE  . MET   B  1 40  ? -34.379 17.148  -10.456  1.00 75.08  ? 341  MET   B CE  1 
ATOM   3693  N  N   . HIS   B  1 41  ? -40.396 18.513  -11.151  1.00 60.72  ? 342  HIS   B N   1 
ATOM   3694  C  CA  . HIS   B  1 41  ? -41.646 18.611  -10.387  1.00 55.70  ? 342  HIS   B CA  1 
ATOM   3695  C  C   . HIS   B  1 41  ? -42.769 18.991  -11.338  1.00 54.21  ? 342  HIS   B C   1 
ATOM   3696  O  O   . HIS   B  1 41  ? -43.149 20.165  -11.434  1.00 53.72  ? 342  HIS   B O   1 
ATOM   3697  C  CB  . HIS   B  1 41  ? -41.538 19.639  -9.260   1.00 58.07  ? 342  HIS   B CB  1 
ATOM   3698  C  CG  . HIS   B  1 41  ? -40.220 19.612  -8.561   1.00 62.66  ? 342  HIS   B CG  1 
ATOM   3699  N  ND1 . HIS   B  1 41  ? -39.856 18.595  -7.704   1.00 60.40  ? 342  HIS   B ND1 1 
ATOM   3700  C  CD2 . HIS   B  1 41  ? -39.166 20.461  -8.611   1.00 64.51  ? 342  HIS   B CD2 1 
ATOM   3701  C  CE1 . HIS   B  1 41  ? -38.636 18.824  -7.249   1.00 63.32  ? 342  HIS   B CE1 1 
ATOM   3702  N  NE2 . HIS   B  1 41  ? -38.195 19.949  -7.784   1.00 65.55  ? 342  HIS   B NE2 1 
ATOM   3703  N  N   . PRO   B  1 42  ? -43.329 18.024  -12.067  1.00 58.13  ? 343  PRO   B N   1 
ATOM   3704  C  CA  . PRO   B  1 42  ? -44.319 18.404  -13.091  1.00 55.56  ? 343  PRO   B CA  1 
ATOM   3705  C  C   . PRO   B  1 42  ? -45.642 18.847  -12.494  1.00 65.79  ? 343  PRO   B C   1 
ATOM   3706  O  O   . PRO   B  1 42  ? -46.223 19.839  -12.955  1.00 66.23  ? 343  PRO   B O   1 
ATOM   3707  C  CB  . PRO   B  1 42  ? -44.449 17.139  -13.953  1.00 53.98  ? 343  PRO   B CB  1 
ATOM   3708  C  CG  . PRO   B  1 42  ? -43.917 16.016  -13.124  1.00 56.78  ? 343  PRO   B CG  1 
ATOM   3709  C  CD  . PRO   B  1 42  ? -43.026 16.583  -12.049  1.00 59.03  ? 343  PRO   B CD  1 
ATOM   3710  N  N   . SER   B  1 43  ? -46.107 18.185  -11.437  1.00 76.49  ? 344  SER   B N   1 
ATOM   3711  C  CA  . SER   B  1 43  ? -47.425 18.439  -10.871  1.00 69.45  ? 344  SER   B CA  1 
ATOM   3712  C  C   . SER   B  1 43  ? -47.336 19.174  -9.537   1.00 63.88  ? 344  SER   B C   1 
ATOM   3713  O  O   . SER   B  1 43  ? -46.396 18.995  -8.759   1.00 62.54  ? 344  SER   B O   1 
ATOM   3714  C  CB  . SER   B  1 43  ? -48.193 17.124  -10.682  1.00 67.61  ? 344  SER   B CB  1 
ATOM   3715  O  OG  . SER   B  1 43  ? -49.578 17.348  -10.469  1.00 74.01  ? 344  SER   B OG  1 
ATOM   3716  N  N   . GLN   B  1 44  ? -48.337 20.010  -9.284   1.00 66.99  ? 345  GLN   B N   1 
ATOM   3717  C  CA  . GLN   B  1 44  ? -48.572 20.563  -7.959   1.00 73.89  ? 345  GLN   B CA  1 
ATOM   3718  C  C   . GLN   B  1 44  ? -49.874 20.054  -7.352   1.00 82.22  ? 345  GLN   B C   1 
ATOM   3719  O  O   . GLN   B  1 44  ? -50.330 20.594  -6.338   1.00 78.61  ? 345  GLN   B O   1 
ATOM   3720  C  CB  . GLN   B  1 44  ? -48.575 22.088  -8.009   1.00 71.47  ? 345  GLN   B CB  1 
ATOM   3721  C  CG  . GLN   B  1 44  ? -47.273 22.682  -8.481   1.00 72.97  ? 345  GLN   B CG  1 
ATOM   3722  C  CD  . GLN   B  1 44  ? -47.403 24.168  -8.731   1.00 84.07  ? 345  GLN   B CD  1 
ATOM   3723  O  OE1 . GLN   B  1 44  ? -47.625 24.604  -9.865   1.00 93.57  ? 345  GLN   B OE1 1 
ATOM   3724  N  NE2 . GLN   B  1 44  ? -47.286 24.958  -7.669   1.00 80.55  ? 345  GLN   B NE2 1 
ATOM   3725  N  N   . HIS   B  1 45  ? -50.475 19.023  -7.950   1.00 88.31  ? 346  HIS   B N   1 
ATOM   3726  C  CA  . HIS   B  1 45  ? -51.685 18.409  -7.414   1.00 87.93  ? 346  HIS   B CA  1 
ATOM   3727  C  C   . HIS   B  1 45  ? -51.405 17.833  -6.035   1.00 88.81  ? 346  HIS   B C   1 
ATOM   3728  O  O   . HIS   B  1 45  ? -50.559 16.943  -5.891   1.00 89.23  ? 346  HIS   B O   1 
ATOM   3729  C  CB  . HIS   B  1 45  ? -52.177 17.307  -8.357   1.00 82.13  ? 346  HIS   B CB  1 
ATOM   3730  C  CG  . HIS   B  1 45  ? -53.630 16.965  -8.199   1.00 81.52  ? 346  HIS   B CG  1 
ATOM   3731  N  ND1 . HIS   B  1 45  ? -54.137 15.719  -8.504   1.00 82.84  ? 346  HIS   B ND1 1 
ATOM   3732  C  CD2 . HIS   B  1 45  ? -54.687 17.710  -7.793   1.00 81.58  ? 346  HIS   B CD2 1 
ATOM   3733  C  CE1 . HIS   B  1 45  ? -55.441 15.709  -8.288   1.00 83.52  ? 346  HIS   B CE1 1 
ATOM   3734  N  NE2 . HIS   B  1 45  ? -55.799 16.904  -7.855   1.00 83.00  ? 346  HIS   B NE2 1 
ATOM   3735  N  N   . ALA   B  1 46  ? -52.117 18.346  -5.027   1.00 87.64  ? 347  ALA   B N   1 
ATOM   3736  C  CA  . ALA   B  1 46  ? -51.972 17.925  -3.639   1.00 77.51  ? 347  ALA   B CA  1 
ATOM   3737  C  C   . ALA   B  1 46  ? -53.313 17.432  -3.105   1.00 75.40  ? 347  ALA   B C   1 
ATOM   3738  O  O   . ALA   B  1 46  ? -54.369 17.960  -3.463   1.00 66.95  ? 347  ALA   B O   1 
ATOM   3739  C  CB  . ALA   B  1 46  ? -51.435 19.070  -2.769   1.00 67.51  ? 347  ALA   B CB  1 
ATOM   3740  N  N   . ARG   B  1 47  ? -53.265 16.419  -2.236   1.00 86.77  ? 348  ARG   B N   1 
ATOM   3741  C  CA  . ARG   B  1 47  ? -54.480 15.747  -1.788   1.00 94.36  ? 348  ARG   B CA  1 
ATOM   3742  C  C   . ARG   B  1 47  ? -55.281 16.546  -0.757   1.00 104.29 ? 348  ARG   B C   1 
ATOM   3743  O  O   . ARG   B  1 47  ? -56.407 16.148  -0.440   1.00 109.21 ? 348  ARG   B O   1 
ATOM   3744  C  CB  . ARG   B  1 47  ? -54.122 14.357  -1.240   1.00 91.98  ? 348  ARG   B CB  1 
ATOM   3745  C  CG  . ARG   B  1 47  ? -54.095 13.250  -2.309   1.00 90.28  ? 348  ARG   B CG  1 
ATOM   3746  C  CD  . ARG   B  1 47  ? -53.380 11.969  -1.851   1.00 95.07  ? 348  ARG   B CD  1 
ATOM   3747  N  NE  . ARG   B  1 47  ? -53.999 11.350  -0.679   1.00 103.78 ? 348  ARG   B NE  1 
ATOM   3748  C  CZ  . ARG   B  1 47  ? -55.032 10.510  -0.722   1.00 103.80 ? 348  ARG   B CZ  1 
ATOM   3749  N  NH1 . ARG   B  1 47  ? -55.577 10.181  -1.891   1.00 99.36  ? 348  ARG   B NH1 1 
ATOM   3750  N  NH2 . ARG   B  1 47  ? -55.520 10.002  0.409    1.00 101.47 ? 348  ARG   B NH2 1 
ATOM   3751  N  N   . ARG   B  1 48  ? -54.753 17.673  -0.250   1.00 104.09 ? 349  ARG   B N   1 
ATOM   3752  C  CA  . ARG   B  1 48  ? -55.436 18.528  0.720    1.00 97.10  ? 349  ARG   B CA  1 
ATOM   3753  C  C   . ARG   B  1 48  ? -55.148 19.999  0.408    1.00 100.69 ? 349  ARG   B C   1 
ATOM   3754  O  O   . ARG   B  1 48  ? -54.256 20.281  -0.397   1.00 101.93 ? 349  ARG   B O   1 
ATOM   3755  C  CB  . ARG   B  1 48  ? -54.987 18.144  2.132    1.00 91.67  ? 349  ARG   B CB  1 
ATOM   3756  C  CG  . ARG   B  1 48  ? -53.537 17.698  2.213    1.00 84.73  ? 349  ARG   B CG  1 
ATOM   3757  C  CD  . ARG   B  1 48  ? -53.002 17.841  3.608    1.00 83.13  ? 349  ARG   B CD  1 
ATOM   3758  N  NE  . ARG   B  1 48  ? -53.399 19.123  4.171    1.00 85.86  ? 349  ARG   B NE  1 
ATOM   3759  C  CZ  . ARG   B  1 48  ? -54.343 19.261  5.093    1.00 99.80  ? 349  ARG   B CZ  1 
ATOM   3760  N  NH1 . ARG   B  1 48  ? -54.967 18.184  5.551    1.00 104.67 ? 349  ARG   B NH1 1 
ATOM   3761  N  NH2 . ARG   B  1 48  ? -54.660 20.466  5.555    1.00 104.58 ? 349  ARG   B NH2 1 
ATOM   3762  N  N   . PRO   B  1 49  ? -55.861 20.976  1.003    1.00 114.54 ? 350  PRO   B N   1 
ATOM   3763  C  CA  . PRO   B  1 49  ? -55.601 22.379  0.641    1.00 121.80 ? 350  PRO   B CA  1 
ATOM   3764  C  C   . PRO   B  1 49  ? -54.294 22.913  1.216    1.00 128.95 ? 350  PRO   B C   1 
ATOM   3765  O  O   . PRO   B  1 49  ? -53.336 22.156  1.401    1.00 124.73 ? 350  PRO   B O   1 
ATOM   3766  C  CB  . PRO   B  1 49  ? -56.815 23.113  1.221    1.00 124.53 ? 350  PRO   B CB  1 
ATOM   3767  C  CG  . PRO   B  1 49  ? -57.130 22.328  2.443    1.00 128.57 ? 350  PRO   B CG  1 
ATOM   3768  C  CD  . PRO   B  1 49  ? -56.911 20.880  2.034    1.00 125.34 ? 350  PRO   B CD  1 
ATOM   3769  N  N   . GLU   B  1 50  ? -54.243 24.215  1.509    1.00 136.47 ? 351  GLU   B N   1 
ATOM   3770  C  CA  . GLU   B  1 50  ? -52.992 24.846  1.923    1.00 133.27 ? 351  GLU   B CA  1 
ATOM   3771  C  C   . GLU   B  1 50  ? -52.694 24.579  3.390    1.00 118.85 ? 351  GLU   B C   1 
ATOM   3772  O  O   . GLU   B  1 50  ? -51.635 24.035  3.730    1.00 109.53 ? 351  GLU   B O   1 
ATOM   3773  C  CB  . GLU   B  1 50  ? -53.048 26.357  1.660    1.00 137.76 ? 351  GLU   B CB  1 
ATOM   3774  C  CG  . GLU   B  1 50  ? -52.730 26.779  0.217    1.00 133.81 ? 351  GLU   B CG  1 
ATOM   3775  C  CD  . GLU   B  1 50  ? -51.499 27.686  0.098    1.00 126.36 ? 351  GLU   B CD  1 
ATOM   3776  O  OE1 . GLU   B  1 50  ? -50.548 27.507  0.895    1.00 124.21 ? 351  GLU   B OE1 1 
ATOM   3777  O  OE2 . GLU   B  1 50  ? -51.492 28.580  -0.788   1.00 120.28 ? 351  GLU   B OE2 1 
ATOM   3778  N  N   . ASP   B  1 51  ? -53.620 24.959  4.272    1.00 115.57 ? 352  ASP   B N   1 
ATOM   3779  C  CA  . ASP   B  1 51  ? -53.413 24.934  5.716    1.00 112.39 ? 352  ASP   B CA  1 
ATOM   3780  C  C   . ASP   B  1 51  ? -54.344 23.911  6.372    1.00 110.32 ? 352  ASP   B C   1 
ATOM   3781  O  O   . ASP   B  1 51  ? -54.694 22.894  5.749    1.00 104.68 ? 352  ASP   B O   1 
ATOM   3782  C  CB  . ASP   B  1 51  ? -53.593 26.355  6.270    1.00 106.24 ? 352  ASP   B CB  1 
ATOM   3783  C  CG  . ASP   B  1 51  ? -52.317 27.191  6.174    1.00 99.32  ? 352  ASP   B CG  1 
ATOM   3784  O  OD1 . ASP   B  1 51  ? -51.317 26.803  6.814    1.00 93.21  ? 352  ASP   B OD1 1 
ATOM   3785  O  OD2 . ASP   B  1 51  ? -52.292 28.198  5.434    1.00 96.13  ? 352  ASP   B OD2 1 
ATOM   3786  N  N   . VAL   B  1 52  ? -54.740 24.178  7.617    1.00 112.98 ? 353  VAL   B N   1 
ATOM   3787  C  CA  . VAL   B  1 52  ? -55.545 23.224  8.369    1.00 112.22 ? 353  VAL   B CA  1 
ATOM   3788  C  C   . VAL   B  1 52  ? -56.881 23.016  7.658    1.00 118.67 ? 353  VAL   B C   1 
ATOM   3789  O  O   . VAL   B  1 52  ? -57.686 23.947  7.507    1.00 119.69 ? 353  VAL   B O   1 
ATOM   3790  C  CB  . VAL   B  1 52  ? -55.710 23.681  9.835    1.00 97.42  ? 353  VAL   B CB  1 
ATOM   3791  C  CG1 . VAL   B  1 52  ? -56.202 25.114  9.906    1.00 102.11 ? 353  VAL   B CG1 1 
ATOM   3792  C  CG2 . VAL   B  1 52  ? -56.636 22.724  10.619   1.00 84.82  ? 353  VAL   B CG2 1 
ATOM   3793  N  N   . ALA   B  1 53  ? -57.124 21.779  7.229    1.00 110.58 ? 354  ALA   B N   1 
ATOM   3794  C  CA  . ALA   B  1 53  ? -58.251 21.456  6.369    1.00 94.96  ? 354  ALA   B CA  1 
ATOM   3795  C  C   . ALA   B  1 53  ? -59.548 21.333  7.166    1.00 87.97  ? 354  ALA   B C   1 
ATOM   3796  O  O   . ALA   B  1 53  ? -59.548 20.981  8.350    1.00 89.81  ? 354  ALA   B O   1 
ATOM   3797  C  CB  . ALA   B  1 53  ? -57.980 20.155  5.612    1.00 90.78  ? 354  ALA   B CB  1 
ATOM   3798  N  N   . THR   B  1 54  ? -60.662 21.635  6.502    1.00 80.98  ? 355  THR   B N   1 
ATOM   3799  C  CA  . THR   B  1 54  ? -61.974 21.347  7.063    1.00 76.75  ? 355  THR   B CA  1 
ATOM   3800  C  C   . THR   B  1 54  ? -62.149 19.833  7.235    1.00 72.79  ? 355  THR   B C   1 
ATOM   3801  O  O   . THR   B  1 54  ? -61.303 19.027  6.833    1.00 75.33  ? 355  THR   B O   1 
ATOM   3802  C  CB  . THR   B  1 54  ? -63.076 21.937  6.172    1.00 77.90  ? 355  THR   B CB  1 
ATOM   3803  O  OG1 . THR   B  1 54  ? -62.888 21.508  4.818    1.00 80.86  ? 355  THR   B OG1 1 
ATOM   3804  C  CG2 . THR   B  1 54  ? -63.031 23.452  6.198    1.00 72.59  ? 355  THR   B CG2 1 
ATOM   3805  N  N   . LYS   B  1 55  ? -63.261 19.442  7.854    1.00 74.38  ? 356  LYS   B N   1 
ATOM   3806  C  CA  . LYS   B  1 55  ? -63.520 18.019  8.032    1.00 70.43  ? 356  LYS   B CA  1 
ATOM   3807  C  C   . LYS   B  1 55  ? -63.809 17.334  6.702    1.00 64.32  ? 356  LYS   B C   1 
ATOM   3808  O  O   . LYS   B  1 55  ? -63.355 16.209  6.468    1.00 65.24  ? 356  LYS   B O   1 
ATOM   3809  C  CB  . LYS   B  1 55  ? -64.679 17.808  8.999    1.00 68.77  ? 356  LYS   B CB  1 
ATOM   3810  C  CG  . LYS   B  1 55  ? -64.936 16.352  9.296    1.00 65.73  ? 356  LYS   B CG  1 
ATOM   3811  C  CD  . LYS   B  1 55  ? -65.944 16.194  10.411   1.00 71.06  ? 356  LYS   B CD  1 
ATOM   3812  C  CE  . LYS   B  1 55  ? -66.065 14.737  10.802   1.00 65.89  ? 356  LYS   B CE  1 
ATOM   3813  N  NZ  . LYS   B  1 55  ? -67.291 14.548  11.606   1.00 74.84  ? 356  LYS   B NZ  1 
ATOM   3814  N  N   . ASP   B  1 56  ? -64.565 17.985  5.818    1.00 73.12  ? 357  ASP   B N   1 
ATOM   3815  C  CA  . ASP   B  1 56  ? -64.863 17.360  4.533    1.00 72.40  ? 357  ASP   B CA  1 
ATOM   3816  C  C   . ASP   B  1 56  ? -63.630 17.243  3.653    1.00 65.90  ? 357  ASP   B C   1 
ATOM   3817  O  O   . ASP   B  1 56  ? -63.630 16.420  2.736    1.00 73.69  ? 357  ASP   B O   1 
ATOM   3818  C  CB  . ASP   B  1 56  ? -65.982 18.114  3.799    1.00 73.18  ? 357  ASP   B CB  1 
ATOM   3819  C  CG  . ASP   B  1 56  ? -65.623 19.556  3.453    1.00 80.42  ? 357  ASP   B CG  1 
ATOM   3820  O  OD1 . ASP   B  1 56  ? -66.540 20.293  3.035    1.00 83.20  ? 357  ASP   B OD1 1 
ATOM   3821  O  OD2 . ASP   B  1 56  ? -64.450 19.963  3.565    1.00 81.11  ? 357  ASP   B OD2 1 
ATOM   3822  N  N   . GLN   B  1 57  ? -62.582 18.031  3.922    1.00 59.32  ? 358  GLN   B N   1 
ATOM   3823  C  CA  . GLN   B  1 57  ? -61.303 17.855  3.237    1.00 62.92  ? 358  GLN   B CA  1 
ATOM   3824  C  C   . GLN   B  1 57  ? -60.555 16.637  3.769    1.00 68.23  ? 358  GLN   B C   1 
ATOM   3825  O  O   . GLN   B  1 57  ? -60.234 15.709  3.016    1.00 66.90  ? 358  GLN   B O   1 
ATOM   3826  C  CB  . GLN   B  1 57  ? -60.442 19.113  3.390    1.00 65.89  ? 358  GLN   B CB  1 
ATOM   3827  C  CG  . GLN   B  1 57  ? -60.503 20.075  2.206    1.00 75.28  ? 358  GLN   B CG  1 
ATOM   3828  C  CD  . GLN   B  1 57  ? -60.411 21.538  2.629    1.00 82.68  ? 358  GLN   B CD  1 
ATOM   3829  O  OE1 . GLN   B  1 57  ? -59.973 21.850  3.738    1.00 84.63  ? 358  GLN   B OE1 1 
ATOM   3830  N  NE2 . GLN   B  1 57  ? -60.832 22.440  1.747    1.00 79.84  ? 358  GLN   B NE2 1 
ATOM   3831  N  N   . LEU   B  1 58  ? -60.276 16.618  5.077    1.00 70.89  ? 359  LEU   B N   1 
ATOM   3832  C  CA  . LEU   B  1 58  ? -59.346 15.633  5.618    1.00 61.22  ? 359  LEU   B CA  1 
ATOM   3833  C  C   . LEU   B  1 58  ? -59.964 14.238  5.751    1.00 58.32  ? 359  LEU   B C   1 
ATOM   3834  O  O   . LEU   B  1 58  ? -59.285 13.239  5.477    1.00 48.80  ? 359  LEU   B O   1 
ATOM   3835  C  CB  . LEU   B  1 58  ? -58.807 16.114  6.963    1.00 57.75  ? 359  LEU   B CB  1 
ATOM   3836  C  CG  . LEU   B  1 58  ? -57.905 15.105  7.675    1.00 57.56  ? 359  LEU   B CG  1 
ATOM   3837  C  CD1 . LEU   B  1 58  ? -56.701 14.793  6.795    1.00 52.52  ? 359  LEU   B CD1 1 
ATOM   3838  C  CD2 . LEU   B  1 58  ? -57.484 15.563  9.104    1.00 53.77  ? 359  LEU   B CD2 1 
ATOM   3839  N  N   . PHE   B  1 59  ? -61.236 14.129  6.159    1.00 58.12  ? 360  PHE   B N   1 
ATOM   3840  C  CA  . PHE   B  1 59  ? -61.793 12.798  6.414    1.00 57.45  ? 360  PHE   B CA  1 
ATOM   3841  C  C   . PHE   B  1 59  ? -61.757 11.874  5.202    1.00 60.41  ? 360  PHE   B C   1 
ATOM   3842  O  O   . PHE   B  1 59  ? -61.390 10.696  5.370    1.00 52.57  ? 360  PHE   B O   1 
ATOM   3843  C  CB  . PHE   B  1 59  ? -63.224 12.881  6.951    1.00 56.96  ? 360  PHE   B CB  1 
ATOM   3844  C  CG  . PHE   B  1 59  ? -63.772 11.535  7.372    1.00 66.49  ? 360  PHE   B CG  1 
ATOM   3845  C  CD1 . PHE   B  1 59  ? -63.456 11.004  8.629    1.00 70.39  ? 360  PHE   B CD1 1 
ATOM   3846  C  CD2 . PHE   B  1 59  ? -64.566 10.784  6.511    1.00 60.60  ? 360  PHE   B CD2 1 
ATOM   3847  C  CE1 . PHE   B  1 59  ? -63.934 9.762   9.023    1.00 66.74  ? 360  PHE   B CE1 1 
ATOM   3848  C  CE2 . PHE   B  1 59  ? -65.053 9.542   6.892    1.00 64.54  ? 360  PHE   B CE2 1 
ATOM   3849  C  CZ  . PHE   B  1 59  ? -64.735 9.028   8.154    1.00 71.20  ? 360  PHE   B CZ  1 
ATOM   3850  N  N   . PRO   B  1 60  ? -62.146 12.303  3.986    1.00 60.53  ? 361  PRO   B N   1 
ATOM   3851  C  CA  . PRO   B  1 60  ? -62.168 11.347  2.865    1.00 48.47  ? 361  PRO   B CA  1 
ATOM   3852  C  C   . PRO   B  1 60  ? -60.807 10.769  2.561    1.00 48.25  ? 361  PRO   B C   1 
ATOM   3853  O  O   . PRO   B  1 60  ? -60.703 9.578   2.233    1.00 49.88  ? 361  PRO   B O   1 
ATOM   3854  C  CB  . PRO   B  1 60  ? -62.716 12.186  1.707    1.00 54.83  ? 361  PRO   B CB  1 
ATOM   3855  C  CG  . PRO   B  1 60  ? -63.511 13.263  2.366    1.00 59.65  ? 361  PRO   B CG  1 
ATOM   3856  C  CD  . PRO   B  1 60  ? -62.694 13.609  3.578    1.00 56.03  ? 361  PRO   B CD  1 
ATOM   3857  N  N   . LEU   B  1 61  ? -59.753 11.582  2.679    1.00 51.53  ? 362  LEU   B N   1 
ATOM   3858  C  CA  . LEU   B  1 61  ? -58.392 11.061  2.579    1.00 54.69  ? 362  LEU   B CA  1 
ATOM   3859  C  C   . LEU   B  1 61  ? -58.145 9.982   3.623    1.00 59.16  ? 362  LEU   B C   1 
ATOM   3860  O  O   . LEU   B  1 61  ? -57.565 8.929   3.321    1.00 49.49  ? 362  LEU   B O   1 
ATOM   3861  C  CB  . LEU   B  1 61  ? -57.383 12.192  2.758    1.00 47.98  ? 362  LEU   B CB  1 
ATOM   3862  C  CG  . LEU   B  1 61  ? -57.498 13.406  1.855    1.00 52.20  ? 362  LEU   B CG  1 
ATOM   3863  C  CD1 . LEU   B  1 61  ? -56.464 14.432  2.264    1.00 56.76  ? 362  LEU   B CD1 1 
ATOM   3864  C  CD2 . LEU   B  1 61  ? -57.295 12.966  0.423    1.00 56.99  ? 362  LEU   B CD2 1 
ATOM   3865  N  N   . ALA   B  1 62  ? -58.592 10.234  4.861    1.00 63.47  ? 363  ALA   B N   1 
ATOM   3866  C  CA  . ALA   B  1 62  ? -58.336 9.323   5.972    1.00 62.35  ? 363  ALA   B CA  1 
ATOM   3867  C  C   . ALA   B  1 62  ? -59.128 8.029   5.827    1.00 60.07  ? 363  ALA   B C   1 
ATOM   3868  O  O   . ALA   B  1 62  ? -58.602 6.941   6.094    1.00 54.69  ? 363  ALA   B O   1 
ATOM   3869  C  CB  . ALA   B  1 62  ? -58.682 10.011  7.285    1.00 61.12  ? 363  ALA   B CB  1 
ATOM   3870  N  N   . LYS   B  1 63  ? -60.394 8.128   5.408    1.00 60.62  ? 364  LYS   B N   1 
ATOM   3871  C  CA  . LYS   B  1 63  ? -61.170 6.921   5.155    1.00 62.75  ? 364  LYS   B CA  1 
ATOM   3872  C  C   . LYS   B  1 63  ? -60.502 6.060   4.094    1.00 59.74  ? 364  LYS   B C   1 
ATOM   3873  O  O   . LYS   B  1 63  ? -60.531 4.828   4.174    1.00 60.62  ? 364  LYS   B O   1 
ATOM   3874  C  CB  . LYS   B  1 63  ? -62.600 7.274   4.737    1.00 61.71  ? 364  LYS   B CB  1 
ATOM   3875  C  CG  . LYS   B  1 63  ? -63.514 6.045   4.652    1.00 70.68  ? 364  LYS   B CG  1 
ATOM   3876  C  CD  . LYS   B  1 63  ? -64.903 6.355   4.096    1.00 71.05  ? 364  LYS   B CD  1 
ATOM   3877  C  CE  . LYS   B  1 63  ? -65.745 5.090   3.984    1.00 73.85  ? 364  LYS   B CE  1 
ATOM   3878  N  NZ  . LYS   B  1 63  ? -65.114 4.053   3.116    1.00 69.84  ? 364  LYS   B NZ  1 
ATOM   3879  N  N   . GLU   B  1 64  ? -59.870 6.692   3.106    1.00 50.55  ? 365  GLU   B N   1 
ATOM   3880  C  CA  . GLU   B  1 64  ? -59.204 5.919   2.066    1.00 60.49  ? 365  GLU   B CA  1 
ATOM   3881  C  C   . GLU   B  1 64  ? -58.024 5.130   2.623    1.00 55.84  ? 365  GLU   B C   1 
ATOM   3882  O  O   . GLU   B  1 64  ? -57.857 3.946   2.301    1.00 56.13  ? 365  GLU   B O   1 
ATOM   3883  C  CB  . GLU   B  1 64  ? -58.765 6.843   0.931    1.00 70.21  ? 365  GLU   B CB  1 
ATOM   3884  C  CG  . GLU   B  1 64  ? -58.423 6.124   -0.356   1.00 83.02  ? 365  GLU   B CG  1 
ATOM   3885  C  CD  . GLU   B  1 64  ? -56.932 6.083   -0.623   1.00 93.32  ? 365  GLU   B CD  1 
ATOM   3886  O  OE1 . GLU   B  1 64  ? -56.304 5.033   -0.357   1.00 97.02  ? 365  GLU   B OE1 1 
ATOM   3887  O  OE2 . GLU   B  1 64  ? -56.390 7.104   -1.101   1.00 95.61  ? 365  GLU   B OE2 1 
ATOM   3888  N  N   . PHE   B  1 65  ? -57.195 5.757   3.464    1.00 59.11  ? 366  PHE   B N   1 
ATOM   3889  C  CA  . PHE   B  1 65  ? -56.014 5.064   3.973    1.00 55.21  ? 366  PHE   B CA  1 
ATOM   3890  C  C   . PHE   B  1 65  ? -56.395 3.944   4.930    1.00 62.43  ? 366  PHE   B C   1 
ATOM   3891  O  O   . PHE   B  1 65  ? -55.891 2.820   4.810    1.00 66.42  ? 366  PHE   B O   1 
ATOM   3892  C  CB  . PHE   B  1 65  ? -55.070 6.043   4.663    1.00 59.95  ? 366  PHE   B CB  1 
ATOM   3893  C  CG  . PHE   B  1 65  ? -53.928 5.373   5.379    1.00 58.32  ? 366  PHE   B CG  1 
ATOM   3894  C  CD1 . PHE   B  1 65  ? -52.957 4.679   4.662    1.00 54.91  ? 366  PHE   B CD1 1 
ATOM   3895  C  CD2 . PHE   B  1 65  ? -53.833 5.426   6.761    1.00 56.13  ? 366  PHE   B CD2 1 
ATOM   3896  C  CE1 . PHE   B  1 65  ? -51.909 4.055   5.306    1.00 48.58  ? 366  PHE   B CE1 1 
ATOM   3897  C  CE2 . PHE   B  1 65  ? -52.785 4.807   7.416    1.00 51.22  ? 366  PHE   B CE2 1 
ATOM   3898  C  CZ  . PHE   B  1 65  ? -51.825 4.119   6.688    1.00 48.81  ? 366  PHE   B CZ  1 
ATOM   3899  N  N   . ILE   B  1 66  ? -57.271 4.236   5.899    1.00 60.50  ? 367  ILE   B N   1 
ATOM   3900  C  CA  . ILE   B  1 66  ? -57.734 3.204   6.827    1.00 58.97  ? 367  ILE   B CA  1 
ATOM   3901  C  C   . ILE   B  1 66  ? -58.340 2.036   6.053    1.00 62.12  ? 367  ILE   B C   1 
ATOM   3902  O  O   . ILE   B  1 66  ? -57.993 0.869   6.281    1.00 60.47  ? 367  ILE   B O   1 
ATOM   3903  C  CB  . ILE   B  1 66  ? -58.737 3.800   7.835    1.00 58.20  ? 367  ILE   B CB  1 
ATOM   3904  C  CG1 . ILE   B  1 66  ? -58.163 5.053   8.503    1.00 50.39  ? 367  ILE   B CG1 1 
ATOM   3905  C  CG2 . ILE   B  1 66  ? -59.145 2.760   8.876    1.00 57.85  ? 367  ILE   B CG2 1 
ATOM   3906  C  CD1 . ILE   B  1 66  ? -57.023 4.775   9.429    1.00 45.99  ? 367  ILE   B CD1 1 
ATOM   3907  N  N   . ASP   B  1 67  ? -59.246 2.340   5.112    1.00 62.48  ? 368  ASP   B N   1 
ATOM   3908  C  CA  . ASP   B  1 67  ? -59.823 1.315   4.241    1.00 61.06  ? 368  ASP   B CA  1 
ATOM   3909  C  C   . ASP   B  1 67  ? -58.735 0.503   3.543    1.00 58.47  ? 368  ASP   B C   1 
ATOM   3910  O  O   . ASP   B  1 67  ? -58.775 -0.733  3.523    1.00 52.54  ? 368  ASP   B O   1 
ATOM   3911  C  CB  . ASP   B  1 67  ? -60.737 1.957   3.196    1.00 57.13  ? 368  ASP   B CB  1 
ATOM   3912  C  CG  . ASP   B  1 67  ? -62.058 2.414   3.764    1.00 62.88  ? 368  ASP   B CG  1 
ATOM   3913  O  OD1 . ASP   B  1 67  ? -62.291 2.208   4.968    1.00 69.58  ? 368  ASP   B OD1 1 
ATOM   3914  O  OD2 . ASP   B  1 67  ? -62.871 2.983   3.007    1.00 66.51  ? 368  ASP   B OD2 1 
ATOM   3915  N  N   . GLN   B  1 68  ? -57.762 1.193   2.947    1.00 53.08  ? 369  GLN   B N   1 
ATOM   3916  C  CA  . GLN   B  1 68  ? -56.644 0.507   2.316    1.00 53.19  ? 369  GLN   B CA  1 
ATOM   3917  C  C   . GLN   B  1 68  ? -55.907 -0.381  3.316    1.00 55.23  ? 369  GLN   B C   1 
ATOM   3918  O  O   . GLN   B  1 68  ? -55.653 -1.560  3.044    1.00 58.52  ? 369  GLN   B O   1 
ATOM   3919  C  CB  . GLN   B  1 68  ? -55.712 1.539   1.689    1.00 53.70  ? 369  GLN   B CB  1 
ATOM   3920  C  CG  . GLN   B  1 68  ? -54.474 0.973   1.017    1.00 52.53  ? 369  GLN   B CG  1 
ATOM   3921  C  CD  . GLN   B  1 68  ? -53.547 2.078   0.553    1.00 60.13  ? 369  GLN   B CD  1 
ATOM   3922  O  OE1 . GLN   B  1 68  ? -53.991 3.193   0.257    1.00 63.39  ? 369  GLN   B OE1 1 
ATOM   3923  N  NE2 . GLN   B  1 68  ? -52.252 1.784   0.502    1.00 63.50  ? 369  GLN   B NE2 1 
ATOM   3924  N  N   . TYR   B  1 69  ? -55.585 0.154   4.498    1.00 60.71  ? 370  TYR   B N   1 
ATOM   3925  C  CA  . TYR   B  1 69  ? -54.819 -0.634  5.468    1.00 56.15  ? 370  TYR   B CA  1 
ATOM   3926  C  C   . TYR   B  1 69  ? -55.609 -1.841  5.976    1.00 52.98  ? 370  TYR   B C   1 
ATOM   3927  O  O   . TYR   B  1 69  ? -55.050 -2.940  6.112    1.00 51.06  ? 370  TYR   B O   1 
ATOM   3928  C  CB  . TYR   B  1 69  ? -54.364 0.237   6.642    1.00 56.96  ? 370  TYR   B CB  1 
ATOM   3929  C  CG  . TYR   B  1 69  ? -53.939 -0.581  7.841    1.00 54.07  ? 370  TYR   B CG  1 
ATOM   3930  C  CD1 . TYR   B  1 69  ? -52.705 -1.217  7.875    1.00 54.20  ? 370  TYR   B CD1 1 
ATOM   3931  C  CD2 . TYR   B  1 69  ? -54.789 -0.744  8.920    1.00 50.87  ? 370  TYR   B CD2 1 
ATOM   3932  C  CE1 . TYR   B  1 69  ? -52.329 -1.992  8.959    1.00 54.97  ? 370  TYR   B CE1 1 
ATOM   3933  C  CE2 . TYR   B  1 69  ? -54.420 -1.508  10.016   1.00 66.25  ? 370  TYR   B CE2 1 
ATOM   3934  C  CZ  . TYR   B  1 69  ? -53.186 -2.130  10.036   1.00 62.37  ? 370  TYR   B CZ  1 
ATOM   3935  O  OH  . TYR   B  1 69  ? -52.826 -2.889  11.138   1.00 56.26  ? 370  TYR   B OH  1 
ATOM   3936  N  N   . TYR   B  1 70  ? -56.904 -1.665  6.273    1.00 44.03  ? 371  TYR   B N   1 
ATOM   3937  C  CA  . TYR   B  1 70  ? -57.674 -2.815  6.738    1.00 44.11  ? 371  TYR   B CA  1 
ATOM   3938  C  C   . TYR   B  1 70  ? -57.919 -3.798  5.615    1.00 52.55  ? 371  TYR   B C   1 
ATOM   3939  O  O   . TYR   B  1 70  ? -58.032 -5.000  5.872    1.00 59.21  ? 371  TYR   B O   1 
ATOM   3940  C  CB  . TYR   B  1 70  ? -58.987 -2.377  7.395    1.00 50.93  ? 371  TYR   B CB  1 
ATOM   3941  C  CG  . TYR   B  1 70  ? -58.789 -2.060  8.871    1.00 61.34  ? 371  TYR   B CG  1 
ATOM   3942  C  CD1 . TYR   B  1 70  ? -58.587 -0.750  9.302    1.00 61.27  ? 371  TYR   B CD1 1 
ATOM   3943  C  CD2 . TYR   B  1 70  ? -58.749 -3.080  9.827    1.00 61.34  ? 371  TYR   B CD2 1 
ATOM   3944  C  CE1 . TYR   B  1 70  ? -58.380 -0.463  10.644   1.00 62.49  ? 371  TYR   B CE1 1 
ATOM   3945  C  CE2 . TYR   B  1 70  ? -58.549 -2.800  11.176   1.00 59.33  ? 371  TYR   B CE2 1 
ATOM   3946  C  CZ  . TYR   B  1 70  ? -58.365 -1.491  11.576   1.00 63.60  ? 371  TYR   B CZ  1 
ATOM   3947  O  OH  . TYR   B  1 70  ? -58.161 -1.203  12.908   1.00 66.84  ? 371  TYR   B OH  1 
ATOM   3948  N  N   . SER   B  1 71  ? -57.969 -3.310  4.370    1.00 61.86  ? 372  SER   B N   1 
ATOM   3949  C  CA  . SER   B  1 71  ? -58.028 -4.206  3.223    1.00 66.88  ? 372  SER   B CA  1 
ATOM   3950  C  C   . SER   B  1 71  ? -56.749 -5.023  3.114    1.00 61.23  ? 372  SER   B C   1 
ATOM   3951  O  O   . SER   B  1 71  ? -56.796 -6.238  2.890    1.00 70.91  ? 372  SER   B O   1 
ATOM   3952  C  CB  . SER   B  1 71  ? -58.278 -3.409  1.940    1.00 78.53  ? 372  SER   B CB  1 
ATOM   3953  O  OG  . SER   B  1 71  ? -59.545 -2.765  1.974    1.00 84.11  ? 372  SER   B OG  1 
ATOM   3954  N  N   . SER   B  1 72  ? -55.596 -4.371  3.287    1.00 52.45  ? 373  SER   B N   1 
ATOM   3955  C  CA  . SER   B  1 72  ? -54.315 -5.072  3.231    1.00 50.92  ? 373  SER   B CA  1 
ATOM   3956  C  C   . SER   B  1 72  ? -54.327 -6.338  4.074    1.00 61.17  ? 373  SER   B C   1 
ATOM   3957  O  O   . SER   B  1 72  ? -53.766 -7.363  3.669    1.00 59.50  ? 373  SER   B O   1 
ATOM   3958  C  CB  . SER   B  1 72  ? -53.197 -4.160  3.727    1.00 51.25  ? 373  SER   B CB  1 
ATOM   3959  O  OG  . SER   B  1 72  ? -53.138 -4.240  5.149    1.00 55.76  ? 373  SER   B OG  1 
ATOM   3960  N  N   . ILE   B  1 73  ? -54.974 -6.285  5.246    1.00 60.44  ? 374  ILE   B N   1 
ATOM   3961  C  CA  . ILE   B  1 73  ? -54.852 -7.342  6.249    1.00 68.19  ? 374  ILE   B CA  1 
ATOM   3962  C  C   . ILE   B  1 73  ? -56.130 -8.159  6.356    1.00 65.94  ? 374  ILE   B C   1 
ATOM   3963  O  O   . ILE   B  1 73  ? -56.486 -8.633  7.441    1.00 68.31  ? 374  ILE   B O   1 
ATOM   3964  C  CB  . ILE   B  1 73  ? -54.463 -6.761  7.620    1.00 60.82  ? 374  ILE   B CB  1 
ATOM   3965  C  CG1 . ILE   B  1 73  ? -55.339 -5.536  7.930    1.00 60.63  ? 374  ILE   B CG1 1 
ATOM   3966  C  CG2 . ILE   B  1 73  ? -52.982 -6.389  7.625    1.00 50.00  ? 374  ILE   B CG2 1 
ATOM   3967  C  CD1 . ILE   B  1 73  ? -55.784 -5.377  9.386    1.00 39.95  ? 374  ILE   B CD1 1 
ATOM   3968  N  N   . LYS   B  1 74  ? -56.816 -8.345  5.232    1.00 70.54  ? 375  LYS   B N   1 
ATOM   3969  C  CA  . LYS   B  1 74  ? -57.934 -9.288  5.146    1.00 80.08  ? 375  LYS   B CA  1 
ATOM   3970  C  C   . LYS   B  1 74  ? -59.014 -8.976  6.181    1.00 81.08  ? 375  LYS   B C   1 
ATOM   3971  O  O   . LYS   B  1 74  ? -59.590 -9.875  6.805    1.00 83.32  ? 375  LYS   B O   1 
ATOM   3972  C  CB  . LYS   B  1 74  ? -57.434 -10.735 5.277    1.00 83.71  ? 375  LYS   B CB  1 
ATOM   3973  C  CG  . LYS   B  1 74  ? -56.172 -11.035 4.459    1.00 76.65  ? 375  LYS   B CG  1 
ATOM   3974  C  CD  . LYS   B  1 74  ? -56.450 -11.937 3.268    1.00 76.24  ? 375  LYS   B CD  1 
ATOM   3975  C  CE  . LYS   B  1 74  ? -55.333 -11.845 2.250    1.00 68.65  ? 375  LYS   B CE  1 
ATOM   3976  N  NZ  . LYS   B  1 74  ? -55.174 -10.448 1.725    1.00 62.79  ? 375  LYS   B NZ  1 
ATOM   3977  N  N   . ARG   B  1 75  ? -59.279 -7.679  6.367    1.00 75.78  ? 376  ARG   B N   1 
ATOM   3978  C  CA  . ARG   B  1 75  ? -60.493 -7.240  7.043    1.00 76.09  ? 376  ARG   B CA  1 
ATOM   3979  C  C   . ARG   B  1 75  ? -61.278 -6.390  6.053    1.00 82.33  ? 376  ARG   B C   1 
ATOM   3980  O  O   . ARG   B  1 75  ? -61.678 -6.887  4.999    1.00 74.09  ? 376  ARG   B O   1 
ATOM   3981  C  CB  . ARG   B  1 75  ? -60.172 -6.528  8.333    1.00 63.09  ? 376  ARG   B CB  1 
ATOM   3982  C  CG  . ARG   B  1 75  ? -58.974 -7.158  9.038    1.00 64.69  ? 376  ARG   B CG  1 
ATOM   3983  C  CD  . ARG   B  1 75  ? -59.306 -7.478  10.456   1.00 83.48  ? 376  ARG   B CD  1 
ATOM   3984  N  NE  . ARG   B  1 75  ? -59.363 -8.912  10.674   1.00 92.22  ? 376  ARG   B NE  1 
ATOM   3985  C  CZ  . ARG   B  1 75  ? -59.425 -9.469  11.874   1.00 98.11  ? 376  ARG   B CZ  1 
ATOM   3986  N  NH1 . ARG   B  1 75  ? -59.467 -10.787 11.977   1.00 102.31 ? 376  ARG   B NH1 1 
ATOM   3987  N  NH2 . ARG   B  1 75  ? -59.441 -8.708  12.965   1.00 94.80  ? 376  ARG   B NH2 1 
ATOM   3988  N  N   . PHE   B  1 76  ? -61.473 -5.107  6.356    1.00 84.61  ? 377  PHE   B N   1 
ATOM   3989  C  CA  . PHE   B  1 76  ? -62.449 -4.250  5.698    1.00 81.21  ? 377  PHE   B CA  1 
ATOM   3990  C  C   . PHE   B  1 76  ? -63.846 -4.693  6.128    1.00 82.78  ? 377  PHE   B C   1 
ATOM   3991  O  O   . PHE   B  1 76  ? -64.292 -5.800  5.797    1.00 80.36  ? 377  PHE   B O   1 
ATOM   3992  C  CB  . PHE   B  1 76  ? -62.303 -4.261  4.165    1.00 80.41  ? 377  PHE   B CB  1 
ATOM   3993  C  CG  . PHE   B  1 76  ? -63.223 -3.288  3.481    1.00 74.78  ? 377  PHE   B CG  1 
ATOM   3994  C  CD1 . PHE   B  1 76  ? -64.461 -3.695  3.018    1.00 79.03  ? 377  PHE   B CD1 1 
ATOM   3995  C  CD2 . PHE   B  1 76  ? -62.863 -1.952  3.336    1.00 75.66  ? 377  PHE   B CD2 1 
ATOM   3996  C  CE1 . PHE   B  1 76  ? -65.317 -2.798  2.418    1.00 88.60  ? 377  PHE   B CE1 1 
ATOM   3997  C  CE2 . PHE   B  1 76  ? -63.719 -1.051  2.737    1.00 79.29  ? 377  PHE   B CE2 1 
ATOM   3998  C  CZ  . PHE   B  1 76  ? -64.944 -1.477  2.278    1.00 87.84  ? 377  PHE   B CZ  1 
ATOM   3999  N  N   . GLY   B  1 77  ? -64.551 -3.825  6.852    1.00 84.46  ? 378  GLY   B N   1 
ATOM   4000  C  CA  . GLY   B  1 77  ? -65.844 -4.147  7.413    1.00 83.38  ? 378  GLY   B CA  1 
ATOM   4001  C  C   . GLY   B  1 77  ? -65.801 -4.779  8.788    1.00 86.15  ? 378  GLY   B C   1 
ATOM   4002  O  O   . GLY   B  1 77  ? -66.838 -4.832  9.468    1.00 93.28  ? 378  GLY   B O   1 
ATOM   4003  N  N   . SER   B  1 78  ? -64.631 -5.261  9.212    1.00 79.39  ? 379  SER   B N   1 
ATOM   4004  C  CA  . SER   B  1 78  ? -64.454 -5.839  10.535   1.00 64.46  ? 379  SER   B CA  1 
ATOM   4005  C  C   . SER   B  1 78  ? -64.855 -4.833  11.600   1.00 67.67  ? 379  SER   B C   1 
ATOM   4006  O  O   . SER   B  1 78  ? -64.979 -3.633  11.339   1.00 64.65  ? 379  SER   B O   1 
ATOM   4007  C  CB  . SER   B  1 78  ? -63.000 -6.236  10.752   1.00 60.92  ? 379  SER   B CB  1 
ATOM   4008  O  OG  . SER   B  1 78  ? -62.198 -5.064  10.816   1.00 65.26  ? 379  SER   B OG  1 
ATOM   4009  N  N   . LYS   B  1 79  ? -65.050 -5.327  12.824   1.00 65.97  ? 380  LYS   B N   1 
ATOM   4010  C  CA  . LYS   B  1 79  ? -65.379 -4.404  13.901   1.00 63.16  ? 380  LYS   B CA  1 
ATOM   4011  C  C   . LYS   B  1 79  ? -64.239 -3.413  14.111   1.00 64.32  ? 380  LYS   B C   1 
ATOM   4012  O  O   . LYS   B  1 79  ? -64.466 -2.198  14.158   1.00 64.07  ? 380  LYS   B O   1 
ATOM   4013  C  CB  . LYS   B  1 79  ? -65.724 -5.175  15.177   1.00 64.28  ? 380  LYS   B CB  1 
ATOM   4014  C  CG  . LYS   B  1 79  ? -66.915 -4.569  15.957   1.00 82.32  ? 380  LYS   B CG  1 
ATOM   4015  C  CD  . LYS   B  1 79  ? -67.726 -5.617  16.746   1.00 87.42  ? 380  LYS   B CD  1 
ATOM   4016  C  CE  . LYS   B  1 79  ? -69.077 -5.937  16.080   1.00 90.15  ? 380  LYS   B CE  1 
ATOM   4017  N  NZ  . LYS   B  1 79  ? -69.984 -4.755  15.960   1.00 86.92  ? 380  LYS   B NZ  1 
ATOM   4018  N  N   . ALA   B  1 80  ? -62.997 -3.906  14.135   1.00 61.64  ? 381  ALA   B N   1 
ATOM   4019  C  CA  . ALA   B  1 80  ? -61.849 -3.025  14.338   1.00 60.73  ? 381  ALA   B CA  1 
ATOM   4020  C  C   . ALA   B  1 80  ? -61.825 -1.898  13.312   1.00 59.06  ? 381  ALA   B C   1 
ATOM   4021  O  O   . ALA   B  1 80  ? -61.518 -0.745  13.639   1.00 49.67  ? 381  ALA   B O   1 
ATOM   4022  C  CB  . ALA   B  1 80  ? -60.555 -3.836  14.274   1.00 59.78  ? 381  ALA   B CB  1 
ATOM   4023  N  N   . HIS   B  1 81  ? -62.160 -2.214  12.063   1.00 71.15  ? 382  HIS   B N   1 
ATOM   4024  C  CA  . HIS   B  1 81  ? -62.112 -1.205  11.012   1.00 64.75  ? 382  HIS   B CA  1 
ATOM   4025  C  C   . HIS   B  1 81  ? -63.230 -0.181  11.183   1.00 61.50  ? 382  HIS   B C   1 
ATOM   4026  O  O   . HIS   B  1 81  ? -62.997 1.031   11.093   1.00 60.99  ? 382  HIS   B O   1 
ATOM   4027  C  CB  . HIS   B  1 81  ? -62.188 -1.889  9.652    1.00 68.07  ? 382  HIS   B CB  1 
ATOM   4028  C  CG  . HIS   B  1 81  ? -62.306 -0.942  8.503    1.00 76.27  ? 382  HIS   B CG  1 
ATOM   4029  N  ND1 . HIS   B  1 81  ? -62.752 -1.341  7.262    1.00 81.27  ? 382  HIS   B ND1 1 
ATOM   4030  C  CD2 . HIS   B  1 81  ? -62.030 0.380   8.399    1.00 78.48  ? 382  HIS   B CD2 1 
ATOM   4031  C  CE1 . HIS   B  1 81  ? -62.749 -0.305  6.443    1.00 81.60  ? 382  HIS   B CE1 1 
ATOM   4032  N  NE2 . HIS   B  1 81  ? -62.315 0.751   7.108    1.00 80.91  ? 382  HIS   B NE2 1 
ATOM   4033  N  N   . MET   B  1 82  ? -64.454 -0.649  11.449   1.00 60.54  ? 383  MET   B N   1 
ATOM   4034  C  CA  . MET   B  1 82  ? -65.567 0.280   11.616   1.00 65.76  ? 383  MET   B CA  1 
ATOM   4035  C  C   . MET   B  1 82  ? -65.348 1.191   12.817   1.00 69.36  ? 383  MET   B C   1 
ATOM   4036  O  O   . MET   B  1 82  ? -65.597 2.400   12.741   1.00 73.54  ? 383  MET   B O   1 
ATOM   4037  C  CB  . MET   B  1 82  ? -66.888 -0.485  11.741   1.00 64.23  ? 383  MET   B CB  1 
ATOM   4038  C  CG  . MET   B  1 82  ? -67.270 -1.277  10.499   1.00 62.35  ? 383  MET   B CG  1 
ATOM   4039  S  SD  . MET   B  1 82  ? -66.883 -0.365  8.990    1.00 74.23  ? 383  MET   B SD  1 
ATOM   4040  C  CE  . MET   B  1 82  ? -68.106 0.943   9.093    1.00 81.50  ? 383  MET   B CE  1 
ATOM   4041  N  N   . GLU   B  1 83  ? -64.867 0.627   13.931   1.00 66.10  ? 384  GLU   B N   1 
ATOM   4042  C  CA  . GLU   B  1 83  ? -64.541 1.440   15.098   1.00 59.62  ? 384  GLU   B CA  1 
ATOM   4043  C  C   . GLU   B  1 83  ? -63.476 2.467   14.765   1.00 57.96  ? 384  GLU   B C   1 
ATOM   4044  O  O   . GLU   B  1 83  ? -63.571 3.630   15.173   1.00 59.42  ? 384  GLU   B O   1 
ATOM   4045  C  CB  . GLU   B  1 83  ? -64.069 0.546   16.242   1.00 59.70  ? 384  GLU   B CB  1 
ATOM   4046  C  CG  . GLU   B  1 83  ? -65.183 -0.229  16.906   1.00 74.68  ? 384  GLU   B CG  1 
ATOM   4047  C  CD  . GLU   B  1 83  ? -64.682 -1.461  17.609   1.00 79.51  ? 384  GLU   B CD  1 
ATOM   4048  O  OE1 . GLU   B  1 83  ? -63.496 -1.807  17.415   1.00 74.90  ? 384  GLU   B OE1 1 
ATOM   4049  O  OE2 . GLU   B  1 83  ? -65.475 -2.083  18.348   1.00 87.47  ? 384  GLU   B OE2 1 
ATOM   4050  N  N   . ARG   B  1 84  ? -62.458 2.051   14.008   1.00 50.45  ? 385  ARG   B N   1 
ATOM   4051  C  CA  . ARG   B  1 84  ? -61.378 2.958   13.646   1.00 55.30  ? 385  ARG   B CA  1 
ATOM   4052  C  C   . ARG   B  1 84  ? -61.894 4.154   12.845   1.00 63.24  ? 385  ARG   B C   1 
ATOM   4053  O  O   . ARG   B  1 84  ? -61.492 5.299   13.093   1.00 69.75  ? 385  ARG   B O   1 
ATOM   4054  C  CB  . ARG   B  1 84  ? -60.322 2.191   12.862   1.00 52.14  ? 385  ARG   B CB  1 
ATOM   4055  C  CG  . ARG   B  1 84  ? -59.076 2.983   12.603   1.00 53.18  ? 385  ARG   B CG  1 
ATOM   4056  C  CD  . ARG   B  1 84  ? -58.189 3.028   13.820   1.00 44.37  ? 385  ARG   B CD  1 
ATOM   4057  N  NE  . ARG   B  1 84  ? -56.986 3.797   13.527   1.00 51.35  ? 385  ARG   B NE  1 
ATOM   4058  C  CZ  . ARG   B  1 84  ? -56.815 5.072   13.865   1.00 53.51  ? 385  ARG   B CZ  1 
ATOM   4059  N  NH1 . ARG   B  1 84  ? -57.762 5.716   14.538   1.00 54.20  ? 385  ARG   B NH1 1 
ATOM   4060  N  NH2 . ARG   B  1 84  ? -55.685 5.699   13.554   1.00 42.91  ? 385  ARG   B NH2 1 
ATOM   4061  N  N   . LEU   B  1 85  ? -62.789 3.911   11.885   1.00 57.59  ? 386  LEU   B N   1 
ATOM   4062  C  CA  . LEU   B  1 85  ? -63.398 5.017   11.157   1.00 58.02  ? 386  LEU   B CA  1 
ATOM   4063  C  C   . LEU   B  1 85  ? -64.088 5.985   12.112   1.00 58.50  ? 386  LEU   B C   1 
ATOM   4064  O  O   . LEU   B  1 85  ? -63.906 7.206   12.016   1.00 55.47  ? 386  LEU   B O   1 
ATOM   4065  C  CB  . LEU   B  1 85  ? -64.379 4.479   10.117   1.00 58.86  ? 386  LEU   B CB  1 
ATOM   4066  C  CG  . LEU   B  1 85  ? -63.762 3.694   8.957    1.00 52.82  ? 386  LEU   B CG  1 
ATOM   4067  C  CD1 . LEU   B  1 85  ? -64.840 3.171   8.029    1.00 59.00  ? 386  LEU   B CD1 1 
ATOM   4068  C  CD2 . LEU   B  1 85  ? -62.769 4.553   8.203    1.00 42.93  ? 386  LEU   B CD2 1 
ATOM   4069  N  N   . GLU   B  1 86  ? -64.877 5.453   13.055   1.00 67.00  ? 387  GLU   B N   1 
ATOM   4070  C  CA  . GLU   B  1 86  ? -65.543 6.306   14.036   1.00 71.17  ? 387  GLU   B CA  1 
ATOM   4071  C  C   . GLU   B  1 86  ? -64.541 6.996   14.948   1.00 65.63  ? 387  GLU   B C   1 
ATOM   4072  O  O   . GLU   B  1 86  ? -64.790 8.121   15.402   1.00 63.47  ? 387  GLU   B O   1 
ATOM   4073  C  CB  . GLU   B  1 86  ? -66.542 5.497   14.872   1.00 87.82  ? 387  GLU   B CB  1 
ATOM   4074  C  CG  . GLU   B  1 86  ? -67.982 5.521   14.346   1.00 108.98 ? 387  GLU   B CG  1 
ATOM   4075  C  CD  . GLU   B  1 86  ? -68.330 4.307   13.480   1.00 123.47 ? 387  GLU   B CD  1 
ATOM   4076  O  OE1 . GLU   B  1 86  ? -68.433 3.190   14.037   1.00 127.61 ? 387  GLU   B OE1 1 
ATOM   4077  O  OE2 . GLU   B  1 86  ? -68.498 4.467   12.245   1.00 126.80 ? 387  GLU   B OE2 1 
ATOM   4078  N  N   . GLU   B  1 87  ? -63.403 6.345   15.220   1.00 59.62  ? 388  GLU   B N   1 
ATOM   4079  C  CA  . GLU   B  1 87  ? -62.379 6.953   16.065   1.00 64.20  ? 388  GLU   B CA  1 
ATOM   4080  C  C   . GLU   B  1 87  ? -61.720 8.135   15.359   1.00 63.25  ? 388  GLU   B C   1 
ATOM   4081  O  O   . GLU   B  1 87  ? -61.535 9.207   15.958   1.00 46.22  ? 388  GLU   B O   1 
ATOM   4082  C  CB  . GLU   B  1 87  ? -61.338 5.901   16.459   1.00 63.34  ? 388  GLU   B CB  1 
ATOM   4083  C  CG  . GLU   B  1 87  ? -60.616 6.181   17.764   1.00 62.52  ? 388  GLU   B CG  1 
ATOM   4084  C  CD  . GLU   B  1 87  ? -59.338 5.369   17.924   1.00 65.06  ? 388  GLU   B CD  1 
ATOM   4085  O  OE1 . GLU   B  1 87  ? -58.981 4.610   16.998   1.00 67.39  ? 388  GLU   B OE1 1 
ATOM   4086  O  OE2 . GLU   B  1 87  ? -58.677 5.501   18.975   1.00 67.43  ? 388  GLU   B OE2 1 
ATOM   4087  N  N   . VAL   B  1 88  ? -61.370 7.960   14.079   1.00 62.66  ? 389  VAL   B N   1 
ATOM   4088  C  CA  . VAL   B  1 88  ? -60.808 9.060   13.301   1.00 60.69  ? 389  VAL   B CA  1 
ATOM   4089  C  C   . VAL   B  1 88  ? -61.848 10.153  13.088   1.00 64.53  ? 389  VAL   B C   1 
ATOM   4090  O  O   . VAL   B  1 88  ? -61.544 11.349  13.179   1.00 62.40  ? 389  VAL   B O   1 
ATOM   4091  C  CB  . VAL   B  1 88  ? -60.258 8.540   11.964   1.00 54.59  ? 389  VAL   B CB  1 
ATOM   4092  C  CG1 . VAL   B  1 88  ? -59.743 9.707   11.104   1.00 52.41  ? 389  VAL   B CG1 1 
ATOM   4093  C  CG2 . VAL   B  1 88  ? -59.168 7.505   12.210   1.00 48.13  ? 389  VAL   B CG2 1 
ATOM   4094  N  N   . ASN   B  1 89  ? -63.089 9.762   12.804   1.00 64.35  ? 390  ASN   B N   1 
ATOM   4095  C  CA  . ASN   B  1 89  ? -64.148 10.743  12.603   1.00 71.52  ? 390  ASN   B CA  1 
ATOM   4096  C  C   . ASN   B  1 89  ? -64.259 11.687  13.800   1.00 72.60  ? 390  ASN   B C   1 
ATOM   4097  O  O   . ASN   B  1 89  ? -64.154 12.910  13.651   1.00 73.41  ? 390  ASN   B O   1 
ATOM   4098  C  CB  . ASN   B  1 89  ? -65.471 10.025  12.342   1.00 76.41  ? 390  ASN   B CB  1 
ATOM   4099  C  CG  . ASN   B  1 89  ? -66.446 10.878  11.568   1.00 88.77  ? 390  ASN   B CG  1 
ATOM   4100  O  OD1 . ASN   B  1 89  ? -66.923 11.898  12.066   1.00 89.93  ? 390  ASN   B OD1 1 
ATOM   4101  N  ND2 . ASN   B  1 89  ? -66.757 10.462  10.339   1.00 96.79  ? 390  ASN   B ND2 1 
ATOM   4102  N  N   . LYS   B  1 90  ? -64.447 11.129  15.006   1.00 66.00  ? 391  LYS   B N   1 
ATOM   4103  C  CA  . LYS   B  1 90  ? -64.604 11.961  16.198   1.00 65.70  ? 391  LYS   B CA  1 
ATOM   4104  C  C   . LYS   B  1 90  ? -63.342 12.758  16.495   1.00 59.23  ? 391  LYS   B C   1 
ATOM   4105  O  O   . LYS   B  1 90  ? -63.416 13.878  17.018   1.00 64.99  ? 391  LYS   B O   1 
ATOM   4106  C  CB  . LYS   B  1 90  ? -64.980 11.077  17.394   1.00 73.83  ? 391  LYS   B CB  1 
ATOM   4107  C  CG  . LYS   B  1 90  ? -64.269 11.393  18.698   1.00 78.41  ? 391  LYS   B CG  1 
ATOM   4108  C  CD  . LYS   B  1 90  ? -64.216 10.153  19.598   1.00 88.20  ? 391  LYS   B CD  1 
ATOM   4109  C  CE  . LYS   B  1 90  ? -63.517 10.419  20.923   1.00 83.10  ? 391  LYS   B CE  1 
ATOM   4110  N  NZ  . LYS   B  1 90  ? -64.465 10.858  21.980   1.00 78.94  ? 391  LYS   B NZ  1 
ATOM   4111  N  N   . GLU   B  1 91  ? -62.181 12.197  16.163   1.00 42.66  ? 392  GLU   B N   1 
ATOM   4112  C  CA  . GLU   B  1 91  ? -60.917 12.880  16.415   1.00 51.12  ? 392  GLU   B CA  1 
ATOM   4113  C  C   . GLU   B  1 91  ? -60.788 14.139  15.562   1.00 71.13  ? 392  GLU   B C   1 
ATOM   4114  O  O   . GLU   B  1 91  ? -60.418 15.206  16.073   1.00 62.90  ? 392  GLU   B O   1 
ATOM   4115  C  CB  . GLU   B  1 91  ? -59.755 11.922  16.160   1.00 39.34  ? 392  GLU   B CB  1 
ATOM   4116  C  CG  . GLU   B  1 91  ? -58.432 12.393  16.749   1.00 66.20  ? 392  GLU   B CG  1 
ATOM   4117  C  CD  . GLU   B  1 91  ? -57.438 11.260  16.979   1.00 67.47  ? 392  GLU   B CD  1 
ATOM   4118  O  OE1 . GLU   B  1 91  ? -56.326 11.560  17.470   1.00 71.45  ? 392  GLU   B OE1 1 
ATOM   4119  O  OE2 . GLU   B  1 91  ? -57.766 10.083  16.670   1.00 56.03  ? 392  GLU   B OE2 1 
ATOM   4120  N  N   . ILE   B  1 92  ? -61.079 14.030  14.252   1.00 78.76  ? 393  ILE   B N   1 
ATOM   4121  C  CA  . ILE   B  1 92  ? -61.084 15.198  13.368   1.00 71.66  ? 393  ILE   B CA  1 
ATOM   4122  C  C   . ILE   B  1 92  ? -62.104 16.224  13.841   1.00 73.75  ? 393  ILE   B C   1 
ATOM   4123  O  O   . ILE   B  1 92  ? -61.856 17.433  13.780   1.00 76.75  ? 393  ILE   B O   1 
ATOM   4124  C  CB  . ILE   B  1 92  ? -61.354 14.774  11.912   1.00 77.43  ? 393  ILE   B CB  1 
ATOM   4125  C  CG1 . ILE   B  1 92  ? -60.190 13.949  11.354   1.00 68.15  ? 393  ILE   B CG1 1 
ATOM   4126  C  CG2 . ILE   B  1 92  ? -61.618 15.997  11.042   1.00 81.51  ? 393  ILE   B CG2 1 
ATOM   4127  C  CD1 . ILE   B  1 92  ? -60.573 13.091  10.152   1.00 61.14  ? 393  ILE   B CD1 1 
ATOM   4128  N  N   . ASP   B  1 93  ? -63.268 15.755  14.316   1.00 84.91  ? 394  ASP   B N   1 
ATOM   4129  C  CA  . ASP   B  1 93  ? -64.299 16.633  14.878   1.00 87.87  ? 394  ASP   B CA  1 
ATOM   4130  C  C   . ASP   B  1 93  ? -63.767 17.496  16.010   1.00 89.26  ? 394  ASP   B C   1 
ATOM   4131  O  O   . ASP   B  1 93  ? -64.164 18.657  16.162   1.00 98.64  ? 394  ASP   B O   1 
ATOM   4132  C  CB  . ASP   B  1 93  ? -65.464 15.803  15.417   1.00 89.41  ? 394  ASP   B CB  1 
ATOM   4133  C  CG  . ASP   B  1 93  ? -66.464 15.435  14.360   1.00 98.02  ? 394  ASP   B CG  1 
ATOM   4134  O  OD1 . ASP   B  1 93  ? -66.814 16.304  13.531   1.00 100.44 ? 394  ASP   B OD1 1 
ATOM   4135  O  OD2 . ASP   B  1 93  ? -66.913 14.270  14.366   1.00 103.40 ? 394  ASP   B OD2 1 
ATOM   4136  N  N   . THR   B  1 94  ? -62.891 16.935  16.835   1.00 73.10  ? 395  THR   B N   1 
ATOM   4137  C  CA  . THR   B  1 94  ? -62.510 17.567  18.084   1.00 73.84  ? 395  THR   B CA  1 
ATOM   4138  C  C   . THR   B  1 94  ? -61.105 18.164  18.083   1.00 76.71  ? 395  THR   B C   1 
ATOM   4139  O  O   . THR   B  1 94  ? -60.854 19.116  18.823   1.00 88.32  ? 395  THR   B O   1 
ATOM   4140  C  CB  . THR   B  1 94  ? -62.651 16.552  19.226   1.00 72.29  ? 395  THR   B CB  1 
ATOM   4141  O  OG1 . THR   B  1 94  ? -61.842 15.405  18.952   1.00 78.97  ? 395  THR   B OG1 1 
ATOM   4142  C  CG2 . THR   B  1 94  ? -64.087 16.083  19.320   1.00 62.74  ? 395  THR   B CG2 1 
ATOM   4143  N  N   . THR   B  1 95  ? -60.188 17.651  17.265   1.00 75.07  ? 396  THR   B N   1 
ATOM   4144  C  CA  . THR   B  1 95  ? -58.831 18.178  17.193   1.00 73.97  ? 396  THR   B CA  1 
ATOM   4145  C  C   . THR   B  1 95  ? -58.417 18.604  15.788   1.00 75.58  ? 396  THR   B C   1 
ATOM   4146  O  O   . THR   B  1 95  ? -57.253 18.979  15.591   1.00 75.35  ? 396  THR   B O   1 
ATOM   4147  C  CB  . THR   B  1 95  ? -57.822 17.141  17.710   1.00 80.32  ? 396  THR   B CB  1 
ATOM   4148  O  OG1 . THR   B  1 95  ? -57.757 16.038  16.794   1.00 87.49  ? 396  THR   B OG1 1 
ATOM   4149  C  CG2 . THR   B  1 95  ? -58.214 16.629  19.090   1.00 80.65  ? 396  THR   B CG2 1 
ATOM   4150  N  N   . SER   B  1 96  ? -59.319 18.533  14.809   1.00 69.04  ? 397  SER   B N   1 
ATOM   4151  C  CA  . SER   B  1 96  ? -59.063 18.940  13.426   1.00 72.73  ? 397  SER   B CA  1 
ATOM   4152  C  C   . SER   B  1 96  ? -58.003 18.083  12.748   1.00 64.08  ? 397  SER   B C   1 
ATOM   4153  O  O   . SER   B  1 96  ? -57.483 18.466  11.695   1.00 60.86  ? 397  SER   B O   1 
ATOM   4154  C  CB  . SER   B  1 96  ? -58.668 20.424  13.336   1.00 86.41  ? 397  SER   B CB  1 
ATOM   4155  O  OG  . SER   B  1 96  ? -59.750 21.272  13.689   1.00 93.77  ? 397  SER   B OG  1 
ATOM   4156  N  N   . THR   B  1 97  ? -57.684 16.925  13.317   1.00 65.66  ? 398  THR   B N   1 
ATOM   4157  C  CA  . THR   B  1 97  ? -56.646 16.045  12.776   1.00 63.78  ? 398  THR   B CA  1 
ATOM   4158  C  C   . THR   B  1 97  ? -56.961 14.618  13.243   1.00 59.01  ? 398  THR   B C   1 
ATOM   4159  O  O   . THR   B  1 97  ? -58.085 14.339  13.678   1.00 56.97  ? 398  THR   B O   1 
ATOM   4160  C  CB  . THR   B  1 97  ? -55.253 16.541  13.206   1.00 65.30  ? 398  THR   B CB  1 
ATOM   4161  O  OG1 . THR   B  1 97  ? -54.229 15.741  12.605   1.00 62.93  ? 398  THR   B OG1 1 
ATOM   4162  C  CG2 . THR   B  1 97  ? -55.111 16.479  14.705   1.00 72.11  ? 398  THR   B CG2 1 
ATOM   4163  N  N   . TYR   B  1 98  ? -55.990 13.711  13.118   1.00 52.09  ? 399  TYR   B N   1 
ATOM   4164  C  CA  . TYR   B  1 98  ? -56.086 12.392  13.738   1.00 47.67  ? 399  TYR   B CA  1 
ATOM   4165  C  C   . TYR   B  1 98  ? -54.686 11.797  13.846   1.00 45.79  ? 399  TYR   B C   1 
ATOM   4166  O  O   . TYR   B  1 98  ? -53.705 12.369  13.362   1.00 54.53  ? 399  TYR   B O   1 
ATOM   4167  C  CB  . TYR   B  1 98  ? -57.044 11.466  12.978   1.00 49.88  ? 399  TYR   B CB  1 
ATOM   4168  C  CG  . TYR   B  1 98  ? -56.540 10.951  11.650   1.00 51.18  ? 399  TYR   B CG  1 
ATOM   4169  C  CD1 . TYR   B  1 98  ? -55.914 9.711   11.553   1.00 46.62  ? 399  TYR   B CD1 1 
ATOM   4170  C  CD2 . TYR   B  1 98  ? -56.726 11.691  10.491   1.00 48.53  ? 399  TYR   B CD2 1 
ATOM   4171  C  CE1 . TYR   B  1 98  ? -55.465 9.242   10.345   1.00 43.92  ? 399  TYR   B CE1 1 
ATOM   4172  C  CE2 . TYR   B  1 98  ? -56.273 11.242  9.288    1.00 47.96  ? 399  TYR   B CE2 1 
ATOM   4173  C  CZ  . TYR   B  1 98  ? -55.652 10.016  9.210    1.00 52.11  ? 399  TYR   B CZ  1 
ATOM   4174  O  OH  . TYR   B  1 98  ? -55.217 9.574   7.982    1.00 60.13  ? 399  TYR   B OH  1 
ATOM   4175  N  N   . GLN   B  1 99  ? -54.604 10.638  14.500   1.00 46.98  ? 400  GLN   B N   1 
ATOM   4176  C  CA  . GLN   B  1 99  ? -53.344 10.047  14.940   1.00 45.32  ? 400  GLN   B CA  1 
ATOM   4177  C  C   . GLN   B  1 99  ? -53.274 8.600   14.489   1.00 48.06  ? 400  GLN   B C   1 
ATOM   4178  O  O   . GLN   B  1 99  ? -54.243 7.844   14.630   1.00 49.34  ? 400  GLN   B O   1 
ATOM   4179  C  CB  . GLN   B  1 99  ? -53.193 10.113  16.474   1.00 43.50  ? 400  GLN   B CB  1 
ATOM   4180  C  CG  . GLN   B  1 99  ? -53.229 11.515  17.014   1.00 48.04  ? 400  GLN   B CG  1 
ATOM   4181  C  CD  . GLN   B  1 99  ? -52.057 12.316  16.540   1.00 54.26  ? 400  GLN   B CD  1 
ATOM   4182  O  OE1 . GLN   B  1 99  ? -50.969 11.776  16.341   1.00 58.01  ? 400  GLN   B OE1 1 
ATOM   4183  N  NE2 . GLN   B  1 99  ? -52.263 13.612  16.343   1.00 60.51  ? 400  GLN   B NE2 1 
ATOM   4184  N  N   . LEU   B  1 100 ? -52.122 8.218   13.958   1.00 45.68  ? 401  LEU   B N   1 
ATOM   4185  C  CA  . LEU   B  1 100 ? -51.966 6.917   13.338   1.00 50.01  ? 401  LEU   B CA  1 
ATOM   4186  C  C   . LEU   B  1 100 ? -51.642 5.887   14.402   1.00 45.63  ? 401  LEU   B C   1 
ATOM   4187  O  O   . LEU   B  1 100 ? -50.717 6.081   15.187   1.00 42.13  ? 401  LEU   B O   1 
ATOM   4188  C  CB  . LEU   B  1 100 ? -50.856 6.958   12.292   1.00 43.57  ? 401  LEU   B CB  1 
ATOM   4189  C  CG  . LEU   B  1 100 ? -51.150 7.830   11.073   1.00 38.99  ? 401  LEU   B CG  1 
ATOM   4190  C  CD1 . LEU   B  1 100 ? -49.908 8.002   10.254   1.00 42.63  ? 401  LEU   B CD1 1 
ATOM   4191  C  CD2 . LEU   B  1 100 ? -52.225 7.196   10.256   1.00 31.14  ? 401  LEU   B CD2 1 
ATOM   4192  N  N   . LYS   B  1 101 ? -52.397 4.794   14.425   1.00 41.59  ? 402  LYS   B N   1 
ATOM   4193  C  CA  . LYS   B  1 101 ? -51.924 3.619   15.145   1.00 40.54  ? 402  LYS   B CA  1 
ATOM   4194  C  C   . LYS   B  1 101 ? -50.501 3.275   14.715   1.00 43.01  ? 402  LYS   B C   1 
ATOM   4195  O  O   . LYS   B  1 101 ? -50.069 3.624   13.613   1.00 52.28  ? 402  LYS   B O   1 
ATOM   4196  C  CB  . LYS   B  1 101 ? -52.848 2.424   14.908   1.00 38.19  ? 402  LYS   B CB  1 
ATOM   4197  C  CG  . LYS   B  1 101 ? -54.176 2.501   15.638   1.00 46.97  ? 402  LYS   B CG  1 
ATOM   4198  C  CD  . LYS   B  1 101 ? -54.090 3.340   16.907   1.00 48.19  ? 402  LYS   B CD  1 
ATOM   4199  C  CE  . LYS   B  1 101 ? -55.379 3.269   17.715   1.00 55.12  ? 402  LYS   B CE  1 
ATOM   4200  N  NZ  . LYS   B  1 101 ? -55.689 4.577   18.365   1.00 58.36  ? 402  LYS   B NZ  1 
ATOM   4201  N  N   . ASP   B  1 102 ? -49.766 2.587   15.583   1.00 44.82  ? 403  ASP   B N   1 
ATOM   4202  C  CA  . ASP   B  1 102 ? -48.400 2.201   15.260   1.00 43.21  ? 403  ASP   B CA  1 
ATOM   4203  C  C   . ASP   B  1 102 ? -48.347 1.282   14.061   1.00 42.72  ? 403  ASP   B C   1 
ATOM   4204  O  O   . ASP   B  1 102 ? -47.406 1.353   13.265   1.00 45.97  ? 403  ASP   B O   1 
ATOM   4205  C  CB  . ASP   B  1 102 ? -47.760 1.495   16.447   1.00 51.10  ? 403  ASP   B CB  1 
ATOM   4206  C  CG  . ASP   B  1 102 ? -47.425 2.436   17.561   1.00 62.01  ? 403  ASP   B CG  1 
ATOM   4207  O  OD1 . ASP   B  1 102 ? -47.674 3.651   17.385   1.00 58.88  ? 403  ASP   B OD1 1 
ATOM   4208  O  OD2 . ASP   B  1 102 ? -46.915 1.960   18.602   1.00 69.07  ? 403  ASP   B OD2 1 
ATOM   4209  N  N   . THR   B  1 103 ? -49.296 0.352   13.966   1.00 48.02  ? 404  THR   B N   1 
ATOM   4210  C  CA  . THR   B  1 103 ? -49.353 -0.526  12.802   1.00 53.34  ? 404  THR   B CA  1 
ATOM   4211  C  C   . THR   B  1 103 ? -49.634 0.281   11.535   1.00 50.35  ? 404  THR   B C   1 
ATOM   4212  O  O   . THR   B  1 103 ? -48.941 0.142   10.521   1.00 37.95  ? 404  THR   B O   1 
ATOM   4213  C  CB  . THR   B  1 103 ? -50.417 -1.609  13.016   1.00 53.33  ? 404  THR   B CB  1 
ATOM   4214  O  OG1 . THR   B  1 103 ? -51.594 -1.039  13.616   1.00 51.38  ? 404  THR   B OG1 1 
ATOM   4215  C  CG2 . THR   B  1 103 ? -49.870 -2.695  13.906   1.00 50.56  ? 404  THR   B CG2 1 
ATOM   4216  N  N   . GLU   B  1 104 ? -50.633 1.162   11.603   1.00 52.95  ? 405  GLU   B N   1 
ATOM   4217  C  CA  . GLU   B  1 104 ? -50.912 2.092   10.522   1.00 49.20  ? 405  GLU   B CA  1 
ATOM   4218  C  C   . GLU   B  1 104 ? -49.645 2.811   10.066   1.00 54.33  ? 405  GLU   B C   1 
ATOM   4219  O  O   . GLU   B  1 104 ? -49.306 2.795   8.880    1.00 66.30  ? 405  GLU   B O   1 
ATOM   4220  C  CB  . GLU   B  1 104 ? -51.997 3.073   10.985   1.00 50.46  ? 405  GLU   B CB  1 
ATOM   4221  C  CG  . GLU   B  1 104 ? -53.393 2.416   11.079   1.00 42.28  ? 405  GLU   B CG  1 
ATOM   4222  C  CD  . GLU   B  1 104 ? -54.383 3.209   11.890   1.00 46.53  ? 405  GLU   B CD  1 
ATOM   4223  O  OE1 . GLU   B  1 104 ? -55.458 2.668   12.217   1.00 56.73  ? 405  GLU   B OE1 1 
ATOM   4224  O  OE2 . GLU   B  1 104 ? -54.087 4.365   12.233   1.00 58.37  ? 405  GLU   B OE2 1 
ATOM   4225  N  N   . LEU   B  1 105 ? -48.905 3.405   11.001   1.00 54.41  ? 406  LEU   B N   1 
ATOM   4226  C  CA  . LEU   B  1 105 ? -47.735 4.193   10.620   1.00 43.67  ? 406  LEU   B CA  1 
ATOM   4227  C  C   . LEU   B  1 105 ? -46.654 3.335   9.978    1.00 47.90  ? 406  LEU   B C   1 
ATOM   4228  O  O   . LEU   B  1 105 ? -45.934 3.814   9.096    1.00 48.13  ? 406  LEU   B O   1 
ATOM   4229  C  CB  . LEU   B  1 105 ? -47.162 4.919   11.838   1.00 44.56  ? 406  LEU   B CB  1 
ATOM   4230  C  CG  . LEU   B  1 105 ? -45.912 5.795   11.677   1.00 42.46  ? 406  LEU   B CG  1 
ATOM   4231  C  CD1 . LEU   B  1 105 ? -46.275 7.252   11.315   1.00 44.01  ? 406  LEU   B CD1 1 
ATOM   4232  C  CD2 . LEU   B  1 105 ? -45.025 5.744   12.931   1.00 27.36  ? 406  LEU   B CD2 1 
ATOM   4233  N  N   . ILE   B  1 106 ? -46.493 2.079   10.404   1.00 39.47  ? 407  ILE   B N   1 
ATOM   4234  C  CA  . ILE   B  1 106 ? -45.452 1.274   9.769    1.00 41.38  ? 407  ILE   B CA  1 
ATOM   4235  C  C   . ILE   B  1 106 ? -45.889 0.865   8.371    1.00 53.37  ? 407  ILE   B C   1 
ATOM   4236  O  O   . ILE   B  1 106 ? -45.089 0.859   7.427    1.00 51.99  ? 407  ILE   B O   1 
ATOM   4237  C  CB  . ILE   B  1 106 ? -45.098 0.047   10.623   1.00 37.58  ? 407  ILE   B CB  1 
ATOM   4238  C  CG1 . ILE   B  1 106 ? -44.446 0.486   11.929   1.00 31.27  ? 407  ILE   B CG1 1 
ATOM   4239  C  CG2 . ILE   B  1 106 ? -44.181 -0.890  9.833    1.00 40.76  ? 407  ILE   B CG2 1 
ATOM   4240  C  CD1 . ILE   B  1 106 ? -44.837 -0.397  13.081   1.00 32.11  ? 407  ILE   B CD1 1 
ATOM   4241  N  N   . TYR   B  1 107 ? -47.169 0.521   8.224    1.00 51.11  ? 408  TYR   B N   1 
ATOM   4242  C  CA  . TYR   B  1 107 ? -47.718 0.171   6.925    1.00 53.86  ? 408  TYR   B CA  1 
ATOM   4243  C  C   . TYR   B  1 107 ? -47.516 1.304   5.925    1.00 51.49  ? 408  TYR   B C   1 
ATOM   4244  O  O   . TYR   B  1 107 ? -46.943 1.107   4.846    1.00 45.13  ? 408  TYR   B O   1 
ATOM   4245  C  CB  . TYR   B  1 107 ? -49.197 -0.172  7.089    1.00 53.69  ? 408  TYR   B CB  1 
ATOM   4246  C  CG  . TYR   B  1 107 ? -49.923 -0.317  5.791    1.00 60.19  ? 408  TYR   B CG  1 
ATOM   4247  C  CD1 . TYR   B  1 107 ? -49.832 -1.495  5.052    1.00 65.41  ? 408  TYR   B CD1 1 
ATOM   4248  C  CD2 . TYR   B  1 107 ? -50.697 0.729   5.286    1.00 59.01  ? 408  TYR   B CD2 1 
ATOM   4249  C  CE1 . TYR   B  1 107 ? -50.500 -1.634  3.837    1.00 62.79  ? 408  TYR   B CE1 1 
ATOM   4250  C  CE2 . TYR   B  1 107 ? -51.373 0.603   4.075    1.00 50.68  ? 408  TYR   B CE2 1 
ATOM   4251  C  CZ  . TYR   B  1 107 ? -51.272 -0.585  3.355    1.00 61.05  ? 408  TYR   B CZ  1 
ATOM   4252  O  OH  . TYR   B  1 107 ? -51.934 -0.724  2.146    1.00 73.13  ? 408  TYR   B OH  1 
ATOM   4253  N  N   . GLY   B  1 108 ? -47.953 2.509   6.286    1.00 47.89  ? 409  GLY   B N   1 
ATOM   4254  C  CA  . GLY   B  1 108 ? -47.825 3.636   5.378    1.00 42.36  ? 409  GLY   B CA  1 
ATOM   4255  C  C   . GLY   B  1 108 ? -46.385 3.974   5.038    1.00 49.41  ? 409  GLY   B C   1 
ATOM   4256  O  O   . GLY   B  1 108 ? -46.072 4.299   3.890    1.00 63.48  ? 409  GLY   B O   1 
ATOM   4257  N  N   . ALA   B  1 109 ? -45.487 3.908   6.025    1.00 45.03  ? 410  ALA   B N   1 
ATOM   4258  C  CA  . ALA   B  1 109 ? -44.090 4.220   5.736    1.00 44.44  ? 410  ALA   B CA  1 
ATOM   4259  C  C   . ALA   B  1 109 ? -43.521 3.248   4.711    1.00 40.89  ? 410  ALA   B C   1 
ATOM   4260  O  O   . ALA   B  1 109 ? -42.814 3.648   3.786    1.00 45.17  ? 410  ALA   B O   1 
ATOM   4261  C  CB  . ALA   B  1 109 ? -43.265 4.187   7.018    1.00 34.20  ? 410  ALA   B CB  1 
ATOM   4262  N  N   . LYS   B  1 110 ? -43.828 1.967   4.857    1.00 42.89  ? 411  LYS   B N   1 
ATOM   4263  C  CA  . LYS   B  1 110 ? -43.323 0.991   3.910    1.00 40.15  ? 411  LYS   B CA  1 
ATOM   4264  C  C   . LYS   B  1 110 ? -43.946 1.208   2.544    1.00 46.51  ? 411  LYS   B C   1 
ATOM   4265  O  O   . LYS   B  1 110 ? -43.280 1.039   1.521    1.00 51.82  ? 411  LYS   B O   1 
ATOM   4266  C  CB  . LYS   B  1 110 ? -43.610 -0.421  4.421    1.00 40.84  ? 411  LYS   B CB  1 
ATOM   4267  C  CG  . LYS   B  1 110 ? -42.457 -1.038  5.171    1.00 38.16  ? 411  LYS   B CG  1 
ATOM   4268  C  CD  . LYS   B  1 110 ? -42.914 -1.899  6.314    1.00 40.08  ? 411  LYS   B CD  1 
ATOM   4269  C  CE  . LYS   B  1 110 ? -41.711 -2.553  7.001    1.00 41.53  ? 411  LYS   B CE  1 
ATOM   4270  N  NZ  . LYS   B  1 110 ? -42.118 -3.635  7.950    1.00 35.36  ? 411  LYS   B NZ  1 
ATOM   4271  N  N   . HIS   B  1 111 ? -45.212 1.613   2.506    1.00 46.22  ? 412  HIS   B N   1 
ATOM   4272  C  CA  . HIS   B  1 111 ? -45.882 1.754   1.224    1.00 49.06  ? 412  HIS   B CA  1 
ATOM   4273  C  C   . HIS   B  1 111 ? -45.511 3.051   0.515    1.00 59.73  ? 412  HIS   B C   1 
ATOM   4274  O  O   . HIS   B  1 111 ? -45.577 3.116   -0.721   1.00 58.70  ? 412  HIS   B O   1 
ATOM   4275  C  CB  . HIS   B  1 111 ? -47.394 1.628   1.406    1.00 42.78  ? 412  HIS   B CB  1 
ATOM   4276  C  CG  . HIS   B  1 111 ? -47.866 0.210   1.394    1.00 45.94  ? 412  HIS   B CG  1 
ATOM   4277  N  ND1 . HIS   B  1 111 ? -47.253 -0.774  2.136    1.00 52.81  ? 412  HIS   B ND1 1 
ATOM   4278  C  CD2 . HIS   B  1 111 ? -48.860 -0.402  0.708    1.00 53.80  ? 412  HIS   B CD2 1 
ATOM   4279  C  CE1 . HIS   B  1 111 ? -47.855 -1.929  1.919    1.00 54.88  ? 412  HIS   B CE1 1 
ATOM   4280  N  NE2 . HIS   B  1 111 ? -48.836 -1.732  1.058    1.00 55.19  ? 412  HIS   B NE2 1 
ATOM   4281  N  N   . ALA   B  1 112 ? -45.106 4.087   1.252    1.00 48.73  ? 413  ALA   B N   1 
ATOM   4282  C  CA  . ALA   B  1 112 ? -44.578 5.255   0.560    1.00 46.12  ? 413  ALA   B CA  1 
ATOM   4283  C  C   . ALA   B  1 112 ? -43.262 4.923   -0.136   1.00 47.23  ? 413  ALA   B C   1 
ATOM   4284  O  O   . ALA   B  1 112 ? -43.022 5.367   -1.266   1.00 44.26  ? 413  ALA   B O   1 
ATOM   4285  C  CB  . ALA   B  1 112 ? -44.400 6.409   1.533    1.00 46.81  ? 413  ALA   B CB  1 
ATOM   4286  N  N   . TRP   B  1 113 ? -42.406 4.132   0.519    1.00 39.37  ? 414  TRP   B N   1 
ATOM   4287  C  CA  . TRP   B  1 113 ? -41.216 3.623   -0.152   1.00 41.72  ? 414  TRP   B CA  1 
ATOM   4288  C  C   . TRP   B  1 113 ? -41.591 2.740   -1.335   1.00 46.03  ? 414  TRP   B C   1 
ATOM   4289  O  O   . TRP   B  1 113 ? -40.998 2.844   -2.414   1.00 48.63  ? 414  TRP   B O   1 
ATOM   4290  C  CB  . TRP   B  1 113 ? -40.344 2.846   0.834    1.00 31.32  ? 414  TRP   B CB  1 
ATOM   4291  C  CG  . TRP   B  1 113 ? -39.045 2.337   0.259    1.00 40.14  ? 414  TRP   B CG  1 
ATOM   4292  C  CD1 . TRP   B  1 113 ? -38.508 2.626   -0.980   1.00 39.53  ? 414  TRP   B CD1 1 
ATOM   4293  C  CD2 . TRP   B  1 113 ? -38.116 1.447   0.896    1.00 41.27  ? 414  TRP   B CD2 1 
ATOM   4294  N  NE1 . TRP   B  1 113 ? -37.312 1.967   -1.138   1.00 38.88  ? 414  TRP   B NE1 1 
ATOM   4295  C  CE2 . TRP   B  1 113 ? -37.047 1.247   0.003    1.00 42.65  ? 414  TRP   B CE2 1 
ATOM   4296  C  CE3 . TRP   B  1 113 ? -38.078 0.813   2.143    1.00 48.58  ? 414  TRP   B CE3 1 
ATOM   4297  C  CZ2 . TRP   B  1 113 ? -35.962 0.428   0.317    1.00 52.33  ? 414  TRP   B CZ2 1 
ATOM   4298  C  CZ3 . TRP   B  1 113 ? -36.998 -0.000  2.451    1.00 43.14  ? 414  TRP   B CZ3 1 
ATOM   4299  C  CH2 . TRP   B  1 113 ? -35.957 -0.182  1.548    1.00 51.70  ? 414  TRP   B CH2 1 
ATOM   4300  N  N   . ARG   B  1 114 ? -42.563 1.856   -1.144   1.00 44.56  ? 415  ARG   B N   1 
ATOM   4301  C  CA  . ARG   B  1 114 ? -42.943 0.914   -2.182   1.00 37.77  ? 415  ARG   B CA  1 
ATOM   4302  C  C   . ARG   B  1 114 ? -43.568 1.616   -3.385   1.00 51.40  ? 415  ARG   B C   1 
ATOM   4303  O  O   . ARG   B  1 114 ? -43.513 1.087   -4.501   1.00 62.92  ? 415  ARG   B O   1 
ATOM   4304  C  CB  . ARG   B  1 114 ? -43.914 -0.107  -1.578   1.00 29.06  ? 415  ARG   B CB  1 
ATOM   4305  C  CG  . ARG   B  1 114 ? -44.374 -1.165  -2.536   1.00 28.81  ? 415  ARG   B CG  1 
ATOM   4306  C  CD  . ARG   B  1 114 ? -45.611 -1.885  -2.027   1.00 32.68  ? 415  ARG   B CD  1 
ATOM   4307  N  NE  . ARG   B  1 114 ? -45.794 -3.141  -2.733   1.00 39.80  ? 415  ARG   B NE  1 
ATOM   4308  C  CZ  . ARG   B  1 114 ? -46.774 -3.984  -2.475   1.00 43.83  ? 415  ARG   B CZ  1 
ATOM   4309  N  NH1 . ARG   B  1 114 ? -46.877 -5.108  -3.169   1.00 43.35  ? 415  ARG   B NH1 1 
ATOM   4310  N  NH2 . ARG   B  1 114 ? -47.648 -3.694  -1.520   1.00 47.20  ? 415  ARG   B NH2 1 
ATOM   4311  N  N   . ASN   B  1 115 ? -44.150 2.794   -3.178   1.00 47.65  ? 416  ASN   B N   1 
ATOM   4312  C  CA  . ASN   B  1 115 ? -44.781 3.582   -4.222   1.00 39.21  ? 416  ASN   B CA  1 
ATOM   4313  C  C   . ASN   B  1 115 ? -43.842 4.590   -4.848   1.00 45.90  ? 416  ASN   B C   1 
ATOM   4314  O  O   . ASN   B  1 115 ? -44.268 5.365   -5.714   1.00 54.12  ? 416  ASN   B O   1 
ATOM   4315  C  CB  . ASN   B  1 115 ? -45.979 4.332   -3.654   1.00 33.85  ? 416  ASN   B CB  1 
ATOM   4316  C  CG  . ASN   B  1 115 ? -47.054 3.410   -3.185   1.00 45.54  ? 416  ASN   B CG  1 
ATOM   4317  O  OD1 . ASN   B  1 115 ? -47.032 2.212   -3.494   1.00 45.38  ? 416  ASN   B OD1 1 
ATOM   4318  N  ND2 . ASN   B  1 115 ? -48.012 3.949   -2.428   1.00 50.55  ? 416  ASN   B ND2 1 
ATOM   4319  N  N   . ALA   B  1 116 ? -42.599 4.637   -4.400   1.00 40.37  ? 417  ALA   B N   1 
ATOM   4320  C  CA  . ALA   B  1 116 ? -41.682 5.667   -4.863   1.00 42.89  ? 417  ALA   B CA  1 
ATOM   4321  C  C   . ALA   B  1 116 ? -41.224 5.259   -6.258   1.00 50.70  ? 417  ALA   B C   1 
ATOM   4322  O  O   . ALA   B  1 116 ? -40.382 4.369   -6.422   1.00 44.82  ? 417  ALA   B O   1 
ATOM   4323  C  CB  . ALA   B  1 116 ? -40.522 5.835   -3.887   1.00 29.61  ? 417  ALA   B CB  1 
ATOM   4324  N  N   . SER   B  1 117 ? -41.796 5.917   -7.269   1.00 44.26  ? 418  SER   B N   1 
ATOM   4325  C  CA  A SER   B  1 117 ? -41.562 5.513   -8.648   0.60 46.46  ? 418  SER   B CA  1 
ATOM   4326  C  CA  B SER   B  1 117 ? -41.562 5.523   -8.654   0.40 46.28  ? 418  SER   B CA  1 
ATOM   4327  C  C   . SER   B  1 117 ? -40.116 5.704   -9.084   1.00 49.47  ? 418  SER   B C   1 
ATOM   4328  O  O   . SER   B  1 117 ? -39.693 5.067   -10.055  1.00 49.28  ? 418  SER   B O   1 
ATOM   4329  C  CB  A SER   B  1 117 ? -42.489 6.291   -9.585   0.60 43.97  ? 418  SER   B CB  1 
ATOM   4330  C  CB  B SER   B  1 117 ? -42.463 6.325   -9.592   0.40 43.98  ? 418  SER   B CB  1 
ATOM   4331  O  OG  A SER   B  1 117 ? -42.276 7.688   -9.477   0.60 41.86  ? 418  SER   B OG  1 
ATOM   4332  O  OG  B SER   B  1 117 ? -43.801 5.875   -9.527   0.40 40.16  ? 418  SER   B OG  1 
ATOM   4333  N  N   . ARG   B  1 118 ? -39.349 6.555   -8.394   1.00 36.04  ? 419  ARG   B N   1 
ATOM   4334  C  CA  . ARG   B  1 118 ? -37.986 6.823   -8.812   1.00 27.65  ? 419  ARG   B CA  1 
ATOM   4335  C  C   . ARG   B  1 118 ? -36.952 5.924   -8.160   1.00 39.84  ? 419  ARG   B C   1 
ATOM   4336  O  O   . ARG   B  1 118 ? -35.780 5.995   -8.536   1.00 44.72  ? 419  ARG   B O   1 
ATOM   4337  C  CB  . ARG   B  1 118 ? -37.649 8.280   -8.536   1.00 31.02  ? 419  ARG   B CB  1 
ATOM   4338  C  CG  . ARG   B  1 118 ? -38.661 9.215   -9.202   1.00 42.34  ? 419  ARG   B CG  1 
ATOM   4339  C  CD  . ARG   B  1 118 ? -38.318 10.679  -8.987   1.00 40.65  ? 419  ARG   B CD  1 
ATOM   4340  N  NE  . ARG   B  1 118 ? -38.888 11.526  -10.028  1.00 41.95  ? 419  ARG   B NE  1 
ATOM   4341  C  CZ  . ARG   B  1 118 ? -38.962 12.853  -9.959   1.00 50.75  ? 419  ARG   B CZ  1 
ATOM   4342  N  NH1 . ARG   B  1 118 ? -38.514 13.483  -8.882   1.00 51.54  ? 419  ARG   B NH1 1 
ATOM   4343  N  NH2 . ARG   B  1 118 ? -39.503 13.550  -10.956  1.00 50.08  ? 419  ARG   B NH2 1 
ATOM   4344  N  N   . CYS   B  1 119 ? -37.340 5.068   -7.219   1.00 37.59  ? 420  CYS   B N   1 
ATOM   4345  C  CA  . CYS   B  1 119 ? -36.365 4.334   -6.425   1.00 39.45  ? 420  CYS   B CA  1 
ATOM   4346  C  C   . CYS   B  1 119 ? -36.070 2.986   -7.070   1.00 33.70  ? 420  CYS   B C   1 
ATOM   4347  O  O   . CYS   B  1 119 ? -36.941 2.098   -7.106   1.00 29.54  ? 420  CYS   B O   1 
ATOM   4348  C  CB  . CYS   B  1 119 ? -36.861 4.140   -4.987   1.00 44.43  ? 420  CYS   B CB  1 
ATOM   4349  S  SG  . CYS   B  1 119 ? -35.738 3.155   -3.943   1.00 46.37  ? 420  CYS   B SG  1 
ATOM   4350  N  N   . VAL   B  1 120 ? -34.826 2.819   -7.524   1.00 33.17  ? 421  VAL   B N   1 
ATOM   4351  C  CA  . VAL   B  1 120 ? -34.378 1.538   -8.050   1.00 34.10  ? 421  VAL   B CA  1 
ATOM   4352  C  C   . VAL   B  1 120 ? -34.257 0.482   -6.963   1.00 43.53  ? 421  VAL   B C   1 
ATOM   4353  O  O   . VAL   B  1 120 ? -34.280 -0.716  -7.271   1.00 44.90  ? 421  VAL   B O   1 
ATOM   4354  C  CB  . VAL   B  1 120 ? -33.039 1.717   -8.791   1.00 39.69  ? 421  VAL   B CB  1 
ATOM   4355  C  CG1 . VAL   B  1 120 ? -31.939 2.062   -7.816   1.00 36.39  ? 421  VAL   B CG1 1 
ATOM   4356  C  CG2 . VAL   B  1 120 ? -32.684 0.467   -9.627   1.00 36.66  ? 421  VAL   B CG2 1 
ATOM   4357  N  N   . GLY   B  1 121 ? -34.170 0.888   -5.690   1.00 45.22  ? 422  GLY   B N   1 
ATOM   4358  C  CA  . GLY   B  1 121 ? -33.907 0.010   -4.572   1.00 38.75  ? 422  GLY   B CA  1 
ATOM   4359  C  C   . GLY   B  1 121 ? -35.105 -0.609  -3.883   1.00 45.95  ? 422  GLY   B C   1 
ATOM   4360  O  O   . GLY   B  1 121 ? -34.929 -1.220  -2.821   1.00 51.25  ? 422  GLY   B O   1 
ATOM   4361  N  N   . ARG   B  1 122 ? -36.312 -0.525  -4.461   1.00 37.98  ? 423  ARG   B N   1 
ATOM   4362  C  CA  . ARG   B  1 122 ? -37.527 -0.950  -3.758   1.00 39.53  ? 423  ARG   B CA  1 
ATOM   4363  C  C   . ARG   B  1 122 ? -37.696 -2.461  -3.624   1.00 44.33  ? 423  ARG   B C   1 
ATOM   4364  O  O   . ARG   B  1 122 ? -38.713 -2.874  -3.060   1.00 51.71  ? 423  ARG   B O   1 
ATOM   4365  C  CB  . ARG   B  1 122 ? -38.771 -0.410  -4.452   1.00 28.87  ? 423  ARG   B CB  1 
ATOM   4366  C  CG  . ARG   B  1 122 ? -38.972 1.075   -4.363   1.00 31.13  ? 423  ARG   B CG  1 
ATOM   4367  C  CD  . ARG   B  1 122 ? -40.178 1.454   -5.232   1.00 42.18  ? 423  ARG   B CD  1 
ATOM   4368  N  NE  . ARG   B  1 122 ? -39.811 1.724   -6.629   1.00 35.58  ? 423  ARG   B NE  1 
ATOM   4369  C  CZ  . ARG   B  1 122 ? -40.683 1.846   -7.641   1.00 48.59  ? 423  ARG   B CZ  1 
ATOM   4370  N  NH1 . ARG   B  1 122 ? -41.988 1.696   -7.425   1.00 36.15  ? 423  ARG   B NH1 1 
ATOM   4371  N  NH2 . ARG   B  1 122 ? -40.254 2.112   -8.880   1.00 47.74  ? 423  ARG   B NH2 1 
ATOM   4372  N  N   . ILE   B  1 123 ? -36.775 -3.295  -4.114   1.00 38.26  ? 424  ILE   B N   1 
ATOM   4373  C  CA  . ILE   B  1 123 ? -36.893 -4.728  -3.852   1.00 37.57  ? 424  ILE   B CA  1 
ATOM   4374  C  C   . ILE   B  1 123 ? -36.953 -4.999  -2.343   1.00 46.51  ? 424  ILE   B C   1 
ATOM   4375  O  O   . ILE   B  1 123 ? -37.560 -5.987  -1.906   1.00 43.56  ? 424  ILE   B O   1 
ATOM   4376  C  CB  . ILE   B  1 123 ? -35.741 -5.496  -4.540   1.00 33.58  ? 424  ILE   B CB  1 
ATOM   4377  C  CG1 . ILE   B  1 123 ? -35.917 -7.007  -4.388   1.00 38.54  ? 424  ILE   B CG1 1 
ATOM   4378  C  CG2 . ILE   B  1 123 ? -34.376 -5.098  -3.968   1.00 44.49  ? 424  ILE   B CG2 1 
ATOM   4379  C  CD1 . ILE   B  1 123 ? -36.976 -7.615  -5.289   1.00 45.74  ? 424  ILE   B CD1 1 
ATOM   4380  N  N   . GLN   B  1 124 ? -36.390 -4.099  -1.525   1.00 49.41  ? 425  GLN   B N   1 
ATOM   4381  C  CA  . GLN   B  1 124 ? -36.300 -4.246  -0.071   1.00 48.90  ? 425  GLN   B CA  1 
ATOM   4382  C  C   . GLN   B  1 124 ? -37.440 -3.589  0.697    1.00 56.54  ? 425  GLN   B C   1 
ATOM   4383  O  O   . GLN   B  1 124 ? -37.357 -3.503  1.923    1.00 67.65  ? 425  GLN   B O   1 
ATOM   4384  C  CB  . GLN   B  1 124 ? -35.007 -3.624  0.444    1.00 53.50  ? 425  GLN   B CB  1 
ATOM   4385  C  CG  . GLN   B  1 124 ? -33.793 -3.936  -0.353   1.00 60.87  ? 425  GLN   B CG  1 
ATOM   4386  C  CD  . GLN   B  1 124 ? -33.206 -5.270  0.010    1.00 71.78  ? 425  GLN   B CD  1 
ATOM   4387  O  OE1 . GLN   B  1 124 ? -33.613 -5.902  0.989    1.00 74.28  ? 425  GLN   B OE1 1 
ATOM   4388  N  NE2 . GLN   B  1 124 ? -32.233 -5.714  -0.780   1.00 85.00  ? 425  GLN   B NE2 1 
ATOM   4389  N  N   . TRP   B  1 125 ? -38.484 -3.113  0.016    1.00 61.46  ? 426  TRP   B N   1 
ATOM   4390  C  CA  . TRP   B  1 125 ? -39.379 -2.118  0.603    1.00 51.59  ? 426  TRP   B CA  1 
ATOM   4391  C  C   . TRP   B  1 125 ? -40.006 -2.594  1.913    1.00 51.13  ? 426  TRP   B C   1 
ATOM   4392  O  O   . TRP   B  1 125 ? -40.198 -1.794  2.834    1.00 48.01  ? 426  TRP   B O   1 
ATOM   4393  C  CB  . TRP   B  1 125 ? -40.466 -1.747  -0.405   1.00 48.28  ? 426  TRP   B CB  1 
ATOM   4394  C  CG  . TRP   B  1 125 ? -41.425 -2.849  -0.629   1.00 41.85  ? 426  TRP   B CG  1 
ATOM   4395  C  CD1 . TRP   B  1 125 ? -41.298 -3.876  -1.510   1.00 42.84  ? 426  TRP   B CD1 1 
ATOM   4396  C  CD2 . TRP   B  1 125 ? -42.659 -3.063  0.070    1.00 41.89  ? 426  TRP   B CD2 1 
ATOM   4397  N  NE1 . TRP   B  1 125 ? -42.384 -4.722  -1.406   1.00 51.73  ? 426  TRP   B NE1 1 
ATOM   4398  C  CE2 . TRP   B  1 125 ? -43.229 -4.242  -0.439   1.00 44.87  ? 426  TRP   B CE2 1 
ATOM   4399  C  CE3 . TRP   B  1 125 ? -43.337 -2.367  1.072    1.00 48.41  ? 426  TRP   B CE3 1 
ATOM   4400  C  CZ2 . TRP   B  1 125 ? -44.453 -4.739  0.015    1.00 35.27  ? 426  TRP   B CZ2 1 
ATOM   4401  C  CZ3 . TRP   B  1 125 ? -44.553 -2.866  1.523    1.00 48.69  ? 426  TRP   B CZ3 1 
ATOM   4402  C  CH2 . TRP   B  1 125 ? -45.098 -4.037  0.990    1.00 34.16  ? 426  TRP   B CH2 1 
ATOM   4403  N  N   . SER   B  1 126 ? -40.348 -3.883  2.017    1.00 47.46  ? 427  SER   B N   1 
ATOM   4404  C  CA  . SER   B  1 126 ? -40.998 -4.390  3.220    1.00 50.46  ? 427  SER   B CA  1 
ATOM   4405  C  C   . SER   B  1 126 ? -40.026 -4.680  4.363    1.00 57.52  ? 427  SER   B C   1 
ATOM   4406  O  O   . SER   B  1 126 ? -40.469 -5.017  5.470    1.00 54.92  ? 427  SER   B O   1 
ATOM   4407  C  CB  . SER   B  1 126 ? -41.791 -5.650  2.882    1.00 59.15  ? 427  SER   B CB  1 
ATOM   4408  O  OG  . SER   B  1 126 ? -40.943 -6.616  2.295    1.00 68.88  ? 427  SER   B OG  1 
ATOM   4409  N  N   . LYS   B  1 127 ? -38.723 -4.564  4.122    1.00 55.79  ? 428  LYS   B N   1 
ATOM   4410  C  CA  . LYS   B  1 127 ? -37.707 -4.749  5.158    1.00 61.84  ? 428  LYS   B CA  1 
ATOM   4411  C  C   . LYS   B  1 127 ? -37.150 -3.377  5.540    1.00 59.91  ? 428  LYS   B C   1 
ATOM   4412  O  O   . LYS   B  1 127 ? -36.015 -3.011  5.243    1.00 70.94  ? 428  LYS   B O   1 
ATOM   4413  C  CB  . LYS   B  1 127 ? -36.618 -5.701  4.669    1.00 62.69  ? 428  LYS   B CB  1 
ATOM   4414  C  CG  . LYS   B  1 127 ? -35.573 -6.039  5.714    1.00 75.04  ? 428  LYS   B CG  1 
ATOM   4415  C  CD  . LYS   B  1 127 ? -34.260 -6.503  5.091    1.00 78.08  ? 428  LYS   B CD  1 
ATOM   4416  C  CE  . LYS   B  1 127 ? -33.123 -6.453  6.115    1.00 78.52  ? 428  LYS   B CE  1 
ATOM   4417  N  NZ  . LYS   B  1 127 ? -32.231 -7.650  6.108    1.00 77.04  ? 428  LYS   B NZ  1 
ATOM   4418  N  N   . LEU   B  1 128 ? -38.018 -2.589  6.167    1.00 46.68  ? 429  LEU   B N   1 
ATOM   4419  C  CA  . LEU   B  1 128 ? -37.714 -1.230  6.585    1.00 37.73  ? 429  LEU   B CA  1 
ATOM   4420  C  C   . LEU   B  1 128 ? -37.907 -1.148  8.088    1.00 53.75  ? 429  LEU   B C   1 
ATOM   4421  O  O   . LEU   B  1 128 ? -38.751 -1.848  8.658    1.00 67.39  ? 429  LEU   B O   1 
ATOM   4422  C  CB  . LEU   B  1 128 ? -38.635 -0.208  5.915    1.00 24.91  ? 429  LEU   B CB  1 
ATOM   4423  C  CG  . LEU   B  1 128 ? -38.466 1.279   6.259    1.00 22.79  ? 429  LEU   B CG  1 
ATOM   4424  C  CD1 . LEU   B  1 128 ? -37.148 1.855   5.740    1.00 22.43  ? 429  LEU   B CD1 1 
ATOM   4425  C  CD2 . LEU   B  1 128 ? -39.624 2.072   5.687    1.00 23.65  ? 429  LEU   B CD2 1 
ATOM   4426  N  N   . GLN   B  1 129 ? -37.120 -0.302  8.732    1.00 41.52  ? 430  GLN   B N   1 
ATOM   4427  C  CA  . GLN   B  1 129 ? -37.174 -0.144  10.173   1.00 34.73  ? 430  GLN   B CA  1 
ATOM   4428  C  C   . GLN   B  1 129 ? -37.697 1.257   10.468   1.00 45.74  ? 430  GLN   B C   1 
ATOM   4429  O  O   . GLN   B  1 129 ? -37.054 2.247   10.105   1.00 53.66  ? 430  GLN   B O   1 
ATOM   4430  C  CB  . GLN   B  1 129 ? -35.793 -0.379  10.780   1.00 39.89  ? 430  GLN   B CB  1 
ATOM   4431  C  CG  . GLN   B  1 129 ? -35.748 -0.267  12.285   1.00 45.94  ? 430  GLN   B CG  1 
ATOM   4432  C  CD  . GLN   B  1 129 ? -36.434 -1.420  12.953   1.00 50.67  ? 430  GLN   B CD  1 
ATOM   4433  O  OE1 . GLN   B  1 129 ? -36.157 -2.588  12.659   1.00 49.88  ? 430  GLN   B OE1 1 
ATOM   4434  N  NE2 . GLN   B  1 129 ? -37.350 -1.109  13.848   1.00 55.66  ? 430  GLN   B NE2 1 
ATOM   4435  N  N   . VAL   B  1 130 ? -38.870 1.337   11.101   1.00 49.61  ? 431  VAL   B N   1 
ATOM   4436  C  CA  . VAL   B  1 130 ? -39.546 2.602   11.392   1.00 38.13  ? 431  VAL   B CA  1 
ATOM   4437  C  C   . VAL   B  1 130 ? -39.297 2.958   12.849   1.00 44.62  ? 431  VAL   B C   1 
ATOM   4438  O  O   . VAL   B  1 130 ? -39.578 2.153   13.742   1.00 48.42  ? 431  VAL   B O   1 
ATOM   4439  C  CB  . VAL   B  1 130 ? -41.057 2.496   11.111   1.00 32.38  ? 431  VAL   B CB  1 
ATOM   4440  C  CG1 . VAL   B  1 130 ? -41.764 3.804   11.403   1.00 30.64  ? 431  VAL   B CG1 1 
ATOM   4441  C  CG2 . VAL   B  1 130 ? -41.293 2.082   9.680    1.00 40.51  ? 431  VAL   B CG2 1 
ATOM   4442  N  N   . PHE   B  1 131 ? -38.775 4.156   13.093   1.00 38.53  ? 432  PHE   B N   1 
ATOM   4443  C  CA  . PHE   B  1 131 ? -38.528 4.669   14.436   1.00 34.99  ? 432  PHE   B CA  1 
ATOM   4444  C  C   . PHE   B  1 131 ? -39.540 5.774   14.695   1.00 42.73  ? 432  PHE   B C   1 
ATOM   4445  O  O   . PHE   B  1 131 ? -39.384 6.896   14.202   1.00 45.30  ? 432  PHE   B O   1 
ATOM   4446  C  CB  . PHE   B  1 131 ? -37.104 5.191   14.576   1.00 39.90  ? 432  PHE   B CB  1 
ATOM   4447  C  CG  . PHE   B  1 131 ? -36.067 4.125   14.481   1.00 46.77  ? 432  PHE   B CG  1 
ATOM   4448  C  CD1 . PHE   B  1 131 ? -36.227 2.927   15.155   1.00 39.75  ? 432  PHE   B CD1 1 
ATOM   4449  C  CD2 . PHE   B  1 131 ? -34.941 4.306   13.700   1.00 47.18  ? 432  PHE   B CD2 1 
ATOM   4450  C  CE1 . PHE   B  1 131 ? -35.293 1.937   15.051   1.00 36.41  ? 432  PHE   B CE1 1 
ATOM   4451  C  CE2 . PHE   B  1 131 ? -33.988 3.322   13.615   1.00 45.52  ? 432  PHE   B CE2 1 
ATOM   4452  C  CZ  . PHE   B  1 131 ? -34.163 2.139   14.280   1.00 42.86  ? 432  PHE   B CZ  1 
ATOM   4453  N  N   . ASP   B  1 132 ? -40.570 5.452   15.474   1.00 39.17  ? 433  ASP   B N   1 
ATOM   4454  C  CA  . ASP   B  1 132 ? -41.618 6.413   15.781   1.00 32.81  ? 433  ASP   B CA  1 
ATOM   4455  C  C   . ASP   B  1 132 ? -41.074 7.475   16.725   1.00 40.03  ? 433  ASP   B C   1 
ATOM   4456  O  O   . ASP   B  1 132 ? -40.527 7.162   17.785   1.00 55.67  ? 433  ASP   B O   1 
ATOM   4457  C  CB  . ASP   B  1 132 ? -42.802 5.694   16.415   1.00 25.57  ? 433  ASP   B CB  1 
ATOM   4458  C  CG  . ASP   B  1 132 ? -43.964 6.603   16.681   1.00 37.07  ? 433  ASP   B CG  1 
ATOM   4459  O  OD1 . ASP   B  1 132 ? -45.043 6.044   16.988   1.00 48.49  ? 433  ASP   B OD1 1 
ATOM   4460  O  OD2 . ASP   B  1 132 ? -43.821 7.856   16.584   1.00 32.00  ? 433  ASP   B OD2 1 
ATOM   4461  N  N   . ALA   B  1 133 ? -41.211 8.729   16.328   1.00 36.69  ? 434  ALA   B N   1 
ATOM   4462  C  CA  . ALA   B  1 133 ? -40.643 9.848   17.064   1.00 25.51  ? 434  ALA   B CA  1 
ATOM   4463  C  C   . ALA   B  1 133 ? -41.664 10.953  17.181   1.00 39.71  ? 434  ALA   B C   1 
ATOM   4464  O  O   . ALA   B  1 133 ? -41.309 12.139  17.230   1.00 35.62  ? 434  ALA   B O   1 
ATOM   4465  C  CB  . ALA   B  1 133 ? -39.380 10.390  16.388   1.00 35.63  ? 434  ALA   B CB  1 
ATOM   4466  N  N   . ARG   B  1 134 ? -42.941 10.581  17.178   1.00 29.98  ? 435  ARG   B N   1 
ATOM   4467  C  CA  . ARG   B  1 134 ? -43.998 11.569  17.272   1.00 39.67  ? 435  ARG   B CA  1 
ATOM   4468  C  C   . ARG   B  1 134 ? -44.099 12.182  18.660   1.00 49.00  ? 435  ARG   B C   1 
ATOM   4469  O  O   . ARG   B  1 134 ? -44.794 13.189  18.818   1.00 64.58  ? 435  ARG   B O   1 
ATOM   4470  C  CB  . ARG   B  1 134 ? -45.309 10.917  16.854   1.00 41.78  ? 435  ARG   B CB  1 
ATOM   4471  C  CG  . ARG   B  1 134 ? -45.275 10.495  15.386   1.00 42.45  ? 435  ARG   B CG  1 
ATOM   4472  C  CD  . ARG   B  1 134 ? -46.504 9.750   14.994   1.00 39.80  ? 435  ARG   B CD  1 
ATOM   4473  N  NE  . ARG   B  1 134 ? -46.501 8.390   15.515   1.00 40.13  ? 435  ARG   B NE  1 
ATOM   4474  C  CZ  . ARG   B  1 134 ? -47.577 7.610   15.490   1.00 47.69  ? 435  ARG   B CZ  1 
ATOM   4475  N  NH1 . ARG   B  1 134 ? -48.711 8.086   14.973   1.00 50.64  ? 435  ARG   B NH1 1 
ATOM   4476  N  NH2 . ARG   B  1 134 ? -47.533 6.374   15.971   1.00 46.34  ? 435  ARG   B NH2 1 
ATOM   4477  N  N   . ASP   B  1 135 ? -43.405 11.623  19.656   1.00 44.82  ? 436  ASP   B N   1 
ATOM   4478  C  CA  . ASP   B  1 135 ? -43.384 12.211  20.989   1.00 46.55  ? 436  ASP   B CA  1 
ATOM   4479  C  C   . ASP   B  1 135 ? -42.413 13.378  21.084   1.00 50.29  ? 436  ASP   B C   1 
ATOM   4480  O  O   . ASP   B  1 135 ? -42.381 14.053  22.115   1.00 60.14  ? 436  ASP   B O   1 
ATOM   4481  C  CB  . ASP   B  1 135 ? -43.041 11.139  22.027   1.00 43.60  ? 436  ASP   B CB  1 
ATOM   4482  C  CG  . ASP   B  1 135 ? -41.614 10.642  21.909   1.00 53.61  ? 436  ASP   B CG  1 
ATOM   4483  O  OD1 . ASP   B  1 135 ? -41.171 9.828   22.756   1.00 55.31  ? 436  ASP   B OD1 1 
ATOM   4484  O  OD2 . ASP   B  1 135 ? -40.925 11.062  20.965   1.00 57.88  ? 436  ASP   B OD2 1 
ATOM   4485  N  N   . CYS   B  1 136 ? -41.665 13.652  20.018   1.00 43.18  ? 437  CYS   B N   1 
ATOM   4486  C  CA  . CYS   B  1 136 ? -40.570 14.615  20.063   1.00 39.96  ? 437  CYS   B CA  1 
ATOM   4487  C  C   . CYS   B  1 136 ? -41.080 16.048  20.177   1.00 42.34  ? 437  CYS   B C   1 
ATOM   4488  O  O   . CYS   B  1 136 ? -42.116 16.398  19.609   1.00 40.08  ? 437  CYS   B O   1 
ATOM   4489  C  CB  . CYS   B  1 136 ? -39.709 14.453  18.816   1.00 36.05  ? 437  CYS   B CB  1 
ATOM   4490  S  SG  . CYS   B  1 136 ? -38.139 15.301  18.852   1.00 46.91  ? 437  CYS   B SG  1 
ATOM   4491  N  N   . THR   B  1 137 ? -40.365 16.880  20.957   1.00 50.82  ? 438  THR   B N   1 
ATOM   4492  C  CA  . THR   B  1 137 ? -40.786 18.264  21.179   1.00 42.62  ? 438  THR   B CA  1 
ATOM   4493  C  C   . THR   B  1 137 ? -39.714 19.328  20.936   1.00 40.21  ? 438  THR   B C   1 
ATOM   4494  O  O   . THR   B  1 137 ? -40.081 20.498  20.767   1.00 42.10  ? 438  THR   B O   1 
ATOM   4495  C  CB  . THR   B  1 137 ? -41.334 18.452  22.609   1.00 46.26  ? 438  THR   B CB  1 
ATOM   4496  O  OG1 . THR   B  1 137 ? -40.258 18.685  23.535   1.00 44.81  ? 438  THR   B OG1 1 
ATOM   4497  C  CG2 . THR   B  1 137 ? -42.138 17.232  23.061   1.00 37.02  ? 438  THR   B CG2 1 
ATOM   4498  N  N   . THR   B  1 138 ? -38.422 18.997  20.915   1.00 43.34  ? 439  THR   B N   1 
ATOM   4499  C  CA  . THR   B  1 138 ? -37.395 20.020  20.722   1.00 32.29  ? 439  THR   B CA  1 
ATOM   4500  C  C   . THR   B  1 138 ? -36.375 19.604  19.674   1.00 47.17  ? 439  THR   B C   1 
ATOM   4501  O  O   . THR   B  1 138 ? -36.219 18.420  19.340   1.00 42.59  ? 439  THR   B O   1 
ATOM   4502  C  CB  . THR   B  1 138 ? -36.625 20.343  22.004   1.00 45.50  ? 439  THR   B CB  1 
ATOM   4503  O  OG1 . THR   B  1 138 ? -35.907 19.172  22.433   1.00 45.44  ? 439  THR   B OG1 1 
ATOM   4504  C  CG2 . THR   B  1 138 ? -37.571 20.818  23.097   1.00 46.33  ? 439  THR   B CG2 1 
ATOM   4505  N  N   . ALA   B  1 139 ? -35.660 20.622  19.184   1.00 46.97  ? 440  ALA   B N   1 
ATOM   4506  C  CA  . ALA   B  1 139 ? -34.494 20.402  18.340   1.00 47.11  ? 440  ALA   B CA  1 
ATOM   4507  C  C   . ALA   B  1 139 ? -33.524 19.416  18.975   1.00 53.32  ? 440  ALA   B C   1 
ATOM   4508  O  O   . ALA   B  1 139 ? -32.939 18.571  18.282   1.00 57.60  ? 440  ALA   B O   1 
ATOM   4509  C  CB  . ALA   B  1 139 ? -33.799 21.734  18.064   1.00 47.07  ? 440  ALA   B CB  1 
ATOM   4510  N  N   . HIS   B  1 140 ? -33.347 19.505  20.300   1.00 58.13  ? 441  HIS   B N   1 
ATOM   4511  C  CA  . HIS   B  1 140 ? -32.433 18.613  21.012   1.00 41.59  ? 441  HIS   B CA  1 
ATOM   4512  C  C   . HIS   B  1 140 ? -32.911 17.170  20.951   1.00 39.35  ? 441  HIS   B C   1 
ATOM   4513  O  O   . HIS   B  1 140 ? -32.142 16.271  20.601   1.00 48.00  ? 441  HIS   B O   1 
ATOM   4514  C  CB  . HIS   B  1 140 ? -32.277 19.058  22.469   1.00 48.44  ? 441  HIS   B CB  1 
ATOM   4515  C  CG  . HIS   B  1 140 ? -31.206 20.082  22.677   1.00 41.76  ? 441  HIS   B CG  1 
ATOM   4516  N  ND1 . HIS   B  1 140 ? -31.467 21.437  22.700   1.00 42.57  ? 441  HIS   B ND1 1 
ATOM   4517  C  CD2 . HIS   B  1 140 ? -29.871 19.950  22.870   1.00 40.20  ? 441  HIS   B CD2 1 
ATOM   4518  C  CE1 . HIS   B  1 140 ? -30.337 22.094  22.908   1.00 46.88  ? 441  HIS   B CE1 1 
ATOM   4519  N  NE2 . HIS   B  1 140 ? -29.354 21.217  23.008   1.00 41.63  ? 441  HIS   B NE2 1 
ATOM   4520  N  N   . GLY   B  1 141 ? -34.177 16.926  21.302   1.00 38.59  ? 442  GLY   B N   1 
ATOM   4521  C  CA  . GLY   B  1 141 ? -34.744 15.599  21.093   1.00 43.71  ? 442  GLY   B CA  1 
ATOM   4522  C  C   . GLY   B  1 141 ? -34.670 15.131  19.647   1.00 51.84  ? 442  GLY   B C   1 
ATOM   4523  O  O   . GLY   B  1 141 ? -34.457 13.945  19.378   1.00 54.52  ? 442  GLY   B O   1 
ATOM   4524  N  N   . MET   B  1 142 ? -34.855 16.052  18.690   1.00 48.82  ? 443  MET   B N   1 
ATOM   4525  C  CA  . MET   B  1 142 ? -34.691 15.686  17.281   1.00 40.68  ? 443  MET   B CA  1 
ATOM   4526  C  C   . MET   B  1 142 ? -33.292 15.141  17.021   1.00 43.96  ? 443  MET   B C   1 
ATOM   4527  O  O   . MET   B  1 142 ? -33.128 14.077  16.416   1.00 37.44  ? 443  MET   B O   1 
ATOM   4528  C  CB  . MET   B  1 142 ? -34.962 16.891  16.387   1.00 41.90  ? 443  MET   B CB  1 
ATOM   4529  C  CG  . MET   B  1 142 ? -36.392 17.031  15.922   1.00 40.18  ? 443  MET   B CG  1 
ATOM   4530  S  SD  . MET   B  1 142 ? -36.620 18.667  15.212   1.00 50.71  ? 443  MET   B SD  1 
ATOM   4531  C  CE  . MET   B  1 142 ? -36.510 18.286  13.455   1.00 44.58  ? 443  MET   B CE  1 
ATOM   4532  N  N   . PHE   B  1 143 ? -32.271 15.845  17.517   1.00 48.10  ? 444  PHE   B N   1 
ATOM   4533  C  CA  . PHE   B  1 143 ? -30.889 15.412  17.335   1.00 36.23  ? 444  PHE   B CA  1 
ATOM   4534  C  C   . PHE   B  1 143 ? -30.627 14.050  17.980   1.00 39.53  ? 444  PHE   B C   1 
ATOM   4535  O  O   . PHE   B  1 143 ? -29.870 13.238  17.442   1.00 51.24  ? 444  PHE   B O   1 
ATOM   4536  C  CB  . PHE   B  1 143 ? -29.956 16.489  17.893   1.00 42.56  ? 444  PHE   B CB  1 
ATOM   4537  C  CG  . PHE   B  1 143 ? -28.535 16.040  18.065   1.00 46.75  ? 444  PHE   B CG  1 
ATOM   4538  C  CD1 . PHE   B  1 143 ? -28.017 15.800  19.328   1.00 42.90  ? 444  PHE   B CD1 1 
ATOM   4539  C  CD2 . PHE   B  1 143 ? -27.711 15.871  16.969   1.00 37.11  ? 444  PHE   B CD2 1 
ATOM   4540  C  CE1 . PHE   B  1 143 ? -26.708 15.393  19.480   1.00 48.85  ? 444  PHE   B CE1 1 
ATOM   4541  C  CE2 . PHE   B  1 143 ? -26.405 15.469  17.112   1.00 41.21  ? 444  PHE   B CE2 1 
ATOM   4542  C  CZ  . PHE   B  1 143 ? -25.900 15.224  18.369   1.00 49.65  ? 444  PHE   B CZ  1 
ATOM   4543  N  N   . ASN   B  1 144 ? -31.247 13.775  19.127   1.00 48.38  ? 445  ASN   B N   1 
ATOM   4544  C  CA  . ASN   B  1 144 ? -31.055 12.482  19.787   1.00 49.24  ? 445  ASN   B CA  1 
ATOM   4545  C  C   . ASN   B  1 144 ? -31.725 11.363  18.997   1.00 46.68  ? 445  ASN   B C   1 
ATOM   4546  O  O   . ASN   B  1 144 ? -31.205 10.240  18.921   1.00 49.70  ? 445  ASN   B O   1 
ATOM   4547  C  CB  . ASN   B  1 144 ? -31.588 12.554  21.230   1.00 42.91  ? 445  ASN   B CB  1 
ATOM   4548  C  CG  . ASN   B  1 144 ? -31.525 11.213  21.975   1.00 56.32  ? 445  ASN   B CG  1 
ATOM   4549  O  OD1 . ASN   B  1 144 ? -32.488 10.797  22.645   1.00 57.86  ? 445  ASN   B OD1 1 
ATOM   4550  N  ND2 . ASN   B  1 144 ? -30.384 10.546  21.883   1.00 58.12  ? 445  ASN   B ND2 1 
ATOM   4551  N  N   . TYR   B  1 145 ? -32.886 11.650  18.412   1.00 50.36  ? 446  TYR   B N   1 
ATOM   4552  C  CA  . TYR   B  1 145 ? -33.544 10.675  17.551   1.00 54.10  ? 446  TYR   B CA  1 
ATOM   4553  C  C   . TYR   B  1 145 ? -32.746 10.435  16.274   1.00 46.36  ? 446  TYR   B C   1 
ATOM   4554  O  O   . TYR   B  1 145 ? -32.638 9.295   15.808   1.00 43.52  ? 446  TYR   B O   1 
ATOM   4555  C  CB  . TYR   B  1 145 ? -34.949 11.157  17.216   1.00 47.80  ? 446  TYR   B CB  1 
ATOM   4556  C  CG  . TYR   B  1 145 ? -36.033 10.616  18.114   1.00 39.91  ? 446  TYR   B CG  1 
ATOM   4557  C  CD1 . TYR   B  1 145 ? -36.829 11.464  18.875   1.00 35.65  ? 446  TYR   B CD1 1 
ATOM   4558  C  CD2 . TYR   B  1 145 ? -36.294 9.260   18.163   1.00 35.59  ? 446  TYR   B CD2 1 
ATOM   4559  C  CE1 . TYR   B  1 145 ? -37.854 10.958  19.650   1.00 34.12  ? 446  TYR   B CE1 1 
ATOM   4560  C  CE2 . TYR   B  1 145 ? -37.294 8.756   18.937   1.00 32.93  ? 446  TYR   B CE2 1 
ATOM   4561  C  CZ  . TYR   B  1 145 ? -38.065 9.595   19.683   1.00 37.74  ? 446  TYR   B CZ  1 
ATOM   4562  O  OH  . TYR   B  1 145 ? -39.056 9.046   20.457   1.00 52.28  ? 446  TYR   B OH  1 
ATOM   4563  N  N   . ILE   B  1 146 ? -32.165 11.496  15.707   1.00 47.11  ? 447  ILE   B N   1 
ATOM   4564  C  CA  . ILE   B  1 146 ? -31.425 11.371  14.453   1.00 46.92  ? 447  ILE   B CA  1 
ATOM   4565  C  C   . ILE   B  1 146 ? -30.116 10.610  14.674   1.00 47.62  ? 447  ILE   B C   1 
ATOM   4566  O  O   . ILE   B  1 146 ? -29.725 9.770   13.851   1.00 55.02  ? 447  ILE   B O   1 
ATOM   4567  C  CB  . ILE   B  1 146 ? -31.194 12.767  13.836   1.00 41.90  ? 447  ILE   B CB  1 
ATOM   4568  C  CG1 . ILE   B  1 146 ? -32.473 13.297  13.177   1.00 45.97  ? 447  ILE   B CG1 1 
ATOM   4569  C  CG2 . ILE   B  1 146 ? -30.102 12.729  12.820   1.00 39.15  ? 447  ILE   B CG2 1 
ATOM   4570  C  CD1 . ILE   B  1 146 ? -32.332 14.710  12.566   1.00 41.65  ? 447  ILE   B CD1 1 
ATOM   4571  N  N   . CYS   B  1 147 ? -29.435 10.864  15.800   1.00 40.97  ? 448  CYS   B N   1 
ATOM   4572  C  CA  . CYS   B  1 147 ? -28.189 10.157  16.095   1.00 33.52  ? 448  CYS   B CA  1 
ATOM   4573  C  C   . CYS   B  1 147 ? -28.423 8.660   16.252   1.00 40.79  ? 448  CYS   B C   1 
ATOM   4574  O  O   . CYS   B  1 147 ? -27.573 7.845   15.873   1.00 44.51  ? 448  CYS   B O   1 
ATOM   4575  C  CB  . CYS   B  1 147 ? -27.554 10.700  17.374   1.00 45.51  ? 448  CYS   B CB  1 
ATOM   4576  S  SG  . CYS   B  1 147 ? -26.596 12.213  17.268   1.00 48.68  ? 448  CYS   B SG  1 
ATOM   4577  N  N   . ASN   B  1 148 ? -29.541 8.275   16.866   1.00 47.33  ? 449  ASN   B N   1 
ATOM   4578  C  CA  . ASN   B  1 148 ? -29.826 6.852   17.007   1.00 38.18  ? 449  ASN   B CA  1 
ATOM   4579  C  C   . ASN   B  1 148 ? -30.141 6.243   15.651   1.00 43.35  ? 449  ASN   B C   1 
ATOM   4580  O  O   . ASN   B  1 148 ? -29.731 5.115   15.357   1.00 46.84  ? 449  ASN   B O   1 
ATOM   4581  C  CB  . ASN   B  1 148 ? -30.979 6.637   17.989   1.00 44.04  ? 449  ASN   B CB  1 
ATOM   4582  C  CG  . ASN   B  1 148 ? -30.685 7.194   19.388   1.00 38.50  ? 449  ASN   B CG  1 
ATOM   4583  O  OD1 . ASN   B  1 148 ? -29.538 7.444   19.750   1.00 37.08  ? 449  ASN   B OD1 1 
ATOM   4584  N  ND2 . ASN   B  1 148 ? -31.735 7.377   20.175   1.00 40.28  ? 449  ASN   B ND2 1 
ATOM   4585  N  N   . HIS   B  1 149 ? -30.862 6.986   14.810   1.00 44.01  ? 450  HIS   B N   1 
ATOM   4586  C  CA  . HIS   B  1 149 ? -31.109 6.559   13.435   1.00 48.80  ? 450  HIS   B CA  1 
ATOM   4587  C  C   . HIS   B  1 149 ? -29.795 6.277   12.724   1.00 42.13  ? 450  HIS   B C   1 
ATOM   4588  O  O   . HIS   B  1 149 ? -29.560 5.165   12.233   1.00 43.08  ? 450  HIS   B O   1 
ATOM   4589  C  CB  . HIS   B  1 149 ? -31.913 7.641   12.702   1.00 48.91  ? 450  HIS   B CB  1 
ATOM   4590  C  CG  . HIS   B  1 149 ? -32.285 7.300   11.290   1.00 46.46  ? 450  HIS   B CG  1 
ATOM   4591  N  ND1 . HIS   B  1 149 ? -31.656 6.316   10.559   1.00 49.96  ? 450  HIS   B ND1 1 
ATOM   4592  C  CD2 . HIS   B  1 149 ? -33.227 7.826   10.473   1.00 42.87  ? 450  HIS   B CD2 1 
ATOM   4593  C  CE1 . HIS   B  1 149 ? -32.201 6.239   9.361    1.00 46.07  ? 450  HIS   B CE1 1 
ATOM   4594  N  NE2 . HIS   B  1 149 ? -33.153 7.149   9.280    1.00 47.22  ? 450  HIS   B NE2 1 
ATOM   4595  N  N   . VAL   B  1 150 ? -28.920 7.282   12.671   1.00 26.13  ? 451  VAL   B N   1 
ATOM   4596  C  CA  . VAL   B  1 150 ? -27.630 7.113   12.017   1.00 25.79  ? 451  VAL   B CA  1 
ATOM   4597  C  C   . VAL   B  1 150 ? -26.915 5.872   12.534   1.00 45.53  ? 451  VAL   B C   1 
ATOM   4598  O  O   . VAL   B  1 150 ? -26.404 5.062   11.749   1.00 50.55  ? 451  VAL   B O   1 
ATOM   4599  C  CB  . VAL   B  1 150 ? -26.776 8.373   12.212   1.00 33.28  ? 451  VAL   B CB  1 
ATOM   4600  C  CG1 . VAL   B  1 150 ? -25.323 8.056   11.946   1.00 31.96  ? 451  VAL   B CG1 1 
ATOM   4601  C  CG2 . VAL   B  1 150 ? -27.262 9.455   11.285   1.00 28.51  ? 451  VAL   B CG2 1 
ATOM   4602  N  N   . LYS   B  1 151 ? -26.877 5.697   13.868   1.00 50.46  ? 452  LYS   B N   1 
ATOM   4603  C  CA  . LYS   B  1 151 ? -26.079 4.619   14.455   1.00 34.75  ? 452  LYS   B CA  1 
ATOM   4604  C  C   . LYS   B  1 151 ? -26.679 3.255   14.158   1.00 29.45  ? 452  LYS   B C   1 
ATOM   4605  O  O   . LYS   B  1 151 ? -25.948 2.311   13.849   1.00 33.30  ? 452  LYS   B O   1 
ATOM   4606  C  CB  . LYS   B  1 151 ? -25.922 4.807   15.964   1.00 36.42  ? 452  LYS   B CB  1 
ATOM   4607  C  CG  . LYS   B  1 151 ? -25.204 3.627   16.640   1.00 35.14  ? 452  LYS   B CG  1 
ATOM   4608  C  CD  . LYS   B  1 151 ? -24.767 3.980   18.065   1.00 37.88  ? 452  LYS   B CD  1 
ATOM   4609  C  CE  . LYS   B  1 151 ? -23.848 2.928   18.682   1.00 32.00  ? 452  LYS   B CE  1 
ATOM   4610  N  NZ  . LYS   B  1 151 ? -23.473 3.264   20.129   1.00 45.01  ? 452  LYS   B NZ  1 
ATOM   4611  N  N   . TYR   B  1 152 ? -28.001 3.122   14.265   1.00 36.64  ? 453  TYR   B N   1 
ATOM   4612  C  CA  . TYR   B  1 152 ? -28.654 1.875   13.875   1.00 38.90  ? 453  TYR   B CA  1 
ATOM   4613  C  C   . TYR   B  1 152 ? -28.458 1.608   12.384   1.00 43.51  ? 453  TYR   B C   1 
ATOM   4614  O  O   . TYR   B  1 152 ? -28.041 0.514   11.977   1.00 47.84  ? 453  TYR   B O   1 
ATOM   4615  C  CB  . TYR   B  1 152 ? -30.152 1.937   14.214   1.00 42.92  ? 453  TYR   B CB  1 
ATOM   4616  C  CG  . TYR   B  1 152 ? -30.934 0.759   13.682   1.00 46.91  ? 453  TYR   B CG  1 
ATOM   4617  C  CD1 . TYR   B  1 152 ? -31.072 -0.393  14.436   1.00 45.77  ? 453  TYR   B CD1 1 
ATOM   4618  C  CD2 . TYR   B  1 152 ? -31.502 0.782   12.413   1.00 52.39  ? 453  TYR   B CD2 1 
ATOM   4619  C  CE1 . TYR   B  1 152 ? -31.758 -1.481  13.958   1.00 51.57  ? 453  TYR   B CE1 1 
ATOM   4620  C  CE2 . TYR   B  1 152 ? -32.189 -0.315  11.920   1.00 53.82  ? 453  TYR   B CE2 1 
ATOM   4621  C  CZ  . TYR   B  1 152 ? -32.312 -1.440  12.708   1.00 56.33  ? 453  TYR   B CZ  1 
ATOM   4622  O  OH  . TYR   B  1 152 ? -32.996 -2.540  12.259   1.00 63.02  ? 453  TYR   B OH  1 
ATOM   4623  N  N   . ALA   B  1 153 ? -28.758 2.606   11.555   1.00 44.77  ? 454  ALA   B N   1 
ATOM   4624  C  CA  . ALA   B  1 153 ? -28.706 2.418   10.104   1.00 37.09  ? 454  ALA   B CA  1 
ATOM   4625  C  C   . ALA   B  1 153 ? -27.302 2.050   9.636    1.00 39.88  ? 454  ALA   B C   1 
ATOM   4626  O  O   . ALA   B  1 153 ? -27.135 1.189   8.765    1.00 42.09  ? 454  ALA   B O   1 
ATOM   4627  C  CB  . ALA   B  1 153 ? -29.191 3.687   9.410    1.00 26.73  ? 454  ALA   B CB  1 
ATOM   4628  N  N   . THR   B  1 154 ? -26.278 2.670   10.227   1.00 42.00  ? 455  THR   B N   1 
ATOM   4629  C  CA  . THR   B  1 154 ? -24.907 2.446   9.780    1.00 34.43  ? 455  THR   B CA  1 
ATOM   4630  C  C   . THR   B  1 154 ? -24.411 1.052   10.180   1.00 47.70  ? 455  THR   B C   1 
ATOM   4631  O  O   . THR   B  1 154 ? -23.811 0.338   9.366    1.00 53.30  ? 455  THR   B O   1 
ATOM   4632  C  CB  . THR   B  1 154 ? -24.014 3.551   10.347   1.00 37.94  ? 455  THR   B CB  1 
ATOM   4633  O  OG1 . THR   B  1 154 ? -24.528 4.843   9.947    1.00 32.00  ? 455  THR   B OG1 1 
ATOM   4634  C  CG2 . THR   B  1 154 ? -22.566 3.389   9.890    1.00 32.21  ? 455  THR   B CG2 1 
ATOM   4635  N  N   . ASN   B  1 155 ? -24.649 0.647   11.430   1.00 57.31  ? 456  ASN   B N   1 
ATOM   4636  C  CA  . ASN   B  1 155 ? -24.438 -0.742  11.882   1.00 51.93  ? 456  ASN   B CA  1 
ATOM   4637  C  C   . ASN   B  1 155 ? -23.020 -1.235  11.584   1.00 43.70  ? 456  ASN   B C   1 
ATOM   4638  O  O   . ASN   B  1 155 ? -22.803 -2.378  11.183   1.00 47.23  ? 456  ASN   B O   1 
ATOM   4639  C  CB  . ASN   B  1 155 ? -25.492 -1.674  11.270   1.00 51.01  ? 456  ASN   B CB  1 
ATOM   4640  C  CG  . ASN   B  1 155 ? -25.558 -3.025  11.957   1.00 57.67  ? 456  ASN   B CG  1 
ATOM   4641  O  OD1 . ASN   B  1 155 ? -25.104 -3.178  13.086   1.00 65.37  ? 456  ASN   B OD1 1 
ATOM   4642  N  ND2 . ASN   B  1 155 ? -26.126 -4.010  11.276   1.00 54.32  ? 456  ASN   B ND2 1 
ATOM   4643  N  N   . LYS   B  1 156 ? -22.040 -0.358  11.800   1.00 43.59  ? 457  LYS   B N   1 
ATOM   4644  C  CA  . LYS   B  1 156 ? -20.624 -0.681  11.621   1.00 49.90  ? 457  LYS   B CA  1 
ATOM   4645  C  C   . LYS   B  1 156 ? -20.294 -1.022  10.173   1.00 66.54  ? 457  LYS   B C   1 
ATOM   4646  O  O   . LYS   B  1 156 ? -19.395 -1.829  9.910    1.00 76.75  ? 457  LYS   B O   1 
ATOM   4647  C  CB  . LYS   B  1 156 ? -20.188 -1.820  12.552   1.00 55.25  ? 457  LYS   B CB  1 
ATOM   4648  C  CG  . LYS   B  1 156 ? -20.539 -1.565  14.024   1.00 59.15  ? 457  LYS   B CG  1 
ATOM   4649  C  CD  . LYS   B  1 156 ? -19.472 -2.083  14.989   1.00 67.94  ? 457  LYS   B CD  1 
ATOM   4650  C  CE  . LYS   B  1 156 ? -19.021 -1.019  15.983   1.00 62.26  ? 457  LYS   B CE  1 
ATOM   4651  N  NZ  . LYS   B  1 156 ? -17.752 -1.457  16.621   1.00 72.91  ? 457  LYS   B NZ  1 
ATOM   4652  N  N   . GLY   B  1 157 ? -21.010 -0.404  9.223    1.00 67.31  ? 458  GLY   B N   1 
ATOM   4653  C  CA  . GLY   B  1 157 ? -20.779 -0.606  7.804    1.00 54.92  ? 458  GLY   B CA  1 
ATOM   4654  C  C   . GLY   B  1 157 ? -21.755 -1.536  7.115    1.00 53.80  ? 458  GLY   B C   1 
ATOM   4655  O  O   . GLY   B  1 157 ? -21.895 -1.460  5.898    1.00 67.00  ? 458  GLY   B O   1 
ATOM   4656  N  N   . ASN   B  1 158 ? -22.426 -2.418  7.854    1.00 47.70  ? 459  ASN   B N   1 
ATOM   4657  C  CA  . ASN   B  1 158 ? -23.417 -3.318  7.270    1.00 43.09  ? 459  ASN   B CA  1 
ATOM   4658  C  C   . ASN   B  1 158 ? -24.779 -2.641  7.352    1.00 48.17  ? 459  ASN   B C   1 
ATOM   4659  O  O   . ASN   B  1 158 ? -25.575 -2.900  8.247    1.00 46.56  ? 459  ASN   B O   1 
ATOM   4660  C  CB  . ASN   B  1 158 ? -23.425 -4.648  8.004    1.00 35.21  ? 459  ASN   B CB  1 
ATOM   4661  C  CG  . ASN   B  1 158 ? -24.626 -5.495  7.643    1.00 47.08  ? 459  ASN   B CG  1 
ATOM   4662  O  OD1 . ASN   B  1 158 ? -25.058 -5.501  6.501    1.00 61.59  ? 459  ASN   B OD1 1 
ATOM   4663  N  ND2 . ASN   B  1 158 ? -25.189 -6.188  8.618    1.00 49.86  ? 459  ASN   B ND2 1 
ATOM   4664  N  N   . LEU   B  1 159 ? -25.063 -1.782  6.371    1.00 48.26  ? 460  LEU   B N   1 
ATOM   4665  C  CA  . LEU   B  1 159 ? -26.162 -0.845  6.523    1.00 40.89  ? 460  LEU   B CA  1 
ATOM   4666  C  C   . LEU   B  1 159 ? -27.517 -1.552  6.564    1.00 40.28  ? 460  LEU   B C   1 
ATOM   4667  O  O   . LEU   B  1 159 ? -27.684 -2.684  6.102    1.00 51.64  ? 460  LEU   B O   1 
ATOM   4668  C  CB  . LEU   B  1 159 ? -26.154 0.188   5.401    1.00 35.66  ? 460  LEU   B CB  1 
ATOM   4669  C  CG  . LEU   B  1 159 ? -24.879 0.973   5.088    1.00 46.69  ? 460  LEU   B CG  1 
ATOM   4670  C  CD1 . LEU   B  1 159 ? -25.233 2.251   4.329    1.00 51.18  ? 460  LEU   B CD1 1 
ATOM   4671  C  CD2 . LEU   B  1 159 ? -24.066 1.307   6.297    1.00 41.07  ? 460  LEU   B CD2 1 
ATOM   4672  N  N   . ARG   B  1 160 ? -28.495 -0.837  7.124    1.00 33.77  ? 461  ARG   B N   1 
ATOM   4673  C  CA  . ARG   B  1 160 ? -29.879 -1.265  7.291    1.00 32.47  ? 461  ARG   B CA  1 
ATOM   4674  C  C   . ARG   B  1 160 ? -30.794 -0.111  6.902    1.00 39.94  ? 461  ARG   B C   1 
ATOM   4675  O  O   . ARG   B  1 160 ? -30.455 1.062   7.099    1.00 44.67  ? 461  ARG   B O   1 
ATOM   4676  C  CB  . ARG   B  1 160 ? -30.151 -1.677  8.754    1.00 36.50  ? 461  ARG   B CB  1 
ATOM   4677  C  CG  . ARG   B  1 160 ? -29.550 -3.004  9.125    1.00 47.66  ? 461  ARG   B CG  1 
ATOM   4678  C  CD  . ARG   B  1 160 ? -29.859 -3.396  10.567   1.00 56.81  ? 461  ARG   B CD  1 
ATOM   4679  N  NE  . ARG   B  1 160 ? -29.096 -2.598  11.521   1.00 52.82  ? 461  ARG   B NE  1 
ATOM   4680  C  CZ  . ARG   B  1 160 ? -29.021 -2.860  12.816   1.00 56.35  ? 461  ARG   B CZ  1 
ATOM   4681  N  NH1 . ARG   B  1 160 ? -29.669 -3.900  13.322   1.00 59.10  ? 461  ARG   B NH1 1 
ATOM   4682  N  NH2 . ARG   B  1 160 ? -28.309 -2.074  13.607   1.00 50.61  ? 461  ARG   B NH2 1 
ATOM   4683  N  N   . SER   B  1 161 ? -31.956 -0.425  6.338    1.00 40.36  ? 462  SER   B N   1 
ATOM   4684  C  CA  . SER   B  1 161 ? -32.868 0.649   5.957    1.00 48.85  ? 462  SER   B CA  1 
ATOM   4685  C  C   . SER   B  1 161 ? -33.631 1.129   7.187    1.00 48.16  ? 462  SER   B C   1 
ATOM   4686  O  O   . SER   B  1 161 ? -34.034 0.325   8.032    1.00 37.92  ? 462  SER   B O   1 
ATOM   4687  C  CB  . SER   B  1 161 ? -33.852 0.189   4.878    1.00 49.94  ? 462  SER   B CB  1 
ATOM   4688  O  OG  . SER   B  1 161 ? -33.248 -0.734  3.991    1.00 58.61  ? 462  SER   B OG  1 
ATOM   4689  N  N   . ALA   B  1 162 ? -33.853 2.441   7.272    1.00 41.61  ? 463  ALA   B N   1 
ATOM   4690  C  CA  . ALA   B  1 162 ? -34.608 2.973   8.394    1.00 32.80  ? 463  ALA   B CA  1 
ATOM   4691  C  C   . ALA   B  1 162 ? -35.187 4.339   8.064    1.00 37.12  ? 463  ALA   B C   1 
ATOM   4692  O  O   . ALA   B  1 162 ? -34.601 5.113   7.305    1.00 37.64  ? 463  ALA   B O   1 
ATOM   4693  C  CB  . ALA   B  1 162 ? -33.739 3.087   9.645    1.00 39.42  ? 463  ALA   B CB  1 
ATOM   4694  N  N   . ILE   B  1 163 ? -36.332 4.630   8.684    1.00 43.47  ? 464  ILE   B N   1 
ATOM   4695  C  CA  . ILE   B  1 163 ? -36.958 5.947   8.671    1.00 39.86  ? 464  ILE   B CA  1 
ATOM   4696  C  C   . ILE   B  1 163 ? -37.286 6.316   10.121   1.00 46.45  ? 464  ILE   B C   1 
ATOM   4697  O  O   . ILE   B  1 163 ? -37.582 5.451   10.956   1.00 38.74  ? 464  ILE   B O   1 
ATOM   4698  C  CB  . ILE   B  1 163 ? -38.224 5.975   7.768    1.00 30.34  ? 464  ILE   B CB  1 
ATOM   4699  C  CG1 . ILE   B  1 163 ? -38.677 7.395   7.454    1.00 32.49  ? 464  ILE   B CG1 1 
ATOM   4700  C  CG2 . ILE   B  1 163 ? -39.400 5.272   8.428    1.00 22.35  ? 464  ILE   B CG2 1 
ATOM   4701  C  CD1 . ILE   B  1 163 ? -39.976 7.434   6.619    1.00 28.39  ? 464  ILE   B CD1 1 
ATOM   4702  N  N   . THR   B  1 164 ? -37.196 7.613   10.422   1.00 41.05  ? 465  THR   B N   1 
ATOM   4703  C  CA  . THR   B  1 164 ? -37.544 8.180   11.719   1.00 41.38  ? 465  THR   B CA  1 
ATOM   4704  C  C   . THR   B  1 164 ? -38.588 9.265   11.473   1.00 43.15  ? 465  THR   B C   1 
ATOM   4705  O  O   . THR   B  1 164 ? -38.321 10.216  10.728   1.00 48.09  ? 465  THR   B O   1 
ATOM   4706  C  CB  . THR   B  1 164 ? -36.298 8.751   12.425   1.00 41.93  ? 465  THR   B CB  1 
ATOM   4707  O  OG1 . THR   B  1 164 ? -35.460 7.684   12.908   1.00 35.08  ? 465  THR   B OG1 1 
ATOM   4708  C  CG2 . THR   B  1 164 ? -36.709 9.651   13.603   1.00 40.45  ? 465  THR   B CG2 1 
ATOM   4709  N  N   . ILE   B  1 165 ? -39.771 9.129   12.086   1.00 34.25  ? 466  ILE   B N   1 
ATOM   4710  C  CA  . ILE   B  1 165 ? -40.923 9.958   11.738   1.00 40.09  ? 466  ILE   B CA  1 
ATOM   4711  C  C   . ILE   B  1 165 ? -41.282 10.888  12.902   1.00 35.17  ? 466  ILE   B C   1 
ATOM   4712  O  O   . ILE   B  1 165 ? -41.802 10.466  13.939   1.00 39.29  ? 466  ILE   B O   1 
ATOM   4713  C  CB  . ILE   B  1 165 ? -42.128 9.111   11.312   1.00 49.31  ? 466  ILE   B CB  1 
ATOM   4714  C  CG1 . ILE   B  1 165 ? -41.699 7.999   10.360   1.00 42.17  ? 466  ILE   B CG1 1 
ATOM   4715  C  CG2 . ILE   B  1 165 ? -43.103 9.975   10.548   1.00 55.16  ? 466  ILE   B CG2 1 
ATOM   4716  C  CD1 . ILE   B  1 165 ? -42.874 7.215   9.781    1.00 35.70  ? 466  ILE   B CD1 1 
ATOM   4717  N  N   . PHE   B  1 166 ? -41.059 12.170  12.691   1.00 37.94  ? 467  PHE   B N   1 
ATOM   4718  C  CA  . PHE   B  1 166 ? -41.295 13.214  13.669   1.00 40.39  ? 467  PHE   B CA  1 
ATOM   4719  C  C   . PHE   B  1 166 ? -42.766 13.612  13.662   1.00 43.90  ? 467  PHE   B C   1 
ATOM   4720  O  O   . PHE   B  1 166 ? -43.536 13.127  12.839   1.00 66.01  ? 467  PHE   B O   1 
ATOM   4721  C  CB  . PHE   B  1 166 ? -40.349 14.364  13.352   1.00 35.73  ? 467  PHE   B CB  1 
ATOM   4722  C  CG  . PHE   B  1 166 ? -38.947 14.050  13.684   1.00 44.18  ? 467  PHE   B CG  1 
ATOM   4723  C  CD1 . PHE   B  1 166 ? -38.572 13.853  15.012   1.00 48.79  ? 467  PHE   B CD1 1 
ATOM   4724  C  CD2 . PHE   B  1 166 ? -38.006 13.915  12.692   1.00 30.24  ? 467  PHE   B CD2 1 
ATOM   4725  C  CE1 . PHE   B  1 166 ? -37.276 13.545  15.333   1.00 51.58  ? 467  PHE   B CE1 1 
ATOM   4726  C  CE2 . PHE   B  1 166 ? -36.706 13.603  13.006   1.00 46.76  ? 467  PHE   B CE2 1 
ATOM   4727  C  CZ  . PHE   B  1 166 ? -36.336 13.414  14.327   1.00 46.04  ? 467  PHE   B CZ  1 
ATOM   4728  N  N   . PRO   B  1 167 ? -43.204 14.483  14.581   1.00 44.80  ? 468  PRO   B N   1 
ATOM   4729  C  CA  . PRO   B  1 167 ? -44.643 14.747  14.688   1.00 44.03  ? 468  PRO   B CA  1 
ATOM   4730  C  C   . PRO   B  1 167 ? -45.169 15.376  13.412   1.00 54.52  ? 468  PRO   B C   1 
ATOM   4731  O  O   . PRO   B  1 167 ? -44.496 16.186  12.772   1.00 56.22  ? 468  PRO   B O   1 
ATOM   4732  C  CB  . PRO   B  1 167 ? -44.747 15.720  15.869   1.00 44.29  ? 468  PRO   B CB  1 
ATOM   4733  C  CG  . PRO   B  1 167 ? -43.461 15.618  16.574   1.00 45.40  ? 468  PRO   B CG  1 
ATOM   4734  C  CD  . PRO   B  1 167 ? -42.460 15.363  15.496   1.00 45.37  ? 468  PRO   B CD  1 
ATOM   4735  N  N   . GLN   B  1 168 ? -46.386 14.996  13.046   1.00 57.72  ? 469  GLN   B N   1 
ATOM   4736  C  CA  . GLN   B  1 168 ? -46.946 15.464  11.798   1.00 47.74  ? 469  GLN   B CA  1 
ATOM   4737  C  C   . GLN   B  1 168 ? -47.213 16.966  11.852   1.00 55.74  ? 469  GLN   B C   1 
ATOM   4738  O  O   . GLN   B  1 168 ? -47.064 17.621  12.889   1.00 59.88  ? 469  GLN   B O   1 
ATOM   4739  C  CB  . GLN   B  1 168 ? -48.232 14.718  11.490   1.00 42.02  ? 469  GLN   B CB  1 
ATOM   4740  C  CG  . GLN   B  1 168 ? -49.387 15.188  12.302   1.00 40.66  ? 469  GLN   B CG  1 
ATOM   4741  C  CD  . GLN   B  1 168 ? -50.288 14.053  12.644   1.00 43.43  ? 469  GLN   B CD  1 
ATOM   4742  O  OE1 . GLN   B  1 168 ? -49.863 12.898  12.627   1.00 37.64  ? 469  GLN   B OE1 1 
ATOM   4743  N  NE2 . GLN   B  1 168 ? -51.548 14.361  12.953   1.00 48.29  ? 469  GLN   B NE2 1 
ATOM   4744  N  N   . ARG   B  1 169 ? -47.621 17.506  10.704   1.00 54.65  ? 470  ARG   B N   1 
ATOM   4745  C  CA  . ARG   B  1 169 ? -47.933 18.920  10.588   1.00 52.68  ? 470  ARG   B CA  1 
ATOM   4746  C  C   . ARG   B  1 169 ? -49.327 19.165  11.133   1.00 55.44  ? 470  ARG   B C   1 
ATOM   4747  O  O   . ARG   B  1 169 ? -50.212 18.313  11.018   1.00 62.05  ? 470  ARG   B O   1 
ATOM   4748  C  CB  . ARG   B  1 169 ? -47.831 19.373  9.129    1.00 59.51  ? 470  ARG   B CB  1 
ATOM   4749  C  CG  . ARG   B  1 169 ? -48.087 20.858  8.925    1.00 68.38  ? 470  ARG   B CG  1 
ATOM   4750  C  CD  . ARG   B  1 169 ? -48.092 21.275  7.451    1.00 57.53  ? 470  ARG   B CD  1 
ATOM   4751  N  NE  . ARG   B  1 169 ? -46.749 21.488  6.923    1.00 52.04  ? 470  ARG   B NE  1 
ATOM   4752  C  CZ  . ARG   B  1 169 ? -46.294 20.918  5.814    1.00 66.65  ? 470  ARG   B CZ  1 
ATOM   4753  N  NH1 . ARG   B  1 169 ? -47.085 20.114  5.117    1.00 62.21  ? 470  ARG   B NH1 1 
ATOM   4754  N  NH2 . ARG   B  1 169 ? -45.055 21.157  5.394    1.00 74.82  ? 470  ARG   B NH2 1 
ATOM   4755  N  N   . THR   B  1 170 ? -49.514 20.321  11.766   1.00 54.17  ? 471  THR   B N   1 
ATOM   4756  C  CA  . THR   B  1 170 ? -50.799 20.649  12.375   1.00 58.07  ? 471  THR   B CA  1 
ATOM   4757  C  C   . THR   B  1 170 ? -51.385 21.890  11.711   1.00 65.64  ? 471  THR   B C   1 
ATOM   4758  O  O   . THR   B  1 170 ? -52.355 21.771  10.956   1.00 61.37  ? 471  THR   B O   1 
ATOM   4759  C  CB  . THR   B  1 170 ? -50.671 20.808  13.902   1.00 59.28  ? 471  THR   B CB  1 
ATOM   4760  O  OG1 . THR   B  1 170 ? -49.796 21.896  14.238   1.00 60.49  ? 471  THR   B OG1 1 
ATOM   4761  C  CG2 . THR   B  1 170 ? -50.137 19.520  14.563   1.00 41.38  ? 471  THR   B CG2 1 
ATOM   4762  N  N   . ASP   B  1 171 ? -50.829 23.076  11.950   1.00 65.37  ? 472  ASP   B N   1 
ATOM   4763  C  CA  . ASP   B  1 171 ? -51.348 24.298  11.354   1.00 63.14  ? 472  ASP   B CA  1 
ATOM   4764  C  C   . ASP   B  1 171 ? -50.345 24.954  10.419   1.00 66.14  ? 472  ASP   B C   1 
ATOM   4765  O  O   . ASP   B  1 171 ? -50.568 26.085  9.983    1.00 73.19  ? 472  ASP   B O   1 
ATOM   4766  C  CB  . ASP   B  1 171 ? -51.780 25.284  12.442   1.00 68.89  ? 472  ASP   B CB  1 
ATOM   4767  C  CG  . ASP   B  1 171 ? -50.599 25.918  13.155   1.00 71.87  ? 472  ASP   B CG  1 
ATOM   4768  O  OD1 . ASP   B  1 171 ? -49.611 25.206  13.419   1.00 77.46  ? 472  ASP   B OD1 1 
ATOM   4769  O  OD2 . ASP   B  1 171 ? -50.648 27.130  13.448   1.00 74.22  ? 472  ASP   B OD2 1 
ATOM   4770  N  N   . GLY   B  1 172 ? -49.249 24.277  10.091   1.00 64.72  ? 473  GLY   B N   1 
ATOM   4771  C  CA  . GLY   B  1 172 ? -48.281 24.821  9.168    1.00 63.39  ? 473  GLY   B CA  1 
ATOM   4772  C  C   . GLY   B  1 172 ? -47.289 25.786  9.771    1.00 68.12  ? 473  GLY   B C   1 
ATOM   4773  O  O   . GLY   B  1 172 ? -46.225 26.004  9.185    1.00 56.28  ? 473  GLY   B O   1 
ATOM   4774  N  N   . LYS   B  1 173 ? -47.598 26.376  10.921   1.00 77.95  ? 474  LYS   B N   1 
ATOM   4775  C  CA  . LYS   B  1 173 ? -46.659 27.221  11.638   1.00 88.81  ? 474  LYS   B CA  1 
ATOM   4776  C  C   . LYS   B  1 173 ? -45.939 26.476  12.756   1.00 87.13  ? 474  LYS   B C   1 
ATOM   4777  O  O   . LYS   B  1 173 ? -45.187 27.093  13.512   1.00 91.11  ? 474  LYS   B O   1 
ATOM   4778  C  CB  . LYS   B  1 173 ? -47.377 28.449  12.207   1.00 100.41 ? 474  LYS   B CB  1 
ATOM   4779  C  CG  . LYS   B  1 173 ? -47.834 29.467  11.163   1.00 104.65 ? 474  LYS   B CG  1 
ATOM   4780  C  CD  . LYS   B  1 173 ? -48.253 30.794  11.812   1.00 108.92 ? 474  LYS   B CD  1 
ATOM   4781  C  CE  . LYS   B  1 173 ? -49.567 30.675  12.581   1.00 109.49 ? 474  LYS   B CE  1 
ATOM   4782  N  NZ  . LYS   B  1 173 ? -50.761 30.690  11.670   1.00 105.27 ? 474  LYS   B NZ  1 
ATOM   4783  N  N   . HIS   B  1 174 ? -46.171 25.172  12.894   1.00 80.89  ? 475  HIS   B N   1 
ATOM   4784  C  CA  . HIS   B  1 174 ? -45.509 24.357  13.906   1.00 72.10  ? 475  HIS   B CA  1 
ATOM   4785  C  C   . HIS   B  1 174 ? -44.786 23.194  13.248   1.00 62.76  ? 475  HIS   B C   1 
ATOM   4786  O  O   . HIS   B  1 174 ? -44.738 22.090  13.784   1.00 64.90  ? 475  HIS   B O   1 
ATOM   4787  C  CB  . HIS   B  1 174 ? -46.503 23.845  14.946   1.00 75.37  ? 475  HIS   B CB  1 
ATOM   4788  C  CG  . HIS   B  1 174 ? -47.262 24.923  15.653   1.00 74.78  ? 475  HIS   B CG  1 
ATOM   4789  N  ND1 . HIS   B  1 174 ? -47.023 26.266  15.449   1.00 72.73  ? 475  HIS   B ND1 1 
ATOM   4790  C  CD2 . HIS   B  1 174 ? -48.265 24.853  16.559   1.00 74.17  ? 475  HIS   B CD2 1 
ATOM   4791  C  CE1 . HIS   B  1 174 ? -47.849 26.976  16.193   1.00 76.11  ? 475  HIS   B CE1 1 
ATOM   4792  N  NE2 . HIS   B  1 174 ? -48.612 26.143  16.878   1.00 79.57  ? 475  HIS   B NE2 1 
ATOM   4793  N  N   . ASP   B  1 175 ? -44.227 23.436  12.077   1.00 60.92  ? 476  ASP   B N   1 
ATOM   4794  C  CA  . ASP   B  1 175 ? -43.613 22.362  11.315   1.00 61.59  ? 476  ASP   B CA  1 
ATOM   4795  C  C   . ASP   B  1 175 ? -42.351 21.862  11.990   1.00 54.16  ? 476  ASP   B C   1 
ATOM   4796  O  O   . ASP   B  1 175 ? -41.553 22.646  12.501   1.00 54.47  ? 476  ASP   B O   1 
ATOM   4797  C  CB  . ASP   B  1 175 ? -43.267 22.847  9.909    1.00 65.94  ? 476  ASP   B CB  1 
ATOM   4798  C  CG  . ASP   B  1 175 ? -44.445 22.824  8.988    1.00 66.64  ? 476  ASP   B CG  1 
ATOM   4799  O  OD1 . ASP   B  1 175 ? -45.558 23.106  9.482    1.00 63.94  ? 476  ASP   B OD1 1 
ATOM   4800  O  OD2 . ASP   B  1 175 ? -44.250 22.536  7.781    1.00 67.72  ? 476  ASP   B OD2 1 
ATOM   4801  N  N   . PHE   B  1 176 ? -42.152 20.548  11.946   1.00 51.62  ? 477  PHE   B N   1 
ATOM   4802  C  CA  . PHE   B  1 176 ? -40.851 19.954  12.223   1.00 47.50  ? 477  PHE   B CA  1 
ATOM   4803  C  C   . PHE   B  1 176 ? -40.076 19.798  10.925   1.00 56.24  ? 477  PHE   B C   1 
ATOM   4804  O  O   . PHE   B  1 176 ? -40.593 19.228  9.958    1.00 70.14  ? 477  PHE   B O   1 
ATOM   4805  C  CB  . PHE   B  1 176 ? -41.023 18.604  12.905   1.00 52.40  ? 477  PHE   B CB  1 
ATOM   4806  C  CG  . PHE   B  1 176 ? -41.340 18.722  14.351   1.00 54.20  ? 477  PHE   B CG  1 
ATOM   4807  C  CD1 . PHE   B  1 176 ? -42.551 19.258  14.763   1.00 55.85  ? 477  PHE   B CD1 1 
ATOM   4808  C  CD2 . PHE   B  1 176 ? -40.419 18.338  15.299   1.00 56.81  ? 477  PHE   B CD2 1 
ATOM   4809  C  CE1 . PHE   B  1 176 ? -42.843 19.393  16.091   1.00 51.16  ? 477  PHE   B CE1 1 
ATOM   4810  C  CE2 . PHE   B  1 176 ? -40.705 18.474  16.630   1.00 52.58  ? 477  PHE   B CE2 1 
ATOM   4811  C  CZ  . PHE   B  1 176 ? -41.919 19.002  17.024   1.00 49.15  ? 477  PHE   B CZ  1 
ATOM   4812  N  N   . ARG   B  1 177 ? -38.845 20.306  10.896   1.00 53.89  ? 478  ARG   B N   1 
ATOM   4813  C  CA  . ARG   B  1 177 ? -38.041 20.269  9.678    1.00 56.39  ? 478  ARG   B CA  1 
ATOM   4814  C  C   . ARG   B  1 177 ? -36.601 19.913  10.001   1.00 55.50  ? 478  ARG   B C   1 
ATOM   4815  O  O   . ARG   B  1 177 ? -36.010 20.479  10.925   1.00 70.97  ? 478  ARG   B O   1 
ATOM   4816  C  CB  . ARG   B  1 177 ? -38.058 21.617  8.939    1.00 59.38  ? 478  ARG   B CB  1 
ATOM   4817  C  CG  . ARG   B  1 177 ? -39.394 22.068  8.359    1.00 61.02  ? 478  ARG   B CG  1 
ATOM   4818  C  CD  . ARG   B  1 177 ? -39.995 21.046  7.397    1.00 63.93  ? 478  ARG   B CD  1 
ATOM   4819  N  NE  . ARG   B  1 177 ? -39.153 20.733  6.239    1.00 58.97  ? 478  ARG   B NE  1 
ATOM   4820  C  CZ  . ARG   B  1 177 ? -39.187 21.379  5.075    1.00 52.44  ? 478  ARG   B CZ  1 
ATOM   4821  N  NH1 . ARG   B  1 177 ? -40.016 22.404  4.884    1.00 42.07  ? 478  ARG   B NH1 1 
ATOM   4822  N  NH2 . ARG   B  1 177 ? -38.389 20.985  4.094    1.00 50.87  ? 478  ARG   B NH2 1 
ATOM   4823  N  N   . VAL   B  1 178 ? -36.041 18.986  9.236    1.00 52.88  ? 479  VAL   B N   1 
ATOM   4824  C  CA  . VAL   B  1 178 ? -34.596 18.853  9.094    1.00 47.61  ? 479  VAL   B CA  1 
ATOM   4825  C  C   . VAL   B  1 178 ? -34.195 19.759  7.933    1.00 50.87  ? 479  VAL   B C   1 
ATOM   4826  O  O   . VAL   B  1 178 ? -34.547 19.494  6.783    1.00 53.92  ? 479  VAL   B O   1 
ATOM   4827  C  CB  . VAL   B  1 178 ? -34.191 17.397  8.831    1.00 39.75  ? 479  VAL   B CB  1 
ATOM   4828  C  CG1 . VAL   B  1 178 ? -32.711 17.286  8.574    1.00 26.21  ? 479  VAL   B CG1 1 
ATOM   4829  C  CG2 . VAL   B  1 178 ? -34.588 16.520  9.998    1.00 41.08  ? 479  VAL   B CG2 1 
ATOM   4830  N  N   . TRP   B  1 179 ? -33.487 20.848  8.229    1.00 47.19  ? 480  TRP   B N   1 
ATOM   4831  C  CA  . TRP   B  1 179 ? -33.102 21.780  7.173    1.00 45.60  ? 480  TRP   B CA  1 
ATOM   4832  C  C   . TRP   B  1 179 ? -32.015 21.210  6.270    1.00 49.52  ? 480  TRP   B C   1 
ATOM   4833  O  O   . TRP   B  1 179 ? -31.847 21.691  5.146    1.00 51.12  ? 480  TRP   B O   1 
ATOM   4834  C  CB  . TRP   B  1 179 ? -32.645 23.115  7.773    1.00 43.84  ? 480  TRP   B CB  1 
ATOM   4835  C  CG  . TRP   B  1 179 ? -33.791 23.946  8.289    1.00 51.69  ? 480  TRP   B CG  1 
ATOM   4836  C  CD1 . TRP   B  1 179 ? -34.947 23.482  8.857    1.00 53.24  ? 480  TRP   B CD1 1 
ATOM   4837  C  CD2 . TRP   B  1 179 ? -33.909 25.377  8.254    1.00 45.10  ? 480  TRP   B CD2 1 
ATOM   4838  N  NE1 . TRP   B  1 179 ? -35.770 24.534  9.186    1.00 54.70  ? 480  TRP   B NE1 1 
ATOM   4839  C  CE2 . TRP   B  1 179 ? -35.161 25.707  8.822    1.00 47.49  ? 480  TRP   B CE2 1 
ATOM   4840  C  CE3 . TRP   B  1 179 ? -33.081 26.409  7.802    1.00 50.99  ? 480  TRP   B CE3 1 
ATOM   4841  C  CZ2 . TRP   B  1 179 ? -35.603 27.021  8.950    1.00 44.92  ? 480  TRP   B CZ2 1 
ATOM   4842  C  CZ3 . TRP   B  1 179 ? -33.523 27.720  7.929    1.00 52.93  ? 480  TRP   B CZ3 1 
ATOM   4843  C  CH2 . TRP   B  1 179 ? -34.772 28.012  8.502    1.00 50.97  ? 480  TRP   B CH2 1 
ATOM   4844  N  N   . ASN   B  1 180 ? -31.256 20.227  6.741    1.00 42.70  ? 481  ASN   B N   1 
ATOM   4845  C  CA  . ASN   B  1 180 ? -30.319 19.546  5.865    1.00 42.14  ? 481  ASN   B CA  1 
ATOM   4846  C  C   . ASN   B  1 180 ? -31.096 18.743  4.847    1.00 52.14  ? 481  ASN   B C   1 
ATOM   4847  O  O   . ASN   B  1 180 ? -32.093 18.097  5.196    1.00 50.84  ? 481  ASN   B O   1 
ATOM   4848  C  CB  . ASN   B  1 180 ? -29.427 18.592  6.646    1.00 40.28  ? 481  ASN   B CB  1 
ATOM   4849  C  CG  . ASN   B  1 180 ? -28.701 19.266  7.785    1.00 40.57  ? 481  ASN   B CG  1 
ATOM   4850  O  OD1 . ASN   B  1 180 ? -29.300 19.638  8.790    1.00 41.83  ? 481  ASN   B OD1 1 
ATOM   4851  N  ND2 . ASN   B  1 180 ? -27.389 19.392  7.646    1.00 41.61  ? 481  ASN   B ND2 1 
ATOM   4852  N  N   . SER   B  1 181 ? -30.620 18.767  3.588    1.00 49.05  ? 482  SER   B N   1 
ATOM   4853  C  CA  . SER   B  1 181 ? -31.217 17.939  2.538    1.00 44.98  ? 482  SER   B CA  1 
ATOM   4854  C  C   . SER   B  1 181 ? -30.886 16.469  2.748    1.00 43.34  ? 482  SER   B C   1 
ATOM   4855  O  O   . SER   B  1 181 ? -31.749 15.603  2.571    1.00 45.16  ? 482  SER   B O   1 
ATOM   4856  C  CB  . SER   B  1 181 ? -30.737 18.405  1.172    1.00 40.75  ? 482  SER   B CB  1 
ATOM   4857  O  OG  . SER   B  1 181 ? -29.357 18.728  1.231    1.00 57.77  ? 482  SER   B OG  1 
ATOM   4858  N  N   . GLN   B  1 182 ? -29.655 16.166  3.153    1.00 43.05  ? 483  GLN   B N   1 
ATOM   4859  C  CA  . GLN   B  1 182 ? -29.338 14.861  3.718    1.00 49.43  ? 483  GLN   B CA  1 
ATOM   4860  C  C   . GLN   B  1 182 ? -28.697 15.028  5.091    1.00 56.07  ? 483  GLN   B C   1 
ATOM   4861  O  O   . GLN   B  1 182 ? -28.075 16.055  5.384    1.00 64.53  ? 483  GLN   B O   1 
ATOM   4862  C  CB  . GLN   B  1 182 ? -28.416 14.055  2.817    1.00 47.81  ? 483  GLN   B CB  1 
ATOM   4863  C  CG  . GLN   B  1 182 ? -28.961 13.802  1.414    1.00 51.26  ? 483  GLN   B CG  1 
ATOM   4864  C  CD  . GLN   B  1 182 ? -27.844 13.638  0.389    1.00 57.72  ? 483  GLN   B CD  1 
ATOM   4865  O  OE1 . GLN   B  1 182 ? -27.030 12.708  0.476    1.00 59.62  ? 483  GLN   B OE1 1 
ATOM   4866  N  NE2 . GLN   B  1 182 ? -27.782 14.562  -0.572   1.00 54.73  ? 483  GLN   B NE2 1 
ATOM   4867  N  N   . LEU   B  1 183 ? -28.858 14.004  5.934    1.00 53.39  ? 484  LEU   B N   1 
ATOM   4868  C  CA  . LEU   B  1 183 ? -28.297 14.052  7.284    1.00 42.86  ? 484  LEU   B CA  1 
ATOM   4869  C  C   . LEU   B  1 183 ? -26.795 14.305  7.249    1.00 45.69  ? 484  LEU   B C   1 
ATOM   4870  O  O   . LEU   B  1 183 ? -26.284 15.143  7.992    1.00 47.91  ? 484  LEU   B O   1 
ATOM   4871  C  CB  . LEU   B  1 183 ? -28.619 12.753  8.024    1.00 38.09  ? 484  LEU   B CB  1 
ATOM   4872  C  CG  . LEU   B  1 183 ? -30.103 12.500  8.328    1.00 31.30  ? 484  LEU   B CG  1 
ATOM   4873  C  CD1 . LEU   B  1 183 ? -30.306 11.295  9.241    1.00 27.34  ? 484  LEU   B CD1 1 
ATOM   4874  C  CD2 . LEU   B  1 183 ? -30.735 13.766  8.928    1.00 25.61  ? 484  LEU   B CD2 1 
ATOM   4875  N  N   . ILE   B  1 184 ? -26.082 13.628  6.356    1.00 51.35  ? 485  ILE   B N   1 
ATOM   4876  C  CA  . ILE   B  1 184 ? -24.627 13.718  6.245    1.00 42.73  ? 485  ILE   B CA  1 
ATOM   4877  C  C   . ILE   B  1 184 ? -24.313 14.206  4.841    1.00 53.09  ? 485  ILE   B C   1 
ATOM   4878  O  O   . ILE   B  1 184 ? -24.531 13.471  3.868    1.00 50.51  ? 485  ILE   B O   1 
ATOM   4879  C  CB  . ILE   B  1 184 ? -23.950 12.364  6.511    1.00 42.52  ? 485  ILE   B CB  1 
ATOM   4880  C  CG1 . ILE   B  1 184 ? -24.365 11.808  7.869    1.00 45.49  ? 485  ILE   B CG1 1 
ATOM   4881  C  CG2 . ILE   B  1 184 ? -22.442 12.468  6.468    1.00 36.80  ? 485  ILE   B CG2 1 
ATOM   4882  C  CD1 . ILE   B  1 184 ? -24.022 10.365  8.003    1.00 53.02  ? 485  ILE   B CD1 1 
ATOM   4883  N  N   . ARG   B  1 185 ? -23.824 15.442  4.729    1.00 49.78  ? 486  ARG   B N   1 
ATOM   4884  C  CA  . ARG   B  1 185 ? -23.300 15.963  3.472    1.00 51.60  ? 486  ARG   B CA  1 
ATOM   4885  C  C   . ARG   B  1 185 ? -22.126 16.877  3.774    1.00 58.99  ? 486  ARG   B C   1 
ATOM   4886  O  O   . ARG   B  1 185 ? -22.010 17.433  4.873    1.00 47.76  ? 486  ARG   B O   1 
ATOM   4887  C  CB  . ARG   B  1 185 ? -24.335 16.755  2.665    1.00 55.90  ? 486  ARG   B CB  1 
ATOM   4888  C  CG  . ARG   B  1 185 ? -25.558 15.990  2.251    1.00 54.68  ? 486  ARG   B CG  1 
ATOM   4889  C  CD  . ARG   B  1 185 ? -26.337 16.771  1.221    1.00 58.29  ? 486  ARG   B CD  1 
ATOM   4890  N  NE  . ARG   B  1 185 ? -25.601 16.805  -0.035   1.00 65.56  ? 486  ARG   B NE  1 
ATOM   4891  C  CZ  . ARG   B  1 185 ? -25.998 17.478  -1.103   1.00 62.22  ? 486  ARG   B CZ  1 
ATOM   4892  N  NH1 . ARG   B  1 185 ? -27.126 18.172  -1.065   1.00 49.50  ? 486  ARG   B NH1 1 
ATOM   4893  N  NH2 . ARG   B  1 185 ? -25.262 17.469  -2.202   1.00 72.99  ? 486  ARG   B NH2 1 
ATOM   4894  N  N   . TYR   B  1 186 ? -21.266 17.053  2.774    1.00 55.62  ? 487  TYR   B N   1 
ATOM   4895  C  CA  . TYR   B  1 186 ? -20.098 17.897  2.940    1.00 51.82  ? 487  TYR   B CA  1 
ATOM   4896  C  C   . TYR   B  1 186 ? -20.433 19.354  2.636    1.00 62.92  ? 487  TYR   B C   1 
ATOM   4897  O  O   . TYR   B  1 186 ? -21.350 19.660  1.875    1.00 76.42  ? 487  TYR   B O   1 
ATOM   4898  C  CB  . TYR   B  1 186 ? -18.954 17.405  2.060    1.00 43.03  ? 487  TYR   B CB  1 
ATOM   4899  C  CG  . TYR   B  1 186 ? -18.499 15.997  2.406    1.00 49.86  ? 487  TYR   B CG  1 
ATOM   4900  C  CD1 . TYR   B  1 186 ? -18.720 14.952  1.529    1.00 49.69  ? 487  TYR   B CD1 1 
ATOM   4901  C  CD2 . TYR   B  1 186 ? -17.874 15.709  3.615    1.00 53.61  ? 487  TYR   B CD2 1 
ATOM   4902  C  CE1 . TYR   B  1 186 ? -18.313 13.661  1.832    1.00 47.13  ? 487  TYR   B CE1 1 
ATOM   4903  C  CE2 . TYR   B  1 186 ? -17.456 14.407  3.922    1.00 51.73  ? 487  TYR   B CE2 1 
ATOM   4904  C  CZ  . TYR   B  1 186 ? -17.684 13.389  3.014    1.00 50.05  ? 487  TYR   B CZ  1 
ATOM   4905  O  OH  . TYR   B  1 186 ? -17.296 12.087  3.271    1.00 50.34  ? 487  TYR   B OH  1 
ATOM   4906  N  N   . ALA   B  1 187 ? -19.693 20.252  3.269    1.00 71.49  ? 488  ALA   B N   1 
ATOM   4907  C  CA  . ALA   B  1 187 ? -19.907 21.680  3.109    1.00 70.28  ? 488  ALA   B CA  1 
ATOM   4908  C  C   . ALA   B  1 187 ? -19.215 22.204  1.855    1.00 67.98  ? 488  ALA   B C   1 
ATOM   4909  O  O   . ALA   B  1 187 ? -18.163 21.707  1.441    1.00 71.89  ? 488  ALA   B O   1 
ATOM   4910  C  CB  . ALA   B  1 187 ? -19.390 22.427  4.336    1.00 70.17  ? 488  ALA   B CB  1 
ATOM   4911  N  N   . GLY   B  1 188 ? -19.810 23.237  1.264    1.00 61.08  ? 489  GLY   B N   1 
ATOM   4912  C  CA  . GLY   B  1 188 ? -19.227 23.904  0.115    1.00 56.60  ? 489  GLY   B CA  1 
ATOM   4913  C  C   . GLY   B  1 188 ? -18.928 25.368  0.378    1.00 64.41  ? 489  GLY   B C   1 
ATOM   4914  O  O   . GLY   B  1 188 ? -19.772 26.102  0.901    1.00 69.02  ? 489  GLY   B O   1 
ATOM   4915  N  N   . TYR   B  1 189 ? -17.737 25.815  -0.004   1.00 64.62  ? 490  TYR   B N   1 
ATOM   4916  C  CA  . TYR   B  1 189 ? -17.244 27.129  0.370    1.00 58.46  ? 490  TYR   B CA  1 
ATOM   4917  C  C   . TYR   B  1 189 ? -16.976 27.953  -0.876   1.00 66.11  ? 490  TYR   B C   1 
ATOM   4918  O  O   . TYR   B  1 189 ? -16.381 27.458  -1.842   1.00 64.74  ? 490  TYR   B O   1 
ATOM   4919  C  CB  . TYR   B  1 189 ? -15.980 27.008  1.218    1.00 64.47  ? 490  TYR   B CB  1 
ATOM   4920  C  CG  . TYR   B  1 189 ? -16.176 26.250  2.515    1.00 63.03  ? 490  TYR   B CG  1 
ATOM   4921  C  CD1 . TYR   B  1 189 ? -15.638 24.984  2.686    1.00 61.71  ? 490  TYR   B CD1 1 
ATOM   4922  C  CD2 . TYR   B  1 189 ? -16.902 26.798  3.568    1.00 62.69  ? 490  TYR   B CD2 1 
ATOM   4923  C  CE1 . TYR   B  1 189 ? -15.812 24.285  3.858    1.00 65.54  ? 490  TYR   B CE1 1 
ATOM   4924  C  CE2 . TYR   B  1 189 ? -17.074 26.107  4.759    1.00 67.19  ? 490  TYR   B CE2 1 
ATOM   4925  C  CZ  . TYR   B  1 189 ? -16.519 24.852  4.899    1.00 69.28  ? 490  TYR   B CZ  1 
ATOM   4926  O  OH  . TYR   B  1 189 ? -16.680 24.144  6.070    1.00 67.92  ? 490  TYR   B OH  1 
ATOM   4927  N  N   . LYS   B  1 190 ? -17.398 29.215  -0.833   1.00 65.85  ? 491  LYS   B N   1 
ATOM   4928  C  CA  . LYS   B  1 190 ? -17.349 30.119  -1.977   1.00 66.15  ? 491  LYS   B CA  1 
ATOM   4929  C  C   . LYS   B  1 190 ? -16.074 30.948  -1.870   1.00 78.78  ? 491  LYS   B C   1 
ATOM   4930  O  O   . LYS   B  1 190 ? -16.027 31.943  -1.145   1.00 85.97  ? 491  LYS   B O   1 
ATOM   4931  C  CB  . LYS   B  1 190 ? -18.601 30.989  -2.001   1.00 70.21  ? 491  LYS   B CB  1 
ATOM   4932  C  CG  . LYS   B  1 190 ? -18.797 31.769  -3.280   1.00 78.61  ? 491  LYS   B CG  1 
ATOM   4933  C  CD  . LYS   B  1 190 ? -18.907 30.854  -4.496   1.00 82.77  ? 491  LYS   B CD  1 
ATOM   4934  C  CE  . LYS   B  1 190 ? -18.900 31.673  -5.781   1.00 86.26  ? 491  LYS   B CE  1 
ATOM   4935  N  NZ  . LYS   B  1 190 ? -18.836 30.807  -6.985   1.00 88.39  ? 491  LYS   B NZ  1 
ATOM   4936  N  N   . GLN   B  1 191 ? -15.040 30.551  -2.617   1.00 95.38  ? 492  GLN   B N   1 
ATOM   4937  C  CA  . GLN   B  1 191 ? -13.709 31.135  -2.480   1.00 103.22 ? 492  GLN   B CA  1 
ATOM   4938  C  C   . GLN   B  1 191 ? -13.680 32.607  -2.904   1.00 107.16 ? 492  GLN   B C   1 
ATOM   4939  O  O   . GLN   B  1 191 ? -14.556 33.071  -3.642   1.00 108.47 ? 492  GLN   B O   1 
ATOM   4940  C  CB  . GLN   B  1 191 ? -12.690 30.340  -3.299   1.00 97.27  ? 492  GLN   B CB  1 
ATOM   4941  C  CG  . GLN   B  1 191 ? -12.520 28.887  -2.875   1.00 89.92  ? 492  GLN   B CG  1 
ATOM   4942  C  CD  . GLN   B  1 191 ? -11.776 28.723  -1.559   1.00 88.05  ? 492  GLN   B CD  1 
ATOM   4943  O  OE1 . GLN   B  1 191 ? -11.630 29.666  -0.774   1.00 87.24  ? 492  GLN   B OE1 1 
ATOM   4944  N  NE2 . GLN   B  1 191 ? -11.296 27.513  -1.314   1.00 85.57  ? 492  GLN   B NE2 1 
ATOM   4945  N  N   . PRO   B  1 192 ? -12.676 33.366  -2.439   1.00 102.93 ? 493  PRO   B N   1 
ATOM   4946  C  CA  . PRO   B  1 192 ? -12.568 34.774  -2.863   1.00 100.44 ? 493  PRO   B CA  1 
ATOM   4947  C  C   . PRO   B  1 192 ? -12.319 34.950  -4.357   1.00 106.08 ? 493  PRO   B C   1 
ATOM   4948  O  O   . PRO   B  1 192 ? -12.726 35.967  -4.942   1.00 100.96 ? 493  PRO   B O   1 
ATOM   4949  C  CB  . PRO   B  1 192 ? -11.393 35.295  -2.023   1.00 89.90  ? 493  PRO   B CB  1 
ATOM   4950  C  CG  . PRO   B  1 192 ? -10.618 34.080  -1.628   1.00 83.79  ? 493  PRO   B CG  1 
ATOM   4951  C  CD  . PRO   B  1 192 ? -11.662 33.020  -1.428   1.00 89.97  ? 493  PRO   B CD  1 
ATOM   4952  N  N   . ASP   B  1 193 ? -11.655 33.988  -4.997   1.00 105.95 ? 494  ASP   B N   1 
ATOM   4953  C  CA  . ASP   B  1 193 ? -11.379 34.051  -6.427   1.00 96.87  ? 494  ASP   B CA  1 
ATOM   4954  C  C   . ASP   B  1 193 ? -12.497 33.462  -7.275   1.00 98.65  ? 494  ASP   B C   1 
ATOM   4955  O  O   . ASP   B  1 193 ? -12.239 33.011  -8.399   1.00 103.05 ? 494  ASP   B O   1 
ATOM   4956  C  CB  . ASP   B  1 193 ? -10.050 33.358  -6.732   1.00 94.07  ? 494  ASP   B CB  1 
ATOM   4957  C  CG  . ASP   B  1 193 ? -9.899  32.026  -6.008   1.00 91.14  ? 494  ASP   B CG  1 
ATOM   4958  O  OD1 . ASP   B  1 193 ? -10.256 30.988  -6.615   1.00 81.32  ? 494  ASP   B OD1 1 
ATOM   4959  O  OD2 . ASP   B  1 193 ? -9.423  32.022  -4.839   1.00 89.24  ? 494  ASP   B OD2 1 
ATOM   4960  N  N   . GLY   B  1 194 ? -13.730 33.448  -6.771   1.00 90.88  ? 495  GLY   B N   1 
ATOM   4961  C  CA  . GLY   B  1 194 ? -14.864 33.033  -7.575   1.00 75.51  ? 495  GLY   B CA  1 
ATOM   4962  C  C   . GLY   B  1 194 ? -15.032 31.533  -7.671   1.00 83.04  ? 495  GLY   B C   1 
ATOM   4963  O  O   . GLY   B  1 194 ? -16.133 31.058  -7.964   1.00 82.71  ? 495  GLY   B O   1 
ATOM   4964  N  N   . SER   B  1 195 ? -13.971 30.776  -7.410   1.00 98.75  ? 496  SER   B N   1 
ATOM   4965  C  CA  . SER   B  1 195 ? -14.018 29.318  -7.473   1.00 101.97 ? 496  SER   B CA  1 
ATOM   4966  C  C   . SER   B  1 195 ? -14.780 28.778  -6.258   1.00 95.77  ? 496  SER   B C   1 
ATOM   4967  O  O   . SER   B  1 195 ? -15.343 29.527  -5.455   1.00 96.68  ? 496  SER   B O   1 
ATOM   4968  C  CB  . SER   B  1 195 ? -12.605 28.747  -7.574   1.00 107.58 ? 496  SER   B CB  1 
ATOM   4969  O  OG  . SER   B  1 195 ? -11.862 28.967  -6.389   1.00 107.55 ? 496  SER   B OG  1 
ATOM   4970  N  N   . THR   B  1 196 ? -14.810 27.454  -6.109   1.00 88.90  ? 497  THR   B N   1 
ATOM   4971  C  CA  . THR   B  1 196 ? -15.619 26.850  -5.054   1.00 89.12  ? 497  THR   B CA  1 
ATOM   4972  C  C   . THR   B  1 196 ? -14.962 25.575  -4.547   1.00 89.64  ? 497  THR   B C   1 
ATOM   4973  O  O   . THR   B  1 196 ? -14.795 24.619  -5.308   1.00 93.90  ? 497  THR   B O   1 
ATOM   4974  C  CB  . THR   B  1 196 ? -17.038 26.557  -5.551   1.00 86.05  ? 497  THR   B CB  1 
ATOM   4975  O  OG1 . THR   B  1 196 ? -17.649 27.761  -6.046   1.00 89.29  ? 497  THR   B OG1 1 
ATOM   4976  C  CG2 . THR   B  1 196 ? -17.879 25.988  -4.411   1.00 74.35  ? 497  THR   B CG2 1 
ATOM   4977  N  N   . LEU   B  1 197 ? -14.626 25.557  -3.257   1.00 83.15  ? 498  LEU   B N   1 
ATOM   4978  C  CA  . LEU   B  1 197 ? -14.077 24.386  -2.585   1.00 80.76  ? 498  LEU   B CA  1 
ATOM   4979  C  C   . LEU   B  1 197 ? -15.183 23.668  -1.821   1.00 77.94  ? 498  LEU   B C   1 
ATOM   4980  O  O   . LEU   B  1 197 ? -16.060 24.313  -1.237   1.00 78.90  ? 498  LEU   B O   1 
ATOM   4981  C  CB  . LEU   B  1 197 ? -12.953 24.787  -1.619   1.00 81.29  ? 498  LEU   B CB  1 
ATOM   4982  C  CG  . LEU   B  1 197 ? -12.807 24.028  -0.286   1.00 72.46  ? 498  LEU   B CG  1 
ATOM   4983  C  CD1 . LEU   B  1 197 ? -11.846 22.833  -0.379   1.00 64.38  ? 498  LEU   B CD1 1 
ATOM   4984  C  CD2 . LEU   B  1 197 ? -12.385 24.962  0.840    1.00 78.31  ? 498  LEU   B CD2 1 
ATOM   4985  N  N   . GLY   B  1 198 ? -15.135 22.339  -1.828   1.00 72.88  ? 499  GLY   B N   1 
ATOM   4986  C  CA  . GLY   B  1 198 ? -16.118 21.527  -1.128   1.00 66.52  ? 499  GLY   B CA  1 
ATOM   4987  C  C   . GLY   B  1 198 ? -17.174 20.962  -2.075   1.00 75.50  ? 499  GLY   B C   1 
ATOM   4988  O  O   . GLY   B  1 198 ? -16.851 20.452  -3.148   1.00 76.95  ? 499  GLY   B O   1 
ATOM   4989  N  N   . ASP   B  1 199 ? -18.433 21.047  -1.666   1.00 77.15  ? 500  ASP   B N   1 
ATOM   4990  C  CA  . ASP   B  1 199 ? -19.545 20.562  -2.475   1.00 79.59  ? 500  ASP   B CA  1 
ATOM   4991  C  C   . ASP   B  1 199 ? -20.343 21.762  -2.960   1.00 80.92  ? 500  ASP   B C   1 
ATOM   4992  O  O   . ASP   B  1 199 ? -21.033 22.402  -2.150   1.00 86.93  ? 500  ASP   B O   1 
ATOM   4993  C  CB  . ASP   B  1 199 ? -20.428 19.619  -1.654   1.00 85.28  ? 500  ASP   B CB  1 
ATOM   4994  C  CG  . ASP   B  1 199 ? -21.462 18.883  -2.496   1.00 85.98  ? 500  ASP   B CG  1 
ATOM   4995  O  OD1 . ASP   B  1 199 ? -22.182 19.532  -3.293   1.00 85.45  ? 500  ASP   B OD1 1 
ATOM   4996  O  OD2 . ASP   B  1 199 ? -21.557 17.643  -2.342   1.00 82.36  ? 500  ASP   B OD2 1 
ATOM   4997  N  N   . PRO   B  1 200 ? -20.287 22.110  -4.252   1.00 65.59  ? 501  PRO   B N   1 
ATOM   4998  C  CA  . PRO   B  1 200 ? -20.924 23.360  -4.707   1.00 64.42  ? 501  PRO   B CA  1 
ATOM   4999  C  C   . PRO   B  1 200 ? -22.430 23.405  -4.511   1.00 64.20  ? 501  PRO   B C   1 
ATOM   5000  O  O   . PRO   B  1 200 ? -22.998 24.506  -4.457   1.00 62.83  ? 501  PRO   B O   1 
ATOM   5001  C  CB  . PRO   B  1 200 ? -20.547 23.418  -6.194   1.00 61.03  ? 501  PRO   B CB  1 
ATOM   5002  C  CG  . PRO   B  1 200 ? -19.269 22.676  -6.259   1.00 58.52  ? 501  PRO   B CG  1 
ATOM   5003  C  CD  . PRO   B  1 200 ? -19.405 21.542  -5.281   1.00 50.84  ? 501  PRO   B CD  1 
ATOM   5004  N  N   . ALA   B  1 201 ? -23.091 22.248  -4.395   1.00 53.88  ? 502  ALA   B N   1 
ATOM   5005  C  CA  . ALA   B  1 201 ? -24.537 22.226  -4.210   1.00 53.66  ? 502  ALA   B CA  1 
ATOM   5006  C  C   . ALA   B  1 201 ? -24.943 22.844  -2.881   1.00 65.76  ? 502  ALA   B C   1 
ATOM   5007  O  O   . ALA   B  1 201 ? -26.010 23.461  -2.774   1.00 68.73  ? 502  ALA   B O   1 
ATOM   5008  C  CB  . ALA   B  1 201 ? -25.042 20.788  -4.289   1.00 48.46  ? 502  ALA   B CB  1 
ATOM   5009  N  N   . ASN   B  1 202 ? -24.108 22.686  -1.870   1.00 65.86  ? 503  ASN   B N   1 
ATOM   5010  C  CA  . ASN   B  1 202 ? -24.442 23.051  -0.508   1.00 58.80  ? 503  ASN   B CA  1 
ATOM   5011  C  C   . ASN   B  1 202 ? -23.966 24.439  -0.137   1.00 67.99  ? 503  ASN   B C   1 
ATOM   5012  O  O   . ASN   B  1 202 ? -24.101 24.826  1.025    1.00 82.11  ? 503  ASN   B O   1 
ATOM   5013  C  CB  . ASN   B  1 202 ? -23.842 22.020  0.442    1.00 50.37  ? 503  ASN   B CB  1 
ATOM   5014  C  CG  . ASN   B  1 202 ? -24.427 20.641  0.223    1.00 57.80  ? 503  ASN   B CG  1 
ATOM   5015  O  OD1 . ASN   B  1 202 ? -25.652 20.491  0.098    1.00 57.48  ? 503  ASN   B OD1 1 
ATOM   5016  N  ND2 . ASN   B  1 202 ? -23.560 19.622  0.155    1.00 54.29  ? 503  ASN   B ND2 1 
ATOM   5017  N  N   . VAL   B  1 203 ? -23.416 25.195  -1.092   1.00 67.03  ? 504  VAL   B N   1 
ATOM   5018  C  CA  . VAL   B  1 203 ? -22.887 26.517  -0.773   1.00 67.86  ? 504  VAL   B CA  1 
ATOM   5019  C  C   . VAL   B  1 203 ? -23.937 27.351  -0.052   1.00 66.60  ? 504  VAL   B C   1 
ATOM   5020  O  O   . VAL   B  1 203 ? -23.640 28.020  0.945    1.00 77.24  ? 504  VAL   B O   1 
ATOM   5021  C  CB  . VAL   B  1 203 ? -22.369 27.215  -2.045   1.00 69.53  ? 504  VAL   B CB  1 
ATOM   5022  C  CG1 . VAL   B  1 203 ? -22.017 28.668  -1.750   1.00 70.26  ? 504  VAL   B CG1 1 
ATOM   5023  C  CG2 . VAL   B  1 203 ? -21.159 26.472  -2.608   1.00 65.06  ? 504  VAL   B CG2 1 
ATOM   5024  N  N   . GLN   B  1 204 ? -25.190 27.284  -0.501   1.00 60.21  ? 505  GLN   B N   1 
ATOM   5025  C  CA  . GLN   B  1 204 ? -26.204 28.085  0.170    1.00 62.67  ? 505  GLN   B CA  1 
ATOM   5026  C  C   . GLN   B  1 204 ? -26.481 27.563  1.574    1.00 64.61  ? 505  GLN   B C   1 
ATOM   5027  O  O   . GLN   B  1 204 ? -26.610 28.348  2.519    1.00 64.93  ? 505  GLN   B O   1 
ATOM   5028  C  CB  . GLN   B  1 204 ? -27.494 28.142  -0.642   1.00 62.00  ? 505  GLN   B CB  1 
ATOM   5029  C  CG  . GLN   B  1 204 ? -28.161 29.505  -0.485   1.00 68.63  ? 505  GLN   B CG  1 
ATOM   5030  C  CD  . GLN   B  1 204 ? -29.656 29.486  -0.705   1.00 74.20  ? 505  GLN   B CD  1 
ATOM   5031  O  OE1 . GLN   B  1 204 ? -30.277 28.427  -0.753   1.00 74.94  ? 505  GLN   B OE1 1 
ATOM   5032  N  NE2 . GLN   B  1 204 ? -30.247 30.670  -0.840   1.00 74.27  ? 505  GLN   B NE2 1 
ATOM   5033  N  N   . PHE   B  1 205 ? -26.576 26.245  1.738    1.00 61.82  ? 506  PHE   B N   1 
ATOM   5034  C  CA  . PHE   B  1 205 ? -26.769 25.704  3.076    1.00 52.91  ? 506  PHE   B CA  1 
ATOM   5035  C  C   . PHE   B  1 205 ? -25.537 25.959  3.942    1.00 63.72  ? 506  PHE   B C   1 
ATOM   5036  O  O   . PHE   B  1 205 ? -25.650 26.453  5.071    1.00 74.13  ? 506  PHE   B O   1 
ATOM   5037  C  CB  . PHE   B  1 205 ? -27.102 24.210  3.005    1.00 42.90  ? 506  PHE   B CB  1 
ATOM   5038  C  CG  . PHE   B  1 205 ? -27.567 23.624  4.327    1.00 58.71  ? 506  PHE   B CG  1 
ATOM   5039  C  CD1 . PHE   B  1 205 ? -28.833 23.913  4.827    1.00 56.51  ? 506  PHE   B CD1 1 
ATOM   5040  C  CD2 . PHE   B  1 205 ? -26.742 22.786  5.068    1.00 64.98  ? 506  PHE   B CD2 1 
ATOM   5041  C  CE1 . PHE   B  1 205 ? -29.268 23.382  6.033    1.00 58.51  ? 506  PHE   B CE1 1 
ATOM   5042  C  CE2 . PHE   B  1 205 ? -27.175 22.242  6.288    1.00 64.06  ? 506  PHE   B CE2 1 
ATOM   5043  C  CZ  . PHE   B  1 205 ? -28.438 22.542  6.768    1.00 56.47  ? 506  PHE   B CZ  1 
ATOM   5044  N  N   . THR   B  1 206 ? -24.345 25.653  3.417    1.00 54.15  ? 507  THR   B N   1 
ATOM   5045  C  CA  . THR   B  1 206 ? -23.105 25.916  4.138    1.00 52.71  ? 507  THR   B CA  1 
ATOM   5046  C  C   . THR   B  1 206 ? -22.975 27.376  4.550    1.00 63.84  ? 507  THR   B C   1 
ATOM   5047  O  O   . THR   B  1 206 ? -22.269 27.680  5.515    1.00 64.71  ? 507  THR   B O   1 
ATOM   5048  C  CB  . THR   B  1 206 ? -21.907 25.510  3.281    1.00 53.49  ? 507  THR   B CB  1 
ATOM   5049  O  OG1 . THR   B  1 206 ? -22.017 24.126  2.928    1.00 60.22  ? 507  THR   B OG1 1 
ATOM   5050  C  CG2 . THR   B  1 206 ? -20.591 25.743  4.016    1.00 46.11  ? 507  THR   B CG2 1 
ATOM   5051  N  N   . GLU   B  1 207 ? -23.653 28.292  3.865    1.00 77.93  ? 508  GLU   B N   1 
ATOM   5052  C  CA  . GLU   B  1 207 ? -23.600 29.675  4.322    1.00 83.64  ? 508  GLU   B CA  1 
ATOM   5053  C  C   . GLU   B  1 207 ? -24.617 29.936  5.431    1.00 81.58  ? 508  GLU   B C   1 
ATOM   5054  O  O   . GLU   B  1 207 ? -24.324 30.687  6.367    1.00 85.67  ? 508  GLU   B O   1 
ATOM   5055  C  CB  . GLU   B  1 207 ? -23.782 30.629  3.141    1.00 90.44  ? 508  GLU   B CB  1 
ATOM   5056  C  CG  . GLU   B  1 207 ? -22.505 30.778  2.319    1.00 104.89 ? 508  GLU   B CG  1 
ATOM   5057  C  CD  . GLU   B  1 207 ? -22.709 31.525  1.017    1.00 120.62 ? 508  GLU   B CD  1 
ATOM   5058  O  OE1 . GLU   B  1 207 ? -23.862 31.921  0.739    1.00 128.23 ? 508  GLU   B OE1 1 
ATOM   5059  O  OE2 . GLU   B  1 207 ? -21.715 31.712  0.273    1.00 122.63 ? 508  GLU   B OE2 1 
ATOM   5060  N  N   . ILE   B  1 208 ? -25.799 29.306  5.369    1.00 77.48  ? 509  ILE   B N   1 
ATOM   5061  C  CA  . ILE   B  1 208 ? -26.803 29.514  6.415    1.00 71.10  ? 509  ILE   B CA  1 
ATOM   5062  C  C   . ILE   B  1 208 ? -26.298 28.968  7.742    1.00 73.71  ? 509  ILE   B C   1 
ATOM   5063  O  O   . ILE   B  1 208 ? -26.440 29.605  8.794    1.00 79.21  ? 509  ILE   B O   1 
ATOM   5064  C  CB  . ILE   B  1 208 ? -28.144 28.869  6.028    1.00 59.31  ? 509  ILE   B CB  1 
ATOM   5065  C  CG1 . ILE   B  1 208 ? -28.573 29.308  4.633    1.00 64.99  ? 509  ILE   B CG1 1 
ATOM   5066  C  CG2 . ILE   B  1 208 ? -29.207 29.253  7.037    1.00 53.21  ? 509  ILE   B CG2 1 
ATOM   5067  C  CD1 . ILE   B  1 208 ? -29.853 28.646  4.148    1.00 66.35  ? 509  ILE   B CD1 1 
ATOM   5068  N  N   . CYS   B  1 209 ? -25.718 27.767  7.708    1.00 66.52  ? 510  CYS   B N   1 
ATOM   5069  C  CA  . CYS   B  1 209 ? -24.988 27.238  8.852    1.00 63.01  ? 510  CYS   B CA  1 
ATOM   5070  C  C   . CYS   B  1 209 ? -23.995 28.262  9.393    1.00 74.51  ? 510  CYS   B C   1 
ATOM   5071  O  O   . CYS   B  1 209 ? -24.034 28.619  10.578   1.00 76.35  ? 510  CYS   B O   1 
ATOM   5072  C  CB  . CYS   B  1 209 ? -24.267 25.952  8.453    1.00 56.29  ? 510  CYS   B CB  1 
ATOM   5073  S  SG  . CYS   B  1 209 ? -25.373 24.584  8.093    1.00 59.70  ? 510  CYS   B SG  1 
ATOM   5074  N  N   . ILE   B  1 210 ? -23.082 28.732  8.533    1.00 77.33  ? 511  ILE   B N   1 
ATOM   5075  C  CA  . ILE   B  1 210 ? -22.103 29.733  8.959    1.00 78.54  ? 511  ILE   B CA  1 
ATOM   5076  C  C   . ILE   B  1 210 ? -22.815 30.945  9.534    1.00 82.79  ? 511  ILE   B C   1 
ATOM   5077  O  O   . ILE   B  1 210 ? -22.514 31.401  10.645   1.00 79.76  ? 511  ILE   B O   1 
ATOM   5078  C  CB  . ILE   B  1 210 ? -21.186 30.131  7.791    1.00 70.03  ? 511  ILE   B CB  1 
ATOM   5079  C  CG1 . ILE   B  1 210 ? -20.141 29.053  7.526    1.00 69.13  ? 511  ILE   B CG1 1 
ATOM   5080  C  CG2 . ILE   B  1 210 ? -20.498 31.426  8.106    1.00 72.99  ? 511  ILE   B CG2 1 
ATOM   5081  C  CD1 . ILE   B  1 210 ? -19.499 29.158  6.150    1.00 67.99  ? 511  ILE   B CD1 1 
ATOM   5082  N  N   . GLN   B  1 211 ? -23.794 31.463  8.792    1.00 86.83  ? 512  GLN   B N   1 
ATOM   5083  C  CA  . GLN   B  1 211 ? -24.595 32.601  9.221    1.00 87.39  ? 512  GLN   B CA  1 
ATOM   5084  C  C   . GLN   B  1 211 ? -25.402 32.300  10.479   1.00 78.32  ? 512  GLN   B C   1 
ATOM   5085  O  O   . GLN   B  1 211 ? -25.929 33.225  11.100   1.00 79.64  ? 512  GLN   B O   1 
ATOM   5086  C  CB  . GLN   B  1 211 ? -25.501 33.020  8.051    1.00 94.31  ? 512  GLN   B CB  1 
ATOM   5087  C  CG  . GLN   B  1 211 ? -26.194 34.357  8.188    1.00 99.66  ? 512  GLN   B CG  1 
ATOM   5088  C  CD  . GLN   B  1 211 ? -27.624 34.211  8.663    1.00 103.16 ? 512  GLN   B CD  1 
ATOM   5089  O  OE1 . GLN   B  1 211 ? -28.260 33.169  8.463    1.00 104.20 ? 512  GLN   B OE1 1 
ATOM   5090  N  NE2 . GLN   B  1 211 ? -28.141 35.255  9.301    1.00 102.04 ? 512  GLN   B NE2 1 
ATOM   5091  N  N   . GLN   B  1 212 ? -25.492 31.041  10.885   1.00 73.55  ? 513  GLN   B N   1 
ATOM   5092  C  CA  . GLN   B  1 212 ? -26.188 30.667  12.107   1.00 76.95  ? 513  GLN   B CA  1 
ATOM   5093  C  C   . GLN   B  1 212 ? -25.256 30.467  13.293   1.00 68.22  ? 513  GLN   B C   1 
ATOM   5094  O  O   . GLN   B  1 212 ? -25.725 30.127  14.380   1.00 64.19  ? 513  GLN   B O   1 
ATOM   5095  C  CB  . GLN   B  1 212 ? -27.005 29.399  11.872   1.00 85.64  ? 513  GLN   B CB  1 
ATOM   5096  C  CG  . GLN   B  1 212 ? -28.398 29.687  11.390   1.00 86.29  ? 513  GLN   B CG  1 
ATOM   5097  C  CD  . GLN   B  1 212 ? -29.108 30.624  12.336   1.00 89.03  ? 513  GLN   B CD  1 
ATOM   5098  O  OE1 . GLN   B  1 212 ? -29.207 31.822  12.079   1.00 96.49  ? 513  GLN   B OE1 1 
ATOM   5099  N  NE2 . GLN   B  1 212 ? -29.584 30.089  13.451   1.00 83.37  ? 513  GLN   B NE2 1 
ATOM   5100  N  N   . GLY   B  1 213 ? -23.957 30.670  13.112   1.00 70.84  ? 514  GLY   B N   1 
ATOM   5101  C  CA  . GLY   B  1 213 ? -22.984 30.445  14.165   1.00 68.45  ? 514  GLY   B CA  1 
ATOM   5102  C  C   . GLY   B  1 213 ? -22.028 29.303  13.903   1.00 68.78  ? 514  GLY   B C   1 
ATOM   5103  O  O   . GLY   B  1 213 ? -21.145 29.061  14.739   1.00 66.37  ? 514  GLY   B O   1 
ATOM   5104  N  N   . TRP   B  1 214 ? -22.157 28.577  12.790   1.00 68.80  ? 515  TRP   B N   1 
ATOM   5105  C  CA  . TRP   B  1 214 ? -21.277 27.444  12.545   1.00 66.45  ? 515  TRP   B CA  1 
ATOM   5106  C  C   . TRP   B  1 214 ? -19.853 27.931  12.314   1.00 76.32  ? 515  TRP   B C   1 
ATOM   5107  O  O   . TRP   B  1 214 ? -19.619 28.912  11.599   1.00 75.59  ? 515  TRP   B O   1 
ATOM   5108  C  CB  . TRP   B  1 214 ? -21.764 26.619  11.354   1.00 62.43  ? 515  TRP   B CB  1 
ATOM   5109  C  CG  . TRP   B  1 214 ? -21.062 25.298  11.251   1.00 68.07  ? 515  TRP   B CG  1 
ATOM   5110  C  CD1 . TRP   B  1 214 ? -20.957 24.354  12.232   1.00 64.75  ? 515  TRP   B CD1 1 
ATOM   5111  C  CD2 . TRP   B  1 214 ? -20.362 24.771  10.112   1.00 68.00  ? 515  TRP   B CD2 1 
ATOM   5112  N  NE1 . TRP   B  1 214 ? -20.234 23.275  11.778   1.00 65.49  ? 515  TRP   B NE1 1 
ATOM   5113  C  CE2 . TRP   B  1 214 ? -19.854 23.509  10.482   1.00 67.13  ? 515  TRP   B CE2 1 
ATOM   5114  C  CE3 . TRP   B  1 214 ? -20.108 25.247  8.823    1.00 74.80  ? 515  TRP   B CE3 1 
ATOM   5115  C  CZ2 . TRP   B  1 214 ? -19.113 22.718  9.610    1.00 69.16  ? 515  TRP   B CZ2 1 
ATOM   5116  C  CZ3 . TRP   B  1 214 ? -19.372 24.458  7.954    1.00 73.74  ? 515  TRP   B CZ3 1 
ATOM   5117  C  CH2 . TRP   B  1 214 ? -18.881 23.210  8.353    1.00 73.58  ? 515  TRP   B CH2 1 
ATOM   5118  N  N   . LYS   B  1 215 ? -18.906 27.252  12.950   1.00 80.20  ? 516  LYS   B N   1 
ATOM   5119  C  CA  . LYS   B  1 215 ? -17.481 27.505  12.803   1.00 83.83  ? 516  LYS   B CA  1 
ATOM   5120  C  C   . LYS   B  1 215 ? -16.962 26.594  11.698   1.00 83.45  ? 516  LYS   B C   1 
ATOM   5121  O  O   . LYS   B  1 215 ? -16.730 25.403  11.929   1.00 90.68  ? 516  LYS   B O   1 
ATOM   5122  C  CB  . LYS   B  1 215 ? -16.750 27.257  14.129   1.00 83.33  ? 516  LYS   B CB  1 
ATOM   5123  C  CG  . LYS   B  1 215 ? -17.217 25.988  14.882   1.00 83.98  ? 516  LYS   B CG  1 
ATOM   5124  C  CD  . LYS   B  1 215 ? -18.358 26.256  15.874   1.00 85.31  ? 516  LYS   B CD  1 
ATOM   5125  C  CE  . LYS   B  1 215 ? -17.860 26.116  17.322   1.00 91.00  ? 516  LYS   B CE  1 
ATOM   5126  N  NZ  . LYS   B  1 215 ? -18.210 27.264  18.211   1.00 89.01  ? 516  LYS   B NZ  1 
ATOM   5127  N  N   . PRO   B  1 216 ? -16.798 27.090  10.482   1.00 76.74  ? 517  PRO   B N   1 
ATOM   5128  C  CA  . PRO   B  1 216 ? -16.394 26.215  9.400    1.00 71.77  ? 517  PRO   B CA  1 
ATOM   5129  C  C   . PRO   B  1 216 ? -14.910 25.917  9.487    1.00 74.33  ? 517  PRO   B C   1 
ATOM   5130  O  O   . PRO   B  1 216 ? -14.087 26.841  9.590    1.00 80.83  ? 517  PRO   B O   1 
ATOM   5131  C  CB  . PRO   B  1 216 ? -16.729 27.034  8.147    1.00 77.04  ? 517  PRO   B CB  1 
ATOM   5132  C  CG  . PRO   B  1 216 ? -16.531 28.454  8.592    1.00 80.02  ? 517  PRO   B CG  1 
ATOM   5133  C  CD  . PRO   B  1 216 ? -16.909 28.496  10.052   1.00 79.72  ? 517  PRO   B CD  1 
ATOM   5134  N  N   . PRO   B  1 217 ? -14.526 24.640  9.479    1.00 66.94  ? 518  PRO   B N   1 
ATOM   5135  C  CA  . PRO   B  1 217 ? -13.099 24.310  9.313    1.00 69.27  ? 518  PRO   B CA  1 
ATOM   5136  C  C   . PRO   B  1 217 ? -12.573 24.598  7.902    1.00 71.06  ? 518  PRO   B C   1 
ATOM   5137  O  O   . PRO   B  1 217 ? -11.350 24.677  7.714    1.00 73.50  ? 518  PRO   B O   1 
ATOM   5138  C  CB  . PRO   B  1 217 ? -13.046 22.815  9.655    1.00 65.74  ? 518  PRO   B CB  1 
ATOM   5139  C  CG  . PRO   B  1 217 ? -14.443 22.310  9.361    1.00 59.30  ? 518  PRO   B CG  1 
ATOM   5140  C  CD  . PRO   B  1 217 ? -15.373 23.448  9.661    1.00 56.56  ? 518  PRO   B CD  1 
ATOM   5141  N  N   . ARG   B  1 218 ? -13.461 24.758  6.918    1.00 68.62  ? 519  ARG   B N   1 
ATOM   5142  C  CA  . ARG   B  1 218 ? -13.114 25.242  5.577    1.00 81.04  ? 519  ARG   B CA  1 
ATOM   5143  C  C   . ARG   B  1 218 ? -12.136 24.309  4.859    1.00 90.45  ? 519  ARG   B C   1 
ATOM   5144  O  O   . ARG   B  1 218 ? -11.103 24.733  4.333    1.00 88.79  ? 519  ARG   B O   1 
ATOM   5145  C  CB  . ARG   B  1 218 ? -12.578 26.677  5.624    1.00 81.83  ? 519  ARG   B CB  1 
ATOM   5146  C  CG  . ARG   B  1 218 ? -13.584 27.689  6.168    1.00 81.30  ? 519  ARG   B CG  1 
ATOM   5147  C  CD  . ARG   B  1 218 ? -13.245 29.115  5.743    1.00 83.17  ? 519  ARG   B CD  1 
ATOM   5148  N  NE  . ARG   B  1 218 ? -14.130 29.595  4.681    1.00 84.86  ? 519  ARG   B NE  1 
ATOM   5149  C  CZ  . ARG   B  1 218 ? -15.107 30.482  4.859    1.00 87.94  ? 519  ARG   B CZ  1 
ATOM   5150  N  NH1 . ARG   B  1 218 ? -15.868 30.849  3.830    1.00 86.02  ? 519  ARG   B NH1 1 
ATOM   5151  N  NH2 . ARG   B  1 218 ? -15.321 31.012  6.060    1.00 86.92  ? 519  ARG   B NH2 1 
ATOM   5152  N  N   . GLY   B  1 219 ? -12.487 23.020  4.828    1.00 94.96  ? 520  GLY   B N   1 
ATOM   5153  C  CA  . GLY   B  1 219 ? -11.828 22.039  4.005    1.00 96.07  ? 520  GLY   B CA  1 
ATOM   5154  C  C   . GLY   B  1 219 ? -12.699 21.583  2.851    1.00 96.13  ? 520  GLY   B C   1 
ATOM   5155  O  O   . GLY   B  1 219 ? -13.699 22.220  2.494    1.00 93.97  ? 520  GLY   B O   1 
ATOM   5156  N  N   . ARG   B  1 220 ? -12.316 20.456  2.252    1.00 94.53  ? 521  ARG   B N   1 
ATOM   5157  C  CA  . ARG   B  1 220 ? -13.134 19.896  1.180    1.00 87.16  ? 521  ARG   B CA  1 
ATOM   5158  C  C   . ARG   B  1 220 ? -14.265 19.050  1.749    1.00 90.06  ? 521  ARG   B C   1 
ATOM   5159  O  O   . ARG   B  1 220 ? -15.436 19.258  1.417    1.00 88.28  ? 521  ARG   B O   1 
ATOM   5160  C  CB  . ARG   B  1 220 ? -12.262 19.073  0.229    1.00 82.20  ? 521  ARG   B CB  1 
ATOM   5161  C  CG  . ARG   B  1 220 ? -12.855 18.851  -1.146   1.00 80.41  ? 521  ARG   B CG  1 
ATOM   5162  C  CD  . ARG   B  1 220 ? -11.826 19.221  -2.209   1.00 91.68  ? 521  ARG   B CD  1 
ATOM   5163  N  NE  . ARG   B  1 220 ? -12.406 19.333  -3.547   1.00 91.64  ? 521  ARG   B NE  1 
ATOM   5164  C  CZ  . ARG   B  1 220 ? -12.159 18.494  -4.548   1.00 90.52  ? 521  ARG   B CZ  1 
ATOM   5165  N  NH1 . ARG   B  1 220 ? -11.322 17.477  -4.368   1.00 87.03  ? 521  ARG   B NH1 1 
ATOM   5166  N  NH2 . ARG   B  1 220 ? -12.747 18.676  -5.729   1.00 92.33  ? 521  ARG   B NH2 1 
ATOM   5167  N  N   . PHE   B  1 221 ? -13.938 18.124  2.644    1.00 95.46  ? 522  PHE   B N   1 
ATOM   5168  C  CA  . PHE   B  1 221 ? -14.906 17.184  3.190    1.00 89.85  ? 522  PHE   B CA  1 
ATOM   5169  C  C   . PHE   B  1 221 ? -15.237 17.543  4.639    1.00 87.26  ? 522  PHE   B C   1 
ATOM   5170  O  O   . PHE   B  1 221 ? -14.935 16.804  5.583    1.00 89.65  ? 522  PHE   B O   1 
ATOM   5171  C  CB  . PHE   B  1 221 ? -14.365 15.765  3.048    1.00 87.69  ? 522  PHE   B CB  1 
ATOM   5172  C  CG  . PHE   B  1 221 ? -14.102 15.383  1.627    1.00 85.92  ? 522  PHE   B CG  1 
ATOM   5173  C  CD1 . PHE   B  1 221 ? -13.066 14.533  1.296    1.00 86.03  ? 522  PHE   B CD1 1 
ATOM   5174  C  CD2 . PHE   B  1 221 ? -14.894 15.890  0.613    1.00 91.07  ? 522  PHE   B CD2 1 
ATOM   5175  C  CE1 . PHE   B  1 221 ? -12.825 14.195  -0.022   1.00 89.88  ? 522  PHE   B CE1 1 
ATOM   5176  C  CE2 . PHE   B  1 221 ? -14.662 15.555  -0.708   1.00 94.17  ? 522  PHE   B CE2 1 
ATOM   5177  C  CZ  . PHE   B  1 221 ? -13.626 14.708  -1.028   1.00 93.53  ? 522  PHE   B CZ  1 
ATOM   5178  N  N   . ASP   B  1 222 ? -15.890 18.695  4.802    1.00 74.04  ? 523  ASP   B N   1 
ATOM   5179  C  CA  . ASP   B  1 222 ? -16.394 19.157  6.092    1.00 54.59  ? 523  ASP   B CA  1 
ATOM   5180  C  C   . ASP   B  1 222 ? -17.819 18.645  6.253    1.00 58.20  ? 523  ASP   B C   1 
ATOM   5181  O  O   . ASP   B  1 222 ? -18.720 19.106  5.548    1.00 62.23  ? 523  ASP   B O   1 
ATOM   5182  C  CB  . ASP   B  1 222 ? -16.377 20.686  6.165    1.00 51.32  ? 523  ASP   B CB  1 
ATOM   5183  C  CG  . ASP   B  1 222 ? -14.973 21.273  6.240    1.00 68.95  ? 523  ASP   B CG  1 
ATOM   5184  O  OD1 . ASP   B  1 222 ? -13.993 20.496  6.328    1.00 77.37  ? 523  ASP   B OD1 1 
ATOM   5185  O  OD2 . ASP   B  1 222 ? -14.851 22.519  6.230    1.00 68.55  ? 523  ASP   B OD2 1 
ATOM   5186  N  N   . VAL   B  1 223 ? -18.038 17.702  7.172    1.00 53.60  ? 524  VAL   B N   1 
ATOM   5187  C  CA  . VAL   B  1 223 ? -19.406 17.250  7.413    1.00 41.16  ? 524  VAL   B CA  1 
ATOM   5188  C  C   . VAL   B  1 223 ? -20.202 18.417  7.971    1.00 47.32  ? 524  VAL   B C   1 
ATOM   5189  O  O   . VAL   B  1 223 ? -19.824 19.016  8.983    1.00 54.58  ? 524  VAL   B O   1 
ATOM   5190  C  CB  . VAL   B  1 223 ? -19.452 16.046  8.357    1.00 40.22  ? 524  VAL   B CB  1 
ATOM   5191  C  CG1 . VAL   B  1 223 ? -20.887 15.624  8.583    1.00 33.41  ? 524  VAL   B CG1 1 
ATOM   5192  C  CG2 . VAL   B  1 223 ? -18.615 14.884  7.814    1.00 35.62  ? 524  VAL   B CG2 1 
ATOM   5193  N  N   . LEU   B  1 224 ? -21.280 18.771  7.289    1.00 45.43  ? 525  LEU   B N   1 
ATOM   5194  C  CA  . LEU   B  1 224 ? -22.080 19.898  7.716    1.00 51.84  ? 525  LEU   B CA  1 
ATOM   5195  C  C   . LEU   B  1 224 ? -22.728 19.582  9.059    1.00 49.62  ? 525  LEU   B C   1 
ATOM   5196  O  O   . LEU   B  1 224 ? -22.941 18.415  9.392    1.00 58.80  ? 525  LEU   B O   1 
ATOM   5197  C  CB  . LEU   B  1 224 ? -23.157 20.218  6.684    1.00 52.67  ? 525  LEU   B CB  1 
ATOM   5198  C  CG  . LEU   B  1 224 ? -22.678 20.866  5.392    1.00 56.22  ? 525  LEU   B CG  1 
ATOM   5199  C  CD1 . LEU   B  1 224 ? -23.618 20.489  4.263    1.00 48.55  ? 525  LEU   B CD1 1 
ATOM   5200  C  CD2 . LEU   B  1 224 ? -22.650 22.364  5.586    1.00 68.68  ? 525  LEU   B CD2 1 
ATOM   5201  N  N   . PRO   B  1 225 ? -23.026 20.598  9.854    1.00 41.39  ? 526  PRO   B N   1 
ATOM   5202  C  CA  . PRO   B  1 225 ? -23.828 20.382  11.053   1.00 37.50  ? 526  PRO   B CA  1 
ATOM   5203  C  C   . PRO   B  1 225 ? -25.243 20.020  10.657   1.00 47.37  ? 526  PRO   B C   1 
ATOM   5204  O  O   . PRO   B  1 225 ? -25.614 20.070  9.488    1.00 54.98  ? 526  PRO   B O   1 
ATOM   5205  C  CB  . PRO   B  1 225 ? -23.787 21.740  11.741   1.00 41.27  ? 526  PRO   B CB  1 
ATOM   5206  C  CG  . PRO   B  1 225 ? -23.639 22.689  10.649   1.00 50.71  ? 526  PRO   B CG  1 
ATOM   5207  C  CD  . PRO   B  1 225 ? -22.737 22.025  9.651    1.00 51.25  ? 526  PRO   B CD  1 
ATOM   5208  N  N   . LEU   B  1 226 ? -26.041 19.663  11.653   1.00 47.56  ? 527  LEU   B N   1 
ATOM   5209  C  CA  . LEU   B  1 226 ? -27.479 19.539  11.477   1.00 48.28  ? 527  LEU   B CA  1 
ATOM   5210  C  C   . LEU   B  1 226 ? -28.143 20.876  11.795   1.00 56.57  ? 527  LEU   B C   1 
ATOM   5211  O  O   . LEU   B  1 226 ? -27.682 21.599  12.676   1.00 70.00  ? 527  LEU   B O   1 
ATOM   5212  C  CB  . LEU   B  1 226 ? -28.020 18.444  12.397   1.00 39.54  ? 527  LEU   B CB  1 
ATOM   5213  C  CG  . LEU   B  1 226 ? -27.679 17.020  11.962   1.00 41.06  ? 527  LEU   B CG  1 
ATOM   5214  C  CD1 . LEU   B  1 226 ? -28.083 16.027  13.021   1.00 29.80  ? 527  LEU   B CD1 1 
ATOM   5215  C  CD2 . LEU   B  1 226 ? -28.372 16.680  10.618   1.00 30.29  ? 527  LEU   B CD2 1 
ATOM   5216  N  N   . LEU   B  1 227 ? -29.205 21.222  11.063   1.00 54.00  ? 528  LEU   B N   1 
ATOM   5217  C  CA  . LEU   B  1 227 ? -30.017 22.403  11.391   1.00 51.77  ? 528  LEU   B CA  1 
ATOM   5218  C  C   . LEU   B  1 227 ? -31.425 21.907  11.659   1.00 57.49  ? 528  LEU   B C   1 
ATOM   5219  O  O   . LEU   B  1 227 ? -32.227 21.803  10.735   1.00 53.84  ? 528  LEU   B O   1 
ATOM   5220  C  CB  . LEU   B  1 227 ? -30.037 23.455  10.292   1.00 41.11  ? 528  LEU   B CB  1 
ATOM   5221  C  CG  . LEU   B  1 227 ? -29.442 24.855  10.493   1.00 47.32  ? 528  LEU   B CG  1 
ATOM   5222  C  CD1 . LEU   B  1 227 ? -29.868 25.802  9.369    1.00 51.40  ? 528  LEU   B CD1 1 
ATOM   5223  C  CD2 . LEU   B  1 227 ? -29.798 25.437  11.832   1.00 50.14  ? 528  LEU   B CD2 1 
ATOM   5224  N  N   . LEU   B  1 228 ? -31.737 21.625  12.918   1.00 59.36  ? 529  LEU   B N   1 
ATOM   5225  C  CA  . LEU   B  1 228 ? -32.986 20.966  13.268   1.00 53.80  ? 529  LEU   B CA  1 
ATOM   5226  C  C   . LEU   B  1 228 ? -34.010 21.989  13.750   1.00 53.17  ? 529  LEU   B C   1 
ATOM   5227  O  O   . LEU   B  1 228 ? -33.672 22.877  14.541   1.00 43.03  ? 529  LEU   B O   1 
ATOM   5228  C  CB  . LEU   B  1 228 ? -32.711 19.892  14.315   1.00 45.22  ? 529  LEU   B CB  1 
ATOM   5229  C  CG  . LEU   B  1 228 ? -31.612 18.983  13.737   1.00 43.27  ? 529  LEU   B CG  1 
ATOM   5230  C  CD1 . LEU   B  1 228 ? -31.380 17.807  14.601   1.00 28.99  ? 529  LEU   B CD1 1 
ATOM   5231  C  CD2 . LEU   B  1 228 ? -31.994 18.492  12.359   1.00 39.38  ? 529  LEU   B CD2 1 
ATOM   5232  N  N   . GLN   B  1 229 ? -35.246 21.888  13.228   1.00 50.41  ? 530  GLN   B N   1 
ATOM   5233  C  CA  . GLN   B  1 229 ? -36.353 22.778  13.585   1.00 47.23  ? 530  GLN   B CA  1 
ATOM   5234  C  C   . GLN   B  1 229 ? -37.524 21.973  14.141   1.00 53.75  ? 530  GLN   B C   1 
ATOM   5235  O  O   . GLN   B  1 229 ? -38.023 21.054  13.480   1.00 54.60  ? 530  GLN   B O   1 
ATOM   5236  C  CB  . GLN   B  1 229 ? -36.838 23.591  12.392   1.00 49.53  ? 530  GLN   B CB  1 
ATOM   5237  C  CG  . GLN   B  1 229 ? -38.110 24.393  12.678   1.00 57.92  ? 530  GLN   B CG  1 
ATOM   5238  C  CD  . GLN   B  1 229 ? -38.782 24.982  11.420   1.00 65.08  ? 530  GLN   B CD  1 
ATOM   5239  O  OE1 . GLN   B  1 229 ? -38.212 25.000  10.326   1.00 56.56  ? 530  GLN   B OE1 1 
ATOM   5240  N  NE2 . GLN   B  1 229 ? -40.006 25.464  11.590   1.00 72.37  ? 530  GLN   B NE2 1 
ATOM   5241  N  N   . ALA   B  1 230 ? -37.973 22.342  15.345   1.00 48.11  ? 531  ALA   B N   1 
ATOM   5242  C  CA  . ALA   B  1 230 ? -39.056 21.676  16.049   1.00 42.53  ? 531  ALA   B CA  1 
ATOM   5243  C  C   . ALA   B  1 230 ? -40.184 22.653  16.319   1.00 48.35  ? 531  ALA   B C   1 
ATOM   5244  O  O   . ALA   B  1 230 ? -39.950 23.840  16.556   1.00 54.93  ? 531  ALA   B O   1 
ATOM   5245  C  CB  . ALA   B  1 230 ? -38.584 21.100  17.370   1.00 41.96  ? 531  ALA   B CB  1 
ATOM   5246  N  N   . ASN   B  1 231 ? -41.405 22.125  16.304   1.00 53.14  ? 532  ASN   B N   1 
ATOM   5247  C  CA  . ASN   B  1 231 ? -42.633 22.899  16.467   1.00 61.34  ? 532  ASN   B CA  1 
ATOM   5248  C  C   . ASN   B  1 231 ? -42.535 24.358  16.033   1.00 55.62  ? 532  ASN   B C   1 
ATOM   5249  O  O   . ASN   B  1 231 ? -42.722 25.261  16.853   1.00 56.53  ? 532  ASN   B O   1 
ATOM   5250  C  CB  . ASN   B  1 231 ? -43.088 22.852  17.917   1.00 66.98  ? 532  ASN   B CB  1 
ATOM   5251  C  CG  . ASN   B  1 231 ? -44.586 22.922  18.038   1.00 75.36  ? 532  ASN   B CG  1 
ATOM   5252  O  OD1 . ASN   B  1 231 ? -45.300 22.323  17.234   1.00 78.89  ? 532  ASN   B OD1 1 
ATOM   5253  N  ND2 . ASN   B  1 231 ? -45.077 23.652  19.034   1.00 75.34  ? 532  ASN   B ND2 1 
ATOM   5254  N  N   . GLY   B  1 232 ? -42.217 24.597  14.765   1.00 51.91  ? 533  GLY   B N   1 
ATOM   5255  C  CA  . GLY   B  1 232 ? -42.201 25.937  14.206   1.00 56.95  ? 533  GLY   B CA  1 
ATOM   5256  C  C   . GLY   B  1 232 ? -41.056 26.857  14.597   1.00 62.09  ? 533  GLY   B C   1 
ATOM   5257  O  O   . GLY   B  1 232 ? -40.823 27.875  13.933   1.00 63.14  ? 533  GLY   B O   1 
ATOM   5258  N  N   . ASN   B  1 233 ? -40.322 26.518  15.653   1.00 56.96  ? 534  ASN   B N   1 
ATOM   5259  C  CA  . ASN   B  1 233 ? -39.369 27.457  16.230   1.00 63.32  ? 534  ASN   B CA  1 
ATOM   5260  C  C   . ASN   B  1 233 ? -38.131 27.602  15.342   1.00 61.49  ? 534  ASN   B C   1 
ATOM   5261  O  O   . ASN   B  1 233 ? -37.988 26.942  14.310   1.00 55.95  ? 534  ASN   B O   1 
ATOM   5262  C  CB  . ASN   B  1 233 ? -39.006 27.018  17.646   1.00 61.30  ? 534  ASN   B CB  1 
ATOM   5263  C  CG  . ASN   B  1 233 ? -40.169 27.172  18.605   1.00 59.34  ? 534  ASN   B CG  1 
ATOM   5264  O  OD1 . ASN   B  1 233 ? -40.632 28.288  18.846   1.00 72.05  ? 534  ASN   B OD1 1 
ATOM   5265  N  ND2 . ASN   B  1 233 ? -40.659 26.059  19.142   1.00 51.52  ? 534  ASN   B ND2 1 
ATOM   5266  N  N   . ASP   B  1 234 ? -37.233 28.509  15.743   1.00 63.22  ? 535  ASP   B N   1 
ATOM   5267  C  CA  . ASP   B  1 234 ? -36.001 28.723  14.997   1.00 57.95  ? 535  ASP   B CA  1 
ATOM   5268  C  C   . ASP   B  1 234 ? -35.151 27.453  15.003   1.00 53.31  ? 535  ASP   B C   1 
ATOM   5269  O  O   . ASP   B  1 234 ? -35.145 26.706  15.985   1.00 51.09  ? 535  ASP   B O   1 
ATOM   5270  C  CB  . ASP   B  1 234 ? -35.190 29.876  15.587   1.00 64.34  ? 535  ASP   B CB  1 
ATOM   5271  C  CG  . ASP   B  1 234 ? -35.850 31.228  15.397   1.00 69.79  ? 535  ASP   B CG  1 
ATOM   5272  O  OD1 . ASP   B  1 234 ? -35.188 32.249  15.689   1.00 69.83  ? 535  ASP   B OD1 1 
ATOM   5273  O  OD2 . ASP   B  1 234 ? -37.025 31.273  14.975   1.00 72.34  ? 535  ASP   B OD2 1 
ATOM   5274  N  N   . PRO   B  1 235 ? -34.447 27.173  13.911   1.00 48.84  ? 536  PRO   B N   1 
ATOM   5275  C  CA  . PRO   B  1 235 ? -33.577 25.996  13.872   1.00 52.82  ? 536  PRO   B CA  1 
ATOM   5276  C  C   . PRO   B  1 235 ? -32.377 26.148  14.798   1.00 56.05  ? 536  PRO   B C   1 
ATOM   5277  O  O   . PRO   B  1 235 ? -32.070 27.228  15.310   1.00 64.02  ? 536  PRO   B O   1 
ATOM   5278  C  CB  . PRO   B  1 235 ? -33.165 25.903  12.392   1.00 46.31  ? 536  PRO   B CB  1 
ATOM   5279  C  CG  . PRO   B  1 235 ? -33.538 27.167  11.786   1.00 41.34  ? 536  PRO   B CG  1 
ATOM   5280  C  CD  . PRO   B  1 235 ? -34.684 27.717  12.568   1.00 47.36  ? 536  PRO   B CD  1 
ATOM   5281  N  N   . GLU   B  1 236 ? -31.695 25.022  15.012   1.00 50.43  ? 537  GLU   B N   1 
ATOM   5282  C  CA  . GLU   B  1 236 ? -30.630 24.933  16.003   1.00 57.84  ? 537  GLU   B CA  1 
ATOM   5283  C  C   . GLU   B  1 236 ? -29.505 24.048  15.482   1.00 52.50  ? 537  GLU   B C   1 
ATOM   5284  O  O   . GLU   B  1 236 ? -29.740 22.878  15.171   1.00 55.11  ? 537  GLU   B O   1 
ATOM   5285  C  CB  . GLU   B  1 236 ? -31.181 24.378  17.324   1.00 61.21  ? 537  GLU   B CB  1 
ATOM   5286  C  CG  . GLU   B  1 236 ? -32.041 25.363  18.120   1.00 58.42  ? 537  GLU   B CG  1 
ATOM   5287  C  CD  . GLU   B  1 236 ? -32.645 24.743  19.368   1.00 60.74  ? 537  GLU   B CD  1 
ATOM   5288  O  OE1 . GLU   B  1 236 ? -31.878 24.183  20.196   1.00 60.92  ? 537  GLU   B OE1 1 
ATOM   5289  O  OE2 . GLU   B  1 236 ? -33.889 24.816  19.513   1.00 61.13  ? 537  GLU   B OE2 1 
ATOM   5290  N  N   . LEU   B  1 237 ? -28.285 24.590  15.420   1.00 39.66  ? 538  LEU   B N   1 
ATOM   5291  C  CA  . LEU   B  1 237 ? -27.137 23.812  14.960   1.00 45.71  ? 538  LEU   B CA  1 
ATOM   5292  C  C   . LEU   B  1 237 ? -26.816 22.667  15.922   1.00 52.51  ? 538  LEU   B C   1 
ATOM   5293  O  O   . LEU   B  1 237 ? -26.928 22.814  17.137   1.00 51.21  ? 538  LEU   B O   1 
ATOM   5294  C  CB  . LEU   B  1 237 ? -25.916 24.725  14.791   1.00 38.56  ? 538  LEU   B CB  1 
ATOM   5295  C  CG  . LEU   B  1 237 ? -26.003 25.662  13.572   1.00 57.86  ? 538  LEU   B CG  1 
ATOM   5296  C  CD1 . LEU   B  1 237 ? -24.788 26.568  13.438   1.00 60.44  ? 538  LEU   B CD1 1 
ATOM   5297  C  CD2 . LEU   B  1 237 ? -26.239 24.901  12.260   1.00 45.70  ? 538  LEU   B CD2 1 
ATOM   5298  N  N   . PHE   B  1 238 ? -26.444 21.507  15.366   1.00 54.66  ? 539  PHE   B N   1 
ATOM   5299  C  CA  . PHE   B  1 238 ? -25.899 20.388  16.133   1.00 50.06  ? 539  PHE   B CA  1 
ATOM   5300  C  C   . PHE   B  1 238 ? -24.815 19.705  15.313   1.00 60.29  ? 539  PHE   B C   1 
ATOM   5301  O  O   . PHE   B  1 238 ? -24.970 19.541  14.101   1.00 60.33  ? 539  PHE   B O   1 
ATOM   5302  C  CB  . PHE   B  1 238 ? -26.968 19.350  16.488   1.00 43.42  ? 539  PHE   B CB  1 
ATOM   5303  C  CG  . PHE   B  1 238 ? -28.038 19.857  17.393   1.00 52.06  ? 539  PHE   B CG  1 
ATOM   5304  C  CD1 . PHE   B  1 238 ? -29.138 20.515  16.881   1.00 56.47  ? 539  PHE   B CD1 1 
ATOM   5305  C  CD2 . PHE   B  1 238 ? -27.947 19.678  18.769   1.00 48.43  ? 539  PHE   B CD2 1 
ATOM   5306  C  CE1 . PHE   B  1 238 ? -30.136 20.987  17.726   1.00 60.85  ? 539  PHE   B CE1 1 
ATOM   5307  C  CE2 . PHE   B  1 238 ? -28.938 20.151  19.613   1.00 46.07  ? 539  PHE   B CE2 1 
ATOM   5308  C  CZ  . PHE   B  1 238 ? -30.033 20.802  19.103   1.00 49.04  ? 539  PHE   B CZ  1 
ATOM   5309  N  N   . GLN   B  1 239 ? -23.730 19.284  15.970   1.00 59.03  ? 540  GLN   B N   1 
ATOM   5310  C  CA  . GLN   B  1 239 ? -22.635 18.583  15.299   1.00 60.86  ? 540  GLN   B CA  1 
ATOM   5311  C  C   . GLN   B  1 239 ? -22.770 17.083  15.551   1.00 50.97  ? 540  GLN   B C   1 
ATOM   5312  O  O   . GLN   B  1 239 ? -22.622 16.625  16.683   1.00 50.54  ? 540  GLN   B O   1 
ATOM   5313  C  CB  . GLN   B  1 239 ? -21.283 19.096  15.787   1.00 68.72  ? 540  GLN   B CB  1 
ATOM   5314  C  CG  . GLN   B  1 239 ? -20.097 18.277  15.292   1.00 77.86  ? 540  GLN   B CG  1 
ATOM   5315  C  CD  . GLN   B  1 239 ? -19.334 17.557  16.418   1.00 83.25  ? 540  GLN   B CD  1 
ATOM   5316  O  OE1 . GLN   B  1 239 ? -19.902 17.209  17.467   1.00 79.41  ? 540  GLN   B OE1 1 
ATOM   5317  N  NE2 . GLN   B  1 239 ? -18.039 17.325  16.192   1.00 75.59  ? 540  GLN   B NE2 1 
ATOM   5318  N  N   . ILE   B  1 240 ? -23.064 16.320  14.505   1.00 48.62  ? 541  ILE   B N   1 
ATOM   5319  C  CA  . ILE   B  1 240 ? -23.102 14.858  14.659   1.00 41.09  ? 541  ILE   B CA  1 
ATOM   5320  C  C   . ILE   B  1 240 ? -21.754 14.393  15.188   1.00 48.94  ? 541  ILE   B C   1 
ATOM   5321  O  O   . ILE   B  1 240 ? -20.703 14.846  14.689   1.00 49.37  ? 541  ILE   B O   1 
ATOM   5322  C  CB  . ILE   B  1 240 ? -23.407 14.175  13.311   1.00 44.36  ? 541  ILE   B CB  1 
ATOM   5323  C  CG1 . ILE   B  1 240 ? -24.709 14.698  12.692   1.00 41.71  ? 541  ILE   B CG1 1 
ATOM   5324  C  CG2 . ILE   B  1 240 ? -23.438 12.673  13.480   1.00 37.27  ? 541  ILE   B CG2 1 
ATOM   5325  C  CD1 . ILE   B  1 240 ? -24.699 14.729  11.181   1.00 44.49  ? 541  ILE   B CD1 1 
ATOM   5326  N  N   . PRO   B  1 241 ? -21.702 13.538  16.200   1.00 48.10  ? 542  PRO   B N   1 
ATOM   5327  C  CA  . PRO   B  1 241 ? -20.425 13.007  16.624   1.00 48.42  ? 542  PRO   B CA  1 
ATOM   5328  C  C   . PRO   B  1 241 ? -19.742 12.315  15.461   1.00 47.90  ? 542  PRO   B C   1 
ATOM   5329  O  O   . PRO   B  1 241 ? -20.341 11.444  14.811   1.00 43.26  ? 542  PRO   B O   1 
ATOM   5330  C  CB  . PRO   B  1 241 ? -20.805 12.017  17.737   1.00 51.72  ? 542  PRO   B CB  1 
ATOM   5331  C  CG  . PRO   B  1 241 ? -22.109 12.526  18.241   1.00 46.05  ? 542  PRO   B CG  1 
ATOM   5332  C  CD  . PRO   B  1 241 ? -22.810 13.045  17.035   1.00 44.95  ? 542  PRO   B CD  1 
ATOM   5333  N  N   . PRO   B  1 242 ? -18.501 12.706  15.156   1.00 44.62  ? 543  PRO   B N   1 
ATOM   5334  C  CA  . PRO   B  1 242 ? -17.767 12.080  14.050   1.00 43.78  ? 543  PRO   B CA  1 
ATOM   5335  C  C   . PRO   B  1 242 ? -17.768 10.569  14.101   1.00 54.49  ? 543  PRO   B C   1 
ATOM   5336  O  O   . PRO   B  1 242 ? -17.839 9.914   13.052   1.00 70.40  ? 543  PRO   B O   1 
ATOM   5337  C  CB  . PRO   B  1 242 ? -16.349 12.636  14.226   1.00 49.11  ? 543  PRO   B CB  1 
ATOM   5338  C  CG  . PRO   B  1 242 ? -16.529 13.897  15.009   1.00 44.81  ? 543  PRO   B CG  1 
ATOM   5339  C  CD  . PRO   B  1 242 ? -17.659 13.631  15.924   1.00 46.49  ? 543  PRO   B CD  1 
ATOM   5340  N  N   . GLU   B  1 243 ? -17.692 9.996   15.302   1.00 50.15  ? 544  GLU   B N   1 
ATOM   5341  C  CA  . GLU   B  1 243 ? -17.673 8.548   15.441   1.00 47.20  ? 544  GLU   B CA  1 
ATOM   5342  C  C   . GLU   B  1 243 ? -18.955 7.913   14.923   1.00 49.04  ? 544  GLU   B C   1 
ATOM   5343  O  O   . GLU   B  1 243 ? -18.982 6.702   14.688   1.00 54.82  ? 544  GLU   B O   1 
ATOM   5344  C  CB  . GLU   B  1 243 ? -17.398 8.164   16.913   1.00 38.41  ? 544  GLU   B CB  1 
ATOM   5345  C  CG  . GLU   B  1 243 ? -18.513 8.526   17.909   1.00 36.01  ? 544  GLU   B CG  1 
ATOM   5346  C  CD  . GLU   B  1 243 ? -18.232 9.800   18.658   1.00 49.66  ? 544  GLU   B CD  1 
ATOM   5347  O  OE1 . GLU   B  1 243 ? -17.319 10.522  18.208   1.00 47.02  ? 544  GLU   B OE1 1 
ATOM   5348  O  OE2 . GLU   B  1 243 ? -18.893 10.059  19.705   1.00 60.55  ? 544  GLU   B OE2 1 
ATOM   5349  N  N   . LEU   B  1 244 ? -20.003 8.698   14.697   1.00 41.99  ? 545  LEU   B N   1 
ATOM   5350  C  CA  . LEU   B  1 244 ? -21.227 8.178   14.116   1.00 35.94  ? 545  LEU   B CA  1 
ATOM   5351  C  C   . LEU   B  1 244 ? -21.286 8.340   12.606   1.00 42.38  ? 545  LEU   B C   1 
ATOM   5352  O  O   . LEU   B  1 244 ? -22.206 7.801   11.989   1.00 50.90  ? 545  LEU   B O   1 
ATOM   5353  C  CB  . LEU   B  1 244 ? -22.451 8.850   14.744   1.00 38.44  ? 545  LEU   B CB  1 
ATOM   5354  C  CG  . LEU   B  1 244 ? -22.762 8.683   16.233   1.00 34.81  ? 545  LEU   B CG  1 
ATOM   5355  C  CD1 . LEU   B  1 244 ? -23.812 9.695   16.708   1.00 33.37  ? 545  LEU   B CD1 1 
ATOM   5356  C  CD2 . LEU   B  1 244 ? -23.230 7.272   16.505   1.00 34.80  ? 545  LEU   B CD2 1 
ATOM   5357  N  N   . VAL   B  1 245 ? -20.339 9.058   11.989   1.00 45.04  ? 546  VAL   B N   1 
ATOM   5358  C  CA  . VAL   B  1 245 ? -20.361 9.296   10.534   1.00 45.61  ? 546  VAL   B CA  1 
ATOM   5359  C  C   . VAL   B  1 245 ? -19.361 8.389   9.835    1.00 38.23  ? 546  VAL   B C   1 
ATOM   5360  O  O   . VAL   B  1 245 ? -18.184 8.737   9.712    1.00 43.07  ? 546  VAL   B O   1 
ATOM   5361  C  CB  . VAL   B  1 245 ? -20.049 10.764  10.210   1.00 50.92  ? 546  VAL   B CB  1 
ATOM   5362  C  CG1 . VAL   B  1 245 ? -20.067 10.988  8.723    1.00 53.14  ? 546  VAL   B CG1 1 
ATOM   5363  C  CG2 . VAL   B  1 245 ? -21.040 11.673  10.914   1.00 62.14  ? 546  VAL   B CG2 1 
ATOM   5364  N  N   . LEU   B  1 246 ? -19.808 7.227   9.363    1.00 42.23  ? 547  LEU   B N   1 
ATOM   5365  C  CA  . LEU   B  1 246 ? -18.888 6.320   8.684    1.00 47.18  ? 547  LEU   B CA  1 
ATOM   5366  C  C   . LEU   B  1 246 ? -18.449 6.900   7.331    1.00 46.67  ? 547  LEU   B C   1 
ATOM   5367  O  O   . LEU   B  1 246 ? -19.215 7.571   6.637    1.00 43.29  ? 547  LEU   B O   1 
ATOM   5368  C  CB  . LEU   B  1 246 ? -19.520 4.940   8.525    1.00 42.27  ? 547  LEU   B CB  1 
ATOM   5369  C  CG  . LEU   B  1 246 ? -18.624 3.873   7.894    1.00 41.57  ? 547  LEU   B CG  1 
ATOM   5370  C  CD1 . LEU   B  1 246 ? -17.272 3.922   8.516    1.00 40.26  ? 547  LEU   B CD1 1 
ATOM   5371  C  CD2 . LEU   B  1 246 ? -19.236 2.516   8.131    1.00 42.31  ? 547  LEU   B CD2 1 
ATOM   5372  N  N   . GLU   B  1 247 ? -17.183 6.687   6.981    1.00 43.14  ? 548  GLU   B N   1 
ATOM   5373  C  CA  . GLU   B  1 247 ? -16.584 7.311   5.808    1.00 40.26  ? 548  GLU   B CA  1 
ATOM   5374  C  C   . GLU   B  1 247 ? -15.619 6.333   5.152    1.00 49.88  ? 548  GLU   B C   1 
ATOM   5375  O  O   . GLU   B  1 247 ? -14.918 5.583   5.841    1.00 44.59  ? 548  GLU   B O   1 
ATOM   5376  C  CB  . GLU   B  1 247 ? -15.827 8.599   6.155    1.00 39.42  ? 548  GLU   B CB  1 
ATOM   5377  C  CG  . GLU   B  1 247 ? -16.675 9.844   6.389    1.00 39.23  ? 548  GLU   B CG  1 
ATOM   5378  C  CD  . GLU   B  1 247 ? -15.802 11.056  6.727    1.00 54.41  ? 548  GLU   B CD  1 
ATOM   5379  O  OE1 . GLU   B  1 247 ? -14.915 10.921  7.600    1.00 54.99  ? 548  GLU   B OE1 1 
ATOM   5380  O  OE2 . GLU   B  1 247 ? -15.976 12.134  6.114    1.00 52.72  ? 548  GLU   B OE2 1 
ATOM   5381  N  N   . VAL   B  1 248 ? -15.580 6.343   3.821    1.00 48.99  ? 549  VAL   B N   1 
ATOM   5382  C  CA  . VAL   B  1 248 ? -14.752 5.416   3.065    1.00 47.57  ? 549  VAL   B CA  1 
ATOM   5383  C  C   . VAL   B  1 248 ? -13.751 6.222   2.245    1.00 57.73  ? 549  VAL   B C   1 
ATOM   5384  O  O   . VAL   B  1 248 ? -14.150 7.067   1.440    1.00 68.55  ? 549  VAL   B O   1 
ATOM   5385  C  CB  . VAL   B  1 248 ? -15.589 4.499   2.158    1.00 47.22  ? 549  VAL   B CB  1 
ATOM   5386  C  CG1 . VAL   B  1 248 ? -14.691 3.476   1.463    1.00 51.25  ? 549  VAL   B CG1 1 
ATOM   5387  C  CG2 . VAL   B  1 248 ? -16.687 3.806   2.970    1.00 39.10  ? 549  VAL   B CG2 1 
ATOM   5388  N  N   . PRO   B  1 249 ? -12.448 6.024   2.434    1.00 62.79  ? 550  PRO   B N   1 
ATOM   5389  C  CA  . PRO   B  1 249 ? -11.464 6.694   1.578    1.00 57.41  ? 550  PRO   B CA  1 
ATOM   5390  C  C   . PRO   B  1 249 ? -11.326 5.946   0.268    1.00 67.53  ? 550  PRO   B C   1 
ATOM   5391  O  O   . PRO   B  1 249 ? -11.257 4.714   0.249    1.00 72.64  ? 550  PRO   B O   1 
ATOM   5392  C  CB  . PRO   B  1 249 ? -10.168 6.622   2.397    1.00 71.33  ? 550  PRO   B CB  1 
ATOM   5393  C  CG  . PRO   B  1 249 ? -10.357 5.420   3.320    1.00 72.09  ? 550  PRO   B CG  1 
ATOM   5394  C  CD  . PRO   B  1 249 ? -11.832 5.317   3.582    1.00 65.63  ? 550  PRO   B CD  1 
ATOM   5395  N  N   . ILE   B  1 250 ? -11.289 6.703   -0.828   1.00 65.77  ? 551  ILE   B N   1 
ATOM   5396  C  CA  . ILE   B  1 250 ? -11.367 6.130   -2.170   1.00 56.63  ? 551  ILE   B CA  1 
ATOM   5397  C  C   . ILE   B  1 250 ? -9.956  5.856   -2.676   1.00 57.24  ? 551  ILE   B C   1 
ATOM   5398  O  O   . ILE   B  1 250 ? -9.171  6.782   -2.918   1.00 51.31  ? 551  ILE   B O   1 
ATOM   5399  C  CB  . ILE   B  1 250 ? -12.132 7.028   -3.150   1.00 52.49  ? 551  ILE   B CB  1 
ATOM   5400  C  CG1 . ILE   B  1 250 ? -13.447 7.511   -2.539   1.00 49.10  ? 551  ILE   B CG1 1 
ATOM   5401  C  CG2 . ILE   B  1 250 ? -12.433 6.245   -4.410   1.00 43.22  ? 551  ILE   B CG2 1 
ATOM   5402  C  CD1 . ILE   B  1 250 ? -14.329 6.395   -2.082   1.00 36.47  ? 551  ILE   B CD1 1 
ATOM   5403  N  N   . ARG   B  1 251 ? -9.638  4.575   -2.832   1.00 60.88  ? 552  ARG   B N   1 
ATOM   5404  C  CA  . ARG   B  1 251 ? -8.443  4.131   -3.529   1.00 58.75  ? 552  ARG   B CA  1 
ATOM   5405  C  C   . ARG   B  1 251 ? -8.840  3.267   -4.722   1.00 60.66  ? 552  ARG   B C   1 
ATOM   5406  O  O   . ARG   B  1 251 ? -9.986  2.826   -4.845   1.00 51.80  ? 552  ARG   B O   1 
ATOM   5407  C  CB  . ARG   B  1 251 ? -7.525  3.351   -2.601   1.00 55.25  ? 552  ARG   B CB  1 
ATOM   5408  C  CG  . ARG   B  1 251 ? -8.208  2.228   -1.878   1.00 68.04  ? 552  ARG   B CG  1 
ATOM   5409  C  CD  . ARG   B  1 251 ? -8.622  2.652   -0.467   1.00 67.50  ? 552  ARG   B CD  1 
ATOM   5410  N  NE  . ARG   B  1 251 ? -9.061  1.508   0.324    1.00 60.73  ? 552  ARG   B NE  1 
ATOM   5411  C  CZ  . ARG   B  1 251 ? -10.128 1.528   1.113    1.00 63.01  ? 552  ARG   B CZ  1 
ATOM   5412  N  NH1 . ARG   B  1 251 ? -10.467 0.440   1.789    1.00 63.52  ? 552  ARG   B NH1 1 
ATOM   5413  N  NH2 . ARG   B  1 251 ? -10.861 2.634   1.217    1.00 58.46  ? 552  ARG   B NH2 1 
ATOM   5414  N  N   . HIS   B  1 252 ? -7.869  3.030   -5.611   1.00 63.41  ? 553  HIS   B N   1 
ATOM   5415  C  CA  . HIS   B  1 252 ? -8.117  2.318   -6.856   1.00 54.84  ? 553  HIS   B CA  1 
ATOM   5416  C  C   . HIS   B  1 252 ? -7.338  1.012   -6.906   1.00 59.10  ? 553  HIS   B C   1 
ATOM   5417  O  O   . HIS   B  1 252 ? -6.147  0.987   -6.579   1.00 64.88  ? 553  HIS   B O   1 
ATOM   5418  C  CB  . HIS   B  1 252 ? -7.729  3.158   -8.061   1.00 53.32  ? 553  HIS   B CB  1 
ATOM   5419  C  CG  . HIS   B  1 252 ? -8.260  2.629   -9.355   1.00 62.46  ? 553  HIS   B CG  1 
ATOM   5420  N  ND1 . HIS   B  1 252 ? -7.607  1.660   -10.089  1.00 64.78  ? 553  HIS   B ND1 1 
ATOM   5421  C  CD2 . HIS   B  1 252 ? -9.384  2.930   -10.044  1.00 54.36  ? 553  HIS   B CD2 1 
ATOM   5422  C  CE1 . HIS   B  1 252 ? -8.308  1.386   -11.172  1.00 56.99  ? 553  HIS   B CE1 1 
ATOM   5423  N  NE2 . HIS   B  1 252 ? -9.392  2.140   -11.166  1.00 58.55  ? 553  HIS   B NE2 1 
ATOM   5424  N  N   . PRO   B  1 253 ? -7.970  -0.083  -7.337   1.00 56.30  ? 554  PRO   B N   1 
ATOM   5425  C  CA  . PRO   B  1 253 ? -7.314  -1.401  -7.260   1.00 55.40  ? 554  PRO   B CA  1 
ATOM   5426  C  C   . PRO   B  1 253 ? -6.146  -1.583  -8.209   1.00 61.53  ? 554  PRO   B C   1 
ATOM   5427  O  O   . PRO   B  1 253 ? -5.490  -2.627  -8.144   1.00 65.99  ? 554  PRO   B O   1 
ATOM   5428  C  CB  . PRO   B  1 253 ? -8.446  -2.387  -7.595   1.00 50.86  ? 554  PRO   B CB  1 
ATOM   5429  C  CG  . PRO   B  1 253 ? -9.532  -1.579  -8.165   1.00 52.23  ? 554  PRO   B CG  1 
ATOM   5430  C  CD  . PRO   B  1 253 ? -9.393  -0.174  -7.692   1.00 46.23  ? 554  PRO   B CD  1 
ATOM   5431  N  N   . LYS   B  1 254 ? -5.870  -0.631  -9.100   1.00 69.24  ? 555  LYS   B N   1 
ATOM   5432  C  CA  . LYS   B  1 254 ? -4.701  -0.726  -9.967   1.00 71.52  ? 555  LYS   B CA  1 
ATOM   5433  C  C   . LYS   B  1 254 ? -3.902  0.567   -9.893   1.00 72.39  ? 555  LYS   B C   1 
ATOM   5434  O  O   . LYS   B  1 254 ? -2.679  0.551   -9.719   1.00 72.34  ? 555  LYS   B O   1 
ATOM   5435  C  CB  . LYS   B  1 254 ? -5.111  -1.026  -11.415  1.00 78.29  ? 555  LYS   B CB  1 
ATOM   5436  C  CG  . LYS   B  1 254 ? -5.825  -2.370  -11.608  1.00 83.23  ? 555  LYS   B CG  1 
ATOM   5437  C  CD  . LYS   B  1 254 ? -4.986  -3.568  -11.121  1.00 89.41  ? 555  LYS   B CD  1 
ATOM   5438  C  CE  . LYS   B  1 254 ? -3.980  -4.069  -12.166  1.00 90.48  ? 555  LYS   B CE  1 
ATOM   5439  N  NZ  . LYS   B  1 254 ? -4.599  -4.919  -13.236  1.00 84.71  ? 555  LYS   B NZ  1 
ATOM   5440  N  N   . PHE   B  1 255 ? -4.594  1.692   -10.008  1.00 77.84  ? 556  PHE   B N   1 
ATOM   5441  C  CA  . PHE   B  1 255 ? -3.964  3.005   -9.936   1.00 81.31  ? 556  PHE   B CA  1 
ATOM   5442  C  C   . PHE   B  1 255 ? -3.576  3.285   -8.492   1.00 74.86  ? 556  PHE   B C   1 
ATOM   5443  O  O   . PHE   B  1 255 ? -4.420  3.623   -7.662   1.00 74.61  ? 556  PHE   B O   1 
ATOM   5444  C  CB  . PHE   B  1 255 ? -4.914  4.069   -10.474  1.00 85.63  ? 556  PHE   B CB  1 
ATOM   5445  C  CG  . PHE   B  1 255 ? -5.317  3.849   -11.899  1.00 82.74  ? 556  PHE   B CG  1 
ATOM   5446  C  CD1 . PHE   B  1 255 ? -6.535  4.304   -12.371  1.00 77.90  ? 556  PHE   B CD1 1 
ATOM   5447  C  CD2 . PHE   B  1 255 ? -4.473  3.183   -12.769  1.00 78.87  ? 556  PHE   B CD2 1 
ATOM   5448  C  CE1 . PHE   B  1 255 ? -6.901  4.100   -13.686  1.00 76.91  ? 556  PHE   B CE1 1 
ATOM   5449  C  CE2 . PHE   B  1 255 ? -4.836  2.976   -14.081  1.00 72.90  ? 556  PHE   B CE2 1 
ATOM   5450  C  CZ  . PHE   B  1 255 ? -6.050  3.436   -14.538  1.00 76.46  ? 556  PHE   B CZ  1 
ATOM   5451  N  N   . GLU   B  1 256 ? -2.292  3.122   -8.182   1.00 76.68  ? 557  GLU   B N   1 
ATOM   5452  C  CA  . GLU   B  1 256 ? -1.823  3.444   -6.841   1.00 84.00  ? 557  GLU   B CA  1 
ATOM   5453  C  C   . GLU   B  1 256 ? -1.831  4.945   -6.604   1.00 86.08  ? 557  GLU   B C   1 
ATOM   5454  O  O   . GLU   B  1 256 ? -1.996  5.393   -5.466   1.00 90.93  ? 557  GLU   B O   1 
ATOM   5455  C  CB  . GLU   B  1 256 ? -0.426  2.868   -6.622   1.00 87.00  ? 557  GLU   B CB  1 
ATOM   5456  C  CG  . GLU   B  1 256 ? -0.283  1.476   -7.192   1.00 92.43  ? 557  GLU   B CG  1 
ATOM   5457  C  CD  . GLU   B  1 256 ? 0.757   0.663   -6.477   1.00 104.36 ? 557  GLU   B CD  1 
ATOM   5458  O  OE1 . GLU   B  1 256 ? 1.798   1.235   -6.088   1.00 108.07 ? 557  GLU   B OE1 1 
ATOM   5459  O  OE2 . GLU   B  1 256 ? 0.525   -0.550  -6.303   1.00 112.17 ? 557  GLU   B OE2 1 
ATOM   5460  N  N   . TRP   B  1 257 ? -1.683  5.734   -7.665   1.00 84.02  ? 558  TRP   B N   1 
ATOM   5461  C  CA  . TRP   B  1 257 ? -1.726  7.179   -7.527   1.00 75.84  ? 558  TRP   B CA  1 
ATOM   5462  C  C   . TRP   B  1 257 ? -3.100  7.687   -7.157   1.00 73.36  ? 558  TRP   B C   1 
ATOM   5463  O  O   . TRP   B  1 257 ? -3.258  8.899   -6.982   1.00 78.53  ? 558  TRP   B O   1 
ATOM   5464  C  CB  . TRP   B  1 257 ? -1.267  7.845   -8.826   1.00 74.66  ? 558  TRP   B CB  1 
ATOM   5465  C  CG  . TRP   B  1 257 ? -2.018  7.400   -10.038  1.00 74.10  ? 558  TRP   B CG  1 
ATOM   5466  C  CD1 . TRP   B  1 257 ? -1.610  6.481   -10.963  1.00 80.38  ? 558  TRP   B CD1 1 
ATOM   5467  C  CD2 . TRP   B  1 257 ? -3.300  7.862   -10.473  1.00 69.70  ? 558  TRP   B CD2 1 
ATOM   5468  N  NE1 . TRP   B  1 257 ? -2.562  6.338   -11.944  1.00 76.26  ? 558  TRP   B NE1 1 
ATOM   5469  C  CE2 . TRP   B  1 257 ? -3.610  7.175   -11.664  1.00 75.10  ? 558  TRP   B CE2 1 
ATOM   5470  C  CE3 . TRP   B  1 257 ? -4.217  8.787   -9.973   1.00 70.35  ? 558  TRP   B CE3 1 
ATOM   5471  C  CZ2 . TRP   B  1 257 ? -4.798  7.384   -12.355  1.00 75.81  ? 558  TRP   B CZ2 1 
ATOM   5472  C  CZ3 . TRP   B  1 257 ? -5.399  8.987   -10.660  1.00 74.48  ? 558  TRP   B CZ3 1 
ATOM   5473  C  CH2 . TRP   B  1 257 ? -5.678  8.293   -11.837  1.00 73.68  ? 558  TRP   B CH2 1 
ATOM   5474  N  N   . PHE   B  1 258 ? -4.097  6.808   -7.035   1.00 69.89  ? 559  PHE   B N   1 
ATOM   5475  C  CA  . PHE   B  1 258 ? -5.463  7.286   -6.868   1.00 68.90  ? 559  PHE   B CA  1 
ATOM   5476  C  C   . PHE   B  1 258 ? -5.696  7.819   -5.465   1.00 72.26  ? 559  PHE   B C   1 
ATOM   5477  O  O   . PHE   B  1 258 ? -6.279  8.895   -5.297   1.00 78.86  ? 559  PHE   B O   1 
ATOM   5478  C  CB  . PHE   B  1 258 ? -6.473  6.190   -7.184   1.00 58.22  ? 559  PHE   B CB  1 
ATOM   5479  C  CG  . PHE   B  1 258 ? -7.810  6.720   -7.594   1.00 58.85  ? 559  PHE   B CG  1 
ATOM   5480  C  CD1 . PHE   B  1 258 ? -8.172  6.757   -8.927   1.00 58.67  ? 559  PHE   B CD1 1 
ATOM   5481  C  CD2 . PHE   B  1 258 ? -8.694  7.216   -6.655   1.00 61.28  ? 559  PHE   B CD2 1 
ATOM   5482  C  CE1 . PHE   B  1 258 ? -9.389  7.256   -9.302   1.00 56.52  ? 559  PHE   B CE1 1 
ATOM   5483  C  CE2 . PHE   B  1 258 ? -9.920  7.718   -7.033   1.00 56.41  ? 559  PHE   B CE2 1 
ATOM   5484  C  CZ  . PHE   B  1 258 ? -10.266 7.736   -8.357   1.00 52.35  ? 559  PHE   B CZ  1 
ATOM   5485  N  N   . LYS   B  1 259 ? -5.279  7.069   -4.441   1.00 71.06  ? 560  LYS   B N   1 
ATOM   5486  C  CA  . LYS   B  1 259 ? -5.513  7.534   -3.074   1.00 71.24  ? 560  LYS   B CA  1 
ATOM   5487  C  C   . LYS   B  1 259 ? -4.940  8.932   -2.855   1.00 63.92  ? 560  LYS   B C   1 
ATOM   5488  O  O   . LYS   B  1 259 ? -5.540  9.739   -2.137   1.00 49.42  ? 560  LYS   B O   1 
ATOM   5489  C  CB  . LYS   B  1 259 ? -4.942  6.536   -2.060   1.00 73.61  ? 560  LYS   B CB  1 
ATOM   5490  C  CG  . LYS   B  1 259 ? -3.493  6.100   -2.275   1.00 71.53  ? 560  LYS   B CG  1 
ATOM   5491  C  CD  . LYS   B  1 259 ? -3.339  4.628   -1.892   1.00 66.11  ? 560  LYS   B CD  1 
ATOM   5492  C  CE  . LYS   B  1 259 ? -1.917  4.299   -1.520   1.00 64.00  ? 560  LYS   B CE  1 
ATOM   5493  N  NZ  . LYS   B  1 259 ? -0.968  4.787   -2.545   1.00 70.85  ? 560  LYS   B NZ  1 
ATOM   5494  N  N   . ASP   B  1 260 ? -3.830  9.261   -3.524   1.00 73.98  ? 561  ASP   B N   1 
ATOM   5495  C  CA  . ASP   B  1 260 ? -3.257  10.600  -3.428   1.00 74.30  ? 561  ASP   B CA  1 
ATOM   5496  C  C   . ASP   B  1 260 ? -4.203  11.691  -3.943   1.00 71.96  ? 561  ASP   B C   1 
ATOM   5497  O  O   . ASP   B  1 260 ? -3.977  12.869  -3.648   1.00 74.75  ? 561  ASP   B O   1 
ATOM   5498  C  CB  . ASP   B  1 260 ? -1.924  10.668  -4.189   1.00 79.91  ? 561  ASP   B CB  1 
ATOM   5499  C  CG  . ASP   B  1 260 ? -1.001  9.486   -3.893   1.00 87.53  ? 561  ASP   B CG  1 
ATOM   5500  O  OD1 . ASP   B  1 260 ? -1.146  8.851   -2.817   1.00 89.08  ? 561  ASP   B OD1 1 
ATOM   5501  O  OD2 . ASP   B  1 260 ? -0.121  9.202   -4.748   1.00 87.16  ? 561  ASP   B OD2 1 
ATOM   5502  N  N   . LEU   B  1 261 ? -5.254  11.347  -4.702   1.00 66.17  ? 562  LEU   B N   1 
ATOM   5503  C  CA  . LEU   B  1 261 ? -6.247  12.362  -5.061   1.00 69.48  ? 562  LEU   B CA  1 
ATOM   5504  C  C   . LEU   B  1 261 ? -6.889  12.988  -3.828   1.00 82.62  ? 562  LEU   B C   1 
ATOM   5505  O  O   . LEU   B  1 261 ? -7.434  14.094  -3.919   1.00 85.18  ? 562  LEU   B O   1 
ATOM   5506  C  CB  . LEU   B  1 261 ? -7.341  11.778  -5.964   1.00 52.30  ? 562  LEU   B CB  1 
ATOM   5507  C  CG  . LEU   B  1 261 ? -6.956  11.374  -7.387   1.00 61.52  ? 562  LEU   B CG  1 
ATOM   5508  C  CD1 . LEU   B  1 261 ? -8.069  10.543  -8.050   1.00 60.18  ? 562  LEU   B CD1 1 
ATOM   5509  C  CD2 . LEU   B  1 261 ? -6.671  12.605  -8.215   1.00 64.05  ? 562  LEU   B CD2 1 
ATOM   5510  N  N   . GLY   B  1 262 ? -6.839  12.303  -2.690   1.00 82.92  ? 563  GLY   B N   1 
ATOM   5511  C  CA  . GLY   B  1 262 ? -7.300  12.861  -1.433   1.00 84.93  ? 563  GLY   B CA  1 
ATOM   5512  C  C   . GLY   B  1 262 ? -8.797  12.886  -1.261   1.00 77.92  ? 563  GLY   B C   1 
ATOM   5513  O  O   . GLY   B  1 262 ? -9.332  13.829  -0.676   1.00 71.54  ? 563  GLY   B O   1 
ATOM   5514  N  N   . LEU   B  1 263 ? -9.492  11.868  -1.748   1.00 74.58  ? 564  LEU   B N   1 
ATOM   5515  C  CA  . LEU   B  1 263 ? -10.943 11.842  -1.727   1.00 67.31  ? 564  LEU   B CA  1 
ATOM   5516  C  C   . LEU   B  1 263 ? -11.448 10.803  -0.733   1.00 64.21  ? 564  LEU   B C   1 
ATOM   5517  O  O   . LEU   B  1 263 ? -10.820 9.761   -0.525   1.00 61.15  ? 564  LEU   B O   1 
ATOM   5518  C  CB  . LEU   B  1 263 ? -11.501 11.537  -3.123   1.00 65.03  ? 564  LEU   B CB  1 
ATOM   5519  C  CG  . LEU   B  1 263 ? -11.036 12.443  -4.260   1.00 67.97  ? 564  LEU   B CG  1 
ATOM   5520  C  CD1 . LEU   B  1 263 ? -11.235 11.736  -5.590   1.00 70.15  ? 564  LEU   B CD1 1 
ATOM   5521  C  CD2 . LEU   B  1 263 ? -11.770 13.785  -4.253   1.00 63.70  ? 564  LEU   B CD2 1 
ATOM   5522  N  N   . LYS   B  1 264 ? -12.596 11.108  -0.124   1.00 66.01  ? 565  LYS   B N   1 
ATOM   5523  C  CA  . LYS   B  1 264 ? -13.395 10.146  0.627    1.00 61.16  ? 565  LYS   B CA  1 
ATOM   5524  C  C   . LYS   B  1 264 ? -14.856 10.521  0.444    1.00 56.21  ? 565  LYS   B C   1 
ATOM   5525  O  O   . LYS   B  1 264 ? -15.180 11.664  0.113    1.00 64.26  ? 565  LYS   B O   1 
ATOM   5526  C  CB  . LYS   B  1 264 ? -13.030 10.111  2.128    1.00 56.77  ? 565  LYS   B CB  1 
ATOM   5527  C  CG  . LYS   B  1 264 ? -13.446 11.349  2.941    1.00 61.22  ? 565  LYS   B CG  1 
ATOM   5528  C  CD  . LYS   B  1 264 ? -12.808 11.365  4.337    1.00 68.49  ? 565  LYS   B CD  1 
ATOM   5529  C  CE  . LYS   B  1 264 ? -12.972 12.718  5.009    1.00 77.34  ? 565  LYS   B CE  1 
ATOM   5530  N  NZ  . LYS   B  1 264 ? -12.419 12.714  6.402    1.00 83.22  ? 565  LYS   B NZ  1 
ATOM   5531  N  N   . TRP   B  1 265 ? -15.744 9.550   0.634    1.00 45.67  ? 566  TRP   B N   1 
ATOM   5532  C  CA  . TRP   B  1 265 ? -17.170 9.841   0.692    1.00 40.87  ? 566  TRP   B CA  1 
ATOM   5533  C  C   . TRP   B  1 265 ? -17.732 9.230   1.975    1.00 53.65  ? 566  TRP   B C   1 
ATOM   5534  O  O   . TRP   B  1 265 ? -17.080 8.423   2.650    1.00 55.52  ? 566  TRP   B O   1 
ATOM   5535  C  CB  . TRP   B  1 265 ? -17.914 9.346   -0.565   1.00 39.09  ? 566  TRP   B CB  1 
ATOM   5536  C  CG  . TRP   B  1 265 ? -19.219 10.083  -0.818   1.00 39.91  ? 566  TRP   B CG  1 
ATOM   5537  C  CD1 . TRP   B  1 265 ? -20.490 9.590   -0.656   1.00 42.48  ? 566  TRP   B CD1 1 
ATOM   5538  C  CD2 . TRP   B  1 265 ? -19.375 11.454  -1.234   1.00 36.53  ? 566  TRP   B CD2 1 
ATOM   5539  N  NE1 . TRP   B  1 265 ? -21.423 10.568  -0.940   1.00 38.55  ? 566  TRP   B NE1 1 
ATOM   5540  C  CE2 . TRP   B  1 265 ? -20.764 11.715  -1.309   1.00 38.42  ? 566  TRP   B CE2 1 
ATOM   5541  C  CE3 . TRP   B  1 265 ? -18.477 12.481  -1.552   1.00 39.12  ? 566  TRP   B CE3 1 
ATOM   5542  C  CZ2 . TRP   B  1 265 ? -21.268 12.952  -1.699   1.00 40.23  ? 566  TRP   B CZ2 1 
ATOM   5543  C  CZ3 . TRP   B  1 265 ? -18.982 13.714  -1.924   1.00 43.69  ? 566  TRP   B CZ3 1 
ATOM   5544  C  CH2 . TRP   B  1 265 ? -20.364 13.938  -1.996   1.00 45.42  ? 566  TRP   B CH2 1 
ATOM   5545  N  N   . TYR   B  1 266 ? -18.936 9.657   2.338    1.00 45.63  ? 567  TYR   B N   1 
ATOM   5546  C  CA  . TYR   B  1 266 ? -19.625 9.073   3.473    1.00 46.09  ? 567  TYR   B CA  1 
ATOM   5547  C  C   . TYR   B  1 266 ? -20.394 7.826   3.052    1.00 52.83  ? 567  TYR   B C   1 
ATOM   5548  O  O   . TYR   B  1 266 ? -20.662 7.601   1.872    1.00 56.57  ? 567  TYR   B O   1 
ATOM   5549  C  CB  . TYR   B  1 266 ? -20.572 10.078  4.116    1.00 44.72  ? 567  TYR   B CB  1 
ATOM   5550  C  CG  . TYR   B  1 266 ? -21.496 10.810  3.163    1.00 50.00  ? 567  TYR   B CG  1 
ATOM   5551  C  CD1 . TYR   B  1 266 ? -22.790 10.371  2.941    1.00 56.94  ? 567  TYR   B CD1 1 
ATOM   5552  C  CD2 . TYR   B  1 266 ? -21.084 11.960  2.517    1.00 35.21  ? 567  TYR   B CD2 1 
ATOM   5553  C  CE1 . TYR   B  1 266 ? -23.643 11.050  2.098    1.00 57.70  ? 567  TYR   B CE1 1 
ATOM   5554  C  CE2 . TYR   B  1 266 ? -21.931 12.658  1.688    1.00 40.90  ? 567  TYR   B CE2 1 
ATOM   5555  C  CZ  . TYR   B  1 266 ? -23.207 12.192  1.460    1.00 58.16  ? 567  TYR   B CZ  1 
ATOM   5556  O  OH  . TYR   B  1 266 ? -24.045 12.877  0.602    1.00 63.74  ? 567  TYR   B OH  1 
ATOM   5557  N  N   . GLY   B  1 267 ? -20.767 7.019   4.048    1.00 49.43  ? 568  GLY   B N   1 
ATOM   5558  C  CA  . GLY   B  1 267 ? -21.332 5.708   3.778    1.00 36.24  ? 568  GLY   B CA  1 
ATOM   5559  C  C   . GLY   B  1 267 ? -22.843 5.628   3.828    1.00 42.39  ? 568  GLY   B C   1 
ATOM   5560  O  O   . GLY   B  1 267 ? -23.439 4.634   3.392    1.00 43.61  ? 568  GLY   B O   1 
ATOM   5561  N  N   . LEU   B  1 268 ? -23.484 6.675   4.339    1.00 38.08  ? 569  LEU   B N   1 
ATOM   5562  C  CA  . LEU   B  1 268 ? -24.909 6.615   4.654    1.00 31.26  ? 569  LEU   B CA  1 
ATOM   5563  C  C   . LEU   B  1 268 ? -25.672 7.660   3.863    1.00 47.14  ? 569  LEU   B C   1 
ATOM   5564  O  O   . LEU   B  1 268 ? -25.574 8.869   4.166    1.00 48.34  ? 569  LEU   B O   1 
ATOM   5565  C  CB  . LEU   B  1 268 ? -25.144 6.805   6.152    1.00 29.66  ? 569  LEU   B CB  1 
ATOM   5566  C  CG  . LEU   B  1 268 ? -26.564 6.439   6.573    1.00 34.25  ? 569  LEU   B CG  1 
ATOM   5567  C  CD1 . LEU   B  1 268 ? -26.783 4.970   6.286    1.00 32.93  ? 569  LEU   B CD1 1 
ATOM   5568  C  CD2 . LEU   B  1 268 ? -26.847 6.780   8.067    1.00 32.07  ? 569  LEU   B CD2 1 
ATOM   5569  N  N   . PRO   B  1 269 ? -26.431 7.245   2.851    1.00 41.65  ? 570  PRO   B N   1 
ATOM   5570  C  CA  . PRO   B  1 269 ? -27.357 8.165   2.206    1.00 35.68  ? 570  PRO   B CA  1 
ATOM   5571  C  C   . PRO   B  1 269 ? -28.626 8.225   3.034    1.00 36.95  ? 570  PRO   B C   1 
ATOM   5572  O  O   . PRO   B  1 269 ? -29.238 7.196   3.338    1.00 40.41  ? 570  PRO   B O   1 
ATOM   5573  C  CB  . PRO   B  1 269 ? -27.605 7.523   0.839    1.00 31.26  ? 570  PRO   B CB  1 
ATOM   5574  C  CG  . PRO   B  1 269 ? -27.426 6.046   1.081    1.00 41.01  ? 570  PRO   B CG  1 
ATOM   5575  C  CD  . PRO   B  1 269 ? -26.482 5.891   2.268    1.00 48.20  ? 570  PRO   B CD  1 
ATOM   5576  N  N   . ALA   B  1 270 ? -29.006 9.438   3.417    1.00 29.63  ? 571  ALA   B N   1 
ATOM   5577  C  CA  . ALA   B  1 270 ? -30.116 9.651   4.337    1.00 36.44  ? 571  ALA   B CA  1 
ATOM   5578  C  C   . ALA   B  1 270 ? -30.846 10.894  3.858    1.00 33.39  ? 571  ALA   B C   1 
ATOM   5579  O  O   . ALA   B  1 270 ? -30.365 12.006  4.078    1.00 53.25  ? 571  ALA   B O   1 
ATOM   5580  C  CB  . ALA   B  1 270 ? -29.609 9.810   5.774    1.00 35.53  ? 571  ALA   B CB  1 
ATOM   5581  N  N   . VAL   B  1 271 ? -31.975 10.716  3.196    1.00 27.47  ? 572  VAL   B N   1 
ATOM   5582  C  CA  . VAL   B  1 271 ? -32.677 11.860  2.625    1.00 38.89  ? 572  VAL   B CA  1 
ATOM   5583  C  C   . VAL   B  1 271 ? -33.559 12.469  3.699    1.00 41.59  ? 572  VAL   B C   1 
ATOM   5584  O  O   . VAL   B  1 271 ? -34.300 11.752  4.379    1.00 50.80  ? 572  VAL   B O   1 
ATOM   5585  C  CB  . VAL   B  1 271 ? -33.511 11.449  1.398    1.00 36.67  ? 572  VAL   B CB  1 
ATOM   5586  C  CG1 . VAL   B  1 271 ? -34.159 12.662  0.782    1.00 34.69  ? 572  VAL   B CG1 1 
ATOM   5587  C  CG2 . VAL   B  1 271 ? -32.654 10.791  0.404    1.00 39.09  ? 572  VAL   B CG2 1 
ATOM   5588  N  N   . SER   B  1 272 ? -33.530 13.797  3.828    1.00 31.70  ? 573  SER   B N   1 
ATOM   5589  C  CA  . SER   B  1 272 ? -34.222 14.409  4.958    1.00 48.12  ? 573  SER   B CA  1 
ATOM   5590  C  C   . SER   B  1 272 ? -34.950 15.714  4.644    1.00 52.58  ? 573  SER   B C   1 
ATOM   5591  O  O   . SER   B  1 272 ? -35.335 16.423  5.587    1.00 49.82  ? 573  SER   B O   1 
ATOM   5592  C  CB  . SER   B  1 272 ? -33.236 14.644  6.131    1.00 36.51  ? 573  SER   B CB  1 
ATOM   5593  O  OG  . SER   B  1 272 ? -32.130 15.460  5.769    1.00 36.39  ? 573  SER   B OG  1 
ATOM   5594  N  N   . ASN   B  1 273 ? -35.152 16.058  3.370    1.00 58.57  ? 574  ASN   B N   1 
ATOM   5595  C  CA  . ASN   B  1 273 ? -35.916 17.243  3.001    1.00 46.17  ? 574  ASN   B CA  1 
ATOM   5596  C  C   . ASN   B  1 273 ? -37.301 16.909  2.480    1.00 40.67  ? 574  ASN   B C   1 
ATOM   5597  O  O   . ASN   B  1 273 ? -38.032 17.819  2.080    1.00 47.61  ? 574  ASN   B O   1 
ATOM   5598  C  CB  . ASN   B  1 273 ? -35.169 18.061  1.947    1.00 40.90  ? 574  ASN   B CB  1 
ATOM   5599  C  CG  . ASN   B  1 273 ? -34.738 17.228  0.759    1.00 49.47  ? 574  ASN   B CG  1 
ATOM   5600  O  OD1 . ASN   B  1 273 ? -35.185 16.099  0.578    1.00 54.38  ? 574  ASN   B OD1 1 
ATOM   5601  N  ND2 . ASN   B  1 273 ? -33.837 17.775  -0.048   1.00 46.54  ? 574  ASN   B ND2 1 
ATOM   5602  N  N   . MET   B  1 274 ? -37.688 15.642  2.487    1.00 35.52  ? 575  MET   B N   1 
ATOM   5603  C  CA  . MET   B  1 274 ? -38.908 15.218  1.824    1.00 39.16  ? 575  MET   B CA  1 
ATOM   5604  C  C   . MET   B  1 274 ? -40.059 15.114  2.809    1.00 43.27  ? 575  MET   B C   1 
ATOM   5605  O  O   . MET   B  1 274 ? -39.883 15.158  4.030    1.00 42.18  ? 575  MET   B O   1 
ATOM   5606  C  CB  . MET   B  1 274 ? -38.687 13.897  1.093    1.00 36.56  ? 575  MET   B CB  1 
ATOM   5607  C  CG  . MET   B  1 274 ? -37.955 14.115  -0.243   1.00 33.76  ? 575  MET   B CG  1 
ATOM   5608  S  SD  . MET   B  1 274 ? -37.924 12.660  -1.271   1.00 44.08  ? 575  MET   B SD  1 
ATOM   5609  C  CE  . MET   B  1 274 ? -39.374 12.940  -2.283   1.00 37.72  ? 575  MET   B CE  1 
ATOM   5610  N  N   . LEU   B  1 275 ? -41.257 14.990  2.252    1.00 28.52  ? 576  LEU   B N   1 
ATOM   5611  C  CA  . LEU   B  1 275 ? -42.480 15.001  3.031    1.00 32.53  ? 576  LEU   B CA  1 
ATOM   5612  C  C   . LEU   B  1 275 ? -43.161 13.653  2.891    1.00 40.65  ? 576  LEU   B C   1 
ATOM   5613  O  O   . LEU   B  1 275 ? -43.411 13.200  1.773    1.00 53.16  ? 576  LEU   B O   1 
ATOM   5614  C  CB  . LEU   B  1 275 ? -43.403 16.133  2.570    1.00 44.35  ? 576  LEU   B CB  1 
ATOM   5615  C  CG  . LEU   B  1 275 ? -44.663 16.275  3.420    1.00 45.69  ? 576  LEU   B CG  1 
ATOM   5616  C  CD1 . LEU   B  1 275 ? -45.012 17.741  3.652    1.00 39.84  ? 576  LEU   B CD1 1 
ATOM   5617  C  CD2 . LEU   B  1 275 ? -45.819 15.534  2.765    1.00 43.14  ? 576  LEU   B CD2 1 
ATOM   5618  N  N   . LEU   B  1 276 ? -43.452 13.014  4.015    1.00 35.94  ? 577  LEU   B N   1 
ATOM   5619  C  CA  . LEU   B  1 276 ? -44.179 11.754  4.035    1.00 31.86  ? 577  LEU   B CA  1 
ATOM   5620  C  C   . LEU   B  1 276 ? -45.655 12.051  4.205    1.00 41.49  ? 577  LEU   B C   1 
ATOM   5621  O  O   . LEU   B  1 276 ? -46.035 12.779  5.123    1.00 49.92  ? 577  LEU   B O   1 
ATOM   5622  C  CB  . LEU   B  1 276 ? -43.693 10.856  5.168    1.00 31.27  ? 577  LEU   B CB  1 
ATOM   5623  C  CG  . LEU   B  1 276 ? -44.433 9.537   5.388    1.00 38.32  ? 577  LEU   B CG  1 
ATOM   5624  C  CD1 . LEU   B  1 276 ? -44.276 8.716   4.169    1.00 39.11  ? 577  LEU   B CD1 1 
ATOM   5625  C  CD2 . LEU   B  1 276 ? -43.930 8.749   6.624    1.00 33.18  ? 577  LEU   B CD2 1 
ATOM   5626  N  N   . GLU   B  1 277 ? -46.480 11.496  3.325    1.00 47.95  ? 578  GLU   B N   1 
ATOM   5627  C  CA  . GLU   B  1 277 ? -47.916 11.754  3.323    1.00 47.84  ? 578  GLU   B CA  1 
ATOM   5628  C  C   . GLU   B  1 277 ? -48.639 10.427  3.497    1.00 49.09  ? 578  GLU   B C   1 
ATOM   5629  O  O   . GLU   B  1 277 ? -48.402 9.479   2.734    1.00 44.58  ? 578  GLU   B O   1 
ATOM   5630  C  CB  . GLU   B  1 277 ? -48.345 12.459  2.032    1.00 60.84  ? 578  GLU   B CB  1 
ATOM   5631  C  CG  . GLU   B  1 277 ? -49.774 12.964  2.030    1.00 68.84  ? 578  GLU   B CG  1 
ATOM   5632  C  CD  . GLU   B  1 277 ? -50.738 11.947  1.458    1.00 79.73  ? 578  GLU   B CD  1 
ATOM   5633  O  OE1 . GLU   B  1 277 ? -50.272 11.035  0.745    1.00 84.91  ? 578  GLU   B OE1 1 
ATOM   5634  O  OE2 . GLU   B  1 277 ? -51.957 12.049  1.720    1.00 81.75  ? 578  GLU   B OE2 1 
ATOM   5635  N  N   . ILE   B  1 278 ? -49.485 10.351  4.530    1.00 51.21  ? 579  ILE   B N   1 
ATOM   5636  C  CA  . ILE   B  1 278 ? -50.254 9.156   4.866    1.00 41.20  ? 579  ILE   B CA  1 
ATOM   5637  C  C   . ILE   B  1 278 ? -51.653 9.578   5.290    1.00 44.75  ? 579  ILE   B C   1 
ATOM   5638  O  O   . ILE   B  1 278 ? -51.810 10.358  6.238    1.00 50.30  ? 579  ILE   B O   1 
ATOM   5639  C  CB  . ILE   B  1 278 ? -49.607 8.331   5.985    1.00 36.96  ? 579  ILE   B CB  1 
ATOM   5640  C  CG1 . ILE   B  1 278 ? -48.181 7.943   5.613    1.00 34.64  ? 579  ILE   B CG1 1 
ATOM   5641  C  CG2 . ILE   B  1 278 ? -50.454 7.115   6.239    1.00 43.82  ? 579  ILE   B CG2 1 
ATOM   5642  C  CD1 . ILE   B  1 278 ? -47.452 7.148   6.667    1.00 40.01  ? 579  ILE   B CD1 1 
ATOM   5643  N  N   . GLY   B  1 279 ? -52.663 9.052   4.607    1.00 43.20  ? 580  GLY   B N   1 
ATOM   5644  C  CA  . GLY   B  1 279 ? -54.047 9.351   4.914    1.00 43.28  ? 580  GLY   B CA  1 
ATOM   5645  C  C   . GLY   B  1 279 ? -54.334 10.812  5.167    1.00 47.74  ? 580  GLY   B C   1 
ATOM   5646  O  O   . GLY   B  1 279 ? -55.126 11.147  6.055    1.00 49.19  ? 580  GLY   B O   1 
ATOM   5647  N  N   . GLY   B  1 280 ? -53.697 11.689  4.393    1.00 45.72  ? 581  GLY   B N   1 
ATOM   5648  C  CA  . GLY   B  1 280 ? -53.921 13.115  4.520    1.00 55.72  ? 581  GLY   B CA  1 
ATOM   5649  C  C   . GLY   B  1 280 ? -53.140 13.785  5.626    1.00 58.31  ? 581  GLY   B C   1 
ATOM   5650  O  O   . GLY   B  1 280 ? -53.287 15.003  5.812    1.00 59.51  ? 581  GLY   B O   1 
ATOM   5651  N  N   . LEU   B  1 281 ? -52.330 13.028  6.373    1.00 53.02  ? 582  LEU   B N   1 
ATOM   5652  C  CA  . LEU   B  1 281 ? -51.413 13.576  7.363    1.00 52.47  ? 582  LEU   B CA  1 
ATOM   5653  C  C   . LEU   B  1 281 ? -50.059 13.854  6.724    1.00 42.31  ? 582  LEU   B C   1 
ATOM   5654  O  O   . LEU   B  1 281 ? -49.569 13.065  5.916    1.00 41.88  ? 582  LEU   B O   1 
ATOM   5655  C  CB  . LEU   B  1 281 ? -51.245 12.609  8.540    1.00 49.47  ? 582  LEU   B CB  1 
ATOM   5656  C  CG  . LEU   B  1 281 ? -52.565 12.161  9.159    1.00 40.25  ? 582  LEU   B CG  1 
ATOM   5657  C  CD1 . LEU   B  1 281 ? -52.379 11.112  10.249   1.00 35.18  ? 582  LEU   B CD1 1 
ATOM   5658  C  CD2 . LEU   B  1 281 ? -53.315 13.379  9.660    1.00 37.23  ? 582  LEU   B CD2 1 
ATOM   5659  N  N   . GLU   B  1 282 ? -49.443 14.965  7.111    1.00 43.02  ? 583  GLU   B N   1 
ATOM   5660  C  CA  . GLU   B  1 282 ? -48.215 15.430  6.481    1.00 45.25  ? 583  GLU   B CA  1 
ATOM   5661  C  C   . GLU   B  1 282 ? -47.089 15.398  7.502    1.00 53.28  ? 583  GLU   B C   1 
ATOM   5662  O  O   . GLU   B  1 282 ? -47.023 16.260  8.384    1.00 60.09  ? 583  GLU   B O   1 
ATOM   5663  C  CB  . GLU   B  1 282 ? -48.390 16.838  5.915    1.00 55.91  ? 583  GLU   B CB  1 
ATOM   5664  C  CG  . GLU   B  1 282 ? -49.529 16.982  4.914    1.00 54.95  ? 583  GLU   B CG  1 
ATOM   5665  C  CD  . GLU   B  1 282 ? -49.527 18.333  4.235    1.00 60.88  ? 583  GLU   B CD  1 
ATOM   5666  O  OE1 . GLU   B  1 282 ? -49.356 18.371  2.994    1.00 70.15  ? 583  GLU   B OE1 1 
ATOM   5667  O  OE2 . GLU   B  1 282 ? -49.684 19.356  4.934    1.00 58.65  ? 583  GLU   B OE2 1 
ATOM   5668  N  N   . PHE   B  1 283 ? -46.191 14.425  7.355    1.00 42.08  ? 584  PHE   B N   1 
ATOM   5669  C  CA  . PHE   B  1 283 ? -44.980 14.325  8.164    1.00 35.34  ? 584  PHE   B CA  1 
ATOM   5670  C  C   . PHE   B  1 283 ? -43.830 15.081  7.489    1.00 40.58  ? 584  PHE   B C   1 
ATOM   5671  O  O   . PHE   B  1 283 ? -43.059 14.529  6.698    1.00 43.03  ? 584  PHE   B O   1 
ATOM   5672  C  CB  . PHE   B  1 283 ? -44.655 12.861  8.384    1.00 33.20  ? 584  PHE   B CB  1 
ATOM   5673  C  CG  . PHE   B  1 283 ? -45.727 12.127  9.131    1.00 44.16  ? 584  PHE   B CG  1 
ATOM   5674  C  CD1 . PHE   B  1 283 ? -46.698 11.399  8.443    1.00 47.79  ? 584  PHE   B CD1 1 
ATOM   5675  C  CD2 . PHE   B  1 283 ? -45.777 12.168  10.524   1.00 44.17  ? 584  PHE   B CD2 1 
ATOM   5676  C  CE1 . PHE   B  1 283 ? -47.696 10.704  9.129    1.00 47.89  ? 584  PHE   B CE1 1 
ATOM   5677  C  CE2 . PHE   B  1 283 ? -46.773 11.479  11.223   1.00 46.41  ? 584  PHE   B CE2 1 
ATOM   5678  C  CZ  . PHE   B  1 283 ? -47.736 10.747  10.521   1.00 53.98  ? 584  PHE   B CZ  1 
ATOM   5679  N  N   . SER   B  1 284 ? -43.694 16.367  7.836    1.00 39.21  ? 585  SER   B N   1 
ATOM   5680  C  CA  . SER   B  1 284 ? -42.687 17.241  7.237    1.00 36.80  ? 585  SER   B CA  1 
ATOM   5681  C  C   . SER   B  1 284 ? -41.253 16.912  7.634    1.00 36.39  ? 585  SER   B C   1 
ATOM   5682  O  O   . SER   B  1 284 ? -40.331 17.530  7.095    1.00 42.48  ? 585  SER   B O   1 
ATOM   5683  C  CB  . SER   B  1 284 ? -42.978 18.694  7.612    1.00 43.10  ? 585  SER   B CB  1 
ATOM   5684  O  OG  . SER   B  1 284 ? -43.102 18.844  9.009    1.00 53.79  ? 585  SER   B OG  1 
ATOM   5685  N  N   . ALA   B  1 285 ? -41.030 15.996  8.571    1.00 40.37  ? 586  ALA   B N   1 
ATOM   5686  C  CA  . ALA   B  1 285 ? -39.679 15.579  8.922    1.00 37.28  ? 586  ALA   B CA  1 
ATOM   5687  C  C   . ALA   B  1 285 ? -39.694 14.072  9.069    1.00 39.84  ? 586  ALA   B C   1 
ATOM   5688  O  O   . ALA   B  1 285 ? -40.309 13.551  10.002   1.00 40.82  ? 586  ALA   B O   1 
ATOM   5689  C  CB  . ALA   B  1 285 ? -39.197 16.240  10.202   1.00 47.46  ? 586  ALA   B CB  1 
ATOM   5690  N  N   . CYS   B  1 286 ? -39.018 13.383  8.150    1.00 30.80  ? 587  CYS   B N   1 
ATOM   5691  C  CA  . CYS   B  1 286 ? -39.092 11.935  8.040    1.00 39.04  ? 587  CYS   B CA  1 
ATOM   5692  C  C   . CYS   B  1 286 ? -37.821 11.397  7.401    1.00 58.46  ? 587  CYS   B C   1 
ATOM   5693  O  O   . CYS   B  1 286 ? -37.897 10.757  6.343    1.00 68.31  ? 587  CYS   B O   1 
ATOM   5694  C  CB  . CYS   B  1 286 ? -40.296 11.530  7.188    1.00 46.79  ? 587  CYS   B CB  1 
ATOM   5695  S  SG  . CYS   B  1 286 ? -40.331 12.383  5.547    1.00 43.29  ? 587  CYS   B SG  1 
ATOM   5696  N  N   . PRO   B  1 287 ? -36.646 11.621  7.994    1.00 55.40  ? 588  PRO   B N   1 
ATOM   5697  C  CA  . PRO   B  1 287 ? -35.405 11.215  7.320    1.00 39.92  ? 588  PRO   B CA  1 
ATOM   5698  C  C   . PRO   B  1 287 ? -35.352 9.706   7.136    1.00 46.27  ? 588  PRO   B C   1 
ATOM   5699  O  O   . PRO   B  1 287 ? -35.576 8.947   8.083    1.00 48.44  ? 588  PRO   B O   1 
ATOM   5700  C  CB  . PRO   B  1 287 ? -34.308 11.712  8.267    1.00 40.25  ? 588  PRO   B CB  1 
ATOM   5701  C  CG  . PRO   B  1 287 ? -34.970 11.910  9.579    1.00 37.89  ? 588  PRO   B CG  1 
ATOM   5702  C  CD  . PRO   B  1 287 ? -36.382 12.291  9.280    1.00 39.67  ? 588  PRO   B CD  1 
ATOM   5703  N  N   . PHE   B  1 288 ? -35.091 9.273   5.893    1.00 40.61  ? 589  PHE   B N   1 
ATOM   5704  C  CA  . PHE   B  1 288 ? -34.931 7.861   5.558    1.00 33.52  ? 589  PHE   B CA  1 
ATOM   5705  C  C   . PHE   B  1 288 ? -33.549 7.615   4.969    1.00 25.54  ? 589  PHE   B C   1 
ATOM   5706  O  O   . PHE   B  1 288 ? -32.848 8.544   4.558    1.00 23.74  ? 589  PHE   B O   1 
ATOM   5707  C  CB  . PHE   B  1 288 ? -36.008 7.367   4.578    1.00 38.52  ? 589  PHE   B CB  1 
ATOM   5708  C  CG  . PHE   B  1 288 ? -36.215 8.260   3.398    1.00 44.34  ? 589  PHE   B CG  1 
ATOM   5709  C  CD1 . PHE   B  1 288 ? -35.491 8.060   2.212    1.00 45.05  ? 589  PHE   B CD1 1 
ATOM   5710  C  CD2 . PHE   B  1 288 ? -37.137 9.302   3.463    1.00 39.48  ? 589  PHE   B CD2 1 
ATOM   5711  C  CE1 . PHE   B  1 288 ? -35.677 8.889   1.109    1.00 34.61  ? 589  PHE   B CE1 1 
ATOM   5712  C  CE2 . PHE   B  1 288 ? -37.339 10.142  2.366    1.00 42.81  ? 589  PHE   B CE2 1 
ATOM   5713  C  CZ  . PHE   B  1 288 ? -36.600 9.937   1.185    1.00 39.48  ? 589  PHE   B CZ  1 
ATOM   5714  N  N   . SER   B  1 289 ? -33.159 6.345   4.943    1.00 21.88  ? 590  SER   B N   1 
ATOM   5715  C  CA  . SER   B  1 289 ? -31.770 5.971   4.710    1.00 22.22  ? 590  SER   B CA  1 
ATOM   5716  C  C   . SER   B  1 289 ? -31.730 4.519   4.245    1.00 25.17  ? 590  SER   B C   1 
ATOM   5717  O  O   . SER   B  1 289 ? -32.567 3.701   4.642    1.00 36.31  ? 590  SER   B O   1 
ATOM   5718  C  CB  . SER   B  1 289 ? -30.923 6.151   5.986    1.00 39.15  ? 590  SER   B CB  1 
ATOM   5719  O  OG  . SER   B  1 289 ? -30.401 4.901   6.439    1.00 39.76  ? 590  SER   B OG  1 
ATOM   5720  N  N   . GLY   B  1 290 ? -30.777 4.218   3.374    1.00 31.23  ? 591  GLY   B N   1 
ATOM   5721  C  CA  . GLY   B  1 290 ? -30.564 2.864   2.905    1.00 23.80  ? 591  GLY   B CA  1 
ATOM   5722  C  C   . GLY   B  1 290 ? -29.090 2.703   2.605    1.00 43.59  ? 591  GLY   B C   1 
ATOM   5723  O  O   . GLY   B  1 290 ? -28.262 2.970   3.478    1.00 60.01  ? 591  GLY   B O   1 
ATOM   5724  N  N   . TRP   B  1 291 ? -28.729 2.313   1.383    1.00 46.58  ? 592  TRP   B N   1 
ATOM   5725  C  CA  . TRP   B  1 291 ? -27.326 2.252   1.006    1.00 44.21  ? 592  TRP   B CA  1 
ATOM   5726  C  C   . TRP   B  1 291 ? -27.158 2.724   -0.439   1.00 47.06  ? 592  TRP   B C   1 
ATOM   5727  O  O   . TRP   B  1 291 ? -28.105 2.775   -1.224   1.00 47.59  ? 592  TRP   B O   1 
ATOM   5728  C  CB  . TRP   B  1 291 ? -26.757 0.838   1.227    1.00 39.33  ? 592  TRP   B CB  1 
ATOM   5729  C  CG  . TRP   B  1 291 ? -27.616 -0.217  0.671    1.00 44.23  ? 592  TRP   B CG  1 
ATOM   5730  C  CD1 . TRP   B  1 291 ? -27.719 -0.578  -0.639   1.00 43.10  ? 592  TRP   B CD1 1 
ATOM   5731  C  CD2 . TRP   B  1 291 ? -28.521 -1.060  1.394    1.00 51.39  ? 592  TRP   B CD2 1 
ATOM   5732  N  NE1 . TRP   B  1 291 ? -28.635 -1.598  -0.780   1.00 48.82  ? 592  TRP   B NE1 1 
ATOM   5733  C  CE2 . TRP   B  1 291 ? -29.145 -1.906  0.454    1.00 50.24  ? 592  TRP   B CE2 1 
ATOM   5734  C  CE3 . TRP   B  1 291 ? -28.874 -1.177  2.740    1.00 53.84  ? 592  TRP   B CE3 1 
ATOM   5735  C  CZ2 . TRP   B  1 291 ? -30.095 -2.860  0.820    1.00 54.69  ? 592  TRP   B CZ2 1 
ATOM   5736  C  CZ3 . TRP   B  1 291 ? -29.820 -2.137  3.103    1.00 47.15  ? 592  TRP   B CZ3 1 
ATOM   5737  C  CH2 . TRP   B  1 291 ? -30.415 -2.962  2.150    1.00 55.91  ? 592  TRP   B CH2 1 
ATOM   5738  N  N   . TYR   B  1 292 ? -25.928 3.079   -0.774   1.00 36.61  ? 593  TYR   B N   1 
ATOM   5739  C  CA  . TYR   B  1 292 ? -25.622 3.765   -2.014   1.00 28.77  ? 593  TYR   B CA  1 
ATOM   5740  C  C   . TYR   B  1 292 ? -25.533 2.789   -3.185   1.00 44.94  ? 593  TYR   B C   1 
ATOM   5741  O  O   . TYR   B  1 292 ? -25.000 1.681   -3.055   1.00 42.25  ? 593  TYR   B O   1 
ATOM   5742  C  CB  . TYR   B  1 292 ? -24.277 4.473   -1.897   1.00 35.63  ? 593  TYR   B CB  1 
ATOM   5743  C  CG  . TYR   B  1 292 ? -24.301 5.912   -1.495   1.00 37.19  ? 593  TYR   B CG  1 
ATOM   5744  C  CD1 . TYR   B  1 292 ? -23.500 6.377   -0.447   1.00 44.71  ? 593  TYR   B CD1 1 
ATOM   5745  C  CD2 . TYR   B  1 292 ? -25.081 6.820   -2.180   1.00 40.58  ? 593  TYR   B CD2 1 
ATOM   5746  C  CE1 . TYR   B  1 292 ? -23.487 7.725   -0.093   1.00 48.23  ? 593  TYR   B CE1 1 
ATOM   5747  C  CE2 . TYR   B  1 292 ? -25.083 8.161   -1.836   1.00 50.28  ? 593  TYR   B CE2 1 
ATOM   5748  C  CZ  . TYR   B  1 292 ? -24.287 8.610   -0.798   1.00 54.94  ? 593  TYR   B CZ  1 
ATOM   5749  O  OH  . TYR   B  1 292 ? -24.305 9.950   -0.484   1.00 58.04  ? 593  TYR   B OH  1 
ATOM   5750  N  N   . MET   B  1 293 ? -26.055 3.217   -4.335   1.00 46.62  ? 594  MET   B N   1 
ATOM   5751  C  CA  . MET   B  1 293 ? -25.615 2.679   -5.613   1.00 39.10  ? 594  MET   B CA  1 
ATOM   5752  C  C   . MET   B  1 293 ? -24.380 3.464   -6.013   1.00 27.77  ? 594  MET   B C   1 
ATOM   5753  O  O   . MET   B  1 293 ? -24.387 4.700   -5.967   1.00 38.24  ? 594  MET   B O   1 
ATOM   5754  C  CB  . MET   B  1 293 ? -26.716 2.793   -6.672   1.00 40.23  ? 594  MET   B CB  1 
ATOM   5755  C  CG  . MET   B  1 293 ? -26.494 1.897   -7.857   1.00 45.06  ? 594  MET   B CG  1 
ATOM   5756  S  SD  . MET   B  1 293 ? -27.921 1.911   -8.934   1.00 44.17  ? 594  MET   B SD  1 
ATOM   5757  C  CE  . MET   B  1 293 ? -27.858 3.585   -9.559   1.00 45.43  ? 594  MET   B CE  1 
ATOM   5758  N  N   . GLY   B  1 294 ? -23.299 2.749   -6.329   1.00 26.81  ? 595  GLY   B N   1 
ATOM   5759  C  CA  . GLY   B  1 294 ? -22.010 3.403   -6.540   1.00 29.47  ? 595  GLY   B CA  1 
ATOM   5760  C  C   . GLY   B  1 294 ? -22.069 4.625   -7.442   1.00 50.52  ? 595  GLY   B C   1 
ATOM   5761  O  O   . GLY   B  1 294 ? -21.410 5.633   -7.168   1.00 52.96  ? 595  GLY   B O   1 
ATOM   5762  N  N   . THR   B  1 295 ? -22.860 4.552   -8.535   1.00 46.04  ? 596  THR   B N   1 
ATOM   5763  C  CA  . THR   B  1 295 ? -22.954 5.657   -9.497   1.00 50.21  ? 596  THR   B CA  1 
ATOM   5764  C  C   . THR   B  1 295 ? -23.386 6.966   -8.851   1.00 46.13  ? 596  THR   B C   1 
ATOM   5765  O  O   . THR   B  1 295 ? -23.041 8.037   -9.363   1.00 41.41  ? 596  THR   B O   1 
ATOM   5766  C  CB  . THR   B  1 295 ? -23.943 5.353   -10.625  1.00 49.72  ? 596  THR   B CB  1 
ATOM   5767  O  OG1 . THR   B  1 295 ? -25.283 5.426   -10.116  1.00 37.49  ? 596  THR   B OG1 1 
ATOM   5768  C  CG2 . THR   B  1 295 ? -23.684 3.983   -11.239  1.00 53.12  ? 596  THR   B CG2 1 
ATOM   5769  N  N   . GLU   B  1 296 ? -24.172 6.908   -7.767   1.00 56.48  ? 597  GLU   B N   1 
ATOM   5770  C  CA  . GLU   B  1 296 ? -24.595 8.129   -7.077   1.00 54.16  ? 597  GLU   B CA  1 
ATOM   5771  C  C   . GLU   B  1 296 ? -23.398 8.928   -6.585   1.00 55.22  ? 597  GLU   B C   1 
ATOM   5772  O  O   . GLU   B  1 296 ? -23.380 10.159  -6.690   1.00 55.00  ? 597  GLU   B O   1 
ATOM   5773  C  CB  . GLU   B  1 296 ? -25.509 7.795   -5.899   1.00 53.08  ? 597  GLU   B CB  1 
ATOM   5774  C  CG  . GLU   B  1 296 ? -26.769 7.060   -6.268   1.00 50.98  ? 597  GLU   B CG  1 
ATOM   5775  C  CD  . GLU   B  1 296 ? -27.651 6.807   -5.055   1.00 48.65  ? 597  GLU   B CD  1 
ATOM   5776  O  OE1 . GLU   B  1 296 ? -28.349 7.750   -4.609   1.00 41.25  ? 597  GLU   B OE1 1 
ATOM   5777  O  OE2 . GLU   B  1 296 ? -27.624 5.665   -4.547   1.00 39.95  ? 597  GLU   B OE2 1 
ATOM   5778  N  N   . ILE   B  1 297 ? -22.385 8.241   -6.056   1.00 48.72  ? 598  ILE   B N   1 
ATOM   5779  C  CA  . ILE   B  1 297 ? -21.166 8.910   -5.610   1.00 48.84  ? 598  ILE   B CA  1 
ATOM   5780  C  C   . ILE   B  1 297 ? -20.246 9.209   -6.782   1.00 55.84  ? 598  ILE   B C   1 
ATOM   5781  O  O   . ILE   B  1 297 ? -19.761 10.335  -6.929   1.00 59.90  ? 598  ILE   B O   1 
ATOM   5782  C  CB  . ILE   B  1 297 ? -20.425 8.043   -4.578   1.00 41.90  ? 598  ILE   B CB  1 
ATOM   5783  C  CG1 . ILE   B  1 297 ? -21.307 7.728   -3.381   1.00 38.70  ? 598  ILE   B CG1 1 
ATOM   5784  C  CG2 . ILE   B  1 297 ? -19.146 8.703   -4.194   1.00 38.89  ? 598  ILE   B CG2 1 
ATOM   5785  C  CD1 . ILE   B  1 297 ? -20.890 6.449   -2.684   1.00 38.79  ? 598  ILE   B CD1 1 
ATOM   5786  N  N   . GLY   B  1 298 ? -19.947 8.176   -7.589   1.00 62.90  ? 599  GLY   B N   1 
ATOM   5787  C  CA  . GLY   B  1 298 ? -18.904 8.257   -8.609   1.00 61.53  ? 599  GLY   B CA  1 
ATOM   5788  C  C   . GLY   B  1 298 ? -19.322 8.917   -9.908   1.00 55.65  ? 599  GLY   B C   1 
ATOM   5789  O  O   . GLY   B  1 298 ? -18.495 9.545   -10.582  1.00 51.82  ? 599  GLY   B O   1 
ATOM   5790  N  N   . VAL   B  1 299 ? -20.592 8.813   -10.280  1.00 46.93  ? 600  VAL   B N   1 
ATOM   5791  C  CA  . VAL   B  1 299 ? -21.027 9.512   -11.481  1.00 52.61  ? 600  VAL   B CA  1 
ATOM   5792  C  C   . VAL   B  1 299 ? -21.531 10.902  -11.111  1.00 55.76  ? 600  VAL   B C   1 
ATOM   5793  O  O   . VAL   B  1 299 ? -20.961 11.909  -11.547  1.00 60.37  ? 600  VAL   B O   1 
ATOM   5794  C  CB  . VAL   B  1 299 ? -22.091 8.713   -12.251  1.00 51.87  ? 600  VAL   B CB  1 
ATOM   5795  C  CG1 . VAL   B  1 299 ? -22.551 9.506   -13.455  1.00 61.03  ? 600  VAL   B CG1 1 
ATOM   5796  C  CG2 . VAL   B  1 299 ? -21.536 7.364   -12.678  1.00 38.39  ? 600  VAL   B CG2 1 
ATOM   5797  N  N   . ARG   B  1 300 ? -22.591 10.975  -10.298  1.00 52.02  ? 601  ARG   B N   1 
ATOM   5798  C  CA  . ARG   B  1 300 ? -23.232 12.262  -10.007  1.00 54.42  ? 601  ARG   B CA  1 
ATOM   5799  C  C   . ARG   B  1 300 ? -22.426 13.118  -9.023   1.00 57.86  ? 601  ARG   B C   1 
ATOM   5800  O  O   . ARG   B  1 300 ? -22.222 14.315  -9.259   1.00 60.79  ? 601  ARG   B O   1 
ATOM   5801  C  CB  . ARG   B  1 300 ? -24.645 12.039  -9.457   1.00 48.88  ? 601  ARG   B CB  1 
ATOM   5802  C  CG  . ARG   B  1 300 ? -25.552 11.204  -10.323  1.00 44.29  ? 601  ARG   B CG  1 
ATOM   5803  C  CD  . ARG   B  1 300 ? -25.684 11.814  -11.721  1.00 55.48  ? 601  ARG   B CD  1 
ATOM   5804  N  NE  . ARG   B  1 300 ? -26.101 13.214  -11.710  1.00 47.63  ? 601  ARG   B NE  1 
ATOM   5805  C  CZ  . ARG   B  1 300 ? -27.350 13.602  -11.481  1.00 47.62  ? 601  ARG   B CZ  1 
ATOM   5806  N  NH1 . ARG   B  1 300 ? -28.297 12.689  -11.237  1.00 47.25  ? 601  ARG   B NH1 1 
ATOM   5807  N  NH2 . ARG   B  1 300 ? -27.655 14.895  -11.489  1.00 47.20  ? 601  ARG   B NH2 1 
ATOM   5808  N  N   . ASP   B  1 301 ? -21.976 12.533  -7.907   1.00 63.70  ? 602  ASP   B N   1 
ATOM   5809  C  CA  . ASP   B  1 301 ? -21.362 13.324  -6.835   1.00 64.94  ? 602  ASP   B CA  1 
ATOM   5810  C  C   . ASP   B  1 301 ? -19.978 13.837  -7.233   1.00 63.52  ? 602  ASP   B C   1 
ATOM   5811  O  O   . ASP   B  1 301 ? -19.657 15.020  -7.045   1.00 53.37  ? 602  ASP   B O   1 
ATOM   5812  C  CB  . ASP   B  1 301 ? -21.291 12.499  -5.545   1.00 62.47  ? 602  ASP   B CB  1 
ATOM   5813  C  CG  . ASP   B  1 301 ? -22.595 12.522  -4.771   1.00 64.88  ? 602  ASP   B CG  1 
ATOM   5814  O  OD1 . ASP   B  1 301 ? -23.263 13.581  -4.789   1.00 54.02  ? 602  ASP   B OD1 1 
ATOM   5815  O  OD2 . ASP   B  1 301 ? -22.951 11.490  -4.150   1.00 72.31  ? 602  ASP   B OD2 1 
ATOM   5816  N  N   . TYR   B  1 302 ? -19.147 12.969  -7.799   1.00 64.42  ? 603  TYR   B N   1 
ATOM   5817  C  CA  . TYR   B  1 302 ? -17.809 13.377  -8.192   1.00 62.63  ? 603  TYR   B CA  1 
ATOM   5818  C  C   . TYR   B  1 302 ? -17.727 14.036  -9.569   1.00 54.52  ? 603  TYR   B C   1 
ATOM   5819  O  O   . TYR   B  1 302 ? -16.801 14.826  -9.795   1.00 50.22  ? 603  TYR   B O   1 
ATOM   5820  C  CB  . TYR   B  1 302 ? -16.880 12.168  -8.148   1.00 69.01  ? 603  TYR   B CB  1 
ATOM   5821  C  CG  . TYR   B  1 302 ? -16.458 11.774  -6.747   1.00 66.63  ? 603  TYR   B CG  1 
ATOM   5822  C  CD1 . TYR   B  1 302 ? -16.227 10.444  -6.424   1.00 62.79  ? 603  TYR   B CD1 1 
ATOM   5823  C  CD2 . TYR   B  1 302 ? -16.261 12.728  -5.761   1.00 62.06  ? 603  TYR   B CD2 1 
ATOM   5824  C  CE1 . TYR   B  1 302 ? -15.828 10.072  -5.171   1.00 54.64  ? 603  TYR   B CE1 1 
ATOM   5825  C  CE2 . TYR   B  1 302 ? -15.868 12.360  -4.501   1.00 66.85  ? 603  TYR   B CE2 1 
ATOM   5826  C  CZ  . TYR   B  1 302 ? -15.654 11.026  -4.212   1.00 66.75  ? 603  TYR   B CZ  1 
ATOM   5827  O  OH  . TYR   B  1 302 ? -15.257 10.634  -2.954   1.00 79.21  ? 603  TYR   B OH  1 
ATOM   5828  N  N   . CYS   B  1 303 ? -18.664 13.760  -10.490  1.00 59.03  ? 604  CYS   B N   1 
ATOM   5829  C  CA  . CYS   B  1 303 ? -18.442 14.097  -11.898  1.00 63.32  ? 604  CYS   B CA  1 
ATOM   5830  C  C   . CYS   B  1 303 ? -19.388 15.123  -12.511  1.00 57.11  ? 604  CYS   B C   1 
ATOM   5831  O  O   . CYS   B  1 303 ? -18.966 15.794  -13.454  1.00 57.76  ? 604  CYS   B O   1 
ATOM   5832  C  CB  . CYS   B  1 303 ? -18.485 12.838  -12.762  1.00 67.04  ? 604  CYS   B CB  1 
ATOM   5833  S  SG  . CYS   B  1 303 ? -17.085 11.784  -12.473  1.00 69.89  ? 604  CYS   B SG  1 
ATOM   5834  N  N   . ASP   B  1 304 ? -20.637 15.256  -12.040  1.00 59.57  ? 605  ASP   B N   1 
ATOM   5835  C  CA  . ASP   B  1 304 ? -21.487 16.393  -12.416  1.00 64.54  ? 605  ASP   B CA  1 
ATOM   5836  C  C   . ASP   B  1 304 ? -20.676 17.691  -12.415  1.00 77.53  ? 605  ASP   B C   1 
ATOM   5837  O  O   . ASP   B  1 304 ? -19.712 17.820  -11.653  1.00 86.78  ? 605  ASP   B O   1 
ATOM   5838  C  CB  . ASP   B  1 304 ? -22.678 16.560  -11.455  1.00 62.00  ? 605  ASP   B CB  1 
ATOM   5839  C  CG  . ASP   B  1 304 ? -23.939 15.841  -11.912  1.00 57.96  ? 605  ASP   B CG  1 
ATOM   5840  O  OD1 . ASP   B  1 304 ? -23.820 14.819  -12.631  1.00 56.11  ? 605  ASP   B OD1 1 
ATOM   5841  O  OD2 . ASP   B  1 304 ? -25.053 16.302  -11.527  1.00 50.41  ? 605  ASP   B OD2 1 
ATOM   5842  N  N   . ASN   B  1 305 ? -21.061 18.667  -13.243  1.00 81.46  ? 606  ASN   B N   1 
ATOM   5843  C  CA  . ASN   B  1 305 ? -20.260 19.884  -13.362  1.00 79.92  ? 606  ASN   B CA  1 
ATOM   5844  C  C   . ASN   B  1 305 ? -20.408 20.781  -12.138  1.00 89.17  ? 606  ASN   B C   1 
ATOM   5845  O  O   . ASN   B  1 305 ? -19.406 21.302  -11.625  1.00 96.58  ? 606  ASN   B O   1 
ATOM   5846  C  CB  . ASN   B  1 305 ? -20.632 20.638  -14.639  1.00 74.11  ? 606  ASN   B CB  1 
ATOM   5847  C  CG  . ASN   B  1 305 ? -19.937 20.089  -15.858  1.00 70.45  ? 606  ASN   B CG  1 
ATOM   5848  O  OD1 . ASN   B  1 305 ? -18.794 20.433  -16.131  1.00 72.07  ? 606  ASN   B OD1 1 
ATOM   5849  N  ND2 . ASN   B  1 305 ? -20.616 19.218  -16.589  1.00 67.45  ? 606  ASN   B ND2 1 
ATOM   5850  N  N   . SER   B  1 306 ? -21.643 20.978  -11.653  1.00 80.70  ? 607  SER   B N   1 
ATOM   5851  C  CA  . SER   B  1 306 ? -21.905 21.804  -10.478  1.00 73.07  ? 607  SER   B CA  1 
ATOM   5852  C  C   . SER   B  1 306 ? -21.735 21.020  -9.181   1.00 74.30  ? 607  SER   B C   1 
ATOM   5853  O  O   . SER   B  1 306 ? -22.401 21.311  -8.175   1.00 70.80  ? 607  SER   B O   1 
ATOM   5854  C  CB  . SER   B  1 306 ? -23.299 22.427  -10.550  1.00 62.38  ? 607  SER   B CB  1 
ATOM   5855  O  OG  . SER   B  1 306 ? -23.968 22.033  -11.727  1.00 76.57  ? 607  SER   B OG  1 
ATOM   5856  N  N   . ARG   B  1 307 ? -20.865 20.008  -9.195   1.00 73.22  ? 608  ARG   B N   1 
ATOM   5857  C  CA  . ARG   B  1 307 ? -20.541 19.217  -8.011   1.00 69.33  ? 608  ARG   B CA  1 
ATOM   5858  C  C   . ARG   B  1 307 ? -19.023 19.072  -7.884   1.00 61.96  ? 608  ARG   B C   1 
ATOM   5859  O  O   . ARG   B  1 307 ? -18.304 20.071  -7.985   1.00 64.64  ? 608  ARG   B O   1 
ATOM   5860  C  CB  . ARG   B  1 307 ? -21.254 17.868  -8.080   1.00 64.60  ? 608  ARG   B CB  1 
ATOM   5861  C  CG  . ARG   B  1 307 ? -22.775 18.002  -8.084   1.00 54.41  ? 608  ARG   B CG  1 
ATOM   5862  C  CD  . ARG   B  1 307 ? -23.298 18.614  -6.774   1.00 57.24  ? 608  ARG   B CD  1 
ATOM   5863  N  NE  . ARG   B  1 307 ? -22.897 17.832  -5.603   1.00 56.63  ? 608  ARG   B NE  1 
ATOM   5864  C  CZ  . ARG   B  1 307 ? -23.370 16.620  -5.314   1.00 57.35  ? 608  ARG   B CZ  1 
ATOM   5865  N  NH1 . ARG   B  1 307 ? -24.267 16.043  -6.105   1.00 55.08  ? 608  ARG   B NH1 1 
ATOM   5866  N  NH2 . ARG   B  1 307 ? -22.943 15.978  -4.238   1.00 58.52  ? 608  ARG   B NH2 1 
ATOM   5867  N  N   . TYR   B  1 308 ? -18.506 17.861  -7.673   1.00 54.92  ? 609  TYR   B N   1 
ATOM   5868  C  CA  . TYR   B  1 308 ? -17.078 17.777  -7.373   1.00 61.69  ? 609  TYR   B CA  1 
ATOM   5869  C  C   . TYR   B  1 308 ? -16.198 17.867  -8.613   1.00 66.24  ? 609  TYR   B C   1 
ATOM   5870  O  O   . TYR   B  1 308 ? -15.038 18.282  -8.497   1.00 75.72  ? 609  TYR   B O   1 
ATOM   5871  C  CB  . TYR   B  1 308 ? -16.773 16.521  -6.565   1.00 69.80  ? 609  TYR   B CB  1 
ATOM   5872  C  CG  . TYR   B  1 308 ? -16.814 16.854  -5.099   1.00 77.26  ? 609  TYR   B CG  1 
ATOM   5873  C  CD1 . TYR   B  1 308 ? -18.025 16.906  -4.405   1.00 70.23  ? 609  TYR   B CD1 1 
ATOM   5874  C  CD2 . TYR   B  1 308 ? -15.652 17.189  -4.419   1.00 82.78  ? 609  TYR   B CD2 1 
ATOM   5875  C  CE1 . TYR   B  1 308 ? -18.066 17.239  -3.065   1.00 62.64  ? 609  TYR   B CE1 1 
ATOM   5876  C  CE2 . TYR   B  1 308 ? -15.682 17.521  -3.085   1.00 75.30  ? 609  TYR   B CE2 1 
ATOM   5877  C  CZ  . TYR   B  1 308 ? -16.888 17.543  -2.413   1.00 67.61  ? 609  TYR   B CZ  1 
ATOM   5878  O  OH  . TYR   B  1 308 ? -16.907 17.878  -1.081   1.00 62.57  ? 609  TYR   B OH  1 
ATOM   5879  N  N   . ASN   B  1 309 ? -16.720 17.481  -9.788   1.00 63.83  ? 610  ASN   B N   1 
ATOM   5880  C  CA  . ASN   B  1 309 ? -16.153 17.869  -11.091  1.00 56.98  ? 610  ASN   B CA  1 
ATOM   5881  C  C   . ASN   B  1 309 ? -14.685 17.464  -11.235  1.00 53.17  ? 610  ASN   B C   1 
ATOM   5882  O  O   . ASN   B  1 309 ? -13.871 18.203  -11.792  1.00 43.85  ? 610  ASN   B O   1 
ATOM   5883  C  CB  . ASN   B  1 309 ? -16.317 19.375  -11.320  1.00 53.97  ? 610  ASN   B CB  1 
ATOM   5884  C  CG  . ASN   B  1 309 ? -16.096 19.779  -12.766  1.00 59.48  ? 610  ASN   B CG  1 
ATOM   5885  O  OD1 . ASN   B  1 309 ? -16.211 18.954  -13.679  1.00 62.62  ? 610  ASN   B OD1 1 
ATOM   5886  N  ND2 . ASN   B  1 309 ? -15.780 21.058  -12.985  1.00 47.97  ? 610  ASN   B ND2 1 
ATOM   5887  N  N   . ILE   B  1 310 ? -14.332 16.279  -10.721  1.00 64.23  ? 611  ILE   B N   1 
ATOM   5888  C  CA  . ILE   B  1 310 ? -12.924 15.887  -10.639  1.00 72.46  ? 611  ILE   B CA  1 
ATOM   5889  C  C   . ILE   B  1 310 ? -12.411 15.255  -11.919  1.00 76.72  ? 611  ILE   B C   1 
ATOM   5890  O  O   . ILE   B  1 310 ? -11.252 14.815  -11.955  1.00 78.36  ? 611  ILE   B O   1 
ATOM   5891  C  CB  . ILE   B  1 310 ? -12.675 14.902  -9.481   1.00 70.82  ? 611  ILE   B CB  1 
ATOM   5892  C  CG1 . ILE   B  1 310 ? -13.512 13.640  -9.664   1.00 62.54  ? 611  ILE   B CG1 1 
ATOM   5893  C  CG2 . ILE   B  1 310 ? -13.010 15.549  -8.147   1.00 75.72  ? 611  ILE   B CG2 1 
ATOM   5894  C  CD1 . ILE   B  1 310 ? -13.087 12.531  -8.763   1.00 59.67  ? 611  ILE   B CD1 1 
ATOM   5895  N  N   . LEU   B  1 311 ? -13.232 15.219  -12.976  1.00 73.82  ? 612  LEU   B N   1 
ATOM   5896  C  CA  . LEU   B  1 311 ? -12.915 14.433  -14.168  1.00 64.72  ? 612  LEU   B CA  1 
ATOM   5897  C  C   . LEU   B  1 311 ? -11.599 14.867  -14.811  1.00 66.33  ? 612  LEU   B C   1 
ATOM   5898  O  O   . LEU   B  1 311 ? -10.735 14.025  -15.080  1.00 71.33  ? 612  LEU   B O   1 
ATOM   5899  C  CB  . LEU   B  1 311 ? -14.060 14.522  -15.176  1.00 51.28  ? 612  LEU   B CB  1 
ATOM   5900  C  CG  . LEU   B  1 311 ? -15.200 13.519  -15.033  1.00 41.07  ? 612  LEU   B CG  1 
ATOM   5901  C  CD1 . LEU   B  1 311 ? -16.389 13.938  -15.861  1.00 36.50  ? 612  LEU   B CD1 1 
ATOM   5902  C  CD2 . LEU   B  1 311 ? -14.750 12.152  -15.453  1.00 38.14  ? 612  LEU   B CD2 1 
ATOM   5903  N  N   . GLU   B  1 312 ? -11.431 16.169  -15.088  1.00 61.52  ? 613  GLU   B N   1 
ATOM   5904  C  CA  . GLU   B  1 312 ? -10.180 16.637  -15.688  1.00 71.55  ? 613  GLU   B CA  1 
ATOM   5905  C  C   . GLU   B  1 312 ? -8.982  16.134  -14.897  1.00 74.20  ? 613  GLU   B C   1 
ATOM   5906  O  O   . GLU   B  1 312 ? -8.029  15.586  -15.465  1.00 69.31  ? 613  GLU   B O   1 
ATOM   5907  C  CB  . GLU   B  1 312 ? -10.138 18.170  -15.778  1.00 77.08  ? 613  GLU   B CB  1 
ATOM   5908  C  CG  . GLU   B  1 312 ? -11.446 18.845  -16.119  1.00 84.34  ? 613  GLU   B CG  1 
ATOM   5909  C  CD  . GLU   B  1 312 ? -12.292 19.108  -14.882  1.00 89.66  ? 613  GLU   B CD  1 
ATOM   5910  O  OE1 . GLU   B  1 312 ? -12.191 20.219  -14.314  1.00 92.90  ? 613  GLU   B OE1 1 
ATOM   5911  O  OE2 . GLU   B  1 312 ? -13.046 18.199  -14.468  1.00 81.78  ? 613  GLU   B OE2 1 
ATOM   5912  N  N   . GLU   B  1 313 ? -9.041  16.277  -13.568  1.00 82.41  ? 614  GLU   B N   1 
ATOM   5913  C  CA  . GLU   B  1 313 ? -7.898  15.938  -12.724  1.00 86.68  ? 614  GLU   B CA  1 
ATOM   5914  C  C   . GLU   B  1 313 ? -7.631  14.439  -12.721  1.00 83.28  ? 614  GLU   B C   1 
ATOM   5915  O  O   . GLU   B  1 313 ? -6.472  14.011  -12.741  1.00 87.63  ? 614  GLU   B O   1 
ATOM   5916  C  CB  . GLU   B  1 313 ? -8.131  16.444  -11.304  1.00 88.79  ? 614  GLU   B CB  1 
ATOM   5917  C  CG  . GLU   B  1 313 ? -7.000  17.301  -10.776  1.00 103.14 ? 614  GLU   B CG  1 
ATOM   5918  C  CD  . GLU   B  1 313 ? -6.557  16.870  -9.394   1.00 111.75 ? 614  GLU   B CD  1 
ATOM   5919  O  OE1 . GLU   B  1 313 ? -6.767  15.684  -9.062   1.00 113.21 ? 614  GLU   B OE1 1 
ATOM   5920  O  OE2 . GLU   B  1 313 ? -6.008  17.710  -8.643   1.00 113.69 ? 614  GLU   B OE2 1 
ATOM   5921  N  N   . VAL   B  1 314 ? -8.684  13.622  -12.687  1.00 77.74  ? 615  VAL   B N   1 
ATOM   5922  C  CA  . VAL   B  1 314 ? -8.484  12.186  -12.827  1.00 75.11  ? 615  VAL   B CA  1 
ATOM   5923  C  C   . VAL   B  1 314 ? -8.017  11.855  -14.238  1.00 75.74  ? 615  VAL   B C   1 
ATOM   5924  O  O   . VAL   B  1 314 ? -7.172  10.977  -14.435  1.00 88.01  ? 615  VAL   B O   1 
ATOM   5925  C  CB  . VAL   B  1 314 ? -9.766  11.422  -12.459  1.00 73.16  ? 615  VAL   B CB  1 
ATOM   5926  C  CG1 . VAL   B  1 314 ? -9.536  9.924   -12.564  1.00 73.24  ? 615  VAL   B CG1 1 
ATOM   5927  C  CG2 . VAL   B  1 314 ? -10.219 11.797  -11.060  1.00 64.43  ? 615  VAL   B CG2 1 
ATOM   5928  N  N   . ALA   B  1 315 ? -8.541  12.560  -15.240  1.00 70.51  ? 616  ALA   B N   1 
ATOM   5929  C  CA  . ALA   B  1 315 ? -8.082  12.321  -16.603  1.00 71.92  ? 616  ALA   B CA  1 
ATOM   5930  C  C   . ALA   B  1 315 ? -6.617  12.695  -16.755  1.00 67.76  ? 616  ALA   B C   1 
ATOM   5931  O  O   . ALA   B  1 315 ? -5.841  11.933  -17.338  1.00 68.68  ? 616  ALA   B O   1 
ATOM   5932  C  CB  . ALA   B  1 315 ? -8.941  13.092  -17.608  1.00 77.07  ? 616  ALA   B CB  1 
ATOM   5933  N  N   . LYS   B  1 316 ? -6.218  13.856  -16.223  1.00 67.98  ? 617  LYS   B N   1 
ATOM   5934  C  CA  . LYS   B  1 316 ? -4.832  14.299  -16.360  1.00 68.92  ? 617  LYS   B CA  1 
ATOM   5935  C  C   . LYS   B  1 316 ? -3.870  13.310  -15.710  1.00 71.40  ? 617  LYS   B C   1 
ATOM   5936  O  O   . LYS   B  1 316 ? -2.819  12.990  -16.277  1.00 75.85  ? 617  LYS   B O   1 
ATOM   5937  C  CB  . LYS   B  1 316 ? -4.655  15.690  -15.749  1.00 69.38  ? 617  LYS   B CB  1 
ATOM   5938  C  CG  . LYS   B  1 316 ? -3.218  16.182  -15.812  1.00 81.90  ? 617  LYS   B CG  1 
ATOM   5939  C  CD  . LYS   B  1 316 ? -2.976  17.374  -14.909  1.00 87.62  ? 617  LYS   B CD  1 
ATOM   5940  C  CE  . LYS   B  1 316 ? -1.485  17.701  -14.812  1.00 93.80  ? 617  LYS   B CE  1 
ATOM   5941  N  NZ  . LYS   B  1 316 ? -1.148  18.297  -13.478  1.00 97.16  ? 617  LYS   B NZ  1 
ATOM   5942  N  N   . LYS   B  1 317 ? -4.223  12.811  -14.522  1.00 68.08  ? 618  LYS   B N   1 
ATOM   5943  C  CA  . LYS   B  1 317 ? -3.430  11.775  -13.865  1.00 75.57  ? 618  LYS   B CA  1 
ATOM   5944  C  C   . LYS   B  1 317 ? -3.429  10.473  -14.653  1.00 81.07  ? 618  LYS   B C   1 
ATOM   5945  O  O   . LYS   B  1 317 ? -2.580  9.610   -14.406  1.00 84.04  ? 618  LYS   B O   1 
ATOM   5946  C  CB  . LYS   B  1 317 ? -3.952  11.523  -12.437  1.00 74.71  ? 618  LYS   B CB  1 
ATOM   5947  C  CG  . LYS   B  1 317 ? -3.163  12.207  -11.293  1.00 78.14  ? 618  LYS   B CG  1 
ATOM   5948  C  CD  . LYS   B  1 317 ? -2.106  11.281  -10.691  1.00 77.00  ? 618  LYS   B CD  1 
ATOM   5949  C  CE  . LYS   B  1 317 ? -0.725  11.919  -10.642  1.00 87.56  ? 618  LYS   B CE  1 
ATOM   5950  N  NZ  . LYS   B  1 317 ? -0.612  12.945  -9.568   1.00 97.93  ? 618  LYS   B NZ  1 
ATOM   5951  N  N   . MET   B  1 318 ? -4.358  10.310  -15.592  1.00 77.80  ? 619  MET   B N   1 
ATOM   5952  C  CA  . MET   B  1 318 ? -4.417  9.120   -16.431  1.00 70.63  ? 619  MET   B CA  1 
ATOM   5953  C  C   . MET   B  1 318 ? -3.698  9.287   -17.760  1.00 72.03  ? 619  MET   B C   1 
ATOM   5954  O  O   . MET   B  1 318 ? -3.581  8.305   -18.501  1.00 76.53  ? 619  MET   B O   1 
ATOM   5955  C  CB  . MET   B  1 318 ? -5.875  8.721   -16.694  1.00 66.41  ? 619  MET   B CB  1 
ATOM   5956  C  CG  . MET   B  1 318 ? -6.492  7.907   -15.572  1.00 59.01  ? 619  MET   B CG  1 
ATOM   5957  S  SD  . MET   B  1 318 ? -8.155  7.290   -15.905  1.00 62.02  ? 619  MET   B SD  1 
ATOM   5958  C  CE  . MET   B  1 318 ? -7.850  6.204   -17.298  1.00 73.49  ? 619  MET   B CE  1 
ATOM   5959  N  N   . ASN   B  1 319 ? -3.228  10.497  -18.079  1.00 73.95  ? 620  ASN   B N   1 
ATOM   5960  C  CA  . ASN   B  1 319 ? -2.557  10.810  -19.345  1.00 77.64  ? 620  ASN   B CA  1 
ATOM   5961  C  C   . ASN   B  1 319 ? -3.506  10.616  -20.533  1.00 75.33  ? 620  ASN   B C   1 
ATOM   5962  O  O   . ASN   B  1 319 ? -3.319  9.754   -21.398  1.00 73.87  ? 620  ASN   B O   1 
ATOM   5963  C  CB  . ASN   B  1 319 ? -1.287  9.972   -19.510  1.00 78.72  ? 620  ASN   B CB  1 
ATOM   5964  C  CG  . ASN   B  1 319 ? -0.291  10.216  -18.406  1.00 91.38  ? 620  ASN   B CG  1 
ATOM   5965  O  OD1 . ASN   B  1 319 ? 0.361   11.260  -18.370  1.00 101.24 ? 620  ASN   B OD1 1 
ATOM   5966  N  ND2 . ASN   B  1 319 ? -0.158  9.253   -17.498  1.00 91.27  ? 620  ASN   B ND2 1 
ATOM   5967  N  N   . LEU   B  1 320 ? -4.528  11.461  -20.564  1.00 67.01  ? 621  LEU   B N   1 
ATOM   5968  C  CA  . LEU   B  1 320 ? -5.616  11.312  -21.512  1.00 61.18  ? 621  LEU   B CA  1 
ATOM   5969  C  C   . LEU   B  1 320 ? -5.634  12.486  -22.481  1.00 78.84  ? 621  LEU   B C   1 
ATOM   5970  O  O   . LEU   B  1 320 ? -5.268  13.610  -22.130  1.00 83.87  ? 621  LEU   B O   1 
ATOM   5971  C  CB  . LEU   B  1 320 ? -6.963  11.183  -20.784  1.00 56.93  ? 621  LEU   B CB  1 
ATOM   5972  C  CG  . LEU   B  1 320 ? -7.214  9.801   -20.170  1.00 56.18  ? 621  LEU   B CG  1 
ATOM   5973  C  CD1 . LEU   B  1 320 ? -8.597  9.680   -19.525  1.00 51.90  ? 621  LEU   B CD1 1 
ATOM   5974  C  CD2 . LEU   B  1 320 ? -7.015  8.725   -21.223  1.00 58.59  ? 621  LEU   B CD2 1 
ATOM   5975  N  N   . ASP   B  1 321 ? -6.050  12.199  -23.717  1.00 84.18  ? 622  ASP   B N   1 
ATOM   5976  C  CA  . ASP   B  1 321 ? -6.105  13.181  -24.799  1.00 95.02  ? 622  ASP   B CA  1 
ATOM   5977  C  C   . ASP   B  1 321 ? -7.297  14.101  -24.568  1.00 91.74  ? 622  ASP   B C   1 
ATOM   5978  O  O   . ASP   B  1 321 ? -8.375  13.932  -25.140  1.00 99.50  ? 622  ASP   B O   1 
ATOM   5979  C  CB  . ASP   B  1 321 ? -6.214  12.472  -26.146  1.00 106.58 ? 622  ASP   B CB  1 
ATOM   5980  C  CG  . ASP   B  1 321 ? -6.056  13.418  -27.327  1.00 116.84 ? 622  ASP   B CG  1 
ATOM   5981  O  OD1 . ASP   B  1 321 ? -6.072  12.942  -28.488  1.00 119.46 ? 622  ASP   B OD1 1 
ATOM   5982  O  OD2 . ASP   B  1 321 ? -5.890  14.633  -27.095  1.00 118.71 ? 622  ASP   B OD2 1 
ATOM   5983  N  N   . MET   B  1 322 ? -7.093  15.114  -23.728  1.00 84.84  ? 623  MET   B N   1 
ATOM   5984  C  CA  . MET   B  1 322 ? -8.172  16.003  -23.322  1.00 77.62  ? 623  MET   B CA  1 
ATOM   5985  C  C   . MET   B  1 322 ? -8.370  17.180  -24.270  1.00 79.45  ? 623  MET   B C   1 
ATOM   5986  O  O   . MET   B  1 322 ? -9.043  18.150  -23.898  1.00 81.24  ? 623  MET   B O   1 
ATOM   5987  C  CB  . MET   B  1 322 ? -7.920  16.514  -21.908  1.00 65.84  ? 623  MET   B CB  1 
ATOM   5988  C  CG  . MET   B  1 322 ? -7.691  15.403  -20.910  1.00 76.81  ? 623  MET   B CG  1 
ATOM   5989  S  SD  . MET   B  1 322 ? -7.336  16.055  -19.269  1.00 88.69  ? 623  MET   B SD  1 
ATOM   5990  C  CE  . MET   B  1 322 ? -8.731  17.158  -19.027  1.00 91.30  ? 623  MET   B CE  1 
ATOM   5991  N  N   . ARG   B  1 323 ? -7.815  17.115  -25.485  1.00 74.69  ? 624  ARG   B N   1 
ATOM   5992  C  CA  . ARG   B  1 323 ? -7.923  18.244  -26.401  1.00 66.29  ? 624  ARG   B CA  1 
ATOM   5993  C  C   . ARG   B  1 323 ? -9.266  18.305  -27.116  1.00 68.27  ? 624  ARG   B C   1 
ATOM   5994  O  O   . ARG   B  1 323 ? -9.721  19.405  -27.437  1.00 72.06  ? 624  ARG   B O   1 
ATOM   5995  C  CB  . ARG   B  1 323 ? -6.817  18.199  -27.441  1.00 78.60  ? 624  ARG   B CB  1 
ATOM   5996  C  CG  . ARG   B  1 323 ? -5.518  17.605  -26.965  1.00 87.51  ? 624  ARG   B CG  1 
ATOM   5997  C  CD  . ARG   B  1 323 ? -4.484  17.638  -28.093  1.00 99.47  ? 624  ARG   B CD  1 
ATOM   5998  N  NE  . ARG   B  1 323 ? -4.997  17.198  -29.398  1.00 100.48 ? 624  ARG   B NE  1 
ATOM   5999  C  CZ  . ARG   B  1 323 ? -5.371  18.014  -30.386  1.00 98.23  ? 624  ARG   B CZ  1 
ATOM   6000  N  NH1 . ARG   B  1 323 ? -5.315  19.329  -30.225  1.00 99.48  ? 624  ARG   B NH1 1 
ATOM   6001  N  NH2 . ARG   B  1 323 ? -5.806  17.519  -31.538  1.00 95.21  ? 624  ARG   B NH2 1 
ATOM   6002  N  N   . LYS   B  1 324 ? -9.900  17.161  -27.398  1.00 76.50  ? 625  LYS   B N   1 
ATOM   6003  C  CA  . LYS   B  1 324 ? -11.220 17.132  -28.029  1.00 82.76  ? 625  LYS   B CA  1 
ATOM   6004  C  C   . LYS   B  1 324 ? -12.077 16.037  -27.389  1.00 80.37  ? 625  LYS   B C   1 
ATOM   6005  O  O   . LYS   B  1 324 ? -11.557 15.089  -26.796  1.00 88.71  ? 625  LYS   B O   1 
ATOM   6006  C  CB  . LYS   B  1 324 ? -11.109 16.920  -29.551  1.00 86.45  ? 625  LYS   B CB  1 
ATOM   6007  C  CG  . LYS   B  1 324 ? -12.420 17.144  -30.303  1.00 94.07  ? 625  LYS   B CG  1 
ATOM   6008  C  CD  . LYS   B  1 324 ? -12.354 16.658  -31.747  1.00 102.67 ? 625  LYS   B CD  1 
ATOM   6009  C  CE  . LYS   B  1 324 ? -13.722 16.755  -32.430  1.00 104.73 ? 625  LYS   B CE  1 
ATOM   6010  N  NZ  . LYS   B  1 324 ? -13.700 16.236  -33.831  1.00 103.88 ? 625  LYS   B NZ  1 
ATOM   6011  N  N   . THR   B  1 325 ? -13.409 16.174  -27.505  1.00 65.64  ? 626  THR   B N   1 
ATOM   6012  C  CA  . THR   B  1 325 ? -14.308 15.211  -26.859  1.00 63.22  ? 626  THR   B CA  1 
ATOM   6013  C  C   . THR   B  1 325 ? -14.177 13.808  -27.442  1.00 62.31  ? 626  THR   B C   1 
ATOM   6014  O  O   . THR   B  1 325 ? -14.365 12.822  -26.720  1.00 64.64  ? 626  THR   B O   1 
ATOM   6015  C  CB  . THR   B  1 325 ? -15.773 15.649  -26.967  1.00 59.70  ? 626  THR   B CB  1 
ATOM   6016  O  OG1 . THR   B  1 325 ? -16.139 15.781  -28.346  1.00 81.68  ? 626  THR   B OG1 1 
ATOM   6017  C  CG2 . THR   B  1 325 ? -16.000 16.959  -26.282  1.00 60.23  ? 626  THR   B CG2 1 
ATOM   6018  N  N   . SER   B  1 326 ? -13.862 13.698  -28.733  1.00 58.91  ? 627  SER   B N   1 
ATOM   6019  C  CA  . SER   B  1 326 ? -13.904 12.419  -29.432  1.00 53.19  ? 627  SER   B CA  1 
ATOM   6020  C  C   . SER   B  1 326 ? -13.031 11.353  -28.793  1.00 58.51  ? 627  SER   B C   1 
ATOM   6021  O  O   . SER   B  1 326 ? -13.280 10.161  -29.008  1.00 60.70  ? 627  SER   B O   1 
ATOM   6022  C  CB  . SER   B  1 326 ? -13.462 12.608  -30.872  1.00 46.81  ? 627  SER   B CB  1 
ATOM   6023  O  OG  . SER   B  1 326 ? -13.903 13.866  -31.342  1.00 67.52  ? 627  SER   B OG  1 
ATOM   6024  N  N   . SER   B  1 327 ? -11.989 11.745  -28.052  1.00 51.61  ? 628  SER   B N   1 
ATOM   6025  C  CA  . SER   B  1 327 ? -11.161 10.764  -27.353  1.00 57.06  ? 628  SER   B CA  1 
ATOM   6026  C  C   . SER   B  1 327 ? -11.916 10.041  -26.259  1.00 53.21  ? 628  SER   B C   1 
ATOM   6027  O  O   . SER   B  1 327 ? -11.433 9.012   -25.791  1.00 62.16  ? 628  SER   B O   1 
ATOM   6028  C  CB  . SER   B  1 327 ? -9.947  11.421  -26.719  1.00 56.97  ? 628  SER   B CB  1 
ATOM   6029  O  OG  . SER   B  1 327 ? -10.386 12.393  -25.801  1.00 61.14  ? 628  SER   B OG  1 
ATOM   6030  N  N   . LEU   B  1 328 ? -13.076 10.555  -25.852  1.00 47.74  ? 629  LEU   B N   1 
ATOM   6031  C  CA  . LEU   B  1 328 ? -13.890 9.958   -24.807  1.00 47.51  ? 629  LEU   B CA  1 
ATOM   6032  C  C   . LEU   B  1 328 ? -13.134 9.920   -23.480  1.00 58.55  ? 629  LEU   B C   1 
ATOM   6033  O  O   . LEU   B  1 328 ? -13.274 8.978   -22.693  1.00 57.52  ? 629  LEU   B O   1 
ATOM   6034  C  CB  . LEU   B  1 328 ? -14.375 8.563   -25.217  1.00 49.97  ? 629  LEU   B CB  1 
ATOM   6035  C  CG  . LEU   B  1 328 ? -15.219 8.465   -26.500  1.00 52.00  ? 629  LEU   B CG  1 
ATOM   6036  C  CD1 . LEU   B  1 328 ? -16.091 7.222   -26.457  1.00 42.29  ? 629  LEU   B CD1 1 
ATOM   6037  C  CD2 . LEU   B  1 328 ? -16.108 9.690   -26.682  1.00 48.42  ? 629  LEU   B CD2 1 
ATOM   6038  N  N   . TRP   B  1 329 ? -12.322 10.957  -23.230  1.00 52.53  ? 630  TRP   B N   1 
ATOM   6039  C  CA  . TRP   B  1 329 ? -11.465 10.963  -22.051  1.00 51.52  ? 630  TRP   B CA  1 
ATOM   6040  C  C   . TRP   B  1 329 ? -12.289 11.084  -20.772  1.00 51.14  ? 630  TRP   B C   1 
ATOM   6041  O  O   . TRP   B  1 329 ? -12.039 10.362  -19.800  1.00 53.15  ? 630  TRP   B O   1 
ATOM   6042  C  CB  . TRP   B  1 329 ? -10.422 12.086  -22.169  1.00 56.74  ? 630  TRP   B CB  1 
ATOM   6043  C  CG  . TRP   B  1 329 ? -10.975 13.483  -22.290  1.00 64.58  ? 630  TRP   B CG  1 
ATOM   6044  C  CD1 . TRP   B  1 329 ? -11.180 14.189  -23.443  1.00 67.70  ? 630  TRP   B CD1 1 
ATOM   6045  C  CD2 . TRP   B  1 329 ? -11.369 14.349  -21.216  1.00 66.45  ? 630  TRP   B CD2 1 
ATOM   6046  N  NE1 . TRP   B  1 329 ? -11.687 15.435  -23.154  1.00 73.92  ? 630  TRP   B NE1 1 
ATOM   6047  C  CE2 . TRP   B  1 329 ? -11.819 15.555  -21.794  1.00 75.69  ? 630  TRP   B CE2 1 
ATOM   6048  C  CE3 . TRP   B  1 329 ? -11.386 14.222  -19.826  1.00 62.61  ? 630  TRP   B CE3 1 
ATOM   6049  C  CZ2 . TRP   B  1 329 ? -12.289 16.624  -21.025  1.00 67.82  ? 630  TRP   B CZ2 1 
ATOM   6050  C  CZ3 . TRP   B  1 329 ? -11.848 15.283  -19.068  1.00 59.66  ? 630  TRP   B CZ3 1 
ATOM   6051  C  CH2 . TRP   B  1 329 ? -12.288 16.472  -19.671  1.00 61.01  ? 630  TRP   B CH2 1 
ATOM   6052  N  N   . LYS   B  1 330 ? -13.283 11.980  -20.769  1.00 45.20  ? 631  LYS   B N   1 
ATOM   6053  C  CA  . LYS   B  1 330 ? -14.287 12.009  -19.718  1.00 44.92  ? 631  LYS   B CA  1 
ATOM   6054  C  C   . LYS   B  1 330 ? -14.845 10.620  -19.445  1.00 53.63  ? 631  LYS   B C   1 
ATOM   6055  O  O   . LYS   B  1 330 ? -14.963 10.193  -18.289  1.00 56.11  ? 631  LYS   B O   1 
ATOM   6056  C  CB  . LYS   B  1 330 ? -15.426 12.947  -20.116  1.00 45.02  ? 631  LYS   B CB  1 
ATOM   6057  C  CG  . LYS   B  1 330 ? -15.095 14.434  -20.196  1.00 51.86  ? 631  LYS   B CG  1 
ATOM   6058  C  CD  . LYS   B  1 330 ? -16.399 15.230  -20.025  1.00 57.27  ? 631  LYS   B CD  1 
ATOM   6059  C  CE  . LYS   B  1 330 ? -16.227 16.737  -19.971  1.00 53.43  ? 631  LYS   B CE  1 
ATOM   6060  N  NZ  . LYS   B  1 330 ? -17.535 17.307  -19.513  1.00 61.65  ? 631  LYS   B NZ  1 
ATOM   6061  N  N   . ASP   B  1 331 ? -15.219 9.907   -20.506  1.00 52.56  ? 632  ASP   B N   1 
ATOM   6062  C  CA  . ASP   B  1 331 ? -15.862 8.610   -20.331  1.00 50.55  ? 632  ASP   B CA  1 
ATOM   6063  C  C   . ASP   B  1 331 ? -14.937 7.628   -19.631  1.00 55.36  ? 632  ASP   B C   1 
ATOM   6064  O  O   . ASP   B  1 331 ? -15.370 6.881   -18.744  1.00 47.39  ? 632  ASP   B O   1 
ATOM   6065  C  CB  . ASP   B  1 331 ? -16.307 8.043   -21.680  1.00 38.47  ? 632  ASP   B CB  1 
ATOM   6066  C  CG  . ASP   B  1 331 ? -17.130 9.022   -22.479  1.00 43.83  ? 632  ASP   B CG  1 
ATOM   6067  O  OD1 . ASP   B  1 331 ? -16.525 9.837   -23.207  1.00 50.53  ? 632  ASP   B OD1 1 
ATOM   6068  O  OD2 . ASP   B  1 331 ? -18.378 8.972   -22.401  1.00 44.53  ? 632  ASP   B OD2 1 
ATOM   6069  N  N   . GLN   B  1 332 ? -13.657 7.626   -20.012  1.00 60.48  ? 633  GLN   B N   1 
ATOM   6070  C  CA  . GLN   B  1 332 ? -12.712 6.656   -19.469  1.00 63.75  ? 633  GLN   B CA  1 
ATOM   6071  C  C   . GLN   B  1 332 ? -12.456 6.908   -17.993  1.00 60.30  ? 633  GLN   B C   1 
ATOM   6072  O  O   . GLN   B  1 332 ? -12.505 5.979   -17.179  1.00 54.71  ? 633  GLN   B O   1 
ATOM   6073  C  CB  . GLN   B  1 332 ? -11.406 6.697   -20.255  1.00 61.08  ? 633  GLN   B CB  1 
ATOM   6074  C  CG  . GLN   B  1 332 ? -11.116 5.395   -20.936  1.00 63.10  ? 633  GLN   B CG  1 
ATOM   6075  C  CD  . GLN   B  1 332 ? -9.916  5.471   -21.842  1.00 77.91  ? 633  GLN   B CD  1 
ATOM   6076  O  OE1 . GLN   B  1 332 ? -9.525  6.548   -22.299  1.00 84.63  ? 633  GLN   B OE1 1 
ATOM   6077  N  NE2 . GLN   B  1 332 ? -9.324  4.321   -22.116  1.00 83.09  ? 633  GLN   B NE2 1 
ATOM   6078  N  N   . ALA   B  1 333 ? -12.184 8.163   -17.633  1.00 63.54  ? 634  ALA   B N   1 
ATOM   6079  C  CA  . ALA   B  1 333 ? -12.021 8.516   -16.228  1.00 57.14  ? 634  ALA   B CA  1 
ATOM   6080  C  C   . ALA   B  1 333 ? -13.269 8.160   -15.432  1.00 50.44  ? 634  ALA   B C   1 
ATOM   6081  O  O   . ALA   B  1 333 ? -13.180 7.622   -14.321  1.00 49.49  ? 634  ALA   B O   1 
ATOM   6082  C  CB  . ALA   B  1 333 ? -11.693 10.005  -16.098  1.00 49.72  ? 634  ALA   B CB  1 
ATOM   6083  N  N   . LEU   B  1 334 ? -14.448 8.443   -15.996  1.00 45.08  ? 635  LEU   B N   1 
ATOM   6084  C  CA  . LEU   B  1 334 ? -15.689 8.155   -15.290  1.00 41.47  ? 635  LEU   B CA  1 
ATOM   6085  C  C   . LEU   B  1 334 ? -15.756 6.691   -14.882  1.00 54.45  ? 635  LEU   B C   1 
ATOM   6086  O  O   . LEU   B  1 334 ? -16.149 6.374   -13.752  1.00 59.51  ? 635  LEU   B O   1 
ATOM   6087  C  CB  . LEU   B  1 334 ? -16.898 8.532   -16.149  1.00 42.16  ? 635  LEU   B CB  1 
ATOM   6088  C  CG  . LEU   B  1 334 ? -18.264 8.158   -15.554  1.00 39.17  ? 635  LEU   B CG  1 
ATOM   6089  C  CD1 . LEU   B  1 334 ? -18.515 8.937   -14.297  1.00 40.98  ? 635  LEU   B CD1 1 
ATOM   6090  C  CD2 . LEU   B  1 334 ? -19.385 8.393   -16.559  1.00 53.12  ? 635  LEU   B CD2 1 
ATOM   6091  N  N   . VAL   B  1 335 ? -15.341 5.782   -15.771  1.00 53.71  ? 636  VAL   B N   1 
ATOM   6092  C  CA  . VAL   B  1 335 ? -15.388 4.360   -15.434  1.00 55.09  ? 636  VAL   B CA  1 
ATOM   6093  C  C   . VAL   B  1 335 ? -14.429 4.052   -14.283  1.00 55.26  ? 636  VAL   B C   1 
ATOM   6094  O  O   . VAL   B  1 335 ? -14.795 3.382   -13.307  1.00 53.69  ? 636  VAL   B O   1 
ATOM   6095  C  CB  . VAL   B  1 335 ? -15.095 3.496   -16.673  1.00 47.68  ? 636  VAL   B CB  1 
ATOM   6096  C  CG1 . VAL   B  1 335 ? -14.514 2.168   -16.254  1.00 47.26  ? 636  VAL   B CG1 1 
ATOM   6097  C  CG2 . VAL   B  1 335 ? -16.373 3.251   -17.460  1.00 49.50  ? 636  VAL   B CG2 1 
ATOM   6098  N  N   . GLU   B  1 336 ? -13.196 4.561   -14.367  1.00 45.73  ? 637  GLU   B N   1 
ATOM   6099  C  CA  . GLU   B  1 336 ? -12.200 4.251   -13.350  1.00 50.74  ? 637  GLU   B CA  1 
ATOM   6100  C  C   . GLU   B  1 336 ? -12.622 4.761   -11.976  1.00 57.63  ? 637  GLU   B C   1 
ATOM   6101  O  O   . GLU   B  1 336 ? -12.455 4.066   -10.964  1.00 66.48  ? 637  GLU   B O   1 
ATOM   6102  C  CB  . GLU   B  1 336 ? -10.854 4.844   -13.751  1.00 48.18  ? 637  GLU   B CB  1 
ATOM   6103  C  CG  . GLU   B  1 336 ? -10.236 4.238   -14.998  1.00 49.60  ? 637  GLU   B CG  1 
ATOM   6104  C  CD  . GLU   B  1 336 ? -9.891  2.753   -14.888  1.00 56.13  ? 637  GLU   B CD  1 
ATOM   6105  O  OE1 . GLU   B  1 336 ? -10.147 2.108   -13.856  1.00 61.12  ? 637  GLU   B OE1 1 
ATOM   6106  O  OE2 . GLU   B  1 336 ? -9.348  2.217   -15.862  1.00 64.05  ? 637  GLU   B OE2 1 
ATOM   6107  N  N   . ILE   B  1 337 ? -13.179 5.970   -11.923  1.00 54.14  ? 638  ILE   B N   1 
ATOM   6108  C  CA  . ILE   B  1 337 ? -13.677 6.516   -10.665  1.00 52.61  ? 638  ILE   B CA  1 
ATOM   6109  C  C   . ILE   B  1 337 ? -14.713 5.588   -10.048  1.00 55.58  ? 638  ILE   B C   1 
ATOM   6110  O  O   . ILE   B  1 337 ? -14.702 5.334   -8.841   1.00 58.35  ? 638  ILE   B O   1 
ATOM   6111  C  CB  . ILE   B  1 337 ? -14.246 7.929   -10.888  1.00 45.61  ? 638  ILE   B CB  1 
ATOM   6112  C  CG1 . ILE   B  1 337 ? -13.126 8.878   -11.308  1.00 50.49  ? 638  ILE   B CG1 1 
ATOM   6113  C  CG2 . ILE   B  1 337 ? -14.914 8.429   -9.610   1.00 44.35  ? 638  ILE   B CG2 1 
ATOM   6114  C  CD1 . ILE   B  1 337 ? -13.589 10.275  -11.543  1.00 61.76  ? 638  ILE   B CD1 1 
ATOM   6115  N  N   . ASN   B  1 338 ? -15.618 5.056   -10.863  1.00 57.65  ? 639  ASN   B N   1 
ATOM   6116  C  CA  . ASN   B  1 338 ? -16.656 4.200   -10.305  1.00 57.33  ? 639  ASN   B CA  1 
ATOM   6117  C  C   . ASN   B  1 338 ? -16.113 2.826   -9.943   1.00 55.28  ? 639  ASN   B C   1 
ATOM   6118  O  O   . ASN   B  1 338 ? -16.631 2.185   -9.021   1.00 60.91  ? 639  ASN   B O   1 
ATOM   6119  C  CB  . ASN   B  1 338 ? -17.835 4.103   -11.277  1.00 58.13  ? 639  ASN   B CB  1 
ATOM   6120  C  CG  . ASN   B  1 338 ? -18.730 5.333   -11.219  1.00 52.14  ? 639  ASN   B CG  1 
ATOM   6121  O  OD1 . ASN   B  1 338 ? -19.771 5.336   -10.564  1.00 52.35  ? 639  ASN   B OD1 1 
ATOM   6122  N  ND2 . ASN   B  1 338 ? -18.309 6.393   -11.885  1.00 49.31  ? 639  ASN   B ND2 1 
ATOM   6123  N  N   . ILE   B  1 339 ? -15.067 2.363   -10.636  1.00 49.44  ? 640  ILE   B N   1 
ATOM   6124  C  CA  . ILE   B  1 339 ? -14.381 1.161   -10.177  1.00 44.38  ? 640  ILE   B CA  1 
ATOM   6125  C  C   . ILE   B  1 339 ? -13.710 1.422   -8.836   1.00 58.78  ? 640  ILE   B C   1 
ATOM   6126  O  O   . ILE   B  1 339 ? -13.595 0.516   -8.000   1.00 59.84  ? 640  ILE   B O   1 
ATOM   6127  C  CB  . ILE   B  1 339 ? -13.378 0.680   -11.235  1.00 38.31  ? 640  ILE   B CB  1 
ATOM   6128  C  CG1 . ILE   B  1 339 ? -14.119 0.074   -12.426  1.00 47.75  ? 640  ILE   B CG1 1 
ATOM   6129  C  CG2 . ILE   B  1 339 ? -12.411 -0.352  -10.682  1.00 39.90  ? 640  ILE   B CG2 1 
ATOM   6130  C  CD1 . ILE   B  1 339 ? -13.188 -0.471  -13.447  1.00 39.49  ? 640  ILE   B CD1 1 
ATOM   6131  N  N   . ALA   B  1 340 ? -13.281 2.660   -8.592   1.00 61.98  ? 641  ALA   B N   1 
ATOM   6132  C  CA  . ALA   B  1 340 ? -12.600 2.971   -7.343   1.00 51.55  ? 641  ALA   B CA  1 
ATOM   6133  C  C   . ALA   B  1 340 ? -13.582 3.072   -6.192   1.00 57.15  ? 641  ALA   B C   1 
ATOM   6134  O  O   . ALA   B  1 340 ? -13.338 2.535   -5.106   1.00 62.97  ? 641  ALA   B O   1 
ATOM   6135  C  CB  . ALA   B  1 340 ? -11.826 4.279   -7.484   1.00 51.62  ? 641  ALA   B CB  1 
ATOM   6136  N  N   . VAL   B  1 341 ? -14.685 3.772   -6.418   1.00 53.18  ? 642  VAL   B N   1 
ATOM   6137  C  CA  . VAL   B  1 341 ? -15.706 3.915   -5.391   1.00 46.41  ? 642  VAL   B CA  1 
ATOM   6138  C  C   . VAL   B  1 341 ? -16.180 2.545   -4.923   1.00 53.82  ? 642  VAL   B C   1 
ATOM   6139  O  O   . VAL   B  1 341 ? -16.159 2.231   -3.724   1.00 44.53  ? 642  VAL   B O   1 
ATOM   6140  C  CB  . VAL   B  1 341 ? -16.859 4.767   -5.942   1.00 32.47  ? 642  VAL   B CB  1 
ATOM   6141  C  CG1 . VAL   B  1 341 ? -18.117 4.526   -5.166   1.00 31.08  ? 642  VAL   B CG1 1 
ATOM   6142  C  CG2 . VAL   B  1 341 ? -16.454 6.261   -5.940   1.00 35.64  ? 642  VAL   B CG2 1 
ATOM   6143  N  N   . LEU   B  1 342 ? -16.606 1.704   -5.870   1.00 53.07  ? 643  LEU   B N   1 
ATOM   6144  C  CA  . LEU   B  1 342 ? -17.049 0.355   -5.529   1.00 49.68  ? 643  LEU   B CA  1 
ATOM   6145  C  C   . LEU   B  1 342 ? -15.974 -0.417  -4.771   1.00 53.15  ? 643  LEU   B C   1 
ATOM   6146  O  O   . LEU   B  1 342 ? -16.249 -1.050  -3.750   1.00 52.87  ? 643  LEU   B O   1 
ATOM   6147  C  CB  . LEU   B  1 342 ? -17.442 -0.401  -6.796   1.00 53.52  ? 643  LEU   B CB  1 
ATOM   6148  C  CG  . LEU   B  1 342 ? -18.735 0.054   -7.446   1.00 51.24  ? 643  LEU   B CG  1 
ATOM   6149  C  CD1 . LEU   B  1 342 ? -18.895 -0.597  -8.806   1.00 40.55  ? 643  LEU   B CD1 1 
ATOM   6150  C  CD2 . LEU   B  1 342 ? -19.865 -0.305  -6.506   1.00 43.48  ? 643  LEU   B CD2 1 
ATOM   6151  N  N   . TYR   B  1 343 ? -14.736 -0.382  -5.269   1.00 58.22  ? 644  TYR   B N   1 
ATOM   6152  C  CA  . TYR   B  1 343 ? -13.666 -1.161  -4.652   1.00 57.99  ? 644  TYR   B CA  1 
ATOM   6153  C  C   . TYR   B  1 343 ? -13.363 -0.686  -3.236   1.00 70.62  ? 644  TYR   B C   1 
ATOM   6154  O  O   . TYR   B  1 343 ? -12.942 -1.479  -2.384   1.00 71.10  ? 644  TYR   B O   1 
ATOM   6155  C  CB  . TYR   B  1 343 ? -12.419 -1.079  -5.529   1.00 44.27  ? 644  TYR   B CB  1 
ATOM   6156  C  CG  . TYR   B  1 343 ? -11.142 -1.553  -4.900   1.00 43.56  ? 644  TYR   B CG  1 
ATOM   6157  C  CD1 . TYR   B  1 343 ? -10.857 -2.905  -4.791   1.00 46.95  ? 644  TYR   B CD1 1 
ATOM   6158  C  CD2 . TYR   B  1 343 ? -10.191 -0.646  -4.463   1.00 51.32  ? 644  TYR   B CD2 1 
ATOM   6159  C  CE1 . TYR   B  1 343 ? -9.672  -3.339  -4.241   1.00 55.77  ? 644  TYR   B CE1 1 
ATOM   6160  C  CE2 . TYR   B  1 343 ? -9.002  -1.066  -3.904   1.00 60.56  ? 644  TYR   B CE2 1 
ATOM   6161  C  CZ  . TYR   B  1 343 ? -8.746  -2.413  -3.789   1.00 66.74  ? 644  TYR   B CZ  1 
ATOM   6162  O  OH  . TYR   B  1 343 ? -7.551  -2.826  -3.229   1.00 72.14  ? 644  TYR   B OH  1 
ATOM   6163  N  N   . SER   B  1 344 ? -13.577 0.594   -2.962   1.00 66.20  ? 645  SER   B N   1 
ATOM   6164  C  CA  . SER   B  1 344 ? -13.244 1.108   -1.648   1.00 50.69  ? 645  SER   B CA  1 
ATOM   6165  C  C   . SER   B  1 344 ? -14.309 0.724   -0.630   1.00 56.56  ? 645  SER   B C   1 
ATOM   6166  O  O   . SER   B  1 344 ? -13.989 0.244   0.463    1.00 68.65  ? 645  SER   B O   1 
ATOM   6167  C  CB  . SER   B  1 344 ? -13.057 2.617   -1.734   1.00 47.77  ? 645  SER   B CB  1 
ATOM   6168  O  OG  . SER   B  1 344 ? -11.879 2.908   -2.471   1.00 45.74  ? 645  SER   B OG  1 
ATOM   6169  N  N   . PHE   B  1 345 ? -15.583 0.899   -0.986   1.00 51.06  ? 646  PHE   B N   1 
ATOM   6170  C  CA  . PHE   B  1 345 ? -16.667 0.477   -0.103   1.00 49.98  ? 646  PHE   B CA  1 
ATOM   6171  C  C   . PHE   B  1 345 ? -16.625 -1.023  0.173    1.00 59.22  ? 646  PHE   B C   1 
ATOM   6172  O  O   . PHE   B  1 345 ? -16.947 -1.460  1.277    1.00 68.22  ? 646  PHE   B O   1 
ATOM   6173  C  CB  . PHE   B  1 345 ? -18.015 0.855   -0.707   1.00 35.32  ? 646  PHE   B CB  1 
ATOM   6174  C  CG  . PHE   B  1 345 ? -18.474 2.247   -0.371   1.00 40.24  ? 646  PHE   B CG  1 
ATOM   6175  C  CD1 . PHE   B  1 345 ? -17.735 3.358   -0.773   1.00 42.73  ? 646  PHE   B CD1 1 
ATOM   6176  C  CD2 . PHE   B  1 345 ? -19.654 2.447   0.338    1.00 33.63  ? 646  PHE   B CD2 1 
ATOM   6177  C  CE1 . PHE   B  1 345 ? -18.166 4.652   -0.469   1.00 44.10  ? 646  PHE   B CE1 1 
ATOM   6178  C  CE2 . PHE   B  1 345 ? -20.096 3.732   0.643    1.00 40.19  ? 646  PHE   B CE2 1 
ATOM   6179  C  CZ  . PHE   B  1 345 ? -19.350 4.838   0.243    1.00 41.66  ? 646  PHE   B CZ  1 
ATOM   6180  N  N   . GLN   B  1 346 ? -16.254 -1.831  -0.814   1.00 60.62  ? 647  GLN   B N   1 
ATOM   6181  C  CA  . GLN   B  1 346 ? -16.261 -3.269  -0.580   1.00 61.33  ? 647  GLN   B CA  1 
ATOM   6182  C  C   . GLN   B  1 346 ? -15.072 -3.703  0.252    1.00 63.45  ? 647  GLN   B C   1 
ATOM   6183  O  O   . GLN   B  1 346 ? -15.169 -4.669  1.020    1.00 65.47  ? 647  GLN   B O   1 
ATOM   6184  C  CB  . GLN   B  1 346 ? -16.269 -4.027  -1.905   1.00 55.11  ? 647  GLN   B CB  1 
ATOM   6185  C  CG  . GLN   B  1 346 ? -17.619 -4.052  -2.604   1.00 58.50  ? 647  GLN   B CG  1 
ATOM   6186  C  CD  . GLN   B  1 346 ? -17.505 -4.453  -4.054   1.00 57.90  ? 647  GLN   B CD  1 
ATOM   6187  O  OE1 . GLN   B  1 346 ? -16.414 -4.470  -4.618   1.00 60.49  ? 647  GLN   B OE1 1 
ATOM   6188  N  NE2 . GLN   B  1 346 ? -18.633 -4.767  -4.668   1.00 55.79  ? 647  GLN   B NE2 1 
ATOM   6189  N  N   . SER   B  1 347 ? -13.944 -3.011  0.099    1.00 60.57  ? 648  SER   B N   1 
ATOM   6190  C  CA  . SER   B  1 347 ? -12.762 -3.343  0.877    1.00 52.44  ? 648  SER   B CA  1 
ATOM   6191  C  C   . SER   B  1 347 ? -12.915 -2.963  2.342    1.00 55.62  ? 648  SER   B C   1 
ATOM   6192  O  O   . SER   B  1 347 ? -12.243 -3.551  3.194    1.00 58.44  ? 648  SER   B O   1 
ATOM   6193  C  CB  . SER   B  1 347 ? -11.540 -2.653  0.278    1.00 50.80  ? 648  SER   B CB  1 
ATOM   6194  O  OG  . SER   B  1 347 ? -11.251 -3.182  -1.008   1.00 62.31  ? 648  SER   B OG  1 
ATOM   6195  N  N   . ASP   B  1 348 ? -13.762 -1.978  2.646    1.00 45.01  ? 649  ASP   B N   1 
ATOM   6196  C  CA  . ASP   B  1 348 ? -14.050 -1.563  4.009    1.00 45.52  ? 649  ASP   B CA  1 
ATOM   6197  C  C   . ASP   B  1 348 ? -15.346 -2.176  4.524    1.00 48.06  ? 649  ASP   B C   1 
ATOM   6198  O  O   . ASP   B  1 348 ? -15.998 -1.598  5.385    1.00 51.55  ? 649  ASP   B O   1 
ATOM   6199  C  CB  . ASP   B  1 348 ? -14.099 -0.039  4.092    1.00 37.59  ? 649  ASP   B CB  1 
ATOM   6200  C  CG  . ASP   B  1 348 ? -12.727 0.595   3.954    1.00 46.87  ? 649  ASP   B CG  1 
ATOM   6201  O  OD1 . ASP   B  1 348 ? -11.737 -0.148  3.758    1.00 46.49  ? 649  ASP   B OD1 1 
ATOM   6202  O  OD2 . ASP   B  1 348 ? -12.633 1.840   4.062    1.00 59.79  ? 649  ASP   B OD2 1 
ATOM   6203  N  N   . LYS   B  1 349 ? -15.710 -3.348  4.002    1.00 53.81  ? 650  LYS   B N   1 
ATOM   6204  C  CA  . LYS   B  1 349 ? -16.996 -4.019  4.191    1.00 50.58  ? 650  LYS   B CA  1 
ATOM   6205  C  C   . LYS   B  1 349 ? -18.140 -3.052  4.498    1.00 56.90  ? 650  LYS   B C   1 
ATOM   6206  O  O   . LYS   B  1 349 ? -18.912 -3.267  5.438    1.00 63.67  ? 650  LYS   B O   1 
ATOM   6207  C  CB  . LYS   B  1 349 ? -16.867 -5.092  5.276    1.00 42.29  ? 650  LYS   B CB  1 
ATOM   6208  C  CG  . LYS   B  1 349 ? -15.688 -6.045  5.054    1.00 62.35  ? 650  LYS   B CG  1 
ATOM   6209  C  CD  . LYS   B  1 349 ? -15.739 -7.295  5.947    1.00 80.81  ? 650  LYS   B CD  1 
ATOM   6210  C  CE  . LYS   B  1 349 ? -16.699 -8.368  5.415    1.00 91.46  ? 650  LYS   B CE  1 
ATOM   6211  N  NZ  . LYS   B  1 349 ? -16.102 -9.184  4.308    1.00 96.04  ? 650  LYS   B NZ  1 
ATOM   6212  N  N   . VAL   B  1 350 ? -18.263 -1.987  3.706    1.00 41.59  ? 651  VAL   B N   1 
ATOM   6213  C  CA  . VAL   B  1 350 ? -19.384 -1.054  3.799    1.00 43.65  ? 651  VAL   B CA  1 
ATOM   6214  C  C   . VAL   B  1 350 ? -20.367 -1.358  2.672    1.00 54.80  ? 651  VAL   B C   1 
ATOM   6215  O  O   . VAL   B  1 350 ? -19.971 -1.481  1.499    1.00 59.79  ? 651  VAL   B O   1 
ATOM   6216  C  CB  . VAL   B  1 350 ? -18.901 0.407   3.744    1.00 40.23  ? 651  VAL   B CB  1 
ATOM   6217  C  CG1 . VAL   B  1 350 ? -20.065 1.353   3.784    1.00 34.42  ? 651  VAL   B CG1 1 
ATOM   6218  C  CG2 . VAL   B  1 350 ? -17.953 0.702   4.901    1.00 37.44  ? 651  VAL   B CG2 1 
ATOM   6219  N  N   . THR   B  1 351 ? -21.645 -1.492  3.022    1.00 45.66  ? 652  THR   B N   1 
ATOM   6220  C  CA  . THR   B  1 351 ? -22.628 -1.898  2.032    1.00 46.10  ? 652  THR   B CA  1 
ATOM   6221  C  C   . THR   B  1 351 ? -22.659 -0.923  0.861    1.00 46.28  ? 652  THR   B C   1 
ATOM   6222  O  O   . THR   B  1 351 ? -22.624 0.298   1.036    1.00 52.95  ? 652  THR   B O   1 
ATOM   6223  C  CB  . THR   B  1 351 ? -24.013 -2.019  2.654    1.00 39.67  ? 652  THR   B CB  1 
ATOM   6224  O  OG1 . THR   B  1 351 ? -24.012 -3.107  3.575    1.00 46.17  ? 652  THR   B OG1 1 
ATOM   6225  C  CG2 . THR   B  1 351 ? -25.033 -2.347  1.563    1.00 37.65  ? 652  THR   B CG2 1 
ATOM   6226  N  N   . ILE   B  1 352 ? -22.689 -1.480  -0.343   1.00 45.72  ? 653  ILE   B N   1 
ATOM   6227  C  CA  . ILE   B  1 352 ? -22.818 -0.696  -1.563   1.00 37.49  ? 653  ILE   B CA  1 
ATOM   6228  C  C   . ILE   B  1 352 ? -23.263 -1.667  -2.626   1.00 36.16  ? 653  ILE   B C   1 
ATOM   6229  O  O   . ILE   B  1 352 ? -22.968 -2.864  -2.544   1.00 36.19  ? 653  ILE   B O   1 
ATOM   6230  C  CB  . ILE   B  1 352 ? -21.487 -0.007  -1.940   1.00 38.78  ? 653  ILE   B CB  1 
ATOM   6231  C  CG1 . ILE   B  1 352 ? -21.741 1.165   -2.871   1.00 35.71  ? 653  ILE   B CG1 1 
ATOM   6232  C  CG2 . ILE   B  1 352 ? -20.532 -0.997  -2.494   1.00 30.30  ? 653  ILE   B CG2 1 
ATOM   6233  C  CD1 . ILE   B  1 352 ? -20.477 1.953   -3.164   1.00 41.04  ? 653  ILE   B CD1 1 
ATOM   6234  N  N   . VAL   B  1 353 ? -23.996 -1.160  -3.619   1.00 41.48  ? 654  VAL   B N   1 
ATOM   6235  C  CA  . VAL   B  1 353 ? -24.488 -1.967  -4.728   1.00 40.18  ? 654  VAL   B CA  1 
ATOM   6236  C  C   . VAL   B  1 353 ? -24.096 -1.286  -6.037   1.00 50.27  ? 654  VAL   B C   1 
ATOM   6237  O  O   . VAL   B  1 353 ? -24.161 -0.056  -6.147   1.00 52.00  ? 654  VAL   B O   1 
ATOM   6238  C  CB  . VAL   B  1 353 ? -26.016 -2.184  -4.616   1.00 40.88  ? 654  VAL   B CB  1 
ATOM   6239  C  CG1 . VAL   B  1 353 ? -26.753 -0.851  -4.427   1.00 39.43  ? 654  VAL   B CG1 1 
ATOM   6240  C  CG2 . VAL   B  1 353 ? -26.546 -2.938  -5.812   1.00 43.88  ? 654  VAL   B CG2 1 
ATOM   6241  N  N   . ASP   B  1 354 ? -23.631 -2.076  -7.011   1.00 49.04  ? 655  ASP   B N   1 
ATOM   6242  C  CA  . ASP   B  1 354 ? -23.293 -1.508  -8.308   1.00 47.04  ? 655  ASP   B CA  1 
ATOM   6243  C  C   . ASP   B  1 354 ? -24.551 -1.395  -9.170   1.00 57.47  ? 655  ASP   B C   1 
ATOM   6244  O  O   . ASP   B  1 354 ? -25.610 -1.944  -8.846   1.00 59.52  ? 655  ASP   B O   1 
ATOM   6245  C  CB  . ASP   B  1 354 ? -22.199 -2.320  -9.019   1.00 48.47  ? 655  ASP   B CB  1 
ATOM   6246  C  CG  . ASP   B  1 354 ? -22.661 -3.703  -9.461   1.00 53.14  ? 655  ASP   B CG  1 
ATOM   6247  O  OD1 . ASP   B  1 354 ? -22.140 -4.701  -8.922   1.00 60.95  ? 655  ASP   B OD1 1 
ATOM   6248  O  OD2 . ASP   B  1 354 ? -23.534 -3.805  -10.349  1.00 54.63  ? 655  ASP   B OD2 1 
ATOM   6249  N  N   . HIS   B  1 355 ? -24.432 -0.667  -10.289  1.00 52.90  ? 656  HIS   B N   1 
ATOM   6250  C  CA  . HIS   B  1 355 ? -25.622 -0.399  -11.083  1.00 47.61  ? 656  HIS   B CA  1 
ATOM   6251  C  C   . HIS   B  1 355 ? -26.088 -1.607  -11.886  1.00 49.88  ? 656  HIS   B C   1 
ATOM   6252  O  O   . HIS   B  1 355 ? -27.275 -1.679  -12.227  1.00 47.37  ? 656  HIS   B O   1 
ATOM   6253  C  CB  . HIS   B  1 355 ? -25.395 0.792   -12.001  1.00 48.66  ? 656  HIS   B CB  1 
ATOM   6254  C  CG  . HIS   B  1 355 ? -24.130 0.723   -12.794  1.00 55.79  ? 656  HIS   B CG  1 
ATOM   6255  N  ND1 . HIS   B  1 355 ? -22.903 1.027   -12.254  1.00 54.81  ? 656  HIS   B ND1 1 
ATOM   6256  C  CD2 . HIS   B  1 355 ? -23.909 0.439   -14.098  1.00 55.64  ? 656  HIS   B CD2 1 
ATOM   6257  C  CE1 . HIS   B  1 355 ? -21.973 0.908   -13.183  1.00 57.95  ? 656  HIS   B CE1 1 
ATOM   6258  N  NE2 . HIS   B  1 355 ? -22.557 0.549   -14.312  1.00 59.54  ? 656  HIS   B NE2 1 
ATOM   6259  N  N   . HIS   B  1 356 ? -25.209 -2.581  -12.137  1.00 46.50  ? 657  HIS   B N   1 
ATOM   6260  C  CA  . HIS   B  1 356 ? -25.633 -3.796  -12.832  1.00 45.38  ? 657  HIS   B CA  1 
ATOM   6261  C  C   . HIS   B  1 356 ? -26.520 -4.665  -11.946  1.00 49.52  ? 657  HIS   B C   1 
ATOM   6262  O  O   . HIS   B  1 356 ? -27.605 -5.087  -12.363  1.00 49.09  ? 657  HIS   B O   1 
ATOM   6263  C  CB  . HIS   B  1 356 ? -24.409 -4.565  -13.319  1.00 40.38  ? 657  HIS   B CB  1 
ATOM   6264  C  CG  . HIS   B  1 356 ? -23.503 -3.736  -14.175  1.00 48.31  ? 657  HIS   B CG  1 
ATOM   6265  N  ND1 . HIS   B  1 356 ? -23.743 -3.520  -15.520  1.00 48.43  ? 657  HIS   B ND1 1 
ATOM   6266  C  CD2 . HIS   B  1 356 ? -22.384 -3.033  -13.868  1.00 48.09  ? 657  HIS   B CD2 1 
ATOM   6267  C  CE1 . HIS   B  1 356 ? -22.799 -2.732  -16.006  1.00 50.22  ? 657  HIS   B CE1 1 
ATOM   6268  N  NE2 . HIS   B  1 356 ? -21.959 -2.429  -15.028  1.00 43.07  ? 657  HIS   B NE2 1 
ATOM   6269  N  N   . SER   B  1 357 ? -26.086 -4.934  -10.713  1.00 54.50  ? 658  SER   B N   1 
ATOM   6270  C  CA  . SER   B  1 357 ? -26.903 -5.763  -9.833   1.00 54.05  ? 658  SER   B CA  1 
ATOM   6271  C  C   . SER   B  1 357 ? -28.104 -5.002  -9.269   1.00 46.84  ? 658  SER   B C   1 
ATOM   6272  O  O   . SER   B  1 357 ? -29.130 -5.624  -8.956   1.00 40.24  ? 658  SER   B O   1 
ATOM   6273  C  CB  . SER   B  1 357 ? -26.047 -6.349  -8.708   1.00 60.66  ? 658  SER   B CB  1 
ATOM   6274  O  OG  . SER   B  1 357 ? -25.326 -5.343  -8.026   1.00 61.99  ? 658  SER   B OG  1 
ATOM   6275  N  N   . ALA   B  1 358 ? -28.019 -3.670  -9.166   1.00 32.66  ? 659  ALA   B N   1 
ATOM   6276  C  CA  . ALA   B  1 358 ? -29.164 -2.888  -8.695   1.00 34.90  ? 659  ALA   B CA  1 
ATOM   6277  C  C   . ALA   B  1 358 ? -30.303 -2.912  -9.701   1.00 49.68  ? 659  ALA   B C   1 
ATOM   6278  O  O   . ALA   B  1 358 ? -31.457 -3.196  -9.348   1.00 48.35  ? 659  ALA   B O   1 
ATOM   6279  C  CB  . ALA   B  1 358 ? -28.752 -1.438  -8.441   1.00 36.55  ? 659  ALA   B CB  1 
ATOM   6280  N  N   . THR   B  1 359 ? -29.999 -2.551  -10.953  1.00 52.21  ? 660  THR   B N   1 
ATOM   6281  C  CA  . THR   B  1 359 ? -30.996 -2.589  -12.013  1.00 39.59  ? 660  THR   B CA  1 
ATOM   6282  C  C   . THR   B  1 359 ? -31.517 -4.002  -12.213  1.00 32.89  ? 660  THR   B C   1 
ATOM   6283  O  O   . THR   B  1 359 ? -32.729 -4.217  -12.305  1.00 34.03  ? 660  THR   B O   1 
ATOM   6284  C  CB  . THR   B  1 359 ? -30.388 -2.060  -13.299  1.00 40.16  ? 660  THR   B CB  1 
ATOM   6285  O  OG1 . THR   B  1 359 ? -29.189 -2.791  -13.569  1.00 49.29  ? 660  THR   B OG1 1 
ATOM   6286  C  CG2 . THR   B  1 359 ? -30.072 -0.603  -13.154  1.00 37.63  ? 660  THR   B CG2 1 
ATOM   6287  N  N   . GLU   B  1 360 ? -30.611 -4.980  -12.269  1.00 34.34  ? 661  GLU   B N   1 
ATOM   6288  C  CA  . GLU   B  1 360 ? -31.023 -6.377  -12.382  1.00 46.58  ? 661  GLU   B CA  1 
ATOM   6289  C  C   . GLU   B  1 360 ? -32.068 -6.746  -11.333  1.00 60.08  ? 661  GLU   B C   1 
ATOM   6290  O  O   . GLU   B  1 360 ? -33.065 -7.416  -11.641  1.00 64.37  ? 661  GLU   B O   1 
ATOM   6291  C  CB  . GLU   B  1 360 ? -29.803 -7.285  -12.250  1.00 55.69  ? 661  GLU   B CB  1 
ATOM   6292  C  CG  . GLU   B  1 360 ? -30.140 -8.761  -12.259  1.00 73.22  ? 661  GLU   B CG  1 
ATOM   6293  C  CD  . GLU   B  1 360 ? -28.930 -9.630  -11.972  1.00 85.63  ? 661  GLU   B CD  1 
ATOM   6294  O  OE1 . GLU   B  1 360 ? -27.820 -9.081  -11.799  1.00 86.99  ? 661  GLU   B OE1 1 
ATOM   6295  O  OE2 . GLU   B  1 360 ? -29.091 -10.866 -11.919  1.00 87.48  ? 661  GLU   B OE2 1 
ATOM   6296  N  N   . SER   B  1 361 ? -31.849 -6.321  -10.080  1.00 54.00  ? 662  SER   B N   1 
ATOM   6297  C  CA  A SER   B  1 361 ? -32.802 -6.619  -9.020   0.45 51.00  ? 662  SER   B CA  1 
ATOM   6298  C  CA  B SER   B  1 361 ? -32.803 -6.616  -9.017   0.55 50.66  ? 662  SER   B CA  1 
ATOM   6299  C  C   . SER   B  1 361 ? -34.124 -5.895  -9.244   1.00 42.94  ? 662  SER   B C   1 
ATOM   6300  O  O   . SER   B  1 361 ? -35.196 -6.477  -9.043   1.00 46.69  ? 662  SER   B O   1 
ATOM   6301  C  CB  A SER   B  1 361 ? -32.207 -6.245  -7.661   0.45 57.70  ? 662  SER   B CB  1 
ATOM   6302  C  CB  B SER   B  1 361 ? -32.217 -6.230  -7.657   0.55 57.98  ? 662  SER   B CB  1 
ATOM   6303  O  OG  A SER   B  1 361 ? -31.021 -6.980  -7.401   0.45 61.09  ? 662  SER   B OG  1 
ATOM   6304  O  OG  B SER   B  1 361 ? -32.295 -4.829  -7.436   0.55 60.39  ? 662  SER   B OG  1 
ATOM   6305  N  N   . PHE   B  1 362 ? -34.071 -4.624  -9.657   1.00 37.54  ? 663  PHE   B N   1 
ATOM   6306  C  CA  . PHE   B  1 362 ? -35.309 -3.883  -9.888   1.00 41.02  ? 663  PHE   B CA  1 
ATOM   6307  C  C   . PHE   B  1 362 ? -36.192 -4.551  -10.948  1.00 51.06  ? 663  PHE   B C   1 
ATOM   6308  O  O   . PHE   B  1 362 ? -37.427 -4.497  -10.858  1.00 58.28  ? 663  PHE   B O   1 
ATOM   6309  C  CB  . PHE   B  1 362 ? -35.026 -2.432  -10.280  1.00 31.85  ? 663  PHE   B CB  1 
ATOM   6310  C  CG  . PHE   B  1 362 ? -36.286 -1.619  -10.444  1.00 40.40  ? 663  PHE   B CG  1 
ATOM   6311  C  CD1 . PHE   B  1 362 ? -36.900 -1.032  -9.348   1.00 46.12  ? 663  PHE   B CD1 1 
ATOM   6312  C  CD2 . PHE   B  1 362 ? -36.893 -1.502  -11.685  1.00 51.42  ? 663  PHE   B CD2 1 
ATOM   6313  C  CE1 . PHE   B  1 362 ? -38.079 -0.311  -9.495   1.00 36.73  ? 663  PHE   B CE1 1 
ATOM   6314  C  CE2 . PHE   B  1 362 ? -38.060 -0.789  -11.830  1.00 50.92  ? 663  PHE   B CE2 1 
ATOM   6315  C  CZ  . PHE   B  1 362 ? -38.649 -0.188  -10.731  1.00 41.29  ? 663  PHE   B CZ  1 
ATOM   6316  N  N   . ILE   B  1 363 ? -35.596 -5.165  -11.971  1.00 48.68  ? 664  ILE   B N   1 
ATOM   6317  C  CA  . ILE   B  1 363 ? -36.418 -5.930  -12.906  1.00 51.05  ? 664  ILE   B CA  1 
ATOM   6318  C  C   . ILE   B  1 363 ? -37.127 -7.058  -12.160  1.00 52.62  ? 664  ILE   B C   1 
ATOM   6319  O  O   . ILE   B  1 363 ? -38.348 -7.212  -12.264  1.00 55.29  ? 664  ILE   B O   1 
ATOM   6320  C  CB  . ILE   B  1 363 ? -35.573 -6.444  -14.089  1.00 44.49  ? 664  ILE   B CB  1 
ATOM   6321  C  CG1 . ILE   B  1 363 ? -35.058 -5.271  -14.946  1.00 46.20  ? 664  ILE   B CG1 1 
ATOM   6322  C  CG2 . ILE   B  1 363 ? -36.367 -7.438  -14.923  1.00 35.53  ? 664  ILE   B CG2 1 
ATOM   6323  C  CD1 . ILE   B  1 363 ? -36.091 -4.659  -15.943  1.00 39.48  ? 664  ILE   B CD1 1 
ATOM   6324  N  N   . LYS   B  1 364 ? -36.382 -7.810  -11.335  1.00 54.69  ? 665  LYS   B N   1 
ATOM   6325  C  CA  . LYS   B  1 364 ? -36.985 -8.878  -10.531  1.00 54.12  ? 665  LYS   B CA  1 
ATOM   6326  C  C   . LYS   B  1 364 ? -38.087 -8.346  -9.617   1.00 49.20  ? 665  LYS   B C   1 
ATOM   6327  O  O   . LYS   B  1 364 ? -39.124 -9.004  -9.435   1.00 49.49  ? 665  LYS   B O   1 
ATOM   6328  C  CB  . LYS   B  1 364 ? -35.914 -9.602  -9.711   1.00 49.45  ? 665  LYS   B CB  1 
ATOM   6329  C  CG  . LYS   B  1 364 ? -36.452 -10.623 -8.723   1.00 65.04  ? 665  LYS   B CG  1 
ATOM   6330  C  CD  . LYS   B  1 364 ? -36.166 -12.060 -9.149   1.00 83.50  ? 665  LYS   B CD  1 
ATOM   6331  C  CE  . LYS   B  1 364 ? -37.300 -12.652 -9.992   1.00 96.14  ? 665  LYS   B CE  1 
ATOM   6332  N  NZ  . LYS   B  1 364 ? -38.541 -12.959 -9.202   1.00 95.19  ? 665  LYS   B NZ  1 
ATOM   6333  N  N   . HIS   B  1 365 ? -37.893 -7.151  -9.047   1.00 36.83  ? 666  HIS   B N   1 
ATOM   6334  C  CA  . HIS   B  1 365 ? -38.953 -6.536  -8.246   1.00 46.35  ? 666  HIS   B CA  1 
ATOM   6335  C  C   . HIS   B  1 365 ? -40.196 -6.289  -9.097   1.00 49.04  ? 666  HIS   B C   1 
ATOM   6336  O  O   . HIS   B  1 365 ? -41.305 -6.732  -8.752   1.00 48.60  ? 666  HIS   B O   1 
ATOM   6337  C  CB  . HIS   B  1 365 ? -38.441 -5.234  -7.611   1.00 41.34  ? 666  HIS   B CB  1 
ATOM   6338  C  CG  . HIS   B  1 365 ? -39.471 -4.489  -6.810   1.00 43.00  ? 666  HIS   B CG  1 
ATOM   6339  N  ND1 . HIS   B  1 365 ? -40.053 -5.009  -5.672   1.00 44.20  ? 666  HIS   B ND1 1 
ATOM   6340  C  CD2 . HIS   B  1 365 ? -39.992 -3.246  -6.963   1.00 44.04  ? 666  HIS   B CD2 1 
ATOM   6341  C  CE1 . HIS   B  1 365 ? -40.899 -4.125  -5.171   1.00 39.91  ? 666  HIS   B CE1 1 
ATOM   6342  N  NE2 . HIS   B  1 365 ? -40.883 -3.047  -5.936   1.00 42.14  ? 666  HIS   B NE2 1 
ATOM   6343  N  N   . MET   B  1 366 ? -40.019 -5.594  -10.228  1.00 42.31  ? 667  MET   B N   1 
ATOM   6344  C  CA  . MET   B  1 366 ? -41.106 -5.369  -11.173  1.00 29.43  ? 667  MET   B CA  1 
ATOM   6345  C  C   . MET   B  1 366 ? -41.865 -6.660  -11.458  1.00 34.31  ? 667  MET   B C   1 
ATOM   6346  O  O   . MET   B  1 366 ? -43.101 -6.676  -11.428  1.00 40.14  ? 667  MET   B O   1 
ATOM   6347  C  CB  . MET   B  1 366 ? -40.559 -4.779  -12.474  1.00 40.48  ? 667  MET   B CB  1 
ATOM   6348  C  CG  . MET   B  1 366 ? -40.458 -3.279  -12.519  1.00 48.60  ? 667  MET   B CG  1 
ATOM   6349  S  SD  . MET   B  1 366 ? -40.166 -2.684  -14.201  1.00 47.14  ? 667  MET   B SD  1 
ATOM   6350  C  CE  . MET   B  1 366 ? -41.831 -2.606  -14.850  1.00 43.00  ? 667  MET   B CE  1 
ATOM   6351  N  N   . GLU   B  1 367 ? -41.143 -7.744  -11.782  1.00 34.53  ? 668  GLU   B N   1 
ATOM   6352  C  CA  A GLU   B  1 367 ? -41.787 -9.035  -11.994  0.41 46.10  ? 668  GLU   B CA  1 
ATOM   6353  C  CA  B GLU   B  1 367 ? -41.803 -9.027  -12.007  0.59 45.68  ? 668  GLU   B CA  1 
ATOM   6354  C  C   . GLU   B  1 367 ? -42.751 -9.338  -10.857  1.00 56.12  ? 668  GLU   B C   1 
ATOM   6355  O  O   . GLU   B  1 367 ? -43.959 -9.513  -11.067  1.00 54.70  ? 668  GLU   B O   1 
ATOM   6356  C  CB  A GLU   B  1 367 ? -40.719 -10.128 -12.109  0.41 50.21  ? 668  GLU   B CB  1 
ATOM   6357  C  CB  B GLU   B  1 367 ? -40.786 -10.170 -12.161  0.59 50.63  ? 668  GLU   B CB  1 
ATOM   6358  C  CG  A GLU   B  1 367 ? -41.231 -11.556 -11.984  0.41 49.95  ? 668  GLU   B CG  1 
ATOM   6359  C  CG  B GLU   B  1 367 ? -39.464 -9.855  -12.862  0.59 53.99  ? 668  GLU   B CG  1 
ATOM   6360  C  CD  A GLU   B  1 367 ? -40.101 -12.577 -11.978  0.41 50.93  ? 668  GLU   B CD  1 
ATOM   6361  C  CD  B GLU   B  1 367 ? -39.514 -9.924  -14.393  0.59 49.67  ? 668  GLU   B CD  1 
ATOM   6362  O  OE1 A GLU   B  1 367 ? -39.031 -12.297 -12.561  0.41 49.72  ? 668  GLU   B OE1 1 
ATOM   6363  O  OE1 B GLU   B  1 367 ? -40.065 -8.996  -15.023  0.59 37.90  ? 668  GLU   B OE1 1 
ATOM   6364  O  OE2 A GLU   B  1 367 ? -40.280 -13.659 -11.380  0.41 53.39  ? 668  GLU   B OE2 1 
ATOM   6365  O  OE2 B GLU   B  1 367 ? -38.967 -10.897 -14.956  0.59 34.20  ? 668  GLU   B OE2 1 
ATOM   6366  N  N   . ASN   B  1 368 ? -42.209 -9.372  -9.630   1.00 58.45  ? 669  ASN   B N   1 
ATOM   6367  C  CA  . ASN   B  1 368 ? -42.988 -9.694  -8.438   1.00 55.46  ? 669  ASN   B CA  1 
ATOM   6368  C  C   . ASN   B  1 368 ? -44.203 -8.789  -8.304   1.00 50.81  ? 669  ASN   B C   1 
ATOM   6369  O  O   . ASN   B  1 368 ? -45.334 -9.269  -8.130   1.00 45.97  ? 669  ASN   B O   1 
ATOM   6370  C  CB  . ASN   B  1 368 ? -42.116 -9.563  -7.188   1.00 60.36  ? 669  ASN   B CB  1 
ATOM   6371  C  CG  . ASN   B  1 368 ? -40.928 -10.505 -7.186   1.00 66.17  ? 669  ASN   B CG  1 
ATOM   6372  O  OD1 . ASN   B  1 368 ? -40.984 -11.614 -7.735   1.00 65.84  ? 669  ASN   B OD1 1 
ATOM   6373  N  ND2 . ASN   B  1 368 ? -39.838 -10.070 -6.534   1.00 65.26  ? 669  ASN   B ND2 1 
ATOM   6374  N  N   . GLU   B  1 369 ? -43.983 -7.468  -8.355   1.00 38.62  ? 670  GLU   B N   1 
ATOM   6375  C  CA  . GLU   B  1 369 ? -45.080 -6.527  -8.146   1.00 37.97  ? 670  GLU   B CA  1 
ATOM   6376  C  C   . GLU   B  1 369 ? -46.219 -6.772  -9.139   1.00 56.89  ? 670  GLU   B C   1 
ATOM   6377  O  O   . GLU   B  1 369 ? -47.390 -6.836  -8.747   1.00 58.92  ? 670  GLU   B O   1 
ATOM   6378  C  CB  . GLU   B  1 369 ? -44.557 -5.093  -8.236   1.00 35.94  ? 670  GLU   B CB  1 
ATOM   6379  C  CG  . GLU   B  1 369 ? -43.502 -4.735  -7.190   1.00 49.75  ? 670  GLU   B CG  1 
ATOM   6380  C  CD  . GLU   B  1 369 ? -44.092 -4.219  -5.857   1.00 54.63  ? 670  GLU   B CD  1 
ATOM   6381  O  OE1 . GLU   B  1 369 ? -43.869 -3.006  -5.507   1.00 46.60  ? 670  GLU   B OE1 1 
ATOM   6382  O  OE2 . GLU   B  1 369 ? -44.761 -5.042  -5.180   1.00 44.01  ? 670  GLU   B OE2 1 
ATOM   6383  N  N   . TYR   B  1 370 ? -45.896 -6.931  -10.433  1.00 56.99  ? 671  TYR   B N   1 
ATOM   6384  C  CA  . TYR   B  1 370 ? -46.951 -7.171  -11.411  1.00 48.08  ? 671  TYR   B CA  1 
ATOM   6385  C  C   . TYR   B  1 370 ? -47.677 -8.469  -11.099  1.00 52.96  ? 671  TYR   B C   1 
ATOM   6386  O  O   . TYR   B  1 370 ? -48.912 -8.523  -11.153  1.00 66.20  ? 671  TYR   B O   1 
ATOM   6387  C  CB  . TYR   B  1 370 ? -46.385 -7.177  -12.844  1.00 49.48  ? 671  TYR   B CB  1 
ATOM   6388  C  CG  . TYR   B  1 370 ? -46.327 -5.788  -13.443  1.00 46.83  ? 671  TYR   B CG  1 
ATOM   6389  C  CD1 . TYR   B  1 370 ? -45.230 -4.976  -13.249  1.00 46.35  ? 671  TYR   B CD1 1 
ATOM   6390  C  CD2 . TYR   B  1 370 ? -47.392 -5.278  -14.160  1.00 51.75  ? 671  TYR   B CD2 1 
ATOM   6391  C  CE1 . TYR   B  1 370 ? -45.186 -3.706  -13.764  1.00 52.01  ? 671  TYR   B CE1 1 
ATOM   6392  C  CE2 . TYR   B  1 370 ? -47.359 -4.001  -14.681  1.00 45.98  ? 671  TYR   B CE2 1 
ATOM   6393  C  CZ  . TYR   B  1 370 ? -46.251 -3.216  -14.479  1.00 51.94  ? 671  TYR   B CZ  1 
ATOM   6394  O  OH  . TYR   B  1 370 ? -46.198 -1.934  -14.984  1.00 53.35  ? 671  TYR   B OH  1 
ATOM   6395  N  N   . ARG   B  1 371 ? -46.929 -9.506  -10.707  1.00 43.35  ? 672  ARG   B N   1 
ATOM   6396  C  CA  . ARG   B  1 371 ? -47.509 -10.836 -10.510  1.00 54.55  ? 672  ARG   B CA  1 
ATOM   6397  C  C   . ARG   B  1 371 ? -48.501 -10.868 -9.344   1.00 59.77  ? 672  ARG   B C   1 
ATOM   6398  O  O   . ARG   B  1 371 ? -49.530 -11.550 -9.417   1.00 58.43  ? 672  ARG   B O   1 
ATOM   6399  C  CB  . ARG   B  1 371 ? -46.376 -11.854 -10.315  1.00 61.33  ? 672  ARG   B CB  1 
ATOM   6400  C  CG  . ARG   B  1 371 ? -46.665 -13.050 -9.412   1.00 66.09  ? 672  ARG   B CG  1 
ATOM   6401  C  CD  . ARG   B  1 371 ? -45.350 -13.671 -8.910   1.00 79.67  ? 672  ARG   B CD  1 
ATOM   6402  N  NE  . ARG   B  1 371 ? -44.413 -13.911 -10.008  1.00 96.10  ? 672  ARG   B NE  1 
ATOM   6403  C  CZ  . ARG   B  1 371 ? -43.156 -14.329 -9.863   1.00 104.43 ? 672  ARG   B CZ  1 
ATOM   6404  N  NH1 . ARG   B  1 371 ? -42.658 -14.558 -8.652   1.00 107.43 ? 672  ARG   B NH1 1 
ATOM   6405  N  NH2 . ARG   B  1 371 ? -42.394 -14.514 -10.939  1.00 103.55 ? 672  ARG   B NH2 1 
ATOM   6406  N  N   . CYS   B  1 372 ? -48.235 -10.131 -8.266   1.00 58.51  ? 673  CYS   B N   1 
ATOM   6407  C  CA  . CYS   B  1 372 ? -49.112 -10.218 -7.107   1.00 69.43  ? 673  CYS   B CA  1 
ATOM   6408  C  C   . CYS   B  1 372 ? -49.866 -8.934  -6.787   1.00 75.43  ? 673  CYS   B C   1 
ATOM   6409  O  O   . CYS   B  1 372 ? -50.846 -8.992  -6.046   1.00 87.09  ? 673  CYS   B O   1 
ATOM   6410  C  CB  . CYS   B  1 372 ? -48.316 -10.640 -5.863   1.00 66.63  ? 673  CYS   B CB  1 
ATOM   6411  S  SG  . CYS   B  1 372 ? -47.516 -9.257  -5.095   1.00 62.80  ? 673  CYS   B SG  1 
ATOM   6412  N  N   . ARG   B  1 373 ? -49.441 -7.785  -7.306   1.00 71.28  ? 674  ARG   B N   1 
ATOM   6413  C  CA  . ARG   B  1 373 ? -50.096 -6.518  -7.007   1.00 62.24  ? 674  ARG   B CA  1 
ATOM   6414  C  C   . ARG   B  1 373 ? -50.798 -5.925  -8.211   1.00 62.95  ? 674  ARG   B C   1 
ATOM   6415  O  O   . ARG   B  1 373 ? -51.577 -4.984  -8.049   1.00 61.37  ? 674  ARG   B O   1 
ATOM   6416  C  CB  . ARG   B  1 373 ? -49.075 -5.500  -6.466   1.00 54.42  ? 674  ARG   B CB  1 
ATOM   6417  C  CG  . ARG   B  1 373 ? -49.661 -4.335  -5.694   1.00 45.42  ? 674  ARG   B CG  1 
ATOM   6418  C  CD  . ARG   B  1 373 ? -48.592 -3.317  -5.342   1.00 42.24  ? 674  ARG   B CD  1 
ATOM   6419  N  NE  . ARG   B  1 373 ? -49.125 -2.178  -4.596   1.00 51.67  ? 674  ARG   B NE  1 
ATOM   6420  C  CZ  . ARG   B  1 373 ? -48.457 -1.043  -4.390   1.00 56.28  ? 674  ARG   B CZ  1 
ATOM   6421  N  NH1 . ARG   B  1 373 ? -47.238 -0.890  -4.882   1.00 54.21  ? 674  ARG   B NH1 1 
ATOM   6422  N  NH2 . ARG   B  1 373 ? -49.006 -0.053  -3.692   1.00 53.43  ? 674  ARG   B NH2 1 
ATOM   6423  N  N   . GLY   B  1 374 ? -50.538 -6.445  -9.410   1.00 70.23  ? 675  GLY   B N   1 
ATOM   6424  C  CA  . GLY   B  1 374 ? -51.127 -5.913  -10.620  1.00 65.25  ? 675  GLY   B CA  1 
ATOM   6425  C  C   . GLY   B  1 374 ? -50.423 -4.708  -11.201  1.00 54.98  ? 675  GLY   B C   1 
ATOM   6426  O  O   . GLY   B  1 374 ? -51.036 -3.976  -11.989  1.00 53.20  ? 675  GLY   B O   1 
ATOM   6427  N  N   . GLY   B  1 375 ? -49.172 -4.464  -10.834  1.00 38.34  ? 676  GLY   B N   1 
ATOM   6428  C  CA  . GLY   B  1 375 ? -48.454 -3.332  -11.393  1.00 41.31  ? 676  GLY   B CA  1 
ATOM   6429  C  C   . GLY   B  1 375 ? -47.384 -2.820  -10.455  1.00 49.94  ? 676  GLY   B C   1 
ATOM   6430  O  O   . GLY   B  1 375 ? -47.248 -3.260  -9.316   1.00 56.69  ? 676  GLY   B O   1 
ATOM   6431  N  N   . CYS   B  1 376 ? -46.613 -1.848  -10.967  1.00 52.46  ? 677  CYS   B N   1 
ATOM   6432  C  CA  . CYS   B  1 376 ? -45.529 -1.228  -10.215  1.00 41.80  ? 677  CYS   B CA  1 
ATOM   6433  C  C   . CYS   B  1 376 ? -45.133 0.120   -10.799  1.00 43.90  ? 677  CYS   B C   1 
ATOM   6434  O  O   . CYS   B  1 376 ? -44.480 0.158   -11.848  1.00 51.33  ? 677  CYS   B O   1 
ATOM   6435  C  CB  . CYS   B  1 376 ? -44.305 -2.143  -10.191  1.00 42.30  ? 677  CYS   B CB  1 
ATOM   6436  S  SG  . CYS   B  1 376 ? -42.857 -1.371  -9.447   1.00 47.47  ? 677  CYS   B SG  1 
ATOM   6437  N  N   . PRO   B  1 377 ? -45.452 1.235   -10.136  1.00 44.71  ? 678  PRO   B N   1 
ATOM   6438  C  CA  . PRO   B  1 377 ? -45.085 2.554   -10.681  1.00 32.87  ? 678  PRO   B CA  1 
ATOM   6439  C  C   . PRO   B  1 377 ? -43.573 2.742   -10.747  1.00 44.87  ? 678  PRO   B C   1 
ATOM   6440  O  O   . PRO   B  1 377 ? -42.868 2.575   -9.751   1.00 53.79  ? 678  PRO   B O   1 
ATOM   6441  C  CB  . PRO   B  1 377 ? -45.734 3.535   -9.699   1.00 44.83  ? 678  PRO   B CB  1 
ATOM   6442  C  CG  . PRO   B  1 377 ? -45.782 2.787   -8.388   1.00 47.87  ? 678  PRO   B CG  1 
ATOM   6443  C  CD  . PRO   B  1 377 ? -46.031 1.337   -8.780   1.00 56.58  ? 678  PRO   B CD  1 
ATOM   6444  N  N   . ALA   B  1 378 ? -43.079 3.112   -11.933  1.00 47.01  ? 679  ALA   B N   1 
ATOM   6445  C  CA  . ALA   B  1 378 ? -41.649 3.239   -12.176  1.00 43.73  ? 679  ALA   B CA  1 
ATOM   6446  C  C   . ALA   B  1 378 ? -41.377 4.433   -13.072  1.00 41.69  ? 679  ALA   B C   1 
ATOM   6447  O  O   . ALA   B  1 378 ? -42.097 4.651   -14.046  1.00 54.33  ? 679  ALA   B O   1 
ATOM   6448  C  CB  . ALA   B  1 378 ? -41.087 1.973   -12.820  1.00 41.59  ? 679  ALA   B CB  1 
ATOM   6449  N  N   . ASP   B  1 379 ? -40.325 5.194   -12.754  1.00 39.56  ? 680  ASP   B N   1 
ATOM   6450  C  CA  . ASP   B  1 379 ? -39.975 6.416   -13.487  1.00 39.36  ? 680  ASP   B CA  1 
ATOM   6451  C  C   . ASP   B  1 379 ? -38.684 6.147   -14.268  1.00 50.14  ? 680  ASP   B C   1 
ATOM   6452  O  O   . ASP   B  1 379 ? -37.585 6.174   -13.700  1.00 50.35  ? 680  ASP   B O   1 
ATOM   6453  C  CB  . ASP   B  1 379 ? -39.850 7.593   -12.522  1.00 33.78  ? 680  ASP   B CB  1 
ATOM   6454  C  CG  . ASP   B  1 379 ? -39.580 8.928   -13.216  1.00 40.04  ? 680  ASP   B CG  1 
ATOM   6455  O  OD1 . ASP   B  1 379 ? -40.176 9.950   -12.815  1.00 48.32  ? 680  ASP   B OD1 1 
ATOM   6456  O  OD2 . ASP   B  1 379 ? -38.767 8.975   -14.156  1.00 52.87  ? 680  ASP   B OD2 1 
ATOM   6457  N  N   . TRP   B  1 380 ? -38.834 5.904   -15.582  1.00 48.71  ? 681  TRP   B N   1 
ATOM   6458  C  CA  . TRP   B  1 380 ? -37.726 5.439   -16.416  1.00 41.46  ? 681  TRP   B CA  1 
ATOM   6459  C  C   . TRP   B  1 380 ? -36.551 6.407   -16.385  1.00 37.69  ? 681  TRP   B C   1 
ATOM   6460  O  O   . TRP   B  1 380 ? -35.391 5.985   -16.372  1.00 26.54  ? 681  TRP   B O   1 
ATOM   6461  C  CB  . TRP   B  1 380 ? -38.208 5.249   -17.856  1.00 41.89  ? 681  TRP   B CB  1 
ATOM   6462  C  CG  . TRP   B  1 380 ? -37.273 4.444   -18.715  1.00 31.09  ? 681  TRP   B CG  1 
ATOM   6463  C  CD1 . TRP   B  1 380 ? -37.342 3.100   -18.948  1.00 31.68  ? 681  TRP   B CD1 1 
ATOM   6464  C  CD2 . TRP   B  1 380 ? -36.122 4.917   -19.438  1.00 34.45  ? 681  TRP   B CD2 1 
ATOM   6465  N  NE1 . TRP   B  1 380 ? -36.315 2.710   -19.773  1.00 42.79  ? 681  TRP   B NE1 1 
ATOM   6466  C  CE2 . TRP   B  1 380 ? -35.563 3.806   -20.106  1.00 44.39  ? 681  TRP   B CE2 1 
ATOM   6467  C  CE3 . TRP   B  1 380 ? -35.534 6.166   -19.613  1.00 39.79  ? 681  TRP   B CE3 1 
ATOM   6468  C  CZ2 . TRP   B  1 380 ? -34.426 3.910   -20.931  1.00 42.32  ? 681  TRP   B CZ2 1 
ATOM   6469  C  CZ3 . TRP   B  1 380 ? -34.397 6.266   -20.430  1.00 43.66  ? 681  TRP   B CZ3 1 
ATOM   6470  C  CH2 . TRP   B  1 380 ? -33.858 5.146   -21.075  1.00 35.19  ? 681  TRP   B CH2 1 
ATOM   6471  N  N   . VAL   B  1 381 ? -36.839 7.711   -16.401  1.00 41.65  ? 682  VAL   B N   1 
ATOM   6472  C  CA  . VAL   B  1 381 ? -35.812 8.747   -16.431  1.00 38.65  ? 682  VAL   B CA  1 
ATOM   6473  C  C   . VAL   B  1 381 ? -34.870 8.645   -15.237  1.00 51.55  ? 682  VAL   B C   1 
ATOM   6474  O  O   . VAL   B  1 381 ? -33.682 8.981   -15.353  1.00 55.68  ? 682  VAL   B O   1 
ATOM   6475  C  CB  . VAL   B  1 381 ? -36.497 10.122  -16.474  1.00 36.67  ? 682  VAL   B CB  1 
ATOM   6476  C  CG1 . VAL   B  1 381 ? -35.548 11.201  -15.979  1.00 36.96  ? 682  VAL   B CG1 1 
ATOM   6477  C  CG2 . VAL   B  1 381 ? -37.072 10.415  -17.874  1.00 28.71  ? 682  VAL   B CG2 1 
ATOM   6478  N  N   . TRP   B  1 382 ? -35.382 8.181   -14.078  1.00 41.86  ? 683  TRP   B N   1 
ATOM   6479  C  CA  . TRP   B  1 382 ? -34.669 8.136   -12.801  1.00 37.64  ? 683  TRP   B CA  1 
ATOM   6480  C  C   . TRP   B  1 382 ? -34.182 6.745   -12.416  1.00 41.17  ? 683  TRP   B C   1 
ATOM   6481  O  O   . TRP   B  1 382 ? -33.226 6.643   -11.643  1.00 38.98  ? 683  TRP   B O   1 
ATOM   6482  C  CB  . TRP   B  1 382 ? -35.554 8.650   -11.662  1.00 34.94  ? 683  TRP   B CB  1 
ATOM   6483  C  CG  . TRP   B  1 382 ? -35.658 10.139  -11.566  1.00 45.84  ? 683  TRP   B CG  1 
ATOM   6484  C  CD1 . TRP   B  1 382 ? -36.211 10.990  -12.486  1.00 48.21  ? 683  TRP   B CD1 1 
ATOM   6485  C  CD2 . TRP   B  1 382 ? -35.228 10.963  -10.469  1.00 53.93  ? 683  TRP   B CD2 1 
ATOM   6486  N  NE1 . TRP   B  1 382 ? -36.128 12.297  -12.040  1.00 51.76  ? 683  TRP   B NE1 1 
ATOM   6487  C  CE2 . TRP   B  1 382 ? -35.537 12.303  -10.800  1.00 57.94  ? 683  TRP   B CE2 1 
ATOM   6488  C  CE3 . TRP   B  1 382 ? -34.607 10.701  -9.246   1.00 46.45  ? 683  TRP   B CE3 1 
ATOM   6489  C  CZ2 . TRP   B  1 382 ? -35.232 13.370  -9.953   1.00 50.69  ? 683  TRP   B CZ2 1 
ATOM   6490  C  CZ3 . TRP   B  1 382 ? -34.312 11.769  -8.403   1.00 42.29  ? 683  TRP   B CZ3 1 
ATOM   6491  C  CH2 . TRP   B  1 382 ? -34.617 13.081  -8.766   1.00 45.66  ? 683  TRP   B CH2 1 
ATOM   6492  N  N   . ILE   B  1 383 ? -34.816 5.681   -12.918  1.00 42.16  ? 684  ILE   B N   1 
ATOM   6493  C  CA  . ILE   B  1 383 ? -34.335 4.322   -12.669  1.00 35.62  ? 684  ILE   B CA  1 
ATOM   6494  C  C   . ILE   B  1 383 ? -33.063 4.032   -13.460  1.00 44.34  ? 684  ILE   B C   1 
ATOM   6495  O  O   . ILE   B  1 383 ? -32.176 3.321   -12.985  1.00 46.65  ? 684  ILE   B O   1 
ATOM   6496  C  CB  . ILE   B  1 383 ? -35.432 3.302   -13.017  1.00 32.64  ? 684  ILE   B CB  1 
ATOM   6497  C  CG1 . ILE   B  1 383 ? -36.704 3.540   -12.210  1.00 28.68  ? 684  ILE   B CG1 1 
ATOM   6498  C  CG2 . ILE   B  1 383 ? -34.932 1.897   -12.790  1.00 36.74  ? 684  ILE   B CG2 1 
ATOM   6499  C  CD1 . ILE   B  1 383 ? -36.623 2.994   -10.821  1.00 32.02  ? 684  ILE   B CD1 1 
ATOM   6500  N  N   . VAL   B  1 384 ? -32.964 4.537   -14.688  1.00 45.80  ? 685  VAL   B N   1 
ATOM   6501  C  CA  . VAL   B  1 384 ? -31.846 4.226   -15.579  1.00 37.29  ? 685  VAL   B CA  1 
ATOM   6502  C  C   . VAL   B  1 384 ? -30.588 4.912   -15.078  1.00 40.53  ? 685  VAL   B C   1 
ATOM   6503  O  O   . VAL   B  1 384 ? -30.535 6.149   -15.077  1.00 44.03  ? 685  VAL   B O   1 
ATOM   6504  C  CB  . VAL   B  1 384 ? -32.136 4.659   -17.027  1.00 35.07  ? 685  VAL   B CB  1 
ATOM   6505  C  CG1 . VAL   B  1 384 ? -30.914 4.413   -17.915  1.00 25.97  ? 685  VAL   B CG1 1 
ATOM   6506  C  CG2 . VAL   B  1 384 ? -33.320 3.919   -17.568  1.00 34.68  ? 685  VAL   B CG2 1 
ATOM   6507  N  N   . PRO   B  1 385 ? -29.547 4.167   -14.698  1.00 39.74  ? 686  PRO   B N   1 
ATOM   6508  C  CA  . PRO   B  1 385 ? -28.386 4.800   -14.073  1.00 43.13  ? 686  PRO   B CA  1 
ATOM   6509  C  C   . PRO   B  1 385 ? -27.709 5.772   -15.029  1.00 47.51  ? 686  PRO   B C   1 
ATOM   6510  O  O   . PRO   B  1 385 ? -27.816 5.628   -16.257  1.00 52.35  ? 686  PRO   B O   1 
ATOM   6511  C  CB  . PRO   B  1 385 ? -27.465 3.612   -13.743  1.00 40.05  ? 686  PRO   B CB  1 
ATOM   6512  C  CG  . PRO   B  1 385 ? -28.319 2.400   -13.889  1.00 36.51  ? 686  PRO   B CG  1 
ATOM   6513  C  CD  . PRO   B  1 385 ? -29.380 2.718   -14.862  1.00 34.69  ? 686  PRO   B CD  1 
ATOM   6514  N  N   . PRO   B  1 386 ? -27.013 6.780   -14.506  1.00 44.07  ? 687  PRO   B N   1 
ATOM   6515  C  CA  . PRO   B  1 386 ? -26.447 7.828   -15.364  1.00 41.92  ? 687  PRO   B CA  1 
ATOM   6516  C  C   . PRO   B  1 386 ? -25.139 7.472   -16.052  1.00 53.06  ? 687  PRO   B C   1 
ATOM   6517  O  O   . PRO   B  1 386 ? -24.499 8.371   -16.604  1.00 56.23  ? 687  PRO   B O   1 
ATOM   6518  C  CB  . PRO   B  1 386 ? -26.231 8.976   -14.369  1.00 39.04  ? 687  PRO   B CB  1 
ATOM   6519  C  CG  . PRO   B  1 386 ? -25.929 8.287   -13.122  1.00 28.45  ? 687  PRO   B CG  1 
ATOM   6520  C  CD  . PRO   B  1 386 ? -26.918 7.148   -13.083  1.00 30.39  ? 687  PRO   B CD  1 
ATOM   6521  N  N   . MET   B  1 387 ? -24.695 6.218   -16.018  1.00 56.75  ? 688  MET   B N   1 
ATOM   6522  C  CA  . MET   B  1 387 ? -23.652 5.759   -16.927  1.00 56.58  ? 688  MET   B CA  1 
ATOM   6523  C  C   . MET   B  1 387 ? -24.031 4.369   -17.419  1.00 58.99  ? 688  MET   B C   1 
ATOM   6524  O  O   . MET   B  1 387 ? -24.687 3.597   -16.708  1.00 61.61  ? 688  MET   B O   1 
ATOM   6525  C  CB  . MET   B  1 387 ? -22.252 5.747   -16.281  1.00 49.71  ? 688  MET   B CB  1 
ATOM   6526  C  CG  . MET   B  1 387 ? -22.000 4.600   -15.297  1.00 55.15  ? 688  MET   B CG  1 
ATOM   6527  S  SD  . MET   B  1 387 ? -20.378 4.625   -14.477  1.00 59.72  ? 688  MET   B SD  1 
ATOM   6528  C  CE  . MET   B  1 387 ? -19.415 3.525   -15.516  1.00 63.06  ? 688  MET   B CE  1 
ATOM   6529  N  N   . SER   B  1 388 ? -23.660 4.083   -18.666  1.00 49.85  ? 689  SER   B N   1 
ATOM   6530  C  CA  . SER   B  1 388 ? -23.799 2.746   -19.237  1.00 39.06  ? 689  SER   B CA  1 
ATOM   6531  C  C   . SER   B  1 388 ? -25.251 2.283   -19.297  1.00 38.83  ? 689  SER   B C   1 
ATOM   6532  O  O   . SER   B  1 388 ? -25.537 1.084   -19.207  1.00 42.69  ? 689  SER   B O   1 
ATOM   6533  C  CB  . SER   B  1 388 ? -22.954 1.738   -18.458  1.00 40.96  ? 689  SER   B CB  1 
ATOM   6534  O  OG  . SER   B  1 388 ? -21.620 2.178   -18.418  1.00 48.90  ? 689  SER   B OG  1 
ATOM   6535  N  N   . GLY   B  1 389 ? -26.178 3.220   -19.440  1.00 30.11  ? 690  GLY   B N   1 
ATOM   6536  C  CA  . GLY   B  1 389 ? -27.581 2.861   -19.406  1.00 36.72  ? 690  GLY   B CA  1 
ATOM   6537  C  C   . GLY   B  1 389 ? -27.943 1.647   -20.239  1.00 49.24  ? 690  GLY   B C   1 
ATOM   6538  O  O   . GLY   B  1 389 ? -28.442 0.652   -19.700  1.00 49.78  ? 690  GLY   B O   1 
ATOM   6539  N  N   . SER   B  1 390 ? -27.640 1.699   -21.544  1.00 47.10  ? 691  SER   B N   1 
ATOM   6540  C  CA  . SER   B  1 390 ? -28.103 0.668   -22.464  1.00 47.81  ? 691  SER   B CA  1 
ATOM   6541  C  C   . SER   B  1 390 ? -27.586 -0.726  -22.104  1.00 44.65  ? 691  SER   B C   1 
ATOM   6542  O  O   . SER   B  1 390 ? -28.222 -1.718  -22.479  1.00 54.56  ? 691  SER   B O   1 
ATOM   6543  C  CB  . SER   B  1 390 ? -27.729 1.052   -23.908  1.00 50.32  ? 691  SER   B CB  1 
ATOM   6544  O  OG  . SER   B  1 390 ? -26.893 0.095   -24.546  1.00 54.03  ? 691  SER   B OG  1 
ATOM   6545  N  N   . ILE   B  1 391 ? -26.473 -0.837  -21.379  1.00 42.00  ? 692  ILE   B N   1 
ATOM   6546  C  CA  . ILE   B  1 391 ? -25.977 -2.164  -21.011  1.00 48.60  ? 692  ILE   B CA  1 
ATOM   6547  C  C   . ILE   B  1 391 ? -26.528 -2.612  -19.659  1.00 50.53  ? 692  ILE   B C   1 
ATOM   6548  O  O   . ILE   B  1 391 ? -26.056 -3.606  -19.109  1.00 50.81  ? 692  ILE   B O   1 
ATOM   6549  C  CB  . ILE   B  1 391 ? -24.431 -2.247  -20.987  1.00 50.65  ? 692  ILE   B CB  1 
ATOM   6550  C  CG1 . ILE   B  1 391 ? -23.850 -1.484  -19.803  1.00 55.35  ? 692  ILE   B CG1 1 
ATOM   6551  C  CG2 . ILE   B  1 391 ? -23.827 -1.765  -22.283  1.00 50.94  ? 692  ILE   B CG2 1 
ATOM   6552  C  CD1 . ILE   B  1 391 ? -22.356 -1.593  -19.708  1.00 62.98  ? 692  ILE   B CD1 1 
ATOM   6553  N  N   . THR   B  1 392 ? -27.514 -1.892  -19.095  1.00 48.36  ? 693  THR   B N   1 
ATOM   6554  C  CA  . THR   B  1 392 ? -28.260 -2.388  -17.940  1.00 53.52  ? 693  THR   B CA  1 
ATOM   6555  C  C   . THR   B  1 392 ? -29.679 -2.755  -18.354  1.00 51.18  ? 693  THR   B C   1 
ATOM   6556  O  O   . THR   B  1 392 ? -30.206 -2.225  -19.337  1.00 41.31  ? 693  THR   B O   1 
ATOM   6557  C  CB  . THR   B  1 392 ? -28.320 -1.372  -16.775  1.00 56.12  ? 693  THR   B CB  1 
ATOM   6558  O  OG1 . THR   B  1 392 ? -29.445 -0.492  -16.954  1.00 52.03  ? 693  THR   B OG1 1 
ATOM   6559  C  CG2 . THR   B  1 392 ? -27.047 -0.555  -16.650  1.00 57.21  ? 693  THR   B CG2 1 
ATOM   6560  N  N   . PRO   B  1 393 ? -30.329 -3.680  -17.640  1.00 39.11  ? 694  PRO   B N   1 
ATOM   6561  C  CA  . PRO   B  1 393 ? -31.621 -4.188  -18.142  1.00 46.62  ? 694  PRO   B CA  1 
ATOM   6562  C  C   . PRO   B  1 393 ? -32.721 -3.153  -18.129  1.00 49.65  ? 694  PRO   B C   1 
ATOM   6563  O  O   . PRO   B  1 393 ? -33.610 -3.206  -18.983  1.00 52.59  ? 694  PRO   B O   1 
ATOM   6564  C  CB  . PRO   B  1 393 ? -31.948 -5.355  -17.193  1.00 42.19  ? 694  PRO   B CB  1 
ATOM   6565  C  CG  . PRO   B  1 393 ? -31.165 -5.043  -15.917  1.00 49.51  ? 694  PRO   B CG  1 
ATOM   6566  C  CD  . PRO   B  1 393 ? -29.904 -4.336  -16.385  1.00 45.37  ? 694  PRO   B CD  1 
ATOM   6567  N  N   . VAL   B  1 394 ? -32.699 -2.212  -17.187  1.00 47.13  ? 695  VAL   B N   1 
ATOM   6568  C  CA  . VAL   B  1 394 ? -33.825 -1.300  -17.079  1.00 44.73  ? 695  VAL   B CA  1 
ATOM   6569  C  C   . VAL   B  1 394 ? -33.928 -0.409  -18.302  1.00 41.62  ? 695  VAL   B C   1 
ATOM   6570  O  O   . VAL   B  1 394 ? -35.029 0.065   -18.621  1.00 35.05  ? 695  VAL   B O   1 
ATOM   6571  C  CB  . VAL   B  1 394 ? -33.737 -0.456  -15.791  1.00 39.54  ? 695  VAL   B CB  1 
ATOM   6572  C  CG1 . VAL   B  1 394 ? -34.092 -1.289  -14.599  1.00 36.73  ? 695  VAL   B CG1 1 
ATOM   6573  C  CG2 . VAL   B  1 394 ? -32.359 0.079   -15.633  1.00 39.64  ? 695  VAL   B CG2 1 
ATOM   6574  N  N   . PHE   B  1 395 ? -32.810 -0.181  -19.003  1.00 32.99  ? 696  PHE   B N   1 
ATOM   6575  C  CA  . PHE   B  1 395 ? -32.853 0.642   -20.208  1.00 52.45  ? 696  PHE   B CA  1 
ATOM   6576  C  C   . PHE   B  1 395 ? -33.841 0.085   -21.228  1.00 49.08  ? 696  PHE   B C   1 
ATOM   6577  O  O   . PHE   B  1 395 ? -34.607 0.843   -21.831  1.00 33.78  ? 696  PHE   B O   1 
ATOM   6578  C  CB  . PHE   B  1 395 ? -31.463 0.749   -20.833  1.00 52.19  ? 696  PHE   B CB  1 
ATOM   6579  C  CG  . PHE   B  1 395 ? -31.425 1.571   -22.092  1.00 45.50  ? 696  PHE   B CG  1 
ATOM   6580  C  CD1 . PHE   B  1 395 ? -30.941 2.863   -22.061  1.00 49.58  ? 696  PHE   B CD1 1 
ATOM   6581  C  CD2 . PHE   B  1 395 ? -31.840 1.046   -23.309  1.00 51.66  ? 696  PHE   B CD2 1 
ATOM   6582  C  CE1 . PHE   B  1 395 ? -30.870 3.620   -23.215  1.00 46.73  ? 696  PHE   B CE1 1 
ATOM   6583  C  CE2 . PHE   B  1 395 ? -31.800 1.812   -24.468  1.00 48.71  ? 696  PHE   B CE2 1 
ATOM   6584  C  CZ  . PHE   B  1 395 ? -31.310 3.099   -24.420  1.00 43.68  ? 696  PHE   B CZ  1 
ATOM   6585  N  N   . HIS   B  1 396 ? -33.830 -1.229  -21.441  1.00 44.83  ? 697  HIS   B N   1 
ATOM   6586  C  CA  . HIS   B  1 396 ? -34.713 -1.869  -22.397  1.00 44.11  ? 697  HIS   B CA  1 
ATOM   6587  C  C   . HIS   B  1 396 ? -36.044 -2.280  -21.797  1.00 45.92  ? 697  HIS   B C   1 
ATOM   6588  O  O   . HIS   B  1 396 ? -36.757 -3.074  -22.414  1.00 58.24  ? 697  HIS   B O   1 
ATOM   6589  C  CB  . HIS   B  1 396 ? -34.019 -3.089  -22.996  1.00 45.00  ? 697  HIS   B CB  1 
ATOM   6590  C  CG  . HIS   B  1 396 ? -32.599 -2.830  -23.354  1.00 53.09  ? 697  HIS   B CG  1 
ATOM   6591  N  ND1 . HIS   B  1 396 ? -32.235 -2.154  -24.497  1.00 55.78  ? 697  HIS   B ND1 1 
ATOM   6592  C  CD2 . HIS   B  1 396 ? -31.450 -3.110  -22.698  1.00 54.24  ? 697  HIS   B CD2 1 
ATOM   6593  C  CE1 . HIS   B  1 396 ? -30.918 -2.050  -24.543  1.00 57.46  ? 697  HIS   B CE1 1 
ATOM   6594  N  NE2 . HIS   B  1 396 ? -30.418 -2.619  -23.460  1.00 59.12  ? 697  HIS   B NE2 1 
ATOM   6595  N  N   . GLN   B  1 397 ? -36.404 -1.767  -20.624  1.00 45.35  ? 698  GLN   B N   1 
ATOM   6596  C  CA  . GLN   B  1 397 ? -37.674 -2.105  -19.989  1.00 48.04  ? 698  GLN   B CA  1 
ATOM   6597  C  C   . GLN   B  1 397 ? -38.616 -0.902  -19.996  1.00 50.76  ? 698  GLN   B C   1 
ATOM   6598  O  O   . GLN   B  1 397 ? -38.317 0.137   -19.388  1.00 50.04  ? 698  GLN   B O   1 
ATOM   6599  C  CB  . GLN   B  1 397 ? -37.463 -2.602  -18.561  1.00 45.00  ? 698  GLN   B CB  1 
ATOM   6600  C  CG  . GLN   B  1 397 ? -38.760 -2.848  -17.805  1.00 34.45  ? 698  GLN   B CG  1 
ATOM   6601  C  CD  . GLN   B  1 397 ? -39.383 -4.196  -18.118  1.00 46.10  ? 698  GLN   B CD  1 
ATOM   6602  O  OE1 . GLN   B  1 397 ? -38.709 -5.233  -18.092  1.00 41.16  ? 698  GLN   B OE1 1 
ATOM   6603  N  NE2 . GLN   B  1 397 ? -40.684 -4.191  -18.402  1.00 53.17  ? 698  GLN   B NE2 1 
ATOM   6604  N  N   . GLU   B  1 398 ? -39.759 -1.060  -20.669  1.00 43.81  ? 699  GLU   B N   1 
ATOM   6605  C  CA  . GLU   B  1 398 ? -40.835 -0.081  -20.594  1.00 47.64  ? 699  GLU   B CA  1 
ATOM   6606  C  C   . GLU   B  1 398 ? -41.364 0.021   -19.167  1.00 52.27  ? 699  GLU   B C   1 
ATOM   6607  O  O   . GLU   B  1 398 ? -41.458 -0.979  -18.445  1.00 52.52  ? 699  GLU   B O   1 
ATOM   6608  C  CB  . GLU   B  1 398 ? -41.980 -0.468  -21.541  1.00 46.87  ? 699  GLU   B CB  1 
ATOM   6609  C  CG  . GLU   B  1 398 ? -41.594 -0.552  -23.003  1.00 57.43  ? 699  GLU   B CG  1 
ATOM   6610  C  CD  . GLU   B  1 398 ? -42.790 -0.737  -23.936  1.00 68.48  ? 699  GLU   B CD  1 
ATOM   6611  O  OE1 . GLU   B  1 398 ? -42.773 -0.128  -25.027  1.00 63.07  ? 699  GLU   B OE1 1 
ATOM   6612  O  OE2 . GLU   B  1 398 ? -43.738 -1.484  -23.588  1.00 74.75  ? 699  GLU   B OE2 1 
ATOM   6613  N  N   . MET   B  1 399 ? -41.746 1.234   -18.772  1.00 44.65  ? 700  MET   B N   1 
ATOM   6614  C  CA  . MET   B  1 399 ? -42.267 1.465   -17.436  1.00 49.52  ? 700  MET   B CA  1 
ATOM   6615  C  C   . MET   B  1 399 ? -43.469 2.395   -17.504  1.00 58.72  ? 700  MET   B C   1 
ATOM   6616  O  O   . MET   B  1 399 ? -43.499 3.328   -18.313  1.00 71.66  ? 700  MET   B O   1 
ATOM   6617  C  CB  . MET   B  1 399 ? -41.183 2.055   -16.518  1.00 55.26  ? 700  MET   B CB  1 
ATOM   6618  C  CG  . MET   B  1 399 ? -40.048 1.076   -16.163  1.00 49.21  ? 700  MET   B CG  1 
ATOM   6619  S  SD  . MET   B  1 399 ? -38.559 1.918   -15.596  1.00 44.94  ? 700  MET   B SD  1 
ATOM   6620  C  CE  . MET   B  1 399 ? -37.319 0.619   -15.647  1.00 34.76  ? 700  MET   B CE  1 
ATOM   6621  N  N   . LEU   B  1 400 ? -44.464 2.121   -16.663  1.00 45.17  ? 701  LEU   B N   1 
ATOM   6622  C  CA  . LEU   B  1 400 ? -45.606 3.002   -16.466  1.00 37.81  ? 701  LEU   B CA  1 
ATOM   6623  C  C   . LEU   B  1 400 ? -45.387 3.820   -15.208  1.00 49.68  ? 701  LEU   B C   1 
ATOM   6624  O  O   . LEU   B  1 400 ? -44.966 3.281   -14.181  1.00 54.97  ? 701  LEU   B O   1 
ATOM   6625  C  CB  . LEU   B  1 400 ? -46.905 2.214   -16.304  1.00 32.80  ? 701  LEU   B CB  1 
ATOM   6626  C  CG  . LEU   B  1 400 ? -47.433 1.440   -17.484  1.00 46.62  ? 701  LEU   B CG  1 
ATOM   6627  C  CD1 . LEU   B  1 400 ? -48.780 0.902   -17.109  1.00 46.36  ? 701  LEU   B CD1 1 
ATOM   6628  C  CD2 . LEU   B  1 400 ? -47.499 2.379   -18.689  1.00 43.97  ? 701  LEU   B CD2 1 
ATOM   6629  N  N   . ASN   B  1 401 ? -45.686 5.113   -15.273  1.00 47.83  ? 702  ASN   B N   1 
ATOM   6630  C  CA  . ASN   B  1 401 ? -45.548 5.972   -14.105  1.00 49.85  ? 702  ASN   B CA  1 
ATOM   6631  C  C   . ASN   B  1 401 ? -46.906 6.531   -13.706  1.00 60.28  ? 702  ASN   B C   1 
ATOM   6632  O  O   . ASN   B  1 401 ? -47.626 7.092   -14.543  1.00 54.19  ? 702  ASN   B O   1 
ATOM   6633  C  CB  . ASN   B  1 401 ? -44.553 7.114   -14.337  1.00 46.31  ? 702  ASN   B CB  1 
ATOM   6634  C  CG  . ASN   B  1 401 ? -43.977 7.621   -13.038  1.00 34.94  ? 702  ASN   B CG  1 
ATOM   6635  O  OD1 . ASN   B  1 401 ? -44.227 7.037   -12.011  1.00 43.01  ? 702  ASN   B OD1 1 
ATOM   6636  N  ND2 . ASN   B  1 401 ? -43.203 8.689   -13.077  1.00 34.57  ? 702  ASN   B ND2 1 
ATOM   6637  N  N   . TYR   B  1 402 ? -47.243 6.372   -12.424  1.00 55.14  ? 703  TYR   B N   1 
ATOM   6638  C  CA  . TYR   B  1 402 ? -48.474 6.879   -11.834  1.00 45.02  ? 703  TYR   B CA  1 
ATOM   6639  C  C   . TYR   B  1 402 ? -48.257 6.990   -10.332  1.00 51.30  ? 703  TYR   B C   1 
ATOM   6640  O  O   . TYR   B  1 402 ? -47.317 6.419   -9.777   1.00 34.54  ? 703  TYR   B O   1 
ATOM   6641  C  CB  . TYR   B  1 402 ? -49.674 5.989   -12.159  1.00 38.17  ? 703  TYR   B CB  1 
ATOM   6642  C  CG  . TYR   B  1 402 ? -49.413 4.507   -11.976  1.00 45.72  ? 703  TYR   B CG  1 
ATOM   6643  C  CD1 . TYR   B  1 402 ? -49.775 3.856   -10.806  1.00 51.84  ? 703  TYR   B CD1 1 
ATOM   6644  C  CD2 . TYR   B  1 402 ? -48.797 3.764   -12.970  1.00 43.86  ? 703  TYR   B CD2 1 
ATOM   6645  C  CE1 . TYR   B  1 402 ? -49.543 2.507   -10.632  1.00 46.95  ? 703  TYR   B CE1 1 
ATOM   6646  C  CE2 . TYR   B  1 402 ? -48.563 2.412   -12.807  1.00 48.18  ? 703  TYR   B CE2 1 
ATOM   6647  C  CZ  . TYR   B  1 402 ? -48.938 1.789   -11.637  1.00 49.65  ? 703  TYR   B CZ  1 
ATOM   6648  O  OH  . TYR   B  1 402 ? -48.702 0.443   -11.477  1.00 49.39  ? 703  TYR   B OH  1 
ATOM   6649  N  N   . ARG   B  1 403 ? -49.139 7.738   -9.688   1.00 55.00  ? 704  ARG   B N   1 
ATOM   6650  C  CA  . ARG   B  1 403 ? -48.901 8.252   -8.346   1.00 46.71  ? 704  ARG   B CA  1 
ATOM   6651  C  C   . ARG   B  1 403 ? -49.846 7.576   -7.357   1.00 60.98  ? 704  ARG   B C   1 
ATOM   6652  O  O   . ARG   B  1 403 ? -51.047 7.873   -7.326   1.00 64.50  ? 704  ARG   B O   1 
ATOM   6653  C  CB  . ARG   B  1 403 ? -49.073 9.772   -8.325   1.00 40.74  ? 704  ARG   B CB  1 
ATOM   6654  C  CG  . ARG   B  1 403 ? -47.933 10.539  -8.993   1.00 44.37  ? 704  ARG   B CG  1 
ATOM   6655  C  CD  . ARG   B  1 403 ? -47.385 11.610  -8.067   1.00 58.01  ? 704  ARG   B CD  1 
ATOM   6656  N  NE  . ARG   B  1 403 ? -47.968 12.931  -8.309   1.00 59.92  ? 704  ARG   B NE  1 
ATOM   6657  C  CZ  . ARG   B  1 403 ? -48.167 13.829  -7.351   1.00 59.40  ? 704  ARG   B CZ  1 
ATOM   6658  N  NH1 . ARG   B  1 403 ? -47.868 13.515  -6.099   1.00 49.41  ? 704  ARG   B NH1 1 
ATOM   6659  N  NH2 . ARG   B  1 403 ? -48.688 15.019  -7.631   1.00 61.00  ? 704  ARG   B NH2 1 
ATOM   6660  N  N   . LEU   B  1 404 ? -49.300 6.683   -6.540   1.00 63.99  ? 705  LEU   B N   1 
ATOM   6661  C  CA  . LEU   B  1 404 ? -50.053 6.059   -5.466   1.00 58.37  ? 705  LEU   B CA  1 
ATOM   6662  C  C   . LEU   B  1 404 ? -49.712 6.722   -4.139   1.00 54.74  ? 705  LEU   B C   1 
ATOM   6663  O  O   . LEU   B  1 404 ? -48.591 7.183   -3.932   1.00 54.54  ? 705  LEU   B O   1 
ATOM   6664  C  CB  . LEU   B  1 404 ? -49.745 4.564   -5.380   1.00 51.54  ? 705  LEU   B CB  1 
ATOM   6665  C  CG  . LEU   B  1 404 ? -49.864 3.741   -6.652   1.00 43.77  ? 705  LEU   B CG  1 
ATOM   6666  C  CD1 . LEU   B  1 404 ? -49.380 2.326   -6.399   1.00 37.86  ? 705  LEU   B CD1 1 
ATOM   6667  C  CD2 . LEU   B  1 404 ? -51.300 3.742   -7.152   1.00 48.12  ? 705  LEU   B CD2 1 
ATOM   6668  N  N   . THR   B  1 405 ? -50.703 6.764   -3.230   1.00 56.19  ? 706  THR   B N   1 
ATOM   6669  C  CA  . THR   B  1 405 ? -50.554 7.171   -1.847   1.00 45.76  ? 706  THR   B CA  1 
ATOM   6670  C  C   . THR   B  1 405 ? -50.621 5.941   -0.947   1.00 45.48  ? 706  THR   B C   1 
ATOM   6671  O  O   . THR   B  1 405 ? -51.268 4.950   -1.302   1.00 39.68  ? 706  THR   B O   1 
ATOM   6672  C  CB  . THR   B  1 405 ? -51.652 8.167   -1.457   1.00 54.63  ? 706  THR   B CB  1 
ATOM   6673  O  OG1 . THR   B  1 405 ? -51.450 8.606   -0.110   1.00 72.64  ? 706  THR   B OG1 1 
ATOM   6674  C  CG2 . THR   B  1 405 ? -53.044 7.514   -1.571   1.00 49.19  ? 706  THR   B CG2 1 
ATOM   6675  N  N   . PRO   B  1 406 ? -49.924 5.920   0.214    1.00 49.63  ? 707  PRO   B N   1 
ATOM   6676  C  CA  . PRO   B  1 406 ? -48.986 6.908   0.777    1.00 50.11  ? 707  PRO   B CA  1 
ATOM   6677  C  C   . PRO   B  1 406 ? -47.778 7.150   -0.103   1.00 50.94  ? 707  PRO   B C   1 
ATOM   6678  O  O   . PRO   B  1 406 ? -47.415 6.296   -0.918   1.00 52.10  ? 707  PRO   B O   1 
ATOM   6679  C  CB  . PRO   B  1 406 ? -48.548 6.279   2.109    1.00 42.59  ? 707  PRO   B CB  1 
ATOM   6680  C  CG  . PRO   B  1 406 ? -49.624 5.343   2.439    1.00 46.15  ? 707  PRO   B CG  1 
ATOM   6681  C  CD  . PRO   B  1 406 ? -50.129 4.793   1.140    1.00 44.51  ? 707  PRO   B CD  1 
ATOM   6682  N  N   . SER   B  1 407 ? -47.147 8.303   0.084    1.00 48.85  ? 708  SER   B N   1 
ATOM   6683  C  CA  . SER   B  1 407 ? -46.117 8.731   -0.840   1.00 50.22  ? 708  SER   B CA  1 
ATOM   6684  C  C   . SER   B  1 407 ? -45.123 9.629   -0.130   1.00 47.80  ? 708  SER   B C   1 
ATOM   6685  O  O   . SER   B  1 407 ? -45.439 10.260  0.880    1.00 53.60  ? 708  SER   B O   1 
ATOM   6686  C  CB  . SER   B  1 407 ? -46.727 9.485   -2.021   1.00 61.48  ? 708  SER   B CB  1 
ATOM   6687  O  OG  . SER   B  1 407 ? -47.407 10.644  -1.560   1.00 68.89  ? 708  SER   B OG  1 
ATOM   6688  N  N   . PHE   B  1 408 ? -43.917 9.683   -0.697   1.00 51.12  ? 709  PHE   B N   1 
ATOM   6689  C  CA  . PHE   B  1 408 ? -42.954 10.740  -0.422   1.00 39.00  ? 709  PHE   B CA  1 
ATOM   6690  C  C   . PHE   B  1 408 ? -43.133 11.865  -1.440   1.00 44.71  ? 709  PHE   B C   1 
ATOM   6691  O  O   . PHE   B  1 408 ? -43.448 11.618  -2.606   1.00 45.48  ? 709  PHE   B O   1 
ATOM   6692  C  CB  . PHE   B  1 408 ? -41.526 10.189  -0.453   1.00 23.68  ? 709  PHE   B CB  1 
ATOM   6693  C  CG  . PHE   B  1 408 ? -41.224 9.255   0.696    1.00 31.63  ? 709  PHE   B CG  1 
ATOM   6694  C  CD1 . PHE   B  1 408 ? -41.230 7.877   0.520    1.00 39.44  ? 709  PHE   B CD1 1 
ATOM   6695  C  CD2 . PHE   B  1 408 ? -40.965 9.756   1.958    1.00 31.44  ? 709  PHE   B CD2 1 
ATOM   6696  C  CE1 . PHE   B  1 408 ? -40.958 7.004   1.585    1.00 34.87  ? 709  PHE   B CE1 1 
ATOM   6697  C  CE2 . PHE   B  1 408 ? -40.684 8.893   3.028    1.00 30.70  ? 709  PHE   B CE2 1 
ATOM   6698  C  CZ  . PHE   B  1 408 ? -40.686 7.518   2.841    1.00 31.45  ? 709  PHE   B CZ  1 
ATOM   6699  N  N   . GLU   B  1 409 ? -42.955 13.103  -0.981   1.00 23.13  ? 710  GLU   B N   1 
ATOM   6700  C  CA  . GLU   B  1 409 ? -43.235 14.286  -1.782   1.00 33.55  ? 710  GLU   B CA  1 
ATOM   6701  C  C   . GLU   B  1 409 ? -42.141 15.305  -1.553   1.00 31.59  ? 710  GLU   B C   1 
ATOM   6702  O  O   . GLU   B  1 409 ? -41.567 15.379  -0.473   1.00 50.36  ? 710  GLU   B O   1 
ATOM   6703  C  CB  . GLU   B  1 409 ? -44.579 14.945  -1.423   1.00 24.54  ? 710  GLU   B CB  1 
ATOM   6704  C  CG  . GLU   B  1 409 ? -45.801 14.047  -1.588   1.00 61.06  ? 710  GLU   B CG  1 
ATOM   6705  C  CD  . GLU   B  1 409 ? -46.070 13.641  -3.057   1.00 69.68  ? 710  GLU   B CD  1 
ATOM   6706  O  OE1 . GLU   B  1 409 ? -45.568 14.318  -3.992   1.00 62.99  ? 710  GLU   B OE1 1 
ATOM   6707  O  OE2 . GLU   B  1 409 ? -46.792 12.634  -3.267   1.00 67.96  ? 710  GLU   B OE2 1 
ATOM   6708  N  N   . TYR   B  1 410 ? -41.848 16.091  -2.571   1.00 41.53  ? 711  TYR   B N   1 
ATOM   6709  C  CA  . TYR   B  1 410 ? -40.996 17.225  -2.305   1.00 48.06  ? 711  TYR   B CA  1 
ATOM   6710  C  C   . TYR   B  1 410 ? -41.777 18.267  -1.521   1.00 49.23  ? 711  TYR   B C   1 
ATOM   6711  O  O   . TYR   B  1 410 ? -43.012 18.220  -1.413   1.00 41.02  ? 711  TYR   B O   1 
ATOM   6712  C  CB  . TYR   B  1 410 ? -40.451 17.818  -3.602   1.00 53.36  ? 711  TYR   B CB  1 
ATOM   6713  C  CG  . TYR   B  1 410 ? -39.633 16.820  -4.362   1.00 58.83  ? 711  TYR   B CG  1 
ATOM   6714  C  CD1 . TYR   B  1 410 ? -40.131 16.225  -5.508   1.00 57.46  ? 711  TYR   B CD1 1 
ATOM   6715  C  CD2 . TYR   B  1 410 ? -38.378 16.430  -3.903   1.00 64.13  ? 711  TYR   B CD2 1 
ATOM   6716  C  CE1 . TYR   B  1 410 ? -39.402 15.291  -6.187   1.00 56.94  ? 711  TYR   B CE1 1 
ATOM   6717  C  CE2 . TYR   B  1 410 ? -37.636 15.489  -4.582   1.00 60.12  ? 711  TYR   B CE2 1 
ATOM   6718  C  CZ  . TYR   B  1 410 ? -38.158 14.926  -5.726   1.00 60.17  ? 711  TYR   B CZ  1 
ATOM   6719  O  OH  . TYR   B  1 410 ? -37.443 13.997  -6.430   1.00 67.36  ? 711  TYR   B OH  1 
ATOM   6720  N  N   . GLN   B  1 411 ? -41.029 19.202  -0.949   1.00 47.10  ? 712  GLN   B N   1 
ATOM   6721  C  CA  . GLN   B  1 411 ? -41.583 20.319  -0.204   1.00 43.15  ? 712  GLN   B CA  1 
ATOM   6722  C  C   . GLN   B  1 411 ? -40.603 21.468  -0.330   1.00 40.43  ? 712  GLN   B C   1 
ATOM   6723  O  O   . GLN   B  1 411 ? -39.430 21.254  -0.665   1.00 42.29  ? 712  GLN   B O   1 
ATOM   6724  C  CB  . GLN   B  1 411 ? -41.839 19.956  1.274    1.00 46.37  ? 712  GLN   B CB  1 
ATOM   6725  C  CG  . GLN   B  1 411 ? -40.607 19.611  2.107    1.00 45.38  ? 712  GLN   B CG  1 
ATOM   6726  C  CD  . GLN   B  1 411 ? -40.958 19.073  3.508    1.00 46.12  ? 712  GLN   B CD  1 
ATOM   6727  O  OE1 . GLN   B  1 411 ? -41.785 19.644  4.236    1.00 37.39  ? 712  GLN   B OE1 1 
ATOM   6728  N  NE2 . GLN   B  1 411 ? -40.337 17.957  3.876    1.00 43.42  ? 712  GLN   B NE2 1 
ATOM   6729  N  N   . PRO   B  1 412 ? -41.055 22.697  -0.121   1.00 40.34  ? 713  PRO   B N   1 
ATOM   6730  C  CA  . PRO   B  1 412 ? -40.152 23.837  -0.262   1.00 42.48  ? 713  PRO   B CA  1 
ATOM   6731  C  C   . PRO   B  1 412 ? -39.033 23.782  0.765    1.00 47.52  ? 713  PRO   B C   1 
ATOM   6732  O  O   . PRO   B  1 412 ? -39.183 23.210  1.844    1.00 66.42  ? 713  PRO   B O   1 
ATOM   6733  C  CB  . PRO   B  1 412 ? -41.064 25.040  -0.015   1.00 48.07  ? 713  PRO   B CB  1 
ATOM   6734  C  CG  . PRO   B  1 412 ? -42.475 24.516  -0.134   1.00 41.09  ? 713  PRO   B CG  1 
ATOM   6735  C  CD  . PRO   B  1 412 ? -42.423 23.100  0.252    1.00 42.12  ? 713  PRO   B CD  1 
ATOM   6736  N  N   . ASP   B  1 413 ? -37.894 24.368  0.410    1.00 52.35  ? 714  ASP   B N   1 
ATOM   6737  C  CA  . ASP   B  1 413 ? -36.824 24.554  1.378    1.00 56.48  ? 714  ASP   B CA  1 
ATOM   6738  C  C   . ASP   B  1 413 ? -37.331 25.496  2.461    1.00 67.63  ? 714  ASP   B C   1 
ATOM   6739  O  O   . ASP   B  1 413 ? -37.908 26.543  2.137    1.00 71.99  ? 714  ASP   B O   1 
ATOM   6740  C  CB  . ASP   B  1 413 ? -35.564 25.125  0.718    1.00 57.45  ? 714  ASP   B CB  1 
ATOM   6741  C  CG  . ASP   B  1 413 ? -34.890 24.131  -0.237   1.00 67.69  ? 714  ASP   B CG  1 
ATOM   6742  O  OD1 . ASP   B  1 413 ? -34.860 22.922  0.092    1.00 65.46  ? 714  ASP   B OD1 1 
ATOM   6743  O  OD2 . ASP   B  1 413 ? -34.393 24.557  -1.312   1.00 72.49  ? 714  ASP   B OD2 1 
ATOM   6744  N  N   . PRO   B  1 414 ? -37.153 25.162  3.745    1.00 71.77  ? 715  PRO   B N   1 
ATOM   6745  C  CA  . PRO   B  1 414 ? -37.851 25.918  4.798    1.00 53.98  ? 715  PRO   B CA  1 
ATOM   6746  C  C   . PRO   B  1 414 ? -37.461 27.378  4.862    1.00 59.68  ? 715  PRO   B C   1 
ATOM   6747  O  O   . PRO   B  1 414 ? -38.310 28.215  5.185    1.00 73.51  ? 715  PRO   B O   1 
ATOM   6748  C  CB  . PRO   B  1 414 ? -37.462 25.169  6.075    1.00 47.69  ? 715  PRO   B CB  1 
ATOM   6749  C  CG  . PRO   B  1 414 ? -36.194 24.501  5.748    1.00 53.05  ? 715  PRO   B CG  1 
ATOM   6750  C  CD  . PRO   B  1 414 ? -36.265 24.129  4.304    1.00 64.05  ? 715  PRO   B CD  1 
ATOM   6751  N  N   . TRP   B  1 415 ? -36.214 27.720  4.536    1.00 57.15  ? 716  TRP   B N   1 
ATOM   6752  C  CA  . TRP   B  1 415 ? -35.763 29.099  4.663    1.00 54.90  ? 716  TRP   B CA  1 
ATOM   6753  C  C   . TRP   B  1 415 ? -36.397 30.022  3.638    1.00 66.27  ? 716  TRP   B C   1 
ATOM   6754  O  O   . TRP   B  1 415 ? -36.281 31.245  3.777    1.00 73.07  ? 716  TRP   B O   1 
ATOM   6755  C  CB  . TRP   B  1 415 ? -34.243 29.169  4.551    1.00 54.31  ? 716  TRP   B CB  1 
ATOM   6756  C  CG  . TRP   B  1 415 ? -33.722 28.636  3.267    1.00 62.83  ? 716  TRP   B CG  1 
ATOM   6757  C  CD1 . TRP   B  1 415 ? -33.708 29.276  2.064    1.00 69.20  ? 716  TRP   B CD1 1 
ATOM   6758  C  CD2 . TRP   B  1 415 ? -33.132 27.350  3.044    1.00 62.18  ? 716  TRP   B CD2 1 
ATOM   6759  N  NE1 . TRP   B  1 415 ? -33.143 28.471  1.112    1.00 70.33  ? 716  TRP   B NE1 1 
ATOM   6760  C  CE2 . TRP   B  1 415 ? -32.783 27.282  1.690    1.00 64.81  ? 716  TRP   B CE2 1 
ATOM   6761  C  CE3 . TRP   B  1 415 ? -32.868 26.252  3.859    1.00 62.72  ? 716  TRP   B CE3 1 
ATOM   6762  C  CZ2 . TRP   B  1 415 ? -32.188 26.158  1.133    1.00 58.11  ? 716  TRP   B CZ2 1 
ATOM   6763  C  CZ3 . TRP   B  1 415 ? -32.276 25.138  3.299    1.00 52.48  ? 716  TRP   B CZ3 1 
ATOM   6764  C  CH2 . TRP   B  1 415 ? -31.940 25.103  1.961    1.00 51.17  ? 716  TRP   B CH2 1 
ATOM   6765  N  N   . ASN   B  1 416 ? -37.045 29.479  2.607    1.00 69.24  ? 717  ASN   B N   1 
ATOM   6766  C  CA  . ASN   B  1 416 ? -37.892 30.315  1.768    1.00 71.82  ? 717  ASN   B CA  1 
ATOM   6767  C  C   . ASN   B  1 416 ? -39.179 30.693  2.489    1.00 77.23  ? 717  ASN   B C   1 
ATOM   6768  O  O   . ASN   B  1 416 ? -39.803 31.702  2.136    1.00 80.38  ? 717  ASN   B O   1 
ATOM   6769  C  CB  . ASN   B  1 416 ? -38.210 29.605  0.447    1.00 66.32  ? 717  ASN   B CB  1 
ATOM   6770  C  CG  . ASN   B  1 416 ? -36.960 29.292  -0.378   1.00 68.86  ? 717  ASN   B CG  1 
ATOM   6771  O  OD1 . ASN   B  1 416 ? -35.955 30.011  -0.316   1.00 70.12  ? 717  ASN   B OD1 1 
ATOM   6772  N  ND2 . ASN   B  1 416 ? -37.025 28.215  -1.164   1.00 65.24  ? 717  ASN   B ND2 1 
ATOM   6773  N  N   . THR   B  1 417 ? -39.555 29.932  3.522    1.00 79.07  ? 718  THR   B N   1 
ATOM   6774  C  CA  . THR   B  1 417 ? -40.826 30.078  4.221    1.00 83.78  ? 718  THR   B CA  1 
ATOM   6775  C  C   . THR   B  1 417 ? -40.715 30.600  5.649    1.00 83.39  ? 718  THR   B C   1 
ATOM   6776  O  O   . THR   B  1 417 ? -41.618 31.308  6.102    1.00 89.54  ? 718  THR   B O   1 
ATOM   6777  C  CB  . THR   B  1 417 ? -41.553 28.730  4.267    1.00 81.35  ? 718  THR   B CB  1 
ATOM   6778  O  OG1 . THR   B  1 417 ? -41.434 28.088  2.993    1.00 76.40  ? 718  THR   B OG1 1 
ATOM   6779  C  CG2 . THR   B  1 417 ? -43.033 28.920  4.622    1.00 84.20  ? 718  THR   B CG2 1 
ATOM   6780  N  N   . HIS   B  1 418 ? -39.643 30.277  6.366    1.00 81.15  ? 719  HIS   B N   1 
ATOM   6781  C  CA  . HIS   B  1 418 ? -39.628 30.438  7.816    1.00 82.54  ? 719  HIS   B CA  1 
ATOM   6782  C  C   . HIS   B  1 418 ? -39.492 31.904  8.223    1.00 88.55  ? 719  HIS   B C   1 
ATOM   6783  O  O   . HIS   B  1 418 ? -38.601 32.610  7.743    1.00 85.10  ? 719  HIS   B O   1 
ATOM   6784  C  CB  . HIS   B  1 418 ? -38.489 29.610  8.406    1.00 77.23  ? 719  HIS   B CB  1 
ATOM   6785  C  CG  . HIS   B  1 418 ? -38.395 29.689  9.892    1.00 73.88  ? 719  HIS   B CG  1 
ATOM   6786  N  ND1 . HIS   B  1 418 ? -37.521 30.539  10.535   1.00 79.30  ? 719  HIS   B ND1 1 
ATOM   6787  C  CD2 . HIS   B  1 418 ? -39.075 29.037  10.864   1.00 75.66  ? 719  HIS   B CD2 1 
ATOM   6788  C  CE1 . HIS   B  1 418 ? -37.662 30.404  11.842   1.00 82.16  ? 719  HIS   B CE1 1 
ATOM   6789  N  NE2 . HIS   B  1 418 ? -38.598 29.498  12.067   1.00 79.87  ? 719  HIS   B NE2 1 
ATOM   6790  N  N   . VAL   B  1 419 ? -40.376 32.357  9.116    1.00 98.58  ? 720  VAL   B N   1 
ATOM   6791  C  CA  . VAL   B  1 419 ? -40.303 33.693  9.711    1.00 105.38 ? 720  VAL   B CA  1 
ATOM   6792  C  C   . VAL   B  1 419 ? -39.562 33.582  11.043   1.00 105.05 ? 720  VAL   B C   1 
ATOM   6793  O  O   . VAL   B  1 419 ? -40.047 32.942  11.978   1.00 107.67 ? 720  VAL   B O   1 
ATOM   6794  C  CB  . VAL   B  1 419 ? -41.699 34.301  9.905    1.00 106.41 ? 720  VAL   B CB  1 
ATOM   6795  C  CG1 . VAL   B  1 419 ? -42.027 35.288  8.783    1.00 106.42 ? 720  VAL   B CG1 1 
ATOM   6796  C  CG2 . VAL   B  1 419 ? -42.764 33.195  9.993    1.00 101.89 ? 720  VAL   B CG2 1 
ATOM   6797  N  N   . TRP   B  1 420 ? -38.399 34.228  11.138   1.00 104.35 ? 721  TRP   B N   1 
ATOM   6798  C  CA  . TRP   B  1 420 ? -37.506 34.088  12.282   1.00 103.59 ? 721  TRP   B CA  1 
ATOM   6799  C  C   . TRP   B  1 420 ? -38.006 34.902  13.475   1.00 105.49 ? 721  TRP   B C   1 
ATOM   6800  O  O   . TRP   B  1 420 ? -38.983 35.651  13.383   1.00 107.34 ? 721  TRP   B O   1 
ATOM   6801  C  CB  . TRP   B  1 420 ? -36.095 34.520  11.900   1.00 105.06 ? 721  TRP   B CB  1 
ATOM   6802  C  CG  . TRP   B  1 420 ? -35.401 33.554  11.003   1.00 104.54 ? 721  TRP   B CG  1 
ATOM   6803  C  CD1 . TRP   B  1 420 ? -35.649 33.337  9.677    1.00 101.86 ? 721  TRP   B CD1 1 
ATOM   6804  C  CD2 . TRP   B  1 420 ? -34.336 32.671  11.364   1.00 100.07 ? 721  TRP   B CD2 1 
ATOM   6805  N  NE1 . TRP   B  1 420 ? -34.804 32.371  9.192    1.00 96.77  ? 721  TRP   B NE1 1 
ATOM   6806  C  CE2 . TRP   B  1 420 ? -33.987 31.946  10.207   1.00 96.06  ? 721  TRP   B CE2 1 
ATOM   6807  C  CE3 . TRP   B  1 420 ? -33.641 32.423  12.553   1.00 99.92  ? 721  TRP   B CE3 1 
ATOM   6808  C  CZ2 . TRP   B  1 420 ? -32.975 30.991  10.203   1.00 95.13  ? 721  TRP   B CZ2 1 
ATOM   6809  C  CZ3 . TRP   B  1 420 ? -32.635 31.475  12.548   1.00 98.27  ? 721  TRP   B CZ3 1 
ATOM   6810  C  CH2 . TRP   B  1 420 ? -32.313 30.768  11.380   1.00 97.25  ? 721  TRP   B CH2 1 
ATOM   6811  N  N   . LYS   B  1 421 ? -37.315 34.760  14.611   1.00 105.51 ? 722  LYS   B N   1 
ATOM   6812  C  CA  . LYS   B  1 421 ? -37.659 35.499  15.835   1.00 103.41 ? 722  LYS   B CA  1 
ATOM   6813  C  C   . LYS   B  1 421 ? -36.538 35.544  16.878   1.00 96.68  ? 722  LYS   B C   1 
ATOM   6814  O  O   . LYS   B  1 421 ? -35.533 36.237  16.715   1.00 95.40  ? 722  LYS   B O   1 
ATOM   6815  C  CB  . LYS   B  1 421 ? -38.918 34.903  16.468   1.00 101.86 ? 722  LYS   B CB  1 
ATOM   6816  C  CG  . LYS   B  1 421 ? -38.984 33.385  16.437   1.00 97.67  ? 722  LYS   B CG  1 
ATOM   6817  C  CD  . LYS   B  1 421 ? -40.404 32.892  16.655   1.00 95.46  ? 722  LYS   B CD  1 
ATOM   6818  C  CE  . LYS   B  1 421 ? -40.423 31.431  17.086   1.00 93.94  ? 722  LYS   B CE  1 
ATOM   6819  N  NZ  . LYS   B  1 421 ? -41.803 30.854  17.028   1.00 89.80  ? 722  LYS   B NZ  1 
ATOM   6820  N  N   . PRO   C  1 2   ? 0.906   42.105  -59.256  1.00 112.85 ? 303  PRO   C N   1 
ATOM   6821  C  CA  . PRO   C  1 2   ? 0.771   41.018  -60.233  1.00 115.98 ? 303  PRO   C CA  1 
ATOM   6822  C  C   . PRO   C  1 2   ? 0.736   41.487  -61.706  1.00 117.88 ? 303  PRO   C C   1 
ATOM   6823  O  O   . PRO   C  1 2   ? 0.897   40.681  -62.633  1.00 109.33 ? 303  PRO   C O   1 
ATOM   6824  C  CB  . PRO   C  1 2   ? -0.562  40.371  -59.830  1.00 112.46 ? 303  PRO   C CB  1 
ATOM   6825  C  CG  . PRO   C  1 2   ? -0.728  40.701  -58.337  1.00 107.17 ? 303  PRO   C CG  1 
ATOM   6826  C  CD  . PRO   C  1 2   ? 0.316   41.735  -57.957  1.00 106.63 ? 303  PRO   C CD  1 
ATOM   6827  N  N   . ARG   C  1 3   ? 0.539   42.795  -61.892  1.00 124.11 ? 304  ARG   C N   1 
ATOM   6828  C  CA  . ARG   C  1 3   ? 0.334   43.435  -63.187  1.00 116.57 ? 304  ARG   C CA  1 
ATOM   6829  C  C   . ARG   C  1 3   ? 1.627   43.997  -63.772  1.00 99.68  ? 304  ARG   C C   1 
ATOM   6830  O  O   . ARG   C  1 3   ? 1.580   44.826  -64.689  1.00 101.15 ? 304  ARG   C O   1 
ATOM   6831  C  CB  . ARG   C  1 3   ? -0.704  44.549  -63.031  1.00 122.87 ? 304  ARG   C CB  1 
ATOM   6832  C  CG  . ARG   C  1 3   ? -1.697  44.689  -64.158  1.00 130.01 ? 304  ARG   C CG  1 
ATOM   6833  C  CD  . ARG   C  1 3   ? -2.930  45.447  -63.665  1.00 135.20 ? 304  ARG   C CD  1 
ATOM   6834  N  NE  . ARG   C  1 3   ? -3.952  45.576  -64.706  1.00 139.20 ? 304  ARG   C NE  1 
ATOM   6835  C  CZ  . ARG   C  1 3   ? -4.357  46.728  -65.239  1.00 134.41 ? 304  ARG   C CZ  1 
ATOM   6836  N  NH1 . ARG   C  1 3   ? -3.839  47.874  -64.815  1.00 134.46 ? 304  ARG   C NH1 1 
ATOM   6837  N  NH2 . ARG   C  1 3   ? -5.290  46.738  -66.186  1.00 126.42 ? 304  ARG   C NH2 1 
ATOM   6838  N  N   . PHE   C  1 4   ? 2.775   43.536  -63.271  1.00 84.25  ? 305  PHE   C N   1 
ATOM   6839  C  CA  . PHE   C  1 4   ? 4.070   44.191  -63.424  1.00 72.91  ? 305  PHE   C CA  1 
ATOM   6840  C  C   . PHE   C  1 4   ? 5.100   43.447  -62.573  1.00 59.28  ? 305  PHE   C C   1 
ATOM   6841  O  O   . PHE   C  1 4   ? 4.768   42.951  -61.491  1.00 62.00  ? 305  PHE   C O   1 
ATOM   6842  C  CB  . PHE   C  1 4   ? 3.994   45.658  -62.984  1.00 84.78  ? 305  PHE   C CB  1 
ATOM   6843  C  CG  . PHE   C  1 4   ? 3.945   45.835  -61.478  1.00 100.59 ? 305  PHE   C CG  1 
ATOM   6844  C  CD1 . PHE   C  1 4   ? 5.032   46.360  -60.786  1.00 102.13 ? 305  PHE   C CD1 1 
ATOM   6845  C  CD2 . PHE   C  1 4   ? 2.820   45.440  -60.750  1.00 103.49 ? 305  PHE   C CD2 1 
ATOM   6846  C  CE1 . PHE   C  1 4   ? 4.990   46.502  -59.407  1.00 103.61 ? 305  PHE   C CE1 1 
ATOM   6847  C  CE2 . PHE   C  1 4   ? 2.772   45.579  -59.374  1.00 98.13  ? 305  PHE   C CE2 1 
ATOM   6848  C  CZ  . PHE   C  1 4   ? 3.856   46.111  -58.700  1.00 103.02 ? 305  PHE   C CZ  1 
ATOM   6849  N  N   . LEU   C  1 5   ? 6.342   43.348  -63.042  1.00 44.62  ? 306  LEU   C N   1 
ATOM   6850  C  CA  . LEU   C  1 5   ? 7.427   42.761  -62.266  1.00 43.49  ? 306  LEU   C CA  1 
ATOM   6851  C  C   . LEU   C  1 5   ? 8.636   43.665  -62.410  1.00 53.25  ? 306  LEU   C C   1 
ATOM   6852  O  O   . LEU   C  1 5   ? 9.054   43.966  -63.529  1.00 62.50  ? 306  LEU   C O   1 
ATOM   6853  C  CB  . LEU   C  1 5   ? 7.781   41.347  -62.731  1.00 43.85  ? 306  LEU   C CB  1 
ATOM   6854  C  CG  . LEU   C  1 5   ? 6.661   40.317  -62.711  1.00 49.05  ? 306  LEU   C CG  1 
ATOM   6855  C  CD1 . LEU   C  1 5   ? 7.057   39.079  -63.485  1.00 52.13  ? 306  LEU   C CD1 1 
ATOM   6856  C  CD2 . LEU   C  1 5   ? 6.316   39.980  -61.304  1.00 41.67  ? 306  LEU   C CD2 1 
ATOM   6857  N  N   . LYS   C  1 6   ? 9.182   44.100  -61.287  1.00 49.39  ? 307  LYS   C N   1 
ATOM   6858  C  CA  . LYS   C  1 6   ? 10.291  45.032  -61.276  1.00 50.26  ? 307  LYS   C CA  1 
ATOM   6859  C  C   . LYS   C  1 6   ? 11.593  44.265  -61.115  1.00 55.41  ? 307  LYS   C C   1 
ATOM   6860  O  O   . LYS   C  1 6   ? 11.632  43.245  -60.425  1.00 59.15  ? 307  LYS   C O   1 
ATOM   6861  C  CB  . LYS   C  1 6   ? 10.115  46.042  -60.143  1.00 55.13  ? 307  LYS   C CB  1 
ATOM   6862  C  CG  . LYS   C  1 6   ? 8.997   47.067  -60.398  1.00 58.76  ? 307  LYS   C CG  1 
ATOM   6863  C  CD  . LYS   C  1 6   ? 8.877   48.058  -59.252  1.00 54.85  ? 307  LYS   C CD  1 
ATOM   6864  C  CE  . LYS   C  1 6   ? 7.704   49.015  -59.424  1.00 60.92  ? 307  LYS   C CE  1 
ATOM   6865  N  NZ  . LYS   C  1 6   ? 8.043   50.255  -60.195  1.00 67.45  ? 307  LYS   C NZ  1 
ATOM   6866  N  N   . VAL   C  1 7   ? 12.651  44.744  -61.773  1.00 54.60  ? 308  VAL   C N   1 
ATOM   6867  C  CA  . VAL   C  1 7   ? 14.009  44.259  -61.543  1.00 48.49  ? 308  VAL   C CA  1 
ATOM   6868  C  C   . VAL   C  1 7   ? 14.867  45.430  -61.090  1.00 56.69  ? 308  VAL   C C   1 
ATOM   6869  O  O   . VAL   C  1 7   ? 14.676  46.566  -61.542  1.00 62.82  ? 308  VAL   C O   1 
ATOM   6870  C  CB  . VAL   C  1 7   ? 14.618  43.581  -62.788  1.00 52.18  ? 308  VAL   C CB  1 
ATOM   6871  C  CG1 . VAL   C  1 7   ? 13.576  42.717  -63.483  1.00 55.00  ? 308  VAL   C CG1 1 
ATOM   6872  C  CG2 . VAL   C  1 7   ? 15.243  44.603  -63.737  1.00 56.87  ? 308  VAL   C CG2 1 
ATOM   6873  N  N   . LYS   C  1 8   ? 15.804  45.152  -60.182  1.00 52.60  ? 309  LYS   C N   1 
ATOM   6874  C  CA  . LYS   C  1 8   ? 16.624  46.177  -59.549  1.00 39.33  ? 309  LYS   C CA  1 
ATOM   6875  C  C   . LYS   C  1 8   ? 18.097  45.857  -59.733  1.00 43.55  ? 309  LYS   C C   1 
ATOM   6876  O  O   . LYS   C  1 8   ? 18.500  44.691  -59.672  1.00 53.25  ? 309  LYS   C O   1 
ATOM   6877  C  CB  . LYS   C  1 8   ? 16.311  46.291  -58.055  1.00 55.00  ? 309  LYS   C CB  1 
ATOM   6878  C  CG  . LYS   C  1 8   ? 17.226  47.227  -57.262  1.00 59.47  ? 309  LYS   C CG  1 
ATOM   6879  C  CD  . LYS   C  1 8   ? 16.949  47.131  -55.769  1.00 63.75  ? 309  LYS   C CD  1 
ATOM   6880  C  CE  . LYS   C  1 8   ? 17.974  47.916  -54.962  1.00 70.99  ? 309  LYS   C CE  1 
ATOM   6881  N  NZ  . LYS   C  1 8   ? 17.746  47.740  -53.496  1.00 71.29  ? 309  LYS   C NZ  1 
ATOM   6882  N  N   . ASN   C  1 9   ? 18.890  46.904  -59.957  1.00 40.11  ? 310  ASN   C N   1 
ATOM   6883  C  CA  . ASN   C  1 9   ? 20.343  46.825  -60.014  1.00 40.29  ? 310  ASN   C CA  1 
ATOM   6884  C  C   . ASN   C  1 9   ? 20.904  47.176  -58.636  1.00 60.19  ? 310  ASN   C C   1 
ATOM   6885  O  O   . ASN   C  1 9   ? 20.649  48.271  -58.125  1.00 63.34  ? 310  ASN   C O   1 
ATOM   6886  C  CB  . ASN   C  1 9   ? 20.861  47.788  -61.077  1.00 54.97  ? 310  ASN   C CB  1 
ATOM   6887  C  CG  . ASN   C  1 9   ? 22.341  47.668  -61.299  1.00 65.53  ? 310  ASN   C CG  1 
ATOM   6888  O  OD1 . ASN   C  1 9   ? 23.130  47.992  -60.420  1.00 69.96  ? 310  ASN   C OD1 1 
ATOM   6889  N  ND2 . ASN   C  1 9   ? 22.732  47.218  -62.488  1.00 63.85  ? 310  ASN   C ND2 1 
ATOM   6890  N  N   . TRP   C  1 10  ? 21.664  46.254  -58.033  1.00 60.51  ? 311  TRP   C N   1 
ATOM   6891  C  CA  . TRP   C  1 10  ? 22.129  46.439  -56.660  1.00 58.96  ? 311  TRP   C CA  1 
ATOM   6892  C  C   . TRP   C  1 10  ? 23.416  47.246  -56.567  1.00 62.92  ? 311  TRP   C C   1 
ATOM   6893  O  O   . TRP   C  1 10  ? 23.999  47.340  -55.484  1.00 67.09  ? 311  TRP   C O   1 
ATOM   6894  C  CB  . TRP   C  1 10  ? 22.290  45.085  -55.968  1.00 41.26  ? 311  TRP   C CB  1 
ATOM   6895  C  CG  . TRP   C  1 10  ? 20.972  44.463  -55.718  1.00 41.49  ? 311  TRP   C CG  1 
ATOM   6896  C  CD1 . TRP   C  1 10  ? 20.273  43.669  -56.576  1.00 44.62  ? 311  TRP   C CD1 1 
ATOM   6897  C  CD2 . TRP   C  1 10  ? 20.163  44.598  -54.543  1.00 48.33  ? 311  TRP   C CD2 1 
ATOM   6898  N  NE1 . TRP   C  1 10  ? 19.081  43.290  -56.010  1.00 45.97  ? 311  TRP   C NE1 1 
ATOM   6899  C  CE2 . TRP   C  1 10  ? 18.987  43.847  -54.760  1.00 53.93  ? 311  TRP   C CE2 1 
ATOM   6900  C  CE3 . TRP   C  1 10  ? 20.324  45.263  -53.323  1.00 51.57  ? 311  TRP   C CE3 1 
ATOM   6901  C  CZ2 . TRP   C  1 10  ? 17.966  43.757  -53.805  1.00 50.05  ? 311  TRP   C CZ2 1 
ATOM   6902  C  CZ3 . TRP   C  1 10  ? 19.310  45.171  -52.371  1.00 54.99  ? 311  TRP   C CZ3 1 
ATOM   6903  C  CH2 . TRP   C  1 10  ? 18.150  44.422  -52.618  1.00 56.86  ? 311  TRP   C CH2 1 
ATOM   6904  N  N   . GLU   C  1 11  ? 23.857  47.841  -57.672  1.00 62.27  ? 312  GLU   C N   1 
ATOM   6905  C  CA  . GLU   C  1 11  ? 24.953  48.800  -57.690  1.00 57.99  ? 312  GLU   C CA  1 
ATOM   6906  C  C   . GLU   C  1 11  ? 24.429  50.227  -57.761  1.00 66.04  ? 312  GLU   C C   1 
ATOM   6907  O  O   . GLU   C  1 11  ? 24.772  51.057  -56.918  1.00 82.34  ? 312  GLU   C O   1 
ATOM   6908  C  CB  . GLU   C  1 11  ? 25.875  48.506  -58.881  1.00 57.39  ? 312  GLU   C CB  1 
ATOM   6909  C  CG  . GLU   C  1 11  ? 27.313  48.939  -58.723  1.00 69.29  ? 312  GLU   C CG  1 
ATOM   6910  C  CD  . GLU   C  1 11  ? 28.196  48.457  -59.881  1.00 82.41  ? 312  GLU   C CD  1 
ATOM   6911  O  OE1 . GLU   C  1 11  ? 27.711  47.689  -60.744  1.00 78.22  ? 312  GLU   C OE1 1 
ATOM   6912  O  OE2 . GLU   C  1 11  ? 29.382  48.851  -59.928  1.00 91.19  ? 312  GLU   C OE2 1 
ATOM   6913  N  N   . THR   C  1 12  ? 23.555  50.511  -58.728  1.00 61.82  ? 313  THR   C N   1 
ATOM   6914  C  CA  . THR   C  1 12  ? 23.039  51.851  -58.979  1.00 58.44  ? 313  THR   C CA  1 
ATOM   6915  C  C   . THR   C  1 12  ? 21.666  52.092  -58.369  1.00 57.57  ? 313  THR   C C   1 
ATOM   6916  O  O   . THR   C  1 12  ? 21.205  53.234  -58.364  1.00 67.07  ? 313  THR   C O   1 
ATOM   6917  C  CB  . THR   C  1 12  ? 22.965  52.112  -60.497  1.00 64.17  ? 313  THR   C CB  1 
ATOM   6918  O  OG1 . THR   C  1 12  ? 21.830  51.437  -61.058  1.00 62.81  ? 313  THR   C OG1 1 
ATOM   6919  C  CG2 . THR   C  1 12  ? 24.221  51.592  -61.189  1.00 59.14  ? 313  THR   C CG2 1 
ATOM   6920  N  N   . GLU   C  1 13  ? 21.001  51.046  -57.881  1.00 55.58  ? 314  GLU   C N   1 
ATOM   6921  C  CA  . GLU   C  1 13  ? 19.649  51.088  -57.324  1.00 56.98  ? 314  GLU   C CA  1 
ATOM   6922  C  C   . GLU   C  1 13  ? 18.577  51.467  -58.348  1.00 59.42  ? 314  GLU   C C   1 
ATOM   6923  O  O   . GLU   C  1 13  ? 17.494  51.924  -57.973  1.00 61.44  ? 314  GLU   C O   1 
ATOM   6924  C  CB  . GLU   C  1 13  ? 19.570  52.016  -56.111  1.00 62.25  ? 314  GLU   C CB  1 
ATOM   6925  C  CG  . GLU   C  1 13  ? 19.549  51.249  -54.807  1.00 70.76  ? 314  GLU   C CG  1 
ATOM   6926  C  CD  . GLU   C  1 13  ? 19.680  52.145  -53.602  1.00 77.34  ? 314  GLU   C CD  1 
ATOM   6927  O  OE1 . GLU   C  1 13  ? 18.714  52.205  -52.810  1.00 83.25  ? 314  GLU   C OE1 1 
ATOM   6928  O  OE2 . GLU   C  1 13  ? 20.744  52.790  -53.455  1.00 76.97  ? 314  GLU   C OE2 1 
ATOM   6929  N  N   . VAL   C  1 14  ? 18.825  51.257  -59.629  1.00 56.63  ? 315  VAL   C N   1 
ATOM   6930  C  CA  . VAL   C  1 14  ? 17.813  51.516  -60.646  1.00 58.64  ? 315  VAL   C CA  1 
ATOM   6931  C  C   . VAL   C  1 14  ? 16.822  50.357  -60.683  1.00 60.27  ? 315  VAL   C C   1 
ATOM   6932  O  O   . VAL   C  1 14  ? 17.209  49.182  -60.622  1.00 63.16  ? 315  VAL   C O   1 
ATOM   6933  C  CB  . VAL   C  1 14  ? 18.487  51.734  -62.012  1.00 60.76  ? 315  VAL   C CB  1 
ATOM   6934  C  CG1 . VAL   C  1 14  ? 17.484  51.592  -63.149  1.00 57.02  ? 315  VAL   C CG1 1 
ATOM   6935  C  CG2 . VAL   C  1 14  ? 19.162  53.092  -62.044  1.00 61.82  ? 315  VAL   C CG2 1 
ATOM   6936  N  N   . VAL   C  1 15  ? 15.533  50.676  -60.771  1.00 56.43  ? 316  VAL   C N   1 
ATOM   6937  C  CA  . VAL   C  1 15  ? 14.485  49.669  -60.902  1.00 60.47  ? 316  VAL   C CA  1 
ATOM   6938  C  C   . VAL   C  1 15  ? 13.796  49.839  -62.253  1.00 68.50  ? 316  VAL   C C   1 
ATOM   6939  O  O   . VAL   C  1 15  ? 13.392  50.952  -62.615  1.00 75.12  ? 316  VAL   C O   1 
ATOM   6940  C  CB  . VAL   C  1 15  ? 13.464  49.760  -59.755  1.00 58.47  ? 316  VAL   C CB  1 
ATOM   6941  C  CG1 . VAL   C  1 15  ? 12.390  48.700  -59.915  1.00 55.96  ? 316  VAL   C CG1 1 
ATOM   6942  C  CG2 . VAL   C  1 15  ? 14.152  49.603  -58.444  1.00 42.88  ? 316  VAL   C CG2 1 
ATOM   6943  N  N   . LEU   C  1 16  ? 13.664  48.733  -62.993  1.00 62.94  ? 317  LEU   C N   1 
ATOM   6944  C  CA  . LEU   C  1 16  ? 12.942  48.688  -64.259  1.00 57.55  ? 317  LEU   C CA  1 
ATOM   6945  C  C   . LEU   C  1 16  ? 11.702  47.823  -64.090  1.00 61.48  ? 317  LEU   C C   1 
ATOM   6946  O  O   . LEU   C  1 16  ? 11.702  46.863  -63.313  1.00 62.09  ? 317  LEU   C O   1 
ATOM   6947  C  CB  . LEU   C  1 16  ? 13.819  48.130  -65.392  1.00 46.28  ? 317  LEU   C CB  1 
ATOM   6948  C  CG  . LEU   C  1 16  ? 15.214  48.757  -65.510  1.00 44.42  ? 317  LEU   C CG  1 
ATOM   6949  C  CD1 . LEU   C  1 16  ? 16.090  48.032  -66.519  1.00 40.20  ? 317  LEU   C CD1 1 
ATOM   6950  C  CD2 . LEU   C  1 16  ? 15.108  50.241  -65.832  1.00 43.12  ? 317  LEU   C CD2 1 
ATOM   6951  N  N   . THR   C  1 17  ? 10.638  48.175  -64.811  1.00 63.38  ? 318  THR   C N   1 
ATOM   6952  C  CA  . THR   C  1 17  ? 9.326   47.565  -64.611  1.00 59.55  ? 318  THR   C CA  1 
ATOM   6953  C  C   . THR   C  1 17  ? 8.936   46.779  -65.857  1.00 49.56  ? 318  THR   C C   1 
ATOM   6954  O  O   . THR   C  1 17  ? 8.664   47.361  -66.908  1.00 52.67  ? 318  THR   C O   1 
ATOM   6955  C  CB  . THR   C  1 17  ? 8.286   48.631  -64.277  1.00 63.07  ? 318  THR   C CB  1 
ATOM   6956  O  OG1 . THR   C  1 17  ? 8.897   49.637  -63.457  1.00 63.46  ? 318  THR   C OG1 1 
ATOM   6957  C  CG2 . THR   C  1 17  ? 7.126   48.011  -63.517  1.00 62.50  ? 318  THR   C CG2 1 
ATOM   6958  N  N   . ASP   C  1 18  ? 8.866   45.462  -65.721  1.00 41.54  ? 319  ASP   C N   1 
ATOM   6959  C  CA  . ASP   C  1 18  ? 8.707   44.553  -66.843  1.00 48.15  ? 319  ASP   C CA  1 
ATOM   6960  C  C   . ASP   C  1 18  ? 7.238   44.235  -67.062  1.00 60.58  ? 319  ASP   C C   1 
ATOM   6961  O  O   . ASP   C  1 18  ? 6.601   43.612  -66.205  1.00 58.42  ? 319  ASP   C O   1 
ATOM   6962  C  CB  . ASP   C  1 18  ? 9.482   43.268  -66.583  1.00 54.70  ? 319  ASP   C CB  1 
ATOM   6963  C  CG  . ASP   C  1 18  ? 9.699   42.451  -67.832  1.00 47.14  ? 319  ASP   C CG  1 
ATOM   6964  O  OD1 . ASP   C  1 18  ? 8.705   42.085  -68.480  1.00 43.00  ? 319  ASP   C OD1 1 
ATOM   6965  O  OD2 . ASP   C  1 18  ? 10.875  42.176  -68.151  1.00 49.98  ? 319  ASP   C OD2 1 
ATOM   6966  N  N   . THR   C  1 19  ? 6.713   44.647  -68.216  1.00 66.04  ? 320  THR   C N   1 
ATOM   6967  C  CA  . THR   C  1 19  ? 5.399   44.220  -68.676  1.00 64.17  ? 320  THR   C CA  1 
ATOM   6968  C  C   . THR   C  1 19  ? 5.461   43.331  -69.901  1.00 57.91  ? 320  THR   C C   1 
ATOM   6969  O  O   . THR   C  1 19  ? 4.522   42.566  -70.127  1.00 55.66  ? 320  THR   C O   1 
ATOM   6970  C  CB  . THR   C  1 19  ? 4.514   45.429  -69.002  1.00 67.51  ? 320  THR   C CB  1 
ATOM   6971  O  OG1 . THR   C  1 19  ? 5.341   46.551  -69.356  1.00 80.55  ? 320  THR   C OG1 1 
ATOM   6972  C  CG2 . THR   C  1 19  ? 3.649   45.768  -67.812  1.00 58.64  ? 320  THR   C CG2 1 
ATOM   6973  N  N   . LEU   C  1 20  ? 6.548   43.403  -70.676  1.00 56.46  ? 321  LEU   C N   1 
ATOM   6974  C  CA  . LEU   C  1 20  ? 6.651   42.621  -71.905  1.00 54.83  ? 321  LEU   C CA  1 
ATOM   6975  C  C   . LEU   C  1 20  ? 6.504   41.133  -71.625  1.00 53.19  ? 321  LEU   C C   1 
ATOM   6976  O  O   . LEU   C  1 20  ? 6.006   40.393  -72.473  1.00 44.86  ? 321  LEU   C O   1 
ATOM   6977  C  CB  . LEU   C  1 20  ? 7.979   42.924  -72.599  1.00 46.74  ? 321  LEU   C CB  1 
ATOM   6978  C  CG  . LEU   C  1 20  ? 8.541   42.007  -73.684  1.00 46.50  ? 321  LEU   C CG  1 
ATOM   6979  C  CD1 . LEU   C  1 20  ? 7.738   42.114  -75.001  1.00 46.90  ? 321  LEU   C CD1 1 
ATOM   6980  C  CD2 . LEU   C  1 20  ? 10.033  42.313  -73.916  1.00 39.07  ? 321  LEU   C CD2 1 
ATOM   6981  N  N   . HIS   C  1 21  ? 6.879   40.689  -70.421  1.00 48.07  ? 322  HIS   C N   1 
ATOM   6982  C  CA  . HIS   C  1 21  ? 6.817   39.272  -70.077  1.00 49.44  ? 322  HIS   C CA  1 
ATOM   6983  C  C   . HIS   C  1 21  ? 5.410   38.698  -70.175  1.00 49.06  ? 322  HIS   C C   1 
ATOM   6984  O  O   . HIS   C  1 21  ? 5.262   37.474  -70.130  1.00 57.00  ? 322  HIS   C O   1 
ATOM   6985  C  CB  . HIS   C  1 21  ? 7.343   39.039  -68.654  1.00 53.72  ? 322  HIS   C CB  1 
ATOM   6986  C  CG  . HIS   C  1 21  ? 6.356   39.423  -67.599  1.00 42.63  ? 322  HIS   C CG  1 
ATOM   6987  N  ND1 . HIS   C  1 21  ? 5.346   38.576  -67.183  1.00 43.03  ? 322  HIS   C ND1 1 
ATOM   6988  C  CD2 . HIS   C  1 21  ? 6.169   40.590  -66.938  1.00 39.53  ? 322  HIS   C CD2 1 
ATOM   6989  C  CE1 . HIS   C  1 21  ? 4.599   39.196  -66.287  1.00 49.60  ? 322  HIS   C CE1 1 
ATOM   6990  N  NE2 . HIS   C  1 21  ? 5.079   40.417  -66.117  1.00 50.17  ? 322  HIS   C NE2 1 
ATOM   6991  N  N   . LEU   C  1 22  ? 4.373   39.526  -70.267  1.00 44.60  ? 323  LEU   C N   1 
ATOM   6992  C  CA  . LEU   C  1 22  ? 3.035   38.965  -70.396  1.00 44.14  ? 323  LEU   C CA  1 
ATOM   6993  C  C   . LEU   C  1 22  ? 2.748   38.474  -71.813  1.00 47.43  ? 323  LEU   C C   1 
ATOM   6994  O  O   . LEU   C  1 22  ? 1.737   37.804  -72.029  1.00 49.43  ? 323  LEU   C O   1 
ATOM   6995  C  CB  . LEU   C  1 22  ? 1.984   39.991  -69.955  1.00 42.49  ? 323  LEU   C CB  1 
ATOM   6996  C  CG  . LEU   C  1 22  ? 2.009   40.358  -68.474  1.00 57.15  ? 323  LEU   C CG  1 
ATOM   6997  C  CD1 . LEU   C  1 22  ? 1.727   41.832  -68.240  1.00 56.40  ? 323  LEU   C CD1 1 
ATOM   6998  C  CD2 . LEU   C  1 22  ? 0.987   39.523  -67.748  1.00 69.83  ? 323  LEU   C CD2 1 
ATOM   6999  N  N   . LYS   C  1 23  ? 3.620   38.770  -72.776  1.00 55.57  ? 324  LYS   C N   1 
ATOM   7000  C  CA  . LYS   C  1 23  ? 3.552   38.201  -74.114  1.00 53.42  ? 324  LYS   C CA  1 
ATOM   7001  C  C   . LYS   C  1 23  ? 4.363   36.924  -74.239  1.00 57.52  ? 324  LYS   C C   1 
ATOM   7002  O  O   . LYS   C  1 23  ? 4.768   36.564  -75.352  1.00 66.67  ? 324  LYS   C O   1 
ATOM   7003  C  CB  . LYS   C  1 23  ? 4.050   39.215  -75.149  1.00 59.65  ? 324  LYS   C CB  1 
ATOM   7004  C  CG  . LYS   C  1 23  ? 3.204   40.464  -75.271  1.00 70.69  ? 324  LYS   C CG  1 
ATOM   7005  C  CD  . LYS   C  1 23  ? 2.516   40.546  -76.634  1.00 78.32  ? 324  LYS   C CD  1 
ATOM   7006  C  CE  . LYS   C  1 23  ? 1.098   39.996  -76.582  1.00 80.82  ? 324  LYS   C CE  1 
ATOM   7007  N  NZ  . LYS   C  1 23  ? 0.322   40.318  -77.815  1.00 75.98  ? 324  LYS   C NZ  1 
ATOM   7008  N  N   . SER   C  1 24  ? 4.647   36.255  -73.127  1.00 58.46  ? 325  SER   C N   1 
ATOM   7009  C  CA  . SER   C  1 24  ? 5.510   35.083  -73.156  1.00 61.15  ? 325  SER   C CA  1 
ATOM   7010  C  C   . SER   C  1 24  ? 4.727   33.878  -73.644  1.00 67.14  ? 325  SER   C C   1 
ATOM   7011  O  O   . SER   C  1 24  ? 3.589   33.646  -73.222  1.00 64.27  ? 325  SER   C O   1 
ATOM   7012  C  CB  . SER   C  1 24  ? 6.091   34.809  -71.766  1.00 64.18  ? 325  SER   C CB  1 
ATOM   7013  O  OG  . SER   C  1 24  ? 6.663   33.514  -71.687  1.00 66.50  ? 325  SER   C OG  1 
ATOM   7014  N  N   . THR   C  1 25  ? 5.344   33.108  -74.535  1.00 81.98  ? 326  THR   C N   1 
ATOM   7015  C  CA  . THR   C  1 25  ? 4.643   32.037  -75.230  1.00 89.30  ? 326  THR   C CA  1 
ATOM   7016  C  C   . THR   C  1 25  ? 4.882   30.654  -74.627  1.00 91.24  ? 326  THR   C C   1 
ATOM   7017  O  O   . THR   C  1 25  ? 3.928   29.885  -74.469  1.00 99.38  ? 326  THR   C O   1 
ATOM   7018  C  CB  . THR   C  1 25  ? 5.038   32.036  -76.716  1.00 87.96  ? 326  THR   C CB  1 
ATOM   7019  O  OG1 . THR   C  1 25  ? 6.458   32.213  -76.853  1.00 89.35  ? 326  THR   C OG1 1 
ATOM   7020  C  CG2 . THR   C  1 25  ? 4.312   33.159  -77.466  1.00 79.84  ? 326  THR   C CG2 1 
ATOM   7021  N  N   . LEU   C  1 26  ? 6.118   30.325  -74.255  1.00 82.44  ? 327  LEU   C N   1 
ATOM   7022  C  CA  . LEU   C  1 26  ? 6.477   28.965  -73.876  1.00 79.79  ? 327  LEU   C CA  1 
ATOM   7023  C  C   . LEU   C  1 26  ? 6.913   28.849  -72.412  1.00 75.88  ? 327  LEU   C C   1 
ATOM   7024  O  O   . LEU   C  1 26  ? 7.269   29.832  -71.751  1.00 65.61  ? 327  LEU   C O   1 
ATOM   7025  C  CB  . LEU   C  1 26  ? 7.585   28.439  -74.793  1.00 84.86  ? 327  LEU   C CB  1 
ATOM   7026  C  CG  . LEU   C  1 26  ? 7.222   28.502  -76.282  1.00 86.36  ? 327  LEU   C CG  1 
ATOM   7027  C  CD1 . LEU   C  1 26  ? 8.372   28.050  -77.173  1.00 82.61  ? 327  LEU   C CD1 1 
ATOM   7028  C  CD2 . LEU   C  1 26  ? 5.972   27.671  -76.542  1.00 87.05  ? 327  LEU   C CD2 1 
ATOM   7029  N  N   . GLU   C  1 27  ? 6.870   27.611  -71.911  1.00 67.64  ? 328  GLU   C N   1 
ATOM   7030  C  CA  . GLU   C  1 27  ? 7.318   27.312  -70.558  1.00 60.55  ? 328  GLU   C CA  1 
ATOM   7031  C  C   . GLU   C  1 27  ? 8.832   27.467  -70.430  1.00 62.11  ? 328  GLU   C C   1 
ATOM   7032  O  O   . GLU   C  1 27  ? 9.592   27.147  -71.349  1.00 46.02  ? 328  GLU   C O   1 
ATOM   7033  C  CB  . GLU   C  1 27  ? 6.905   25.889  -70.151  1.00 52.94  ? 328  GLU   C CB  1 
ATOM   7034  C  CG  . GLU   C  1 27  ? 5.411   25.731  -69.861  1.00 54.68  ? 328  GLU   C CG  1 
ATOM   7035  C  CD  . GLU   C  1 27  ? 5.015   24.311  -69.514  1.00 63.07  ? 328  GLU   C CD  1 
ATOM   7036  O  OE1 . GLU   C  1 27  ? 5.901   23.434  -69.524  1.00 68.31  ? 328  GLU   C OE1 1 
ATOM   7037  O  OE2 . GLU   C  1 27  ? 3.819   24.072  -69.231  1.00 68.48  ? 328  GLU   C OE2 1 
ATOM   7038  N  N   . THR   C  1 28  ? 9.272   27.958  -69.269  1.00 67.08  ? 329  THR   C N   1 
ATOM   7039  C  CA  . THR   C  1 28  ? 10.694  28.017  -68.970  1.00 57.08  ? 329  THR   C CA  1 
ATOM   7040  C  C   . THR   C  1 28  ? 11.223  26.730  -68.363  1.00 44.42  ? 329  THR   C C   1 
ATOM   7041  O  O   . THR   C  1 28  ? 12.436  26.507  -68.396  1.00 47.49  ? 329  THR   C O   1 
ATOM   7042  C  CB  . THR   C  1 28  ? 10.985  29.156  -68.004  1.00 56.35  ? 329  THR   C CB  1 
ATOM   7043  O  OG1 . THR   C  1 28  ? 10.115  29.024  -66.867  1.00 60.35  ? 329  THR   C OG1 1 
ATOM   7044  C  CG2 . THR   C  1 28  ? 10.770  30.496  -68.696  1.00 51.84  ? 329  THR   C CG2 1 
ATOM   7045  N  N   . GLY   C  1 29  ? 10.346  25.876  -67.835  1.00 39.45  ? 330  GLY   C N   1 
ATOM   7046  C  CA  . GLY   C  1 29  ? 10.735  24.727  -67.059  1.00 53.60  ? 330  GLY   C CA  1 
ATOM   7047  C  C   . GLY   C  1 29  ? 10.582  24.925  -65.564  1.00 61.70  ? 330  GLY   C C   1 
ATOM   7048  O  O   . GLY   C  1 29  ? 10.417  23.939  -64.825  1.00 56.92  ? 330  GLY   C O   1 
ATOM   7049  N  N   . CYS   C  1 30  ? 10.611  26.176  -65.110  1.00 58.29  ? 331  CYS   C N   1 
ATOM   7050  C  CA  . CYS   C  1 30  ? 10.419  26.496  -63.706  1.00 45.24  ? 331  CYS   C CA  1 
ATOM   7051  C  C   . CYS   C  1 30  ? 8.957   26.312  -63.305  1.00 53.10  ? 331  CYS   C C   1 
ATOM   7052  O  O   . CYS   C  1 30  ? 8.041   26.348  -64.132  1.00 55.49  ? 331  CYS   C O   1 
ATOM   7053  C  CB  . CYS   C  1 30  ? 10.853  27.932  -63.435  1.00 36.75  ? 331  CYS   C CB  1 
ATOM   7054  S  SG  . CYS   C  1 30  ? 12.589  28.290  -63.782  1.00 45.69  ? 331  CYS   C SG  1 
ATOM   7055  N  N   . THR   C  1 31  ? 8.742   26.098  -62.015  1.00 41.81  ? 332  THR   C N   1 
ATOM   7056  C  CA  . THR   C  1 31  ? 7.410   26.182  -61.443  1.00 45.66  ? 332  THR   C CA  1 
ATOM   7057  C  C   . THR   C  1 31  ? 7.475   27.094  -60.229  1.00 51.37  ? 332  THR   C C   1 
ATOM   7058  O  O   . THR   C  1 31  ? 8.537   27.614  -59.878  1.00 64.58  ? 332  THR   C O   1 
ATOM   7059  C  CB  . THR   C  1 31  ? 6.872   24.802  -61.057  1.00 52.72  ? 332  THR   C CB  1 
ATOM   7060  O  OG1 . THR   C  1 31  ? 7.539   24.334  -59.867  1.00 52.12  ? 332  THR   C OG1 1 
ATOM   7061  C  CG2 . THR   C  1 31  ? 7.082   23.814  -62.192  1.00 47.55  ? 332  THR   C CG2 1 
ATOM   7062  N  N   . GLU   C  1 32  ? 6.338   27.285  -59.564  1.00 53.78  ? 333  GLU   C N   1 
ATOM   7063  C  CA  . GLU   C  1 32  ? 6.383   27.973  -58.282  1.00 60.37  ? 333  GLU   C CA  1 
ATOM   7064  C  C   . GLU   C  1 32  ? 7.280   27.253  -57.281  1.00 54.83  ? 333  GLU   C C   1 
ATOM   7065  O  O   . GLU   C  1 32  ? 7.797   27.894  -56.360  1.00 54.68  ? 333  GLU   C O   1 
ATOM   7066  C  CB  . GLU   C  1 32  ? 4.969   28.122  -57.717  1.00 76.95  ? 333  GLU   C CB  1 
ATOM   7067  C  CG  . GLU   C  1 32  ? 4.361   29.484  -57.954  1.00 91.33  ? 333  GLU   C CG  1 
ATOM   7068  C  CD  . GLU   C  1 32  ? 3.387   29.493  -59.112  1.00 107.98 ? 333  GLU   C CD  1 
ATOM   7069  O  OE1 . GLU   C  1 32  ? 2.352   30.189  -58.993  1.00 118.30 ? 333  GLU   C OE1 1 
ATOM   7070  O  OE2 . GLU   C  1 32  ? 3.649   28.804  -60.129  1.00 102.97 ? 333  GLU   C OE2 1 
ATOM   7071  N  N   . TYR   C  1 33  ? 7.517   25.947  -57.472  1.00 49.14  ? 334  TYR   C N   1 
ATOM   7072  C  CA  . TYR   C  1 33  ? 8.201   25.105  -56.502  1.00 49.86  ? 334  TYR   C CA  1 
ATOM   7073  C  C   . TYR   C  1 33  ? 9.610   24.680  -56.894  1.00 50.54  ? 334  TYR   C C   1 
ATOM   7074  O  O   . TYR   C  1 33  ? 10.376  24.266  -56.020  1.00 60.20  ? 334  TYR   C O   1 
ATOM   7075  C  CB  . TYR   C  1 33  ? 7.368   23.848  -56.232  1.00 53.96  ? 334  TYR   C CB  1 
ATOM   7076  C  CG  . TYR   C  1 33  ? 6.036   24.190  -55.656  1.00 62.91  ? 334  TYR   C CG  1 
ATOM   7077  C  CD1 . TYR   C  1 33  ? 5.827   24.154  -54.286  1.00 65.20  ? 334  TYR   C CD1 1 
ATOM   7078  C  CD2 . TYR   C  1 33  ? 4.992   24.598  -56.473  1.00 59.87  ? 334  TYR   C CD2 1 
ATOM   7079  C  CE1 . TYR   C  1 33  ? 4.611   24.489  -53.744  1.00 70.42  ? 334  TYR   C CE1 1 
ATOM   7080  C  CE2 . TYR   C  1 33  ? 3.771   24.936  -55.940  1.00 62.87  ? 334  TYR   C CE2 1 
ATOM   7081  C  CZ  . TYR   C  1 33  ? 3.590   24.872  -54.574  1.00 73.07  ? 334  TYR   C CZ  1 
ATOM   7082  O  OH  . TYR   C  1 33  ? 2.383   25.200  -54.027  1.00 88.71  ? 334  TYR   C OH  1 
ATOM   7083  N  N   . ILE   C  1 34  ? 9.976   24.750  -58.162  1.00 52.35  ? 335  ILE   C N   1 
ATOM   7084  C  CA  . ILE   C  1 34  ? 11.320  24.384  -58.583  1.00 53.07  ? 335  ILE   C CA  1 
ATOM   7085  C  C   . ILE   C  1 34  ? 11.764  25.382  -59.636  1.00 47.64  ? 335  ILE   C C   1 
ATOM   7086  O  O   . ILE   C  1 34  ? 10.953  25.847  -60.440  1.00 52.87  ? 335  ILE   C O   1 
ATOM   7087  C  CB  . ILE   C  1 34  ? 11.373  22.942  -59.113  1.00 57.12  ? 335  ILE   C CB  1 
ATOM   7088  C  CG1 . ILE   C  1 34  ? 12.815  22.458  -59.200  1.00 62.11  ? 335  ILE   C CG1 1 
ATOM   7089  C  CG2 . ILE   C  1 34  ? 10.719  22.862  -60.465  1.00 62.10  ? 335  ILE   C CG2 1 
ATOM   7090  C  CD1 . ILE   C  1 34  ? 12.923  20.952  -59.261  1.00 69.40  ? 335  ILE   C CD1 1 
ATOM   7091  N  N   . CYS   C  1 35  ? 13.040  25.748  -59.602  1.00 39.64  ? 336  CYS   C N   1 
ATOM   7092  C  CA  . CYS   C  1 35  ? 13.611  26.710  -60.532  1.00 41.40  ? 336  CYS   C CA  1 
ATOM   7093  C  C   . CYS   C  1 35  ? 14.741  26.043  -61.282  1.00 48.18  ? 336  CYS   C C   1 
ATOM   7094  O  O   . CYS   C  1 35  ? 15.601  25.405  -60.663  1.00 35.36  ? 336  CYS   C O   1 
ATOM   7095  C  CB  . CYS   C  1 35  ? 14.153  27.949  -59.832  1.00 35.33  ? 336  CYS   C CB  1 
ATOM   7096  S  SG  . CYS   C  1 35  ? 15.379  28.780  -60.844  1.00 43.39  ? 336  CYS   C SG  1 
ATOM   7097  N  N   . MET   C  1 36  ? 14.752  26.228  -62.610  1.00 44.33  ? 337  MET   C N   1 
ATOM   7098  C  CA  . MET   C  1 36  ? 15.643  25.498  -63.500  1.00 37.20  ? 337  MET   C CA  1 
ATOM   7099  C  C   . MET   C  1 36  ? 16.564  26.424  -64.270  1.00 38.98  ? 337  MET   C C   1 
ATOM   7100  O  O   . MET   C  1 36  ? 17.111  26.025  -65.304  1.00 36.52  ? 337  MET   C O   1 
ATOM   7101  C  CB  . MET   C  1 36  ? 14.833  24.619  -64.453  1.00 34.32  ? 337  MET   C CB  1 
ATOM   7102  C  CG  . MET   C  1 36  ? 13.979  23.598  -63.744  1.00 51.98  ? 337  MET   C CG  1 
ATOM   7103  S  SD  . MET   C  1 36  ? 13.752  22.156  -64.784  1.00 64.44  ? 337  MET   C SD  1 
ATOM   7104  C  CE  . MET   C  1 36  ? 12.387  21.345  -63.952  1.00 67.43  ? 337  MET   C CE  1 
ATOM   7105  N  N   . GLY   C  1 37  ? 16.790  27.634  -63.753  1.00 46.49  ? 338  GLY   C N   1 
ATOM   7106  C  CA  . GLY   C  1 37  ? 17.511  28.679  -64.476  1.00 42.10  ? 338  GLY   C CA  1 
ATOM   7107  C  C   . GLY   C  1 37  ? 18.947  28.353  -64.840  1.00 41.00  ? 338  GLY   C C   1 
ATOM   7108  O  O   . GLY   C  1 37  ? 19.563  29.139  -65.571  1.00 46.13  ? 338  GLY   C O   1 
ATOM   7109  N  N   . SER   C  1 38  ? 19.494  27.248  -64.338  1.00 39.23  ? 339  SER   C N   1 
ATOM   7110  C  CA  . SER   C  1 38  ? 20.837  26.781  -64.658  1.00 40.25  ? 339  SER   C CA  1 
ATOM   7111  C  C   . SER   C  1 38  ? 20.839  25.433  -65.377  1.00 43.80  ? 339  SER   C C   1 
ATOM   7112  O  O   . SER   C  1 38  ? 21.917  24.878  -65.646  1.00 43.55  ? 339  SER   C O   1 
ATOM   7113  C  CB  . SER   C  1 38  ? 21.686  26.678  -63.384  1.00 38.72  ? 339  SER   C CB  1 
ATOM   7114  O  OG  . SER   C  1 38  ? 21.311  25.566  -62.573  1.00 44.60  ? 339  SER   C OG  1 
ATOM   7115  N  N   . ILE   C  1 39  ? 19.666  24.863  -65.647  1.00 38.75  ? 340  ILE   C N   1 
ATOM   7116  C  CA  . ILE   C  1 39  ? 19.579  23.751  -66.580  1.00 48.94  ? 340  ILE   C CA  1 
ATOM   7117  C  C   . ILE   C  1 39  ? 19.843  24.256  -67.997  1.00 46.43  ? 340  ILE   C C   1 
ATOM   7118  O  O   . ILE   C  1 39  ? 19.364  25.334  -68.391  1.00 50.75  ? 340  ILE   C O   1 
ATOM   7119  C  CB  . ILE   C  1 39  ? 18.203  23.086  -66.456  1.00 49.23  ? 340  ILE   C CB  1 
ATOM   7120  C  CG1 . ILE   C  1 39  ? 18.031  22.569  -65.034  1.00 48.33  ? 340  ILE   C CG1 1 
ATOM   7121  C  CG2 . ILE   C  1 39  ? 18.069  21.949  -67.454  1.00 54.19  ? 340  ILE   C CG2 1 
ATOM   7122  C  CD1 . ILE   C  1 39  ? 18.906  21.365  -64.754  1.00 55.58  ? 340  ILE   C CD1 1 
ATOM   7123  N  N   . MET   C  1 40  ? 20.635  23.488  -68.763  1.00 39.35  ? 341  MET   C N   1 
ATOM   7124  C  CA  . MET   C  1 40  ? 21.011  23.895  -70.120  1.00 50.53  ? 341  MET   C CA  1 
ATOM   7125  C  C   . MET   C  1 40  ? 19.825  23.801  -71.086  1.00 55.64  ? 341  MET   C C   1 
ATOM   7126  O  O   . MET   C  1 40  ? 19.549  24.752  -71.834  1.00 46.17  ? 341  MET   C O   1 
ATOM   7127  C  CB  . MET   C  1 40  ? 22.186  23.044  -70.614  1.00 57.84  ? 341  MET   C CB  1 
ATOM   7128  C  CG  . MET   C  1 40  ? 22.413  23.085  -72.130  1.00 74.73  ? 341  MET   C CG  1 
ATOM   7129  S  SD  . MET   C  1 40  ? 23.367  24.489  -72.750  1.00 80.85  ? 341  MET   C SD  1 
ATOM   7130  C  CE  . MET   C  1 40  ? 24.835  24.361  -71.698  1.00 81.13  ? 341  MET   C CE  1 
ATOM   7131  N  N   . HIS   C  1 41  ? 19.117  22.655  -71.087  1.00 59.96  ? 342  HIS   C N   1 
ATOM   7132  C  CA  . HIS   C  1 41  ? 17.909  22.436  -71.890  1.00 50.79  ? 342  HIS   C CA  1 
ATOM   7133  C  C   . HIS   C  1 41  ? 16.740  22.174  -70.949  1.00 51.34  ? 342  HIS   C C   1 
ATOM   7134  O  O   . HIS   C  1 41  ? 16.316  21.021  -70.767  1.00 53.42  ? 342  HIS   C O   1 
ATOM   7135  C  CB  . HIS   C  1 41  ? 18.074  21.269  -72.855  1.00 53.48  ? 342  HIS   C CB  1 
ATOM   7136  C  CG  . HIS   C  1 41  ? 19.346  21.318  -73.627  1.00 65.40  ? 342  HIS   C CG  1 
ATOM   7137  N  ND1 . HIS   C  1 41  ? 19.741  22.431  -74.338  1.00 67.31  ? 342  HIS   C ND1 1 
ATOM   7138  C  CD2 . HIS   C  1 41  ? 20.314  20.388  -73.803  1.00 71.81  ? 342  HIS   C CD2 1 
ATOM   7139  C  CE1 . HIS   C  1 41  ? 20.901  22.183  -74.921  1.00 71.24  ? 342  HIS   C CE1 1 
ATOM   7140  N  NE2 . HIS   C  1 41  ? 21.272  20.953  -74.608  1.00 74.30  ? 342  HIS   C NE2 1 
ATOM   7141  N  N   . PRO   C  1 42  ? 16.190  23.215  -70.329  1.00 54.57  ? 343  PRO   C N   1 
ATOM   7142  C  CA  . PRO   C  1 42  ? 15.223  22.983  -69.244  1.00 56.98  ? 343  PRO   C CA  1 
ATOM   7143  C  C   . PRO   C  1 42  ? 13.840  22.586  -69.718  1.00 61.57  ? 343  PRO   C C   1 
ATOM   7144  O  O   . PRO   C  1 42  ? 13.080  22.020  -68.925  1.00 65.86  ? 343  PRO   C O   1 
ATOM   7145  C  CB  . PRO   C  1 42  ? 15.197  24.329  -68.510  1.00 62.88  ? 343  PRO   C CB  1 
ATOM   7146  C  CG  . PRO   C  1 42  ? 15.561  25.334  -69.570  1.00 60.88  ? 343  PRO   C CG  1 
ATOM   7147  C  CD  . PRO   C  1 42  ? 16.498  24.644  -70.527  1.00 54.24  ? 343  PRO   C CD  1 
ATOM   7148  N  N   . SER   C  1 43  ? 13.493  22.837  -70.976  1.00 68.41  ? 344  SER   C N   1 
ATOM   7149  C  CA  . SER   C  1 43  ? 12.125  22.671  -71.448  1.00 66.58  ? 344  SER   C CA  1 
ATOM   7150  C  C   . SER   C  1 43  ? 12.124  21.922  -72.771  1.00 64.56  ? 344  SER   C C   1 
ATOM   7151  O  O   . SER   C  1 43  ? 13.071  22.012  -73.557  1.00 60.29  ? 344  SER   C O   1 
ATOM   7152  C  CB  . SER   C  1 43  ? 11.419  24.041  -71.618  1.00 56.70  ? 344  SER   C CB  1 
ATOM   7153  O  OG  . SER   C  1 43  ? 10.006  23.935  -71.499  1.00 50.81  ? 344  SER   C OG  1 
ATOM   7154  N  N   . GLN   C  1 44  ? 11.056  21.163  -72.996  1.00 71.40  ? 345  GLN   C N   1 
ATOM   7155  C  CA  . GLN   C  1 44  ? 10.768  20.586  -74.304  1.00 76.09  ? 345  GLN   C CA  1 
ATOM   7156  C  C   . GLN   C  1 44  ? 9.476   21.126  -74.899  1.00 82.16  ? 345  GLN   C C   1 
ATOM   7157  O  O   . GLN   C  1 44  ? 8.999   20.588  -75.908  1.00 89.30  ? 345  GLN   C O   1 
ATOM   7158  C  CB  . GLN   C  1 44  ? 10.700  19.066  -74.212  1.00 75.03  ? 345  GLN   C CB  1 
ATOM   7159  C  CG  . GLN   C  1 44  ? 11.940  18.435  -73.639  1.00 79.35  ? 345  GLN   C CG  1 
ATOM   7160  C  CD  . GLN   C  1 44  ? 11.693  16.998  -73.239  1.00 88.58  ? 345  GLN   C CD  1 
ATOM   7161  O  OE1 . GLN   C  1 44  ? 11.381  16.714  -72.081  1.00 95.85  ? 345  GLN   C OE1 1 
ATOM   7162  N  NE2 . GLN   C  1 44  ? 11.813  16.081  -74.200  1.00 84.79  ? 345  GLN   C NE2 1 
ATOM   7163  N  N   . HIS   C  1 45  ? 8.895   22.169  -74.294  1.00 81.38  ? 346  HIS   C N   1 
ATOM   7164  C  CA  . HIS   C  1 45  ? 7.700   22.832  -74.807  1.00 84.42  ? 346  HIS   C CA  1 
ATOM   7165  C  C   . HIS   C  1 45  ? 7.995   23.457  -76.164  1.00 83.54  ? 346  HIS   C C   1 
ATOM   7166  O  O   . HIS   C  1 45  ? 8.789   24.401  -76.258  1.00 72.51  ? 346  HIS   C O   1 
ATOM   7167  C  CB  . HIS   C  1 45  ? 7.210   23.910  -73.830  1.00 78.50  ? 346  HIS   C CB  1 
ATOM   7168  C  CG  . HIS   C  1 45  ? 5.767   24.292  -74.005  1.00 75.12  ? 346  HIS   C CG  1 
ATOM   7169  N  ND1 . HIS   C  1 45  ? 5.292   25.560  -73.738  1.00 75.86  ? 346  HIS   C ND1 1 
ATOM   7170  C  CD2 . HIS   C  1 45  ? 4.693   23.567  -74.398  1.00 75.61  ? 346  HIS   C CD2 1 
ATOM   7171  C  CE1 . HIS   C  1 45  ? 3.991   25.600  -73.962  1.00 74.77  ? 346  HIS   C CE1 1 
ATOM   7172  N  NE2 . HIS   C  1 45  ? 3.603   24.404  -74.364  1.00 75.61  ? 346  HIS   C NE2 1 
ATOM   7173  N  N   . ALA   C  1 46  ? 7.360   22.929  -77.212  1.00 88.20  ? 347  ALA   C N   1 
ATOM   7174  C  CA  . ALA   C  1 46  ? 7.495   23.424  -78.573  1.00 80.66  ? 347  ALA   C CA  1 
ATOM   7175  C  C   . ALA   C  1 46  ? 6.150   23.949  -79.057  1.00 81.06  ? 347  ALA   C C   1 
ATOM   7176  O  O   . ALA   C  1 46  ? 5.091   23.579  -78.541  1.00 77.55  ? 347  ALA   C O   1 
ATOM   7177  C  CB  . ALA   C  1 46  ? 8.012   22.327  -79.519  1.00 74.72  ? 347  ALA   C CB  1 
ATOM   7178  N  N   . ARG   C  1 47  ? 6.201   24.814  -80.071  1.00 92.22  ? 348  ARG   C N   1 
ATOM   7179  C  CA  . ARG   C  1 47  ? 4.993   25.483  -80.545  1.00 97.21  ? 348  ARG   C CA  1 
ATOM   7180  C  C   . ARG   C  1 47  ? 4.190   24.651  -81.548  1.00 97.86  ? 348  ARG   C C   1 
ATOM   7181  O  O   . ARG   C  1 47  ? 2.975   24.855  -81.677  1.00 92.09  ? 348  ARG   C O   1 
ATOM   7182  C  CB  . ARG   C  1 47  ? 5.366   26.842  -81.136  1.00 94.12  ? 348  ARG   C CB  1 
ATOM   7183  C  CG  . ARG   C  1 47  ? 5.610   27.900  -80.075  1.00 88.26  ? 348  ARG   C CG  1 
ATOM   7184  C  CD  . ARG   C  1 47  ? 6.332   29.104  -80.635  1.00 90.69  ? 348  ARG   C CD  1 
ATOM   7185  N  NE  . ARG   C  1 47  ? 5.597   29.756  -81.716  1.00 93.76  ? 348  ARG   C NE  1 
ATOM   7186  C  CZ  . ARG   C  1 47  ? 4.560   30.566  -81.536  1.00 91.30  ? 348  ARG   C CZ  1 
ATOM   7187  N  NH1 . ARG   C  1 47  ? 4.123   30.824  -80.309  1.00 83.14  ? 348  ARG   C NH1 1 
ATOM   7188  N  NH2 . ARG   C  1 47  ? 3.952   31.112  -82.585  1.00 91.98  ? 348  ARG   C NH2 1 
ATOM   7189  N  N   . ARG   C  1 48  ? 4.826   23.708  -82.243  1.00 97.23  ? 349  ARG   C N   1 
ATOM   7190  C  CA  . ARG   C  1 48  ? 4.118   22.815  -83.146  1.00 89.24  ? 349  ARG   C CA  1 
ATOM   7191  C  C   . ARG   C  1 48  ? 4.628   21.390  -82.961  1.00 83.09  ? 349  ARG   C C   1 
ATOM   7192  O  O   . ARG   C  1 48  ? 5.832   21.182  -82.746  1.00 87.09  ? 349  ARG   C O   1 
ATOM   7193  C  CB  . ARG   C  1 48  ? 4.278   23.264  -84.607  1.00 83.39  ? 349  ARG   C CB  1 
ATOM   7194  C  CG  . ARG   C  1 48  ? 5.581   24.000  -84.897  1.00 76.86  ? 349  ARG   C CG  1 
ATOM   7195  C  CD  . ARG   C  1 48  ? 6.475   23.181  -85.792  1.00 81.39  ? 349  ARG   C CD  1 
ATOM   7196  N  NE  . ARG   C  1 48  ? 5.763   22.737  -86.985  1.00 89.02  ? 349  ARG   C NE  1 
ATOM   7197  C  CZ  . ARG   C  1 48  ? 5.264   21.514  -87.146  1.00 99.54  ? 349  ARG   C CZ  1 
ATOM   7198  N  NH1 . ARG   C  1 48  ? 5.403   20.608  -86.188  1.00 105.91 ? 349  ARG   C NH1 1 
ATOM   7199  N  NH2 . ARG   C  1 48  ? 4.628   21.193  -88.263  1.00 102.62 ? 349  ARG   C NH2 1 
ATOM   7200  N  N   . PRO   C  1 49  ? 3.740   20.407  -83.018  1.00 81.45  ? 350  PRO   C N   1 
ATOM   7201  C  CA  . PRO   C  1 49  ? 4.104   19.022  -82.670  1.00 89.72  ? 350  PRO   C CA  1 
ATOM   7202  C  C   . PRO   C  1 49  ? 5.216   18.363  -83.486  1.00 109.60 ? 350  PRO   C C   1 
ATOM   7203  O  O   . PRO   C  1 49  ? 6.041   19.019  -84.132  1.00 106.11 ? 350  PRO   C O   1 
ATOM   7204  C  CB  . PRO   C  1 49  ? 2.788   18.256  -82.876  1.00 85.01  ? 350  PRO   C CB  1 
ATOM   7205  C  CG  . PRO   C  1 49  ? 1.712   19.273  -82.874  1.00 89.18  ? 350  PRO   C CG  1 
ATOM   7206  C  CD  . PRO   C  1 49  ? 2.294   20.649  -82.938  1.00 86.16  ? 350  PRO   C CD  1 
ATOM   7207  N  N   . GLU   C  1 50  ? 5.219   17.026  -83.452  1.00 131.01 ? 351  GLU   C N   1 
ATOM   7208  C  CA  . GLU   C  1 50  ? 6.299   16.191  -83.971  1.00 132.22 ? 351  GLU   C CA  1 
ATOM   7209  C  C   . GLU   C  1 50  ? 6.598   16.427  -85.446  1.00 126.03 ? 351  GLU   C C   1 
ATOM   7210  O  O   . GLU   C  1 50  ? 7.671   16.937  -85.787  1.00 122.87 ? 351  GLU   C O   1 
ATOM   7211  C  CB  . GLU   C  1 50  ? 5.967   14.713  -83.750  1.00 139.78 ? 351  GLU   C CB  1 
ATOM   7212  C  CG  . GLU   C  1 50  ? 6.318   14.193  -82.369  1.00 143.01 ? 351  GLU   C CG  1 
ATOM   7213  C  CD  . GLU   C  1 50  ? 7.410   13.143  -82.418  1.00 143.52 ? 351  GLU   C CD  1 
ATOM   7214  O  OE1 . GLU   C  1 50  ? 7.719   12.669  -83.537  1.00 144.46 ? 351  GLU   C OE1 1 
ATOM   7215  O  OE2 . GLU   C  1 50  ? 7.954   12.798  -81.344  1.00 141.03 ? 351  GLU   C OE2 1 
ATOM   7216  N  N   . ASP   C  1 51  ? 5.674   16.038  -86.325  1.00 125.02 ? 352  ASP   C N   1 
ATOM   7217  C  CA  . ASP   C  1 51  ? 5.875   16.123  -87.761  1.00 117.39 ? 352  ASP   C CA  1 
ATOM   7218  C  C   . ASP   C  1 51  ? 4.934   17.168  -88.363  1.00 112.74 ? 352  ASP   C C   1 
ATOM   7219  O  O   . ASP   C  1 51  ? 4.511   18.110  -87.673  1.00 104.97 ? 352  ASP   C O   1 
ATOM   7220  C  CB  . ASP   C  1 51  ? 5.694   14.734  -88.386  1.00 112.35 ? 352  ASP   C CB  1 
ATOM   7221  C  CG  . ASP   C  1 51  ? 6.995   13.945  -88.438  1.00 105.84 ? 352  ASP   C CG  1 
ATOM   7222  O  OD1 . ASP   C  1 51  ? 8.032   14.495  -88.875  1.00 97.69  ? 352  ASP   C OD1 1 
ATOM   7223  O  OD2 . ASP   C  1 51  ? 6.973   12.767  -88.029  1.00 104.05 ? 352  ASP   C OD2 1 
ATOM   7224  N  N   . VAL   C  1 52  ? 4.606   16.992  -89.651  1.00 114.94 ? 353  VAL   C N   1 
ATOM   7225  C  CA  . VAL   C  1 52  ? 3.911   18.025  -90.415  1.00 111.67 ? 353  VAL   C CA  1 
ATOM   7226  C  C   . VAL   C  1 52  ? 2.543   18.280  -89.796  1.00 112.68 ? 353  VAL   C C   1 
ATOM   7227  O  O   . VAL   C  1 52  ? 1.702   17.374  -89.707  1.00 116.05 ? 353  VAL   C O   1 
ATOM   7228  C  CB  . VAL   C  1 52  ? 3.823   17.626  -91.892  1.00 100.32 ? 353  VAL   C CB  1 
ATOM   7229  C  CG1 . VAL   C  1 52  ? 3.492   16.144  -92.031  1.00 100.58 ? 353  VAL   C CG1 1 
ATOM   7230  C  CG2 . VAL   C  1 52  ? 2.809   18.501  -92.626  1.00 94.23  ? 353  VAL   C CG2 1 
ATOM   7231  N  N   . ALA   C  1 53  ? 2.321   19.522  -89.357  1.00 99.46  ? 354  ALA   C N   1 
ATOM   7232  C  CA  . ALA   C  1 53  ? 1.175   19.860  -88.527  1.00 83.08  ? 354  ALA   C CA  1 
ATOM   7233  C  C   . ALA   C  1 53  ? -0.111  19.954  -89.341  1.00 79.05  ? 354  ALA   C C   1 
ATOM   7234  O  O   . ALA   C  1 53  ? -0.101  20.203  -90.553  1.00 85.52  ? 354  ALA   C O   1 
ATOM   7235  C  CB  . ALA   C  1 53  ? 1.417   21.190  -87.806  1.00 79.37  ? 354  ALA   C CB  1 
ATOM   7236  N  N   . THR   C  1 54  ? -1.231  19.739  -88.654  1.00 72.01  ? 355  THR   C N   1 
ATOM   7237  C  CA  . THR   C  1 54  ? -2.542  20.007  -89.223  1.00 69.92  ? 355  THR   C CA  1 
ATOM   7238  C  C   . THR   C  1 54  ? -2.728  21.521  -89.394  1.00 66.86  ? 355  THR   C C   1 
ATOM   7239  O  O   . THR   C  1 54  ? -1.849  22.329  -89.075  1.00 64.30  ? 355  THR   C O   1 
ATOM   7240  C  CB  . THR   C  1 54  ? -3.647  19.400  -88.346  1.00 70.88  ? 355  THR   C CB  1 
ATOM   7241  O  OG1 . THR   C  1 54  ? -3.617  20.000  -87.046  1.00 75.92  ? 355  THR   C OG1 1 
ATOM   7242  C  CG2 . THR   C  1 54  ? -3.469  17.896  -88.188  1.00 57.18  ? 355  THR   C CG2 1 
ATOM   7243  N  N   . LYS   C  1 55  ? -3.895  21.916  -89.906  1.00 70.44  ? 356  LYS   C N   1 
ATOM   7244  C  CA  . LYS   C  1 55  ? -4.146  23.336  -90.126  1.00 65.81  ? 356  LYS   C CA  1 
ATOM   7245  C  C   . LYS   C  1 55  ? -4.443  24.060  -88.822  1.00 63.15  ? 356  LYS   C C   1 
ATOM   7246  O  O   . LYS   C  1 55  ? -3.984  25.190  -88.622  1.00 59.44  ? 356  LYS   C O   1 
ATOM   7247  C  CB  . LYS   C  1 55  ? -5.293  23.530  -91.108  1.00 70.31  ? 356  LYS   C CB  1 
ATOM   7248  C  CG  . LYS   C  1 55  ? -5.255  24.872  -91.801  1.00 76.22  ? 356  LYS   C CG  1 
ATOM   7249  C  CD  . LYS   C  1 55  ? -6.032  24.817  -93.104  1.00 85.88  ? 356  LYS   C CD  1 
ATOM   7250  C  CE  . LYS   C  1 55  ? -7.377  25.481  -92.946  1.00 88.70  ? 356  LYS   C CE  1 
ATOM   7251  N  NZ  . LYS   C  1 55  ? -7.215  26.960  -92.940  1.00 86.14  ? 356  LYS   C NZ  1 
ATOM   7252  N  N   . ASP   C  1 56  ? -5.228  23.440  -87.928  1.00 72.90  ? 357  ASP   C N   1 
ATOM   7253  C  CA  . ASP   C  1 56  ? -5.533  24.086  -86.654  1.00 73.58  ? 357  ASP   C CA  1 
ATOM   7254  C  C   . ASP   C  1 56  ? -4.316  24.149  -85.746  1.00 65.85  ? 357  ASP   C C   1 
ATOM   7255  O  O   . ASP   C  1 56  ? -4.347  24.885  -84.760  1.00 61.44  ? 357  ASP   C O   1 
ATOM   7256  C  CB  . ASP   C  1 56  ? -6.705  23.397  -85.928  1.00 77.06  ? 357  ASP   C CB  1 
ATOM   7257  C  CG  . ASP   C  1 56  ? -6.428  21.938  -85.543  1.00 81.45  ? 357  ASP   C CG  1 
ATOM   7258  O  OD1 . ASP   C  1 56  ? -5.257  21.543  -85.351  1.00 80.67  ? 357  ASP   C OD1 1 
ATOM   7259  O  OD2 . ASP   C  1 56  ? -7.413  21.176  -85.413  1.00 79.78  ? 357  ASP   C OD2 1 
ATOM   7260  N  N   . GLN   C  1 57  ? -3.251  23.403  -86.068  1.00 62.07  ? 358  GLN   C N   1 
ATOM   7261  C  CA  . GLN   C  1 57  ? -1.980  23.535  -85.365  1.00 64.58  ? 358  GLN   C CA  1 
ATOM   7262  C  C   . GLN   C  1 57  ? -1.148  24.682  -85.923  1.00 64.38  ? 358  GLN   C C   1 
ATOM   7263  O  O   . GLN   C  1 57  ? -0.699  25.555  -85.173  1.00 73.24  ? 358  GLN   C O   1 
ATOM   7264  C  CB  . GLN   C  1 57  ? -1.194  22.223  -85.441  1.00 69.28  ? 358  GLN   C CB  1 
ATOM   7265  C  CG  . GLN   C  1 57  ? -1.593  21.220  -84.368  1.00 76.98  ? 358  GLN   C CG  1 
ATOM   7266  C  CD  . GLN   C  1 57  ? -1.146  19.807  -84.683  1.00 79.80  ? 358  GLN   C CD  1 
ATOM   7267  O  OE1 . GLN   C  1 57  ? -0.167  19.594  -85.407  1.00 76.74  ? 358  GLN   C OE1 1 
ATOM   7268  N  NE2 . GLN   C  1 57  ? -1.865  18.826  -84.137  1.00 77.22  ? 358  GLN   C NE2 1 
ATOM   7269  N  N   . LEU   C  1 58  ? -0.942  24.710  -87.238  1.00 69.57  ? 359  LEU   C N   1 
ATOM   7270  C  CA  . LEU   C  1 58  ? 0.003   25.673  -87.784  1.00 67.26  ? 359  LEU   C CA  1 
ATOM   7271  C  C   . LEU   C  1 58  ? -0.609  27.061  -87.987  1.00 65.16  ? 359  LEU   C C   1 
ATOM   7272  O  O   . LEU   C  1 58  ? 0.092   28.069  -87.829  1.00 51.72  ? 359  LEU   C O   1 
ATOM   7273  C  CB  . LEU   C  1 58  ? 0.586   25.154  -89.095  1.00 57.55  ? 359  LEU   C CB  1 
ATOM   7274  C  CG  . LEU   C  1 58  ? 1.768   26.013  -89.537  1.00 56.90  ? 359  LEU   C CG  1 
ATOM   7275  C  CD1 . LEU   C  1 58  ? 3.004   25.685  -88.693  1.00 56.29  ? 359  LEU   C CD1 1 
ATOM   7276  C  CD2 . LEU   C  1 58  ? 2.037   25.907  -91.047  1.00 54.16  ? 359  LEU   C CD2 1 
ATOM   7277  N  N   . PHE   C  1 59  ? -1.895  27.157  -88.342  1.00 60.53  ? 360  PHE   C N   1 
ATOM   7278  C  CA  . PHE   C  1 59  ? -2.443  28.484  -88.629  1.00 57.15  ? 360  PHE   C CA  1 
ATOM   7279  C  C   . PHE   C  1 59  ? -2.407  29.444  -87.444  1.00 57.05  ? 360  PHE   C C   1 
ATOM   7280  O  O   . PHE   C  1 59  ? -2.039  30.615  -87.653  1.00 53.17  ? 360  PHE   C O   1 
ATOM   7281  C  CB  . PHE   C  1 59  ? -3.877  28.418  -89.164  1.00 56.28  ? 360  PHE   C CB  1 
ATOM   7282  C  CG  . PHE   C  1 59  ? -4.429  29.780  -89.508  1.00 66.79  ? 360  PHE   C CG  1 
ATOM   7283  C  CD1 . PHE   C  1 59  ? -4.057  30.409  -90.689  1.00 72.71  ? 360  PHE   C CD1 1 
ATOM   7284  C  CD2 . PHE   C  1 59  ? -5.271  30.453  -88.634  1.00 74.26  ? 360  PHE   C CD2 1 
ATOM   7285  C  CE1 . PHE   C  1 59  ? -4.536  31.663  -91.003  1.00 73.83  ? 360  PHE   C CE1 1 
ATOM   7286  C  CE2 . PHE   C  1 59  ? -5.753  31.715  -88.943  1.00 75.21  ? 360  PHE   C CE2 1 
ATOM   7287  C  CZ  . PHE   C  1 59  ? -5.383  32.317  -90.128  1.00 75.64  ? 360  PHE   C CZ  1 
ATOM   7288  N  N   . PRO   C  1 60  ? -2.780  29.055  -86.216  1.00 61.12  ? 361  PRO   C N   1 
ATOM   7289  C  CA  . PRO   C  1 60  ? -2.820  30.055  -85.130  1.00 47.49  ? 361  PRO   C CA  1 
ATOM   7290  C  C   . PRO   C  1 60  ? -1.472  30.669  -84.849  1.00 45.84  ? 361  PRO   C C   1 
ATOM   7291  O  O   . PRO   C  1 60  ? -1.388  31.873  -84.563  1.00 45.48  ? 361  PRO   C O   1 
ATOM   7292  C  CB  . PRO   C  1 60  ? -3.352  29.251  -83.943  1.00 56.80  ? 361  PRO   C CB  1 
ATOM   7293  C  CG  . PRO   C  1 60  ? -4.162  28.147  -84.588  1.00 66.56  ? 361  PRO   C CG  1 
ATOM   7294  C  CD  . PRO   C  1 60  ? -3.335  27.761  -85.777  1.00 64.65  ? 361  PRO   C CD  1 
ATOM   7295  N  N   . LEU   C  1 61  ? -0.411  29.864  -84.954  1.00 51.52  ? 362  LEU   C N   1 
ATOM   7296  C  CA  . LEU   C  1 61  ? 0.951   30.387  -84.929  1.00 53.42  ? 362  LEU   C CA  1 
ATOM   7297  C  C   . LEU   C  1 61  ? 1.158   31.434  -86.021  1.00 58.05  ? 362  LEU   C C   1 
ATOM   7298  O  O   . LEU   C  1 61  ? 1.546   32.578  -85.739  1.00 48.00  ? 362  LEU   C O   1 
ATOM   7299  C  CB  . LEU   C  1 61  ? 1.943   29.233  -85.096  1.00 55.21  ? 362  LEU   C CB  1 
ATOM   7300  C  CG  . LEU   C  1 61  ? 1.836   28.007  -84.185  1.00 56.62  ? 362  LEU   C CG  1 
ATOM   7301  C  CD1 . LEU   C  1 61  ? 2.884   26.960  -84.557  1.00 55.51  ? 362  LEU   C CD1 1 
ATOM   7302  C  CD2 . LEU   C  1 61  ? 2.020   28.433  -82.759  1.00 55.24  ? 362  LEU   C CD2 1 
ATOM   7303  N  N   . ALA   C  1 62  ? 0.901   31.052  -87.281  1.00 62.88  ? 363  ALA   C N   1 
ATOM   7304  C  CA  . ALA   C  1 62  ? 1.065   31.976  -88.400  1.00 58.17  ? 363  ALA   C CA  1 
ATOM   7305  C  C   . ALA   C  1 62  ? 0.273   33.257  -88.181  1.00 56.24  ? 363  ALA   C C   1 
ATOM   7306  O  O   . ALA   C  1 62  ? 0.775   34.359  -88.439  1.00 55.13  ? 363  ALA   C O   1 
ATOM   7307  C  CB  . ALA   C  1 62  ? 0.631   31.301  -89.698  1.00 60.77  ? 363  ALA   C CB  1 
ATOM   7308  N  N   . LYS   C  1 63  ? -0.964  33.133  -87.694  1.00 51.93  ? 364  LYS   C N   1 
ATOM   7309  C  CA  . LYS   C  1 63  ? -1.763  34.323  -87.431  1.00 59.72  ? 364  LYS   C CA  1 
ATOM   7310  C  C   . LYS   C  1 63  ? -1.094  35.212  -86.395  1.00 57.77  ? 364  LYS   C C   1 
ATOM   7311  O  O   . LYS   C  1 63  ? -1.115  36.441  -86.521  1.00 60.92  ? 364  LYS   C O   1 
ATOM   7312  C  CB  . LYS   C  1 63  ? -3.174  33.943  -86.976  1.00 67.32  ? 364  LYS   C CB  1 
ATOM   7313  C  CG  . LYS   C  1 63  ? -4.047  35.166  -86.696  1.00 73.06  ? 364  LYS   C CG  1 
ATOM   7314  C  CD  . LYS   C  1 63  ? -5.523  34.835  -86.586  1.00 76.66  ? 364  LYS   C CD  1 
ATOM   7315  C  CE  . LYS   C  1 63  ? -6.316  36.103  -86.323  1.00 73.59  ? 364  LYS   C CE  1 
ATOM   7316  N  NZ  . LYS   C  1 63  ? -5.693  36.909  -85.237  1.00 60.62  ? 364  LYS   C NZ  1 
ATOM   7317  N  N   . GLU   C  1 64  ? -0.487  34.609  -85.370  1.00 43.91  ? 365  GLU   C N   1 
ATOM   7318  C  CA  . GLU   C  1 64  ? 0.188   35.399  -84.346  1.00 51.90  ? 365  GLU   C CA  1 
ATOM   7319  C  C   . GLU   C  1 64  ? 1.345   36.205  -84.933  1.00 51.45  ? 365  GLU   C C   1 
ATOM   7320  O  O   . GLU   C  1 64  ? 1.492   37.402  -84.653  1.00 47.04  ? 365  GLU   C O   1 
ATOM   7321  C  CB  . GLU   C  1 64  ? 0.670   34.481  -83.221  1.00 65.84  ? 365  GLU   C CB  1 
ATOM   7322  C  CG  . GLU   C  1 64  ? 1.566   35.133  -82.178  1.00 74.26  ? 365  GLU   C CG  1 
ATOM   7323  C  CD  . GLU   C  1 64  ? 2.146   34.100  -81.224  1.00 93.94  ? 365  GLU   C CD  1 
ATOM   7324  O  OE1 . GLU   C  1 64  ? 2.113   34.319  -79.987  1.00 100.23 ? 365  GLU   C OE1 1 
ATOM   7325  O  OE2 . GLU   C  1 64  ? 2.620   33.051  -81.721  1.00 95.04  ? 365  GLU   C OE2 1 
ATOM   7326  N  N   . PHE   C  1 65  ? 2.178   35.573  -85.760  1.00 58.30  ? 366  PHE   C N   1 
ATOM   7327  C  CA  . PHE   C  1 65  ? 3.370   36.267  -86.238  1.00 55.99  ? 366  PHE   C CA  1 
ATOM   7328  C  C   . PHE   C  1 65  ? 3.019   37.386  -87.209  1.00 61.96  ? 366  PHE   C C   1 
ATOM   7329  O  O   . PHE   C  1 65  ? 3.568   38.491  -87.111  1.00 65.63  ? 366  PHE   C O   1 
ATOM   7330  C  CB  . PHE   C  1 65  ? 4.335   35.297  -86.899  1.00 51.93  ? 366  PHE   C CB  1 
ATOM   7331  C  CG  . PHE   C  1 65  ? 5.437   35.987  -87.622  1.00 51.37  ? 366  PHE   C CG  1 
ATOM   7332  C  CD1 . PHE   C  1 65  ? 6.390   36.709  -86.912  1.00 45.10  ? 366  PHE   C CD1 1 
ATOM   7333  C  CD2 . PHE   C  1 65  ? 5.505   35.953  -89.015  1.00 49.69  ? 366  PHE   C CD2 1 
ATOM   7334  C  CE1 . PHE   C  1 65  ? 7.409   37.372  -87.571  1.00 44.12  ? 366  PHE   C CE1 1 
ATOM   7335  C  CE2 . PHE   C  1 65  ? 6.518   36.611  -89.688  1.00 36.76  ? 366  PHE   C CE2 1 
ATOM   7336  C  CZ  . PHE   C  1 65  ? 7.473   37.322  -88.966  1.00 45.92  ? 366  PHE   C CZ  1 
ATOM   7337  N  N   . ILE   C  1 66  ? 2.137   37.108  -88.178  1.00 54.43  ? 367  ILE   C N   1 
ATOM   7338  C  CA  . ILE   C  1 66  ? 1.674   38.154  -89.087  1.00 53.51  ? 367  ILE   C CA  1 
ATOM   7339  C  C   . ILE   C  1 66  ? 1.055   39.294  -88.292  1.00 59.54  ? 367  ILE   C C   1 
ATOM   7340  O  O   . ILE   C  1 66  ? 1.344   40.472  -88.534  1.00 56.25  ? 367  ILE   C O   1 
ATOM   7341  C  CB  . ILE   C  1 66  ? 0.665   37.588  -90.105  1.00 59.39  ? 367  ILE   C CB  1 
ATOM   7342  C  CG1 . ILE   C  1 66  ? 1.181   36.312  -90.788  1.00 44.50  ? 367  ILE   C CG1 1 
ATOM   7343  C  CG2 . ILE   C  1 66  ? 0.279   38.667  -91.110  1.00 66.77  ? 367  ILE   C CG2 1 
ATOM   7344  C  CD1 . ILE   C  1 66  ? 2.436   36.470  -91.575  1.00 40.79  ? 367  ILE   C CD1 1 
ATOM   7345  N  N   . ASP   C  1 67  ? 0.184   38.948  -87.330  1.00 64.28  ? 368  ASP   C N   1 
ATOM   7346  C  CA  . ASP   C  1 67  ? -0.418  39.934  -86.432  1.00 57.02  ? 368  ASP   C CA  1 
ATOM   7347  C  C   . ASP   C  1 67  ? 0.647   40.754  -85.715  1.00 51.11  ? 368  ASP   C C   1 
ATOM   7348  O  O   . ASP   C  1 67  ? 0.548   41.982  -85.629  1.00 53.85  ? 368  ASP   C O   1 
ATOM   7349  C  CB  . ASP   C  1 67  ? -1.319  39.242  -85.409  1.00 53.15  ? 368  ASP   C CB  1 
ATOM   7350  C  CG  . ASP   C  1 67  ? -2.702  38.936  -85.947  1.00 60.51  ? 368  ASP   C CG  1 
ATOM   7351  O  OD1 . ASP   C  1 67  ? -2.953  39.127  -87.163  1.00 70.64  ? 368  ASP   C OD1 1 
ATOM   7352  O  OD2 . ASP   C  1 67  ? -3.548  38.506  -85.136  1.00 63.66  ? 368  ASP   C OD2 1 
ATOM   7353  N  N   . GLN   C  1 68  ? 1.681   40.088  -85.200  1.00 41.51  ? 369  GLN   C N   1 
ATOM   7354  C  CA  . GLN   C  1 68  ? 2.791   40.811  -84.598  1.00 44.57  ? 369  GLN   C CA  1 
ATOM   7355  C  C   . GLN   C  1 68  ? 3.488   41.710  -85.605  1.00 48.67  ? 369  GLN   C C   1 
ATOM   7356  O  O   . GLN   C  1 68  ? 3.812   42.863  -85.292  1.00 45.64  ? 369  GLN   C O   1 
ATOM   7357  C  CB  . GLN   C  1 68  ? 3.782   39.825  -83.999  1.00 59.19  ? 369  GLN   C CB  1 
ATOM   7358  C  CG  . GLN   C  1 68  ? 5.015   40.472  -83.406  1.00 62.92  ? 369  GLN   C CG  1 
ATOM   7359  C  CD  . GLN   C  1 68  ? 5.962   39.435  -82.852  1.00 63.84  ? 369  GLN   C CD  1 
ATOM   7360  O  OE1 . GLN   C  1 68  ? 5.540   38.474  -82.198  1.00 69.42  ? 369  GLN   C OE1 1 
ATOM   7361  N  NE2 . GLN   C  1 68  ? 7.249   39.606  -83.127  1.00 56.59  ? 369  GLN   C NE2 1 
ATOM   7362  N  N   . TYR   C  1 69  ? 3.723   41.199  -86.827  1.00 63.06  ? 370  TYR   C N   1 
ATOM   7363  C  CA  . TYR   C  1 69  ? 4.504   41.941  -87.821  1.00 54.70  ? 370  TYR   C CA  1 
ATOM   7364  C  C   . TYR   C  1 69  ? 3.758   43.169  -88.325  1.00 52.10  ? 370  TYR   C C   1 
ATOM   7365  O  O   . TYR   C  1 69  ? 4.368   44.229  -88.530  1.00 47.59  ? 370  TYR   C O   1 
ATOM   7366  C  CB  . TYR   C  1 69  ? 4.887   41.055  -89.011  1.00 48.92  ? 370  TYR   C CB  1 
ATOM   7367  C  CG  . TYR   C  1 69  ? 5.400   41.886  -90.159  1.00 52.28  ? 370  TYR   C CG  1 
ATOM   7368  C  CD1 . TYR   C  1 69  ? 6.660   42.464  -90.121  1.00 54.83  ? 370  TYR   C CD1 1 
ATOM   7369  C  CD2 . TYR   C  1 69  ? 4.598   42.142  -91.261  1.00 66.14  ? 370  TYR   C CD2 1 
ATOM   7370  C  CE1 . TYR   C  1 69  ? 7.112   43.265  -91.164  1.00 54.85  ? 370  TYR   C CE1 1 
ATOM   7371  C  CE2 . TYR   C  1 69  ? 5.047   42.929  -92.309  1.00 67.75  ? 370  TYR   C CE2 1 
ATOM   7372  C  CZ  . TYR   C  1 69  ? 6.297   43.487  -92.253  1.00 59.88  ? 370  TYR   C CZ  1 
ATOM   7373  O  OH  . TYR   C  1 69  ? 6.719   44.268  -93.301  1.00 65.68  ? 370  TYR   C OH  1 
ATOM   7374  N  N   . TYR   C  1 70  ? 2.448   43.041  -88.567  1.00 47.35  ? 371  TYR   C N   1 
ATOM   7375  C  CA  . TYR   C  1 70  ? 1.707   44.211  -89.008  1.00 46.42  ? 371  TYR   C CA  1 
ATOM   7376  C  C   . TYR   C  1 70  ? 1.478   45.166  -87.854  1.00 54.52  ? 371  TYR   C C   1 
ATOM   7377  O  O   . TYR   C  1 70  ? 1.463   46.383  -88.064  1.00 56.41  ? 371  TYR   C O   1 
ATOM   7378  C  CB  . TYR   C  1 70  ? 0.399   43.803  -89.699  1.00 57.41  ? 371  TYR   C CB  1 
ATOM   7379  C  CG  . TYR   C  1 70  ? 0.641   43.485  -91.169  1.00 61.55  ? 371  TYR   C CG  1 
ATOM   7380  C  CD1 . TYR   C  1 70  ? 0.876   42.179  -91.594  1.00 59.61  ? 371  TYR   C CD1 1 
ATOM   7381  C  CD2 . TYR   C  1 70  ? 0.700   44.498  -92.118  1.00 63.22  ? 371  TYR   C CD2 1 
ATOM   7382  C  CE1 . TYR   C  1 70  ? 1.136   41.889  -92.922  1.00 54.99  ? 371  TYR   C CE1 1 
ATOM   7383  C  CE2 . TYR   C  1 70  ? 0.956   44.214  -93.456  1.00 63.00  ? 371  TYR   C CE2 1 
ATOM   7384  C  CZ  . TYR   C  1 70  ? 1.175   42.913  -93.847  1.00 63.60  ? 371  TYR   C CZ  1 
ATOM   7385  O  OH  . TYR   C  1 70  ? 1.435   42.634  -95.167  1.00 72.54  ? 371  TYR   C OH  1 
ATOM   7386  N  N   . SER   C  1 71  ? 1.355   44.644  -86.628  1.00 63.73  ? 372  SER   C N   1 
ATOM   7387  C  CA  . SER   C  1 71  ? 1.323   45.523  -85.466  1.00 65.01  ? 372  SER   C CA  1 
ATOM   7388  C  C   . SER   C  1 71  ? 2.635   46.282  -85.324  1.00 51.83  ? 372  SER   C C   1 
ATOM   7389  O  O   . SER   C  1 71  ? 2.632   47.492  -85.074  1.00 61.30  ? 372  SER   C O   1 
ATOM   7390  C  CB  . SER   C  1 71  ? 1.016   44.724  -84.202  1.00 78.75  ? 372  SER   C CB  1 
ATOM   7391  O  OG  . SER   C  1 71  ? -0.304  44.206  -84.251  1.00 89.44  ? 372  SER   C OG  1 
ATOM   7392  N  N   . SER   C  1 72  ? 3.766   45.600  -85.513  1.00 43.76  ? 373  SER   C N   1 
ATOM   7393  C  CA  . SER   C  1 72  ? 5.060   46.273  -85.401  1.00 47.26  ? 373  SER   C CA  1 
ATOM   7394  C  C   . SER   C  1 72  ? 5.164   47.469  -86.346  1.00 57.46  ? 373  SER   C C   1 
ATOM   7395  O  O   . SER   C  1 72  ? 5.774   48.486  -85.991  1.00 53.05  ? 373  SER   C O   1 
ATOM   7396  C  CB  . SER   C  1 72  ? 6.193   45.293  -85.684  1.00 38.62  ? 373  SER   C CB  1 
ATOM   7397  O  OG  . SER   C  1 72  ? 6.536   45.344  -87.058  1.00 72.84  ? 373  SER   C OG  1 
ATOM   7398  N  N   . ILE   C  1 73  ? 4.578   47.372  -87.548  1.00 72.00  ? 374  ILE   C N   1 
ATOM   7399  C  CA  . ILE   C  1 73  ? 4.719   48.405  -88.587  1.00 66.79  ? 374  ILE   C CA  1 
ATOM   7400  C  C   . ILE   C  1 73  ? 3.533   49.375  -88.602  1.00 63.34  ? 374  ILE   C C   1 
ATOM   7401  O  O   . ILE   C  1 73  ? 3.289   50.032  -89.611  1.00 75.05  ? 374  ILE   C O   1 
ATOM   7402  C  CB  . ILE   C  1 73  ? 4.940   47.787  -89.977  1.00 60.64  ? 374  ILE   C CB  1 
ATOM   7403  C  CG1 . ILE   C  1 73  ? 3.651   47.120  -90.487  1.00 64.31  ? 374  ILE   C CG1 1 
ATOM   7404  C  CG2 . ILE   C  1 73  ? 6.095   46.798  -89.919  1.00 59.26  ? 374  ILE   C CG2 1 
ATOM   7405  C  CD1 . ILE   C  1 73  ? 3.736   46.479  -91.861  1.00 43.27  ? 374  ILE   C CD1 1 
ATOM   7406  N  N   . LYS   C  1 74  ? 2.803   49.487  -87.495  1.00 64.28  ? 375  LYS   C N   1 
ATOM   7407  C  CA  . LYS   C  1 74  ? 1.741   50.485  -87.316  1.00 75.08  ? 375  LYS   C CA  1 
ATOM   7408  C  C   . LYS   C  1 74  ? 0.585   50.298  -88.298  1.00 73.73  ? 375  LYS   C C   1 
ATOM   7409  O  O   . LYS   C  1 74  ? -0.135  51.250  -88.609  1.00 75.58  ? 375  LYS   C O   1 
ATOM   7410  C  CB  . LYS   C  1 74  ? 2.296   51.911  -87.413  1.00 80.80  ? 375  LYS   C CB  1 
ATOM   7411  C  CG  . LYS   C  1 74  ? 3.351   52.250  -86.360  1.00 77.59  ? 375  LYS   C CG  1 
ATOM   7412  C  CD  . LYS   C  1 74  ? 2.712   52.603  -85.016  1.00 77.31  ? 375  LYS   C CD  1 
ATOM   7413  C  CE  . LYS   C  1 74  ? 3.739   52.654  -83.902  1.00 66.28  ? 375  LYS   C CE  1 
ATOM   7414  N  NZ  . LYS   C  1 74  ? 4.370   51.313  -83.663  1.00 61.63  ? 375  LYS   C NZ  1 
ATOM   7415  N  N   . ARG   C  1 75  ? 0.403   49.081  -88.804  1.00 68.51  ? 376  ARG   C N   1 
ATOM   7416  C  CA  . ARG   C  1 75  ? -0.806  48.733  -89.535  1.00 67.68  ? 376  ARG   C CA  1 
ATOM   7417  C  C   . ARG   C  1 75  ? -1.715  47.953  -88.594  1.00 79.05  ? 376  ARG   C C   1 
ATOM   7418  O  O   . ARG   C  1 75  ? -2.058  48.457  -87.514  1.00 86.98  ? 376  ARG   C O   1 
ATOM   7419  C  CB  . ARG   C  1 75  ? -0.468  47.933  -90.797  1.00 57.60  ? 376  ARG   C CB  1 
ATOM   7420  C  CG  . ARG   C  1 75  ? 0.384   48.725  -91.782  1.00 62.80  ? 376  ARG   C CG  1 
ATOM   7421  C  CD  . ARG   C  1 75  ? -0.482  49.766  -92.498  1.00 81.97  ? 376  ARG   C CD  1 
ATOM   7422  N  NE  . ARG   C  1 75  ? 0.278   50.805  -93.193  1.00 92.11  ? 376  ARG   C NE  1 
ATOM   7423  C  CZ  . ARG   C  1 75  ? 0.669   51.945  -92.627  1.00 98.18  ? 376  ARG   C CZ  1 
ATOM   7424  N  NH1 . ARG   C  1 75  ? 1.346   52.848  -93.326  1.00 93.06  ? 376  ARG   C NH1 1 
ATOM   7425  N  NH2 . ARG   C  1 75  ? 0.392   52.181  -91.352  1.00 109.33 ? 376  ARG   C NH2 1 
ATOM   7426  N  N   . PHE   C  1 76  ? -2.067  46.720  -88.984  1.00 76.28  ? 377  PHE   C N   1 
ATOM   7427  C  CA  . PHE   C  1 76  ? -2.948  45.809  -88.247  1.00 79.30  ? 377  PHE   C CA  1 
ATOM   7428  C  C   . PHE   C  1 76  ? -4.405  46.089  -88.589  1.00 83.28  ? 377  PHE   C C   1 
ATOM   7429  O  O   . PHE   C  1 76  ? -4.931  47.173  -88.303  1.00 81.93  ? 377  PHE   C O   1 
ATOM   7430  C  CB  . PHE   C  1 76  ? -2.747  45.866  -86.719  1.00 79.78  ? 377  PHE   C CB  1 
ATOM   7431  C  CG  . PHE   C  1 76  ? -3.703  44.989  -85.951  1.00 75.99  ? 377  PHE   C CG  1 
ATOM   7432  C  CD1 . PHE   C  1 76  ? -3.392  43.663  -85.694  1.00 71.95  ? 377  PHE   C CD1 1 
ATOM   7433  C  CD2 . PHE   C  1 76  ? -4.918  45.482  -85.503  1.00 74.78  ? 377  PHE   C CD2 1 
ATOM   7434  C  CE1 . PHE   C  1 76  ? -4.273  42.848  -85.009  1.00 68.62  ? 377  PHE   C CE1 1 
ATOM   7435  C  CE2 . PHE   C  1 76  ? -5.805  44.672  -84.823  1.00 74.70  ? 377  PHE   C CE2 1 
ATOM   7436  C  CZ  . PHE   C  1 76  ? -5.482  43.355  -84.574  1.00 72.35  ? 377  PHE   C CZ  1 
ATOM   7437  N  N   . GLY   C  1 77  ? -5.075  45.096  -89.170  1.00 81.05  ? 378  GLY   C N   1 
ATOM   7438  C  CA  . GLY   C  1 77  ? -6.388  45.298  -89.732  1.00 81.95  ? 378  GLY   C CA  1 
ATOM   7439  C  C   . GLY   C  1 77  ? -6.376  45.994  -91.069  1.00 79.28  ? 378  GLY   C C   1 
ATOM   7440  O  O   . GLY   C  1 77  ? -7.442  46.145  -91.680  1.00 91.72  ? 378  GLY   C O   1 
ATOM   7441  N  N   . SER   C  1 78  ? -5.203  46.416  -91.541  1.00 75.34  ? 379  SER   C N   1 
ATOM   7442  C  CA  . SER   C  1 78  ? -5.047  47.097  -92.811  1.00 56.75  ? 379  SER   C CA  1 
ATOM   7443  C  C   . SER   C  1 78  ? -5.430  46.166  -93.954  1.00 69.72  ? 379  SER   C C   1 
ATOM   7444  O  O   . SER   C  1 78  ? -5.536  44.948  -93.793  1.00 69.95  ? 379  SER   C O   1 
ATOM   7445  C  CB  . SER   C  1 78  ? -3.603  47.563  -92.986  1.00 54.81  ? 379  SER   C CB  1 
ATOM   7446  O  OG  . SER   C  1 78  ? -2.742  46.457  -93.230  1.00 52.54  ? 379  SER   C OG  1 
ATOM   7447  N  N   . LYS   C  1 79  ? -5.627  46.752  -95.132  1.00 65.47  ? 380  LYS   C N   1 
ATOM   7448  C  CA  . LYS   C  1 79  ? -5.947  45.924  -96.285  1.00 63.75  ? 380  LYS   C CA  1 
ATOM   7449  C  C   . LYS   C  1 79  ? -4.841  44.898  -96.528  1.00 62.70  ? 380  LYS   C C   1 
ATOM   7450  O  O   . LYS   C  1 79  ? -5.122  43.724  -96.799  1.00 68.48  ? 380  LYS   C O   1 
ATOM   7451  C  CB  . LYS   C  1 79  ? -6.200  46.806  -97.515  1.00 67.16  ? 380  LYS   C CB  1 
ATOM   7452  C  CG  . LYS   C  1 79  ? -6.940  46.091  -98.659  1.00 76.50  ? 380  LYS   C CG  1 
ATOM   7453  C  CD  . LYS   C  1 79  ? -7.882  47.019  -99.420  1.00 82.87  ? 380  LYS   C CD  1 
ATOM   7454  C  CE  . LYS   C  1 79  ? -9.204  47.237  -98.670  1.00 88.47  ? 380  LYS   C CE  1 
ATOM   7455  N  NZ  . LYS   C  1 79  ? -10.008 45.990  -98.470  1.00 84.88  ? 380  LYS   C NZ  1 
ATOM   7456  N  N   . ALA   C  1 80  ? -3.577  45.304  -96.368  1.00 54.93  ? 381  ALA   C N   1 
ATOM   7457  C  CA  . ALA   C  1 80  ? -2.472  44.380  -96.616  1.00 64.63  ? 381  ALA   C CA  1 
ATOM   7458  C  C   . ALA   C  1 80  ? -2.424  43.267  -95.574  1.00 70.61  ? 381  ALA   C C   1 
ATOM   7459  O  O   . ALA   C  1 80  ? -2.079  42.123  -95.894  1.00 68.75  ? 381  ALA   C O   1 
ATOM   7460  C  CB  . ALA   C  1 80  ? -1.151  45.144  -96.645  1.00 68.11  ? 381  ALA   C CB  1 
ATOM   7461  N  N   . HIS   C  1 81  ? -2.762  43.588  -94.323  1.00 77.34  ? 382  HIS   C N   1 
ATOM   7462  C  CA  . HIS   C  1 81  ? -2.767  42.594  -93.254  1.00 71.04  ? 382  HIS   C CA  1 
ATOM   7463  C  C   . HIS   C  1 81  ? -3.859  41.549  -93.475  1.00 73.35  ? 382  HIS   C C   1 
ATOM   7464  O  O   . HIS   C  1 81  ? -3.609  40.341  -93.373  1.00 69.62  ? 382  HIS   C O   1 
ATOM   7465  C  CB  . HIS   C  1 81  ? -2.946  43.304  -91.912  1.00 71.23  ? 382  HIS   C CB  1 
ATOM   7466  C  CG  . HIS   C  1 81  ? -2.942  42.388  -90.728  1.00 79.08  ? 382  HIS   C CG  1 
ATOM   7467  N  ND1 . HIS   C  1 81  ? -3.175  42.836  -89.446  1.00 82.83  ? 382  HIS   C ND1 1 
ATOM   7468  C  CD2 . HIS   C  1 81  ? -2.723  41.055  -90.625  1.00 80.74  ? 382  HIS   C CD2 1 
ATOM   7469  C  CE1 . HIS   C  1 81  ? -3.102  41.820  -88.603  1.00 82.13  ? 382  HIS   C CE1 1 
ATOM   7470  N  NE2 . HIS   C  1 81  ? -2.829  40.727  -89.294  1.00 81.85  ? 382  HIS   C NE2 1 
ATOM   7471  N  N   . MET   C  1 82  ? -5.083  41.994  -93.777  1.00 77.74  ? 383  MET   C N   1 
ATOM   7472  C  CA  . MET   C  1 82  ? -6.176  41.048  -93.983  1.00 72.89  ? 383  MET   C CA  1 
ATOM   7473  C  C   . MET   C  1 82  ? -5.920  40.167  -95.202  1.00 70.63  ? 383  MET   C C   1 
ATOM   7474  O  O   . MET   C  1 82  ? -6.201  38.962  -95.173  1.00 70.46  ? 383  MET   C O   1 
ATOM   7475  C  CB  . MET   C  1 82  ? -7.507  41.789  -94.130  1.00 72.80  ? 383  MET   C CB  1 
ATOM   7476  C  CG  . MET   C  1 82  ? -8.025  42.451  -92.875  1.00 66.64  ? 383  MET   C CG  1 
ATOM   7477  S  SD  . MET   C  1 82  ? -7.649  41.425  -91.447  1.00 79.58  ? 383  MET   C SD  1 
ATOM   7478  C  CE  . MET   C  1 82  ? -8.475  42.322  -90.135  1.00 90.82  ? 383  MET   C CE  1 
ATOM   7479  N  N   . GLU   C  1 83  ? -5.393  40.755  -96.282  1.00 66.60  ? 384  GLU   C N   1 
ATOM   7480  C  CA  . GLU   C  1 83  ? -5.018  39.967  -97.451  1.00 61.66  ? 384  GLU   C CA  1 
ATOM   7481  C  C   . GLU   C  1 83  ? -3.988  38.911  -97.085  1.00 59.14  ? 384  GLU   C C   1 
ATOM   7482  O  O   . GLU   C  1 83  ? -4.078  37.764  -97.535  1.00 61.45  ? 384  GLU   C O   1 
ATOM   7483  C  CB  . GLU   C  1 83  ? -4.476  40.881  -98.551  1.00 65.23  ? 384  GLU   C CB  1 
ATOM   7484  C  CG  . GLU   C  1 83  ? -5.425  41.120  -99.711  1.00 67.64  ? 384  GLU   C CG  1 
ATOM   7485  C  CD  . GLU   C  1 83  ? -5.466  42.582  -100.135 1.00 72.57  ? 384  GLU   C CD  1 
ATOM   7486  O  OE1 . GLU   C  1 83  ? -4.530  43.334  -99.778  1.00 66.45  ? 384  GLU   C OE1 1 
ATOM   7487  O  OE2 . GLU   C  1 83  ? -6.433  42.978  -100.828 1.00 83.90  ? 384  GLU   C OE2 1 
ATOM   7488  N  N   . ARG   C  1 84  ? -3.015  39.279  -96.249  1.00 55.00  ? 385  ARG   C N   1 
ATOM   7489  C  CA  . ARG   C  1 84  ? -1.941  38.358  -95.891  1.00 56.41  ? 385  ARG   C CA  1 
ATOM   7490  C  C   . ARG   C  1 84  ? -2.464  37.166  -95.094  1.00 68.11  ? 385  ARG   C C   1 
ATOM   7491  O  O   . ARG   C  1 84  ? -2.053  36.024  -95.330  1.00 72.41  ? 385  ARG   C O   1 
ATOM   7492  C  CB  . ARG   C  1 84  ? -0.865  39.098  -95.102  1.00 47.05  ? 385  ARG   C CB  1 
ATOM   7493  C  CG  . ARG   C  1 84  ? 0.365   38.265  -94.853  1.00 45.91  ? 385  ARG   C CG  1 
ATOM   7494  C  CD  . ARG   C  1 84  ? 1.233   38.164  -96.076  1.00 51.36  ? 385  ARG   C CD  1 
ATOM   7495  N  NE  . ARG   C  1 84  ? 2.411   37.358  -95.782  1.00 63.00  ? 385  ARG   C NE  1 
ATOM   7496  C  CZ  . ARG   C  1 84  ? 2.589   36.105  -96.195  1.00 63.95  ? 385  ARG   C CZ  1 
ATOM   7497  N  NH1 . ARG   C  1 84  ? 1.664   35.513  -96.951  1.00 60.47  ? 385  ARG   C NH1 1 
ATOM   7498  N  NH2 . ARG   C  1 84  ? 3.700   35.447  -95.863  1.00 48.03  ? 385  ARG   C NH2 1 
ATOM   7499  N  N   . LEU   C  1 85  ? -3.363  37.412  -94.138  1.00 69.25  ? 386  LEU   C N   1 
ATOM   7500  C  CA  . LEU   C  1 85  ? -3.984  36.309  -93.411  1.00 60.06  ? 386  LEU   C CA  1 
ATOM   7501  C  C   . LEU   C  1 85  ? -4.654  35.331  -94.372  1.00 61.30  ? 386  LEU   C C   1 
ATOM   7502  O  O   . LEU   C  1 85  ? -4.421  34.117  -94.310  1.00 59.16  ? 386  LEU   C O   1 
ATOM   7503  C  CB  . LEU   C  1 85  ? -4.994  36.855  -92.406  1.00 55.18  ? 386  LEU   C CB  1 
ATOM   7504  C  CG  . LEU   C  1 85  ? -4.524  37.063  -90.968  1.00 57.07  ? 386  LEU   C CG  1 
ATOM   7505  C  CD1 . LEU   C  1 85  ? -3.117  37.616  -90.924  1.00 57.27  ? 386  LEU   C CD1 1 
ATOM   7506  C  CD2 . LEU   C  1 85  ? -5.479  37.989  -90.250  1.00 57.94  ? 386  LEU   C CD2 1 
ATOM   7507  N  N   . GLU   C  1 86  ? -5.476  35.847  -95.288  1.00 61.26  ? 387  GLU   C N   1 
ATOM   7508  C  CA  . GLU   C  1 86  ? -6.144  34.964  -96.232  1.00 71.30  ? 387  GLU   C CA  1 
ATOM   7509  C  C   . GLU   C  1 86  ? -5.154  34.326  -97.203  1.00 69.00  ? 387  GLU   C C   1 
ATOM   7510  O  O   . GLU   C  1 86  ? -5.368  33.191  -97.647  1.00 71.89  ? 387  GLU   C O   1 
ATOM   7511  C  CB  . GLU   C  1 86  ? -7.237  35.723  -96.982  1.00 81.41  ? 387  GLU   C CB  1 
ATOM   7512  C  CG  . GLU   C  1 86  ? -8.154  34.824  -97.808  1.00 97.50  ? 387  GLU   C CG  1 
ATOM   7513  C  CD  . GLU   C  1 86  ? -8.686  33.623  -97.028  1.00 106.56 ? 387  GLU   C CD  1 
ATOM   7514  O  OE1 . GLU   C  1 86  ? -9.305  33.818  -95.954  1.00 108.55 ? 387  GLU   C OE1 1 
ATOM   7515  O  OE2 . GLU   C  1 86  ? -8.480  32.481  -97.498  1.00 106.55 ? 387  GLU   C OE2 1 
ATOM   7516  N  N   . GLU   C  1 87  ? -4.061  35.017  -97.529  1.00 63.61  ? 388  GLU   C N   1 
ATOM   7517  C  CA  . GLU   C  1 87  ? -3.041  34.398  -98.372  1.00 59.70  ? 388  GLU   C CA  1 
ATOM   7518  C  C   . GLU   C  1 87  ? -2.358  33.243  -97.644  1.00 61.83  ? 388  GLU   C C   1 
ATOM   7519  O  O   . GLU   C  1 87  ? -2.149  32.170  -98.228  1.00 48.99  ? 388  GLU   C O   1 
ATOM   7520  C  CB  . GLU   C  1 87  ? -2.019  35.443  -98.813  1.00 55.82  ? 388  GLU   C CB  1 
ATOM   7521  C  CG  . GLU   C  1 87  ? -0.972  34.902  -99.755  1.00 62.85  ? 388  GLU   C CG  1 
ATOM   7522  C  CD  . GLU   C  1 87  ? 0.068   35.928  -100.102 1.00 68.04  ? 388  GLU   C CD  1 
ATOM   7523  O  OE1 . GLU   C  1 87  ? 0.221   36.894  -99.330  1.00 70.42  ? 388  GLU   C OE1 1 
ATOM   7524  O  OE2 . GLU   C  1 87  ? 0.732   35.774  -101.147 1.00 76.92  ? 388  GLU   C OE2 1 
ATOM   7525  N  N   . VAL   C  1 88  ? -2.016  33.440  -96.362  1.00 51.92  ? 389  VAL   C N   1 
ATOM   7526  C  CA  . VAL   C  1 88  ? -1.449  32.348  -95.580  1.00 50.64  ? 389  VAL   C CA  1 
ATOM   7527  C  C   . VAL   C  1 88  ? -2.490  31.251  -95.378  1.00 56.75  ? 389  VAL   C C   1 
ATOM   7528  O  O   . VAL   C  1 88  ? -2.185  30.055  -95.471  1.00 62.85  ? 389  VAL   C O   1 
ATOM   7529  C  CB  . VAL   C  1 88  ? -0.896  32.874  -94.241  1.00 49.58  ? 389  VAL   C CB  1 
ATOM   7530  C  CG1 . VAL   C  1 88  ? -0.353  31.723  -93.399  1.00 51.01  ? 389  VAL   C CG1 1 
ATOM   7531  C  CG2 . VAL   C  1 88  ? 0.196   33.899  -94.486  1.00 48.59  ? 389  VAL   C CG2 1 
ATOM   7532  N  N   . ASN   C  1 89  ? -3.739  31.637  -95.130  1.00 52.33  ? 390  ASN   C N   1 
ATOM   7533  C  CA  . ASN   C  1 89  ? -4.803  30.655  -94.957  1.00 60.19  ? 390  ASN   C CA  1 
ATOM   7534  C  C   . ASN   C  1 89  ? -4.913  29.721  -96.167  1.00 68.74  ? 390  ASN   C C   1 
ATOM   7535  O  O   . ASN   C  1 89  ? -4.802  28.496  -96.031  1.00 66.72  ? 390  ASN   C O   1 
ATOM   7536  C  CB  . ASN   C  1 89  ? -6.119  31.385  -94.692  1.00 67.66  ? 390  ASN   C CB  1 
ATOM   7537  C  CG  . ASN   C  1 89  ? -7.092  30.549  -93.912  1.00 87.16  ? 390  ASN   C CG  1 
ATOM   7538  O  OD1 . ASN   C  1 89  ? -7.337  29.386  -94.244  1.00 82.75  ? 390  ASN   C OD1 1 
ATOM   7539  N  ND2 . ASN   C  1 89  ? -7.646  31.129  -92.845  1.00 104.52 ? 390  ASN   C ND2 1 
ATOM   7540  N  N   . LYS   C  1 90  ? -5.129  30.286  -97.368  1.00 63.89  ? 391  LYS   C N   1 
ATOM   7541  C  CA  . LYS   C  1 90  ? -5.217  29.466  -98.579  1.00 73.53  ? 391  LYS   C CA  1 
ATOM   7542  C  C   . LYS   C  1 90  ? -3.938  28.678  -98.809  1.00 65.06  ? 391  LYS   C C   1 
ATOM   7543  O  O   . LYS   C  1 90  ? -3.977  27.543  -99.305  1.00 67.53  ? 391  LYS   C O   1 
ATOM   7544  C  CB  . LYS   C  1 90  ? -5.512  30.341  -99.807  1.00 87.70  ? 391  LYS   C CB  1 
ATOM   7545  C  CG  . LYS   C  1 90  ? -6.965  30.850  -99.928  1.00 106.06 ? 391  LYS   C CG  1 
ATOM   7546  C  CD  . LYS   C  1 90  ? -7.123  31.941  -101.017 1.00 108.20 ? 391  LYS   C CD  1 
ATOM   7547  C  CE  . LYS   C  1 90  ? -8.518  32.589  -100.981 1.00 105.31 ? 391  LYS   C CE  1 
ATOM   7548  N  NZ  . LYS   C  1 90  ? -8.537  33.975  -101.551 1.00 98.49  ? 391  LYS   C NZ  1 
ATOM   7549  N  N   . GLU   C  1 91  ? -2.796  29.267  -98.454  1.00 60.14  ? 392  GLU   C N   1 
ATOM   7550  C  CA  . GLU   C  1 91  ? -1.515  28.601  -98.649  1.00 65.68  ? 392  GLU   C CA  1 
ATOM   7551  C  C   . GLU   C  1 91  ? -1.416  27.327  -97.811  1.00 76.15  ? 392  GLU   C C   1 
ATOM   7552  O  O   . GLU   C  1 91  ? -1.082  26.257  -98.334  1.00 76.01  ? 392  GLU   C O   1 
ATOM   7553  C  CB  . GLU   C  1 91  ? -0.384  29.572  -98.323  1.00 45.86  ? 392  GLU   C CB  1 
ATOM   7554  C  CG  . GLU   C  1 91  ? 0.950   29.202  -98.925  1.00 64.03  ? 392  GLU   C CG  1 
ATOM   7555  C  CD  . GLU   C  1 91  ? 1.863   30.398  -99.023  1.00 61.17  ? 392  GLU   C CD  1 
ATOM   7556  O  OE1 . GLU   C  1 91  ? 3.064   30.203  -99.314  1.00 60.37  ? 392  GLU   C OE1 1 
ATOM   7557  O  OE2 . GLU   C  1 91  ? 1.370   31.530  -98.797  1.00 56.63  ? 392  GLU   C OE2 1 
ATOM   7558  N  N   . ILE   C  1 92  ? -1.721  27.419  -96.506  1.00 73.61  ? 393  ILE   C N   1 
ATOM   7559  C  CA  . ILE   C  1 92  ? -1.706  26.230  -95.650  1.00 68.54  ? 393  ILE   C CA  1 
ATOM   7560  C  C   . ILE   C  1 92  ? -2.741  25.211  -96.126  1.00 65.77  ? 393  ILE   C C   1 
ATOM   7561  O  O   . ILE   C  1 92  ? -2.479  24.003  -96.127  1.00 69.03  ? 393  ILE   C O   1 
ATOM   7562  C  CB  . ILE   C  1 92  ? -1.930  26.610  -94.169  1.00 73.36  ? 393  ILE   C CB  1 
ATOM   7563  C  CG1 . ILE   C  1 92  ? -0.842  27.552  -93.655  1.00 60.15  ? 393  ILE   C CG1 1 
ATOM   7564  C  CG2 . ILE   C  1 92  ? -1.963  25.368  -93.281  1.00 74.68  ? 393  ILE   C CG2 1 
ATOM   7565  C  CD1 . ILE   C  1 92  ? -1.326  28.425  -92.515  1.00 52.84  ? 393  ILE   C CD1 1 
ATOM   7566  N  N   . ASP   C  1 93  ? -3.930  25.681  -96.543  1.00 65.89  ? 394  ASP   C N   1 
ATOM   7567  C  CA  . ASP   C  1 93  ? -4.989  24.781  -97.013  1.00 69.07  ? 394  ASP   C CA  1 
ATOM   7568  C  C   . ASP   C  1 93  ? -4.551  23.915  -98.188  1.00 78.28  ? 394  ASP   C C   1 
ATOM   7569  O  O   . ASP   C  1 93  ? -5.057  22.798  -98.348  1.00 89.77  ? 394  ASP   C O   1 
ATOM   7570  C  CB  . ASP   C  1 93  ? -6.225  25.569  -97.440  1.00 63.48  ? 394  ASP   C CB  1 
ATOM   7571  C  CG  . ASP   C  1 93  ? -7.190  25.811  -96.310  1.00 77.92  ? 394  ASP   C CG  1 
ATOM   7572  O  OD1 . ASP   C  1 93  ? -7.252  26.965  -95.841  1.00 83.45  ? 394  ASP   C OD1 1 
ATOM   7573  O  OD2 . ASP   C  1 93  ? -7.902  24.862  -95.899  1.00 87.33  ? 394  ASP   C OD2 1 
ATOM   7574  N  N   . THR   C  1 94  ? -3.643  24.410  -99.035  1.00 68.21  ? 395  THR   C N   1 
ATOM   7575  C  CA  . THR   C  1 94  ? -3.262  23.682  -100.235 1.00 74.97  ? 395  THR   C CA  1 
ATOM   7576  C  C   . THR   C  1 94  ? -1.846  23.100  -100.214 1.00 81.94  ? 395  THR   C C   1 
ATOM   7577  O  O   . THR   C  1 94  ? -1.562  22.189  -101.001 1.00 85.32  ? 395  THR   C O   1 
ATOM   7578  C  CB  . THR   C  1 94  ? -3.431  24.585  -101.470 1.00 72.15  ? 395  THR   C CB  1 
ATOM   7579  O  OG1 . THR   C  1 94  ? -2.405  25.582  -101.498 1.00 74.49  ? 395  THR   C OG1 1 
ATOM   7580  C  CG2 . THR   C  1 94  ? -4.785  25.272  -101.420 1.00 65.16  ? 395  THR   C CG2 1 
ATOM   7581  N  N   . THR   C  1 95  ? -0.955  23.574  -99.337  1.00 80.54  ? 396  THR   C N   1 
ATOM   7582  C  CA  . THR   C  1 95  ? 0.406   23.053  -99.282  1.00 80.76  ? 396  THR   C CA  1 
ATOM   7583  C  C   . THR   C  1 95  ? 0.830   22.543  -97.909  1.00 79.94  ? 396  THR   C C   1 
ATOM   7584  O  O   . THR   C  1 95  ? 1.877   21.892  -97.814  1.00 86.00  ? 396  THR   C O   1 
ATOM   7585  C  CB  . THR   C  1 95  ? 1.423   24.124  -99.715  1.00 79.33  ? 396  THR   C CB  1 
ATOM   7586  O  OG1 . THR   C  1 95  ? 1.553   25.106  -98.680  1.00 83.16  ? 396  THR   C OG1 1 
ATOM   7587  C  CG2 . THR   C  1 95  ? 0.986   24.798  -100.996 1.00 78.73  ? 396  THR   C CG2 1 
ATOM   7588  N  N   . SER   C  1 96  ? 0.073   22.829  -96.856  1.00 66.91  ? 397  SER   C N   1 
ATOM   7589  C  CA  . SER   C  1 96  ? 0.352   22.476  -95.471  1.00 70.87  ? 397  SER   C CA  1 
ATOM   7590  C  C   . SER   C  1 96  ? 1.454   23.323  -94.854  1.00 63.07  ? 397  SER   C C   1 
ATOM   7591  O  O   . SER   C  1 96  ? 1.810   23.068  -93.711  1.00 66.69  ? 397  SER   C O   1 
ATOM   7592  C  CB  . SER   C  1 96  ? 0.711   20.994  -95.285  1.00 79.73  ? 397  SER   C CB  1 
ATOM   7593  O  OG  . SER   C  1 96  ? -0.317  20.177  -95.814  1.00 90.34  ? 397  SER   C OG  1 
ATOM   7594  N  N   . THR   C  1 97  ? 2.006   24.307  -95.555  1.00 62.25  ? 398  THR   C N   1 
ATOM   7595  C  CA  . THR   C  1 97  ? 2.955   25.247  -94.948  1.00 61.27  ? 398  THR   C CA  1 
ATOM   7596  C  C   . THR   C  1 97  ? 2.620   26.640  -95.478  1.00 56.68  ? 398  THR   C C   1 
ATOM   7597  O  O   . THR   C  1 97  ? 1.494   26.900  -95.915  1.00 53.18  ? 398  THR   C O   1 
ATOM   7598  C  CB  . THR   C  1 97  ? 4.404   24.800  -95.218  1.00 63.65  ? 398  THR   C CB  1 
ATOM   7599  O  OG1 . THR   C  1 97  ? 5.328   25.619  -94.483  1.00 61.08  ? 398  THR   C OG1 1 
ATOM   7600  C  CG2 . THR   C  1 97  ? 4.728   24.880  -96.694  1.00 57.65  ? 398  THR   C CG2 1 
ATOM   7601  N  N   . TYR   C  1 98  ? 3.574   27.568  -95.397  1.00 53.47  ? 399  TYR   C N   1 
ATOM   7602  C  CA  . TYR   C  1 98  ? 3.458   28.847  -96.091  1.00 41.92  ? 399  TYR   C CA  1 
ATOM   7603  C  C   . TYR   C  1 98  ? 4.820   29.522  -96.106  1.00 57.73  ? 399  TYR   C C   1 
ATOM   7604  O  O   . TYR   C  1 98  ? 5.758   29.085  -95.433  1.00 62.91  ? 399  TYR   C O   1 
ATOM   7605  C  CB  . TYR   C  1 98  ? 2.401   29.761  -95.465  1.00 41.09  ? 399  TYR   C CB  1 
ATOM   7606  C  CG  . TYR   C  1 98  ? 2.814   30.364  -94.154  1.00 46.74  ? 399  TYR   C CG  1 
ATOM   7607  C  CD1 . TYR   C  1 98  ? 3.340   31.647  -94.091  1.00 50.13  ? 399  TYR   C CD1 1 
ATOM   7608  C  CD2 . TYR   C  1 98  ? 2.684   29.651  -92.979  1.00 46.05  ? 399  TYR   C CD2 1 
ATOM   7609  C  CE1 . TYR   C  1 98  ? 3.733   32.189  -92.901  1.00 49.80  ? 399  TYR   C CE1 1 
ATOM   7610  C  CE2 . TYR   C  1 98  ? 3.080   30.185  -91.788  1.00 46.30  ? 399  TYR   C CE2 1 
ATOM   7611  C  CZ  . TYR   C  1 98  ? 3.594   31.454  -91.757  1.00 48.70  ? 399  TYR   C CZ  1 
ATOM   7612  O  OH  . TYR   C  1 98  ? 3.973   31.991  -90.562  1.00 58.99  ? 399  TYR   C OH  1 
ATOM   7613  N  N   . GLN   C  1 99  ? 4.916   30.604  -96.886  1.00 58.83  ? 400  GLN   C N   1 
ATOM   7614  C  CA  . GLN   C  1 99  ? 6.192   31.230  -97.214  1.00 54.56  ? 400  GLN   C CA  1 
ATOM   7615  C  C   . GLN   C  1 99  ? 6.217   32.683  -96.763  1.00 46.72  ? 400  GLN   C C   1 
ATOM   7616  O  O   . GLN   C  1 99  ? 5.260   33.430  -96.978  1.00 48.26  ? 400  GLN   C O   1 
ATOM   7617  C  CB  . GLN   C  1 99  ? 6.469   31.149  -98.721  1.00 37.39  ? 400  GLN   C CB  1 
ATOM   7618  C  CG  . GLN   C  1 99  ? 6.445   29.728  -99.258  1.00 51.61  ? 400  GLN   C CG  1 
ATOM   7619  C  CD  . GLN   C  1 99  ? 7.634   28.883  -98.791  1.00 60.66  ? 400  GLN   C CD  1 
ATOM   7620  O  OE1 . GLN   C  1 99  ? 8.771   29.362  -98.711  1.00 59.53  ? 400  GLN   C OE1 1 
ATOM   7621  N  NE2 . GLN   C  1 99  ? 7.370   27.611  -98.487  1.00 62.14  ? 400  GLN   C NE2 1 
ATOM   7622  N  N   . LEU   C  1 100 ? 7.326   33.087  -96.161  1.00 49.77  ? 401  LEU   C N   1 
ATOM   7623  C  CA  . LEU   C  1 100 ? 7.422   34.423  -95.593  1.00 53.01  ? 401  LEU   C CA  1 
ATOM   7624  C  C   . LEU   C  1 100 ? 7.780   35.416  -96.680  1.00 42.65  ? 401  LEU   C C   1 
ATOM   7625  O  O   . LEU   C  1 100 ? 8.715   35.186  -97.447  1.00 37.55  ? 401  LEU   C O   1 
ATOM   7626  C  CB  . LEU   C  1 100 ? 8.469   34.466  -94.474  1.00 50.83  ? 401  LEU   C CB  1 
ATOM   7627  C  CG  . LEU   C  1 100 ? 8.220   33.543  -93.283  1.00 40.52  ? 401  LEU   C CG  1 
ATOM   7628  C  CD1 . LEU   C  1 100 ? 9.444   33.452  -92.385  1.00 47.61  ? 401  LEU   C CD1 1 
ATOM   7629  C  CD2 . LEU   C  1 100 ? 7.039   34.033  -92.513  1.00 35.40  ? 401  LEU   C CD2 1 
ATOM   7630  N  N   . LYS   C  1 101 ? 7.035   36.518  -96.749  1.00 38.08  ? 402  LYS   C N   1 
ATOM   7631  C  CA  . LYS   C  1 101 ? 7.482   37.685  -97.500  1.00 36.20  ? 402  LYS   C CA  1 
ATOM   7632  C  C   . LYS   C  1 101 ? 8.905   38.060  -97.098  1.00 44.19  ? 402  LYS   C C   1 
ATOM   7633  O  O   . LYS   C  1 101 ? 9.364   37.698  -96.012  1.00 46.36  ? 402  LYS   C O   1 
ATOM   7634  C  CB  . LYS   C  1 101 ? 6.531   38.860  -97.264  1.00 39.47  ? 402  LYS   C CB  1 
ATOM   7635  C  CG  . LYS   C  1 101 ? 5.119   38.614  -97.770  1.00 49.80  ? 402  LYS   C CG  1 
ATOM   7636  C  CD  . LYS   C  1 101 ? 5.089   38.243  -99.256  1.00 58.99  ? 402  LYS   C CD  1 
ATOM   7637  C  CE  . LYS   C  1 101 ? 3.727   37.675  -99.679  1.00 66.32  ? 402  LYS   C CE  1 
ATOM   7638  N  NZ  . LYS   C  1 101 ? 3.738   37.126  -101.078 1.00 73.64  ? 402  LYS   C NZ  1 
ATOM   7639  N  N   . ASP   C  1 102 ? 9.615   38.786  -97.958  1.00 50.98  ? 403  ASP   C N   1 
ATOM   7640  C  CA  . ASP   C  1 102 ? 10.986  39.154  -97.637  1.00 47.46  ? 403  ASP   C CA  1 
ATOM   7641  C  C   . ASP   C  1 102 ? 11.049  40.044  -96.414  1.00 47.39  ? 403  ASP   C C   1 
ATOM   7642  O  O   . ASP   C  1 102 ? 11.966  39.919  -95.596  1.00 43.03  ? 403  ASP   C O   1 
ATOM   7643  C  CB  . ASP   C  1 102 ? 11.636  39.868  -98.814  1.00 56.86  ? 403  ASP   C CB  1 
ATOM   7644  C  CG  . ASP   C  1 102 ? 12.166  38.913  -99.861  1.00 68.86  ? 403  ASP   C CG  1 
ATOM   7645  O  OD1 . ASP   C  1 102 ? 11.857  37.701  -99.782  1.00 69.24  ? 403  ASP   C OD1 1 
ATOM   7646  O  OD2 . ASP   C  1 102 ? 12.899  39.385  -100.757 1.00 68.32  ? 403  ASP   C OD2 1 
ATOM   7647  N  N   . THR   C  1 103 ? 10.117  40.987  -96.301  1.00 46.31  ? 404  THR   C N   1 
ATOM   7648  C  CA  . THR   C  1 103 ? 10.107  41.862  -95.135  1.00 49.99  ? 404  THR   C CA  1 
ATOM   7649  C  C   . THR   C  1 103 ? 9.820   41.067  -93.866  1.00 52.44  ? 404  THR   C C   1 
ATOM   7650  O  O   . THR   C  1 103 ? 10.425  41.315  -92.817  1.00 48.91  ? 404  THR   C O   1 
ATOM   7651  C  CB  . THR   C  1 103 ? 9.070   42.970  -95.324  1.00 52.19  ? 404  THR   C CB  1 
ATOM   7652  O  OG1 . THR   C  1 103 ? 7.839   42.410  -95.813  1.00 42.79  ? 404  THR   C OG1 1 
ATOM   7653  C  CG2 . THR   C  1 103 ? 9.573   43.986  -96.314  1.00 60.65  ? 404  THR   C CG2 1 
ATOM   7654  N  N   . GLU   C  1 104 ? 8.927   40.080  -93.967  1.00 55.20  ? 405  GLU   C N   1 
ATOM   7655  C  CA  . GLU   C  1 104 ? 8.601   39.228  -92.832  1.00 52.14  ? 405  GLU   C CA  1 
ATOM   7656  C  C   . GLU   C  1 104 ? 9.823   38.451  -92.357  1.00 60.01  ? 405  GLU   C C   1 
ATOM   7657  O  O   . GLU   C  1 104 ? 10.103  38.381  -91.156  1.00 60.45  ? 405  GLU   C O   1 
ATOM   7658  C  CB  . GLU   C  1 104 ? 7.464   38.282  -93.230  1.00 43.19  ? 405  GLU   C CB  1 
ATOM   7659  C  CG  . GLU   C  1 104 ? 6.192   39.025  -93.604  1.00 37.00  ? 405  GLU   C CG  1 
ATOM   7660  C  CD  . GLU   C  1 104 ? 5.094   38.115  -94.111  1.00 48.23  ? 405  GLU   C CD  1 
ATOM   7661  O  OE1 . GLU   C  1 104 ? 3.989   38.616  -94.420  1.00 51.76  ? 405  GLU   C OE1 1 
ATOM   7662  O  OE2 . GLU   C  1 104 ? 5.339   36.899  -94.218  1.00 53.78  ? 405  GLU   C OE2 1 
ATOM   7663  N  N   . LEU   C  1 105 ? 10.568  37.864  -93.293  1.00 61.37  ? 406  LEU   C N   1 
ATOM   7664  C  CA  . LEU   C  1 105 ? 11.739  37.077  -92.924  1.00 51.07  ? 406  LEU   C CA  1 
ATOM   7665  C  C   . LEU   C  1 105 ? 12.771  37.934  -92.209  1.00 49.43  ? 406  LEU   C C   1 
ATOM   7666  O  O   . LEU   C  1 105 ? 13.386  37.486  -91.238  1.00 49.14  ? 406  LEU   C O   1 
ATOM   7667  C  CB  . LEU   C  1 105 ? 12.354  36.439  -94.171  1.00 47.71  ? 406  LEU   C CB  1 
ATOM   7668  C  CG  . LEU   C  1 105 ? 13.534  35.469  -94.042  1.00 48.67  ? 406  LEU   C CG  1 
ATOM   7669  C  CD1 . LEU   C  1 105 ? 13.040  34.039  -93.803  1.00 54.48  ? 406  LEU   C CD1 1 
ATOM   7670  C  CD2 . LEU   C  1 105 ? 14.487  35.522  -95.251  1.00 35.02  ? 406  LEU   C CD2 1 
ATOM   7671  N  N   . ILE   C  1 106 ? 12.995  39.163  -92.678  1.00 40.53  ? 407  ILE   C N   1 
ATOM   7672  C  CA  . ILE   C  1 106 ? 13.996  39.998  -92.021  1.00 41.84  ? 407  ILE   C CA  1 
ATOM   7673  C  C   . ILE   C  1 106 ? 13.516  40.384  -90.628  1.00 54.59  ? 407  ILE   C C   1 
ATOM   7674  O  O   . ILE   C  1 106 ? 14.290  40.376  -89.660  1.00 45.17  ? 407  ILE   C O   1 
ATOM   7675  C  CB  . ILE   C  1 106 ? 14.321  41.232  -92.881  1.00 36.70  ? 407  ILE   C CB  1 
ATOM   7676  C  CG1 . ILE   C  1 106 ? 15.035  40.813  -94.157  1.00 30.58  ? 407  ILE   C CG1 1 
ATOM   7677  C  CG2 . ILE   C  1 106 ? 15.191  42.219  -92.121  1.00 39.28  ? 407  ILE   C CG2 1 
ATOM   7678  C  CD1 . ILE   C  1 106 ? 14.542  41.588  -95.349  1.00 35.88  ? 407  ILE   C CD1 1 
ATOM   7679  N  N   . TYR   C  1 107 ? 12.220  40.686  -90.508  1.00 56.28  ? 408  TYR   C N   1 
ATOM   7680  C  CA  . TYR   C  1 107 ? 11.639  41.046  -89.226  1.00 49.38  ? 408  TYR   C CA  1 
ATOM   7681  C  C   . TYR   C  1 107 ? 11.807  39.916  -88.223  1.00 54.39  ? 408  TYR   C C   1 
ATOM   7682  O  O   . TYR   C  1 107 ? 12.278  40.124  -87.096  1.00 50.73  ? 408  TYR   C O   1 
ATOM   7683  C  CB  . TYR   C  1 107 ? 10.162  41.382  -89.408  1.00 47.81  ? 408  TYR   C CB  1 
ATOM   7684  C  CG  . TYR   C  1 107 ? 9.438   41.652  -88.102  1.00 52.96  ? 408  TYR   C CG  1 
ATOM   7685  C  CD1 . TYR   C  1 107 ? 9.608   42.855  -87.418  1.00 46.32  ? 408  TYR   C CD1 1 
ATOM   7686  C  CD2 . TYR   C  1 107 ? 8.584   40.701  -87.546  1.00 52.44  ? 408  TYR   C CD2 1 
ATOM   7687  C  CE1 . TYR   C  1 107 ? 8.939   43.105  -86.220  1.00 56.44  ? 408  TYR   C CE1 1 
ATOM   7688  C  CE2 . TYR   C  1 107 ? 7.908   40.938  -86.357  1.00 53.21  ? 408  TYR   C CE2 1 
ATOM   7689  C  CZ  . TYR   C  1 107 ? 8.087   42.143  -85.696  1.00 61.63  ? 408  TYR   C CZ  1 
ATOM   7690  O  OH  . TYR   C  1 107 ? 7.419   42.380  -84.505  1.00 73.27  ? 408  TYR   C OH  1 
ATOM   7691  N  N   . GLY   C  1 108 ? 11.441  38.703  -88.628  1.00 51.99  ? 409  GLY   C N   1 
ATOM   7692  C  CA  . GLY   C  1 108 ? 11.566  37.569  -87.730  1.00 45.06  ? 409  GLY   C CA  1 
ATOM   7693  C  C   . GLY   C  1 108 ? 13.003  37.289  -87.339  1.00 47.25  ? 409  GLY   C C   1 
ATOM   7694  O  O   . GLY   C  1 108 ? 13.293  37.007  -86.173  1.00 58.79  ? 409  GLY   C O   1 
ATOM   7695  N  N   . ALA   C  1 109 ? 13.928  37.378  -88.297  1.00 43.51  ? 410  ALA   C N   1 
ATOM   7696  C  CA  . ALA   C  1 109 ? 15.311  37.066  -87.968  1.00 38.59  ? 410  ALA   C CA  1 
ATOM   7697  C  C   . ALA   C  1 109 ? 15.861  38.060  -86.950  1.00 38.90  ? 410  ALA   C C   1 
ATOM   7698  O  O   . ALA   C  1 109 ? 16.577  37.679  -86.021  1.00 39.96  ? 410  ALA   C O   1 
ATOM   7699  C  CB  . ALA   C  1 109 ? 16.157  37.037  -89.231  1.00 28.97  ? 410  ALA   C CB  1 
ATOM   7700  N  N   . LYS   C  1 110 ? 15.500  39.334  -87.077  1.00 40.50  ? 411  LYS   C N   1 
ATOM   7701  C  CA  . LYS   C  1 110 ? 16.054  40.309  -86.150  1.00 38.69  ? 411  LYS   C CA  1 
ATOM   7702  C  C   . LYS   C  1 110 ? 15.467  40.123  -84.759  1.00 53.66  ? 411  LYS   C C   1 
ATOM   7703  O  O   . LYS   C  1 110 ? 16.161  40.316  -83.754  1.00 50.05  ? 411  LYS   C O   1 
ATOM   7704  C  CB  . LYS   C  1 110 ? 15.813  41.725  -86.672  1.00 31.34  ? 411  LYS   C CB  1 
ATOM   7705  C  CG  . LYS   C  1 110 ? 16.669  42.061  -87.899  1.00 38.09  ? 411  LYS   C CG  1 
ATOM   7706  C  CD  . LYS   C  1 110 ? 16.419  43.464  -88.427  1.00 39.35  ? 411  LYS   C CD  1 
ATOM   7707  C  CE  . LYS   C  1 110 ? 17.523  43.896  -89.391  1.00 41.54  ? 411  LYS   C CE  1 
ATOM   7708  N  NZ  . LYS   C  1 110 ? 17.257  45.233  -89.992  1.00 40.78  ? 411  LYS   C NZ  1 
ATOM   7709  N  N   . HIS   C  1 111 ? 14.207  39.710  -84.682  1.00 55.32  ? 412  HIS   C N   1 
ATOM   7710  C  CA  . HIS   C  1 111 ? 13.562  39.607  -83.388  1.00 49.61  ? 412  HIS   C CA  1 
ATOM   7711  C  C   . HIS   C  1 111 ? 13.970  38.337  -82.654  1.00 58.48  ? 412  HIS   C C   1 
ATOM   7712  O  O   . HIS   C  1 111 ? 14.026  38.333  -81.419  1.00 62.64  ? 412  HIS   C O   1 
ATOM   7713  C  CB  . HIS   C  1 111 ? 12.045  39.699  -83.561  1.00 44.93  ? 412  HIS   C CB  1 
ATOM   7714  C  CG  . HIS   C  1 111 ? 11.538  41.104  -83.588  1.00 41.98  ? 412  HIS   C CG  1 
ATOM   7715  N  ND1 . HIS   C  1 111 ? 12.240  42.132  -84.174  1.00 47.66  ? 412  HIS   C ND1 1 
ATOM   7716  C  CD2 . HIS   C  1 111 ? 10.414  41.660  -83.080  1.00 48.50  ? 412  HIS   C CD2 1 
ATOM   7717  C  CE1 . HIS   C  1 111 ? 11.567  43.261  -84.037  1.00 48.15  ? 412  HIS   C CE1 1 
ATOM   7718  N  NE2 . HIS   C  1 111 ? 10.453  43.002  -83.378  1.00 52.23  ? 412  HIS   C NE2 1 
ATOM   7719  N  N   . ALA   C  1 112 ? 14.280  37.259  -83.378  1.00 50.97  ? 413  ALA   C N   1 
ATOM   7720  C  CA  . ALA   C  1 112 ? 14.801  36.083  -82.694  1.00 52.27  ? 413  ALA   C CA  1 
ATOM   7721  C  C   . ALA   C  1 112 ? 16.150  36.376  -82.052  1.00 47.86  ? 413  ALA   C C   1 
ATOM   7722  O  O   . ALA   C  1 112 ? 16.461  35.838  -80.986  1.00 45.36  ? 413  ALA   C O   1 
ATOM   7723  C  CB  . ALA   C  1 112 ? 14.908  34.914  -83.663  1.00 46.93  ? 413  ALA   C CB  1 
ATOM   7724  N  N   . TRP   C  1 113 ? 16.958  37.222  -82.686  1.00 48.84  ? 414  TRP   C N   1 
ATOM   7725  C  CA  . TRP   C  1 113 ? 18.157  37.719  -82.029  1.00 46.75  ? 414  TRP   C CA  1 
ATOM   7726  C  C   . TRP   C  1 113 ? 17.783  38.592  -80.838  1.00 44.78  ? 414  TRP   C C   1 
ATOM   7727  O  O   . TRP   C  1 113 ? 18.239  38.363  -79.713  1.00 62.46  ? 414  TRP   C O   1 
ATOM   7728  C  CB  . TRP   C  1 113 ? 19.022  38.487  -83.032  1.00 34.65  ? 414  TRP   C CB  1 
ATOM   7729  C  CG  . TRP   C  1 113 ? 20.333  38.962  -82.448  1.00 43.33  ? 414  TRP   C CG  1 
ATOM   7730  C  CD1 . TRP   C  1 113 ? 20.843  38.667  -81.201  1.00 38.49  ? 414  TRP   C CD1 1 
ATOM   7731  C  CD2 . TRP   C  1 113 ? 21.295  39.818  -83.076  1.00 43.07  ? 414  TRP   C CD2 1 
ATOM   7732  N  NE1 . TRP   C  1 113 ? 22.053  39.286  -81.032  1.00 34.10  ? 414  TRP   C NE1 1 
ATOM   7733  C  CE2 . TRP   C  1 113 ? 22.351  39.998  -82.165  1.00 37.92  ? 414  TRP   C CE2 1 
ATOM   7734  C  CE3 . TRP   C  1 113 ? 21.368  40.449  -84.321  1.00 42.51  ? 414  TRP   C CE3 1 
ATOM   7735  C  CZ2 . TRP   C  1 113 ? 23.465  40.777  -82.466  1.00 42.66  ? 414  TRP   C CZ2 1 
ATOM   7736  C  CZ3 . TRP   C  1 113 ? 22.476  41.227  -84.611  1.00 32.69  ? 414  TRP   C CZ3 1 
ATOM   7737  C  CH2 . TRP   C  1 113 ? 23.508  41.379  -83.694  1.00 43.82  ? 414  TRP   C CH2 1 
ATOM   7738  N  N   . ARG   C  1 114 ? 16.925  39.578  -81.067  1.00 34.95  ? 415  ARG   C N   1 
ATOM   7739  C  CA  . ARG   C  1 114 ? 16.513  40.490  -80.010  1.00 33.61  ? 415  ARG   C CA  1 
ATOM   7740  C  C   . ARG   C  1 114 ? 15.892  39.749  -78.825  1.00 51.56  ? 415  ARG   C C   1 
ATOM   7741  O  O   . ARG   C  1 114 ? 15.959  40.226  -77.685  1.00 61.68  ? 415  ARG   C O   1 
ATOM   7742  C  CB  . ARG   C  1 114 ? 15.526  41.506  -80.598  1.00 32.97  ? 415  ARG   C CB  1 
ATOM   7743  C  CG  . ARG   C  1 114 ? 14.908  42.433  -79.584  1.00 30.54  ? 415  ARG   C CG  1 
ATOM   7744  C  CD  . ARG   C  1 114 ? 13.777  43.228  -80.164  1.00 31.93  ? 415  ARG   C CD  1 
ATOM   7745  N  NE  . ARG   C  1 114 ? 13.589  44.468  -79.424  1.00 39.95  ? 415  ARG   C NE  1 
ATOM   7746  C  CZ  . ARG   C  1 114 ? 12.682  45.377  -79.745  1.00 42.25  ? 415  ARG   C CZ  1 
ATOM   7747  N  NH1 . ARG   C  1 114 ? 12.579  46.493  -79.029  1.00 38.15  ? 415  ARG   C NH1 1 
ATOM   7748  N  NH2 . ARG   C  1 114 ? 11.896  45.168  -80.795  1.00 40.49  ? 415  ARG   C NH2 1 
ATOM   7749  N  N   . ASN   C  1 115 ? 15.302  38.586  -79.067  1.00 46.37  ? 416  ASN   C N   1 
ATOM   7750  C  CA  . ASN   C  1 115 ? 14.683  37.804  -78.011  1.00 38.96  ? 416  ASN   C CA  1 
ATOM   7751  C  C   . ASN   C  1 115 ? 15.609  36.757  -77.422  1.00 44.19  ? 416  ASN   C C   1 
ATOM   7752  O  O   . ASN   C  1 115 ? 15.155  35.966  -76.583  1.00 55.19  ? 416  ASN   C O   1 
ATOM   7753  C  CB  . ASN   C  1 115 ? 13.433  37.094  -78.538  1.00 40.56  ? 416  ASN   C CB  1 
ATOM   7754  C  CG  . ASN   C  1 115 ? 12.359  38.051  -78.969  1.00 49.86  ? 416  ASN   C CG  1 
ATOM   7755  O  OD1 . ASN   C  1 115 ? 12.264  39.180  -78.448  1.00 47.66  ? 416  ASN   C OD1 1 
ATOM   7756  N  ND2 . ASN   C  1 115 ? 11.531  37.616  -79.940  1.00 44.30  ? 416  ASN   C ND2 1 
ATOM   7757  N  N   . ALA   C  1 116 ? 16.865  36.685  -77.867  1.00 31.95  ? 417  ALA   C N   1 
ATOM   7758  C  CA  . ALA   C  1 116 ? 17.777  35.633  -77.404  1.00 42.66  ? 417  ALA   C CA  1 
ATOM   7759  C  C   . ALA   C  1 116 ? 18.261  36.007  -75.992  1.00 51.76  ? 417  ALA   C C   1 
ATOM   7760  O  O   . ALA   C  1 116 ? 19.184  36.817  -75.822  1.00 37.44  ? 417  ALA   C O   1 
ATOM   7761  C  CB  . ALA   C  1 116 ? 18.926  35.447  -78.390  1.00 26.19  ? 417  ALA   C CB  1 
ATOM   7762  N  N   . SER   C  1 117 ? 17.638  35.398  -74.973  1.00 43.39  ? 418  SER   C N   1 
ATOM   7763  C  CA  A SER   C  1 117 ? 17.854  35.872  -73.609  0.63 46.72  ? 418  SER   C CA  1 
ATOM   7764  C  CA  B SER   C  1 117 ? 17.842  35.830  -73.591  0.37 46.08  ? 418  SER   C CA  1 
ATOM   7765  C  C   . SER   C  1 117 ? 19.286  35.681  -73.151  1.00 44.58  ? 418  SER   C C   1 
ATOM   7766  O  O   . SER   C  1 117 ? 19.727  36.391  -72.245  1.00 55.39  ? 418  SER   C O   1 
ATOM   7767  C  CB  A SER   C  1 117 ? 16.909  35.166  -72.638  0.63 45.39  ? 418  SER   C CB  1 
ATOM   7768  C  CB  B SER   C  1 117 ? 16.940  35.035  -72.645  0.37 45.59  ? 418  SER   C CB  1 
ATOM   7769  O  OG  A SER   C  1 117 ? 17.128  33.770  -72.648  0.63 46.73  ? 418  SER   C OG  1 
ATOM   7770  O  OG  B SER   C  1 117 ? 15.599  35.473  -72.715  0.37 45.54  ? 418  SER   C OG  1 
ATOM   7771  N  N   . ARG   C  1 118 ? 20.023  34.761  -73.767  1.00 39.32  ? 419  ARG   C N   1 
ATOM   7772  C  CA  . ARG   C  1 118 ? 21.384  34.466  -73.366  1.00 33.24  ? 419  ARG   C CA  1 
ATOM   7773  C  C   . ARG   C  1 118 ? 22.419  35.355  -74.032  1.00 41.53  ? 419  ARG   C C   1 
ATOM   7774  O  O   . ARG   C  1 118 ? 23.604  35.256  -73.692  1.00 44.52  ? 419  ARG   C O   1 
ATOM   7775  C  CB  . ARG   C  1 118 ? 21.697  33.001  -73.653  1.00 28.16  ? 419  ARG   C CB  1 
ATOM   7776  C  CG  . ARG   C  1 118 ? 20.729  32.059  -72.950  1.00 27.65  ? 419  ARG   C CG  1 
ATOM   7777  C  CD  . ARG   C  1 118 ? 21.086  30.612  -73.238  1.00 32.71  ? 419  ARG   C CD  1 
ATOM   7778  N  NE  . ARG   C  1 118 ? 20.627  29.671  -72.218  1.00 34.78  ? 419  ARG   C NE  1 
ATOM   7779  C  CZ  . ARG   C  1 118 ? 20.413  28.382  -72.463  1.00 48.60  ? 419  ARG   C CZ  1 
ATOM   7780  N  NH1 . ARG   C  1 118 ? 20.581  27.915  -73.693  1.00 55.53  ? 419  ARG   C NH1 1 
ATOM   7781  N  NH2 . ARG   C  1 118 ? 20.003  27.564  -71.501  1.00 44.68  ? 419  ARG   C NH2 1 
ATOM   7782  N  N   . CYS   C  1 119 ? 22.014  36.241  -74.935  1.00 39.71  ? 420  CYS   C N   1 
ATOM   7783  C  CA  . CYS   C  1 119 ? 22.965  36.955  -75.778  1.00 44.87  ? 420  CYS   C CA  1 
ATOM   7784  C  C   . CYS   C  1 119 ? 23.284  38.311  -75.170  1.00 46.95  ? 420  CYS   C C   1 
ATOM   7785  O  O   . CYS   C  1 119 ? 22.406  39.184  -75.079  1.00 45.10  ? 420  CYS   C O   1 
ATOM   7786  C  CB  . CYS   C  1 119 ? 22.427  37.138  -77.197  1.00 42.59  ? 420  CYS   C CB  1 
ATOM   7787  S  SG  . CYS   C  1 119 ? 23.585  38.015  -78.263  1.00 40.83  ? 420  CYS   C SG  1 
ATOM   7788  N  N   . VAL   C  1 120 ? 24.549  38.496  -74.788  1.00 46.73  ? 421  VAL   C N   1 
ATOM   7789  C  CA  . VAL   C  1 120 ? 24.977  39.774  -74.222  1.00 45.56  ? 421  VAL   C CA  1 
ATOM   7790  C  C   . VAL   C  1 120 ? 25.154  40.854  -75.277  1.00 43.19  ? 421  VAL   C C   1 
ATOM   7791  O  O   . VAL   C  1 120 ? 25.278  42.032  -74.922  1.00 48.23  ? 421  VAL   C O   1 
ATOM   7792  C  CB  . VAL   C  1 120 ? 26.267  39.568  -73.401  1.00 42.25  ? 421  VAL   C CB  1 
ATOM   7793  C  CG1 . VAL   C  1 120 ? 27.445  39.237  -74.296  1.00 33.68  ? 421  VAL   C CG1 1 
ATOM   7794  C  CG2 . VAL   C  1 120 ? 26.558  40.786  -72.514  1.00 44.95  ? 421  VAL   C CG2 1 
ATOM   7795  N  N   . GLY   C  1 121 ? 25.124  40.501  -76.563  1.00 49.34  ? 422  GLY   C N   1 
ATOM   7796  C  CA  . GLY   C  1 121 ? 25.435  41.406  -77.651  1.00 41.63  ? 422  GLY   C CA  1 
ATOM   7797  C  C   . GLY   C  1 121 ? 24.249  42.009  -78.374  1.00 47.89  ? 422  GLY   C C   1 
ATOM   7798  O  O   . GLY   C  1 121 ? 24.448  42.682  -79.393  1.00 54.79  ? 422  GLY   C O   1 
ATOM   7799  N  N   . ARG   C  1 122 ? 23.023  41.811  -77.879  1.00 43.47  ? 423  ARG   C N   1 
ATOM   7800  C  CA  . ARG   C  1 122 ? 21.804  42.220  -78.588  1.00 39.03  ? 423  ARG   C CA  1 
ATOM   7801  C  C   . ARG   C  1 122 ? 21.599  43.726  -78.692  1.00 39.35  ? 423  ARG   C C   1 
ATOM   7802  O  O   . ARG   C  1 122 ? 20.550  44.137  -79.203  1.00 43.77  ? 423  ARG   C O   1 
ATOM   7803  C  CB  . ARG   C  1 122 ? 20.557  41.649  -77.935  1.00 35.59  ? 423  ARG   C CB  1 
ATOM   7804  C  CG  . ARG   C  1 122 ? 20.477  40.152  -77.820  1.00 37.12  ? 423  ARG   C CG  1 
ATOM   7805  C  CD  . ARG   C  1 122 ? 19.260  39.780  -76.981  1.00 43.24  ? 423  ARG   C CD  1 
ATOM   7806  N  NE  . ARG   C  1 122 ? 19.557  39.690  -75.548  1.00 41.13  ? 423  ARG   C NE  1 
ATOM   7807  C  CZ  . ARG   C  1 122 ? 18.650  39.415  -74.610  1.00 52.45  ? 423  ARG   C CZ  1 
ATOM   7808  N  NH1 . ARG   C  1 122 ? 17.380  39.214  -74.960  1.00 43.54  ? 423  ARG   C NH1 1 
ATOM   7809  N  NH2 . ARG   C  1 122 ? 19.007  39.331  -73.326  1.00 53.00  ? 423  ARG   C NH2 1 
ATOM   7810  N  N   . ILE   C  1 123 ? 22.512  44.562  -78.207  1.00 43.02  ? 424  ILE   C N   1 
ATOM   7811  C  CA  . ILE   C  1 123 ? 22.321  45.989  -78.423  1.00 44.00  ? 424  ILE   C CA  1 
ATOM   7812  C  C   . ILE   C  1 123 ? 22.380  46.309  -79.912  1.00 48.86  ? 424  ILE   C C   1 
ATOM   7813  O  O   . ILE   C  1 123 ? 21.872  47.351  -80.339  1.00 39.73  ? 424  ILE   C O   1 
ATOM   7814  C  CB  . ILE   C  1 123 ? 23.354  46.820  -77.631  1.00 42.24  ? 424  ILE   C CB  1 
ATOM   7815  C  CG1 . ILE   C  1 123 ? 22.886  48.271  -77.511  1.00 43.91  ? 424  ILE   C CG1 1 
ATOM   7816  C  CG2 . ILE   C  1 123 ? 24.737  46.741  -78.277  1.00 32.12  ? 424  ILE   C CG2 1 
ATOM   7817  C  CD1 . ILE   C  1 123 ? 24.033  49.254  -77.412  1.00 45.98  ? 424  ILE   C CD1 1 
ATOM   7818  N  N   . GLN   C  1 124 ? 22.957  45.408  -80.709  1.00 56.82  ? 425  GLN   C N   1 
ATOM   7819  C  CA  . GLN   C  1 124 ? 23.147  45.526  -82.148  1.00 54.21  ? 425  GLN   C CA  1 
ATOM   7820  C  C   . GLN   C  1 124 ? 22.017  44.898  -82.961  1.00 59.83  ? 425  GLN   C C   1 
ATOM   7821  O  O   . GLN   C  1 124 ? 22.110  44.860  -84.192  1.00 59.80  ? 425  GLN   C O   1 
ATOM   7822  C  CB  . GLN   C  1 124 ? 24.463  44.840  -82.536  1.00 53.95  ? 425  GLN   C CB  1 
ATOM   7823  C  CG  . GLN   C  1 124 ? 25.701  45.515  -82.014  1.00 56.45  ? 425  GLN   C CG  1 
ATOM   7824  C  CD  . GLN   C  1 124 ? 26.055  46.722  -82.841  1.00 71.87  ? 425  GLN   C CD  1 
ATOM   7825  O  OE1 . GLN   C  1 124 ? 26.830  46.624  -83.792  1.00 81.03  ? 425  GLN   C OE1 1 
ATOM   7826  N  NE2 . GLN   C  1 124 ? 25.483  47.873  -82.496  1.00 74.50  ? 425  GLN   C NE2 1 
ATOM   7827  N  N   . TRP   C  1 125 ? 20.954  44.429  -82.300  1.00 59.36  ? 426  TRP   C N   1 
ATOM   7828  C  CA  . TRP   C  1 125 ? 20.046  43.451  -82.894  1.00 57.72  ? 426  TRP   C CA  1 
ATOM   7829  C  C   . TRP   C  1 125 ? 19.399  43.958  -84.183  1.00 55.91  ? 426  TRP   C C   1 
ATOM   7830  O  O   . TRP   C  1 125 ? 19.221  43.191  -85.134  1.00 53.58  ? 426  TRP   C O   1 
ATOM   7831  C  CB  . TRP   C  1 125 ? 18.977  43.073  -81.872  1.00 53.99  ? 426  TRP   C CB  1 
ATOM   7832  C  CG  . TRP   C  1 125 ? 17.996  44.160  -81.648  1.00 45.28  ? 426  TRP   C CG  1 
ATOM   7833  C  CD1 . TRP   C  1 125 ? 18.082  45.152  -80.741  1.00 45.13  ? 426  TRP   C CD1 1 
ATOM   7834  C  CD2 . TRP   C  1 125 ? 16.777  44.377  -82.375  1.00 46.32  ? 426  TRP   C CD2 1 
ATOM   7835  N  NE1 . TRP   C  1 125 ? 16.985  45.990  -80.843  1.00 54.16  ? 426  TRP   C NE1 1 
ATOM   7836  C  CE2 . TRP   C  1 125 ? 16.167  45.526  -81.838  1.00 53.05  ? 426  TRP   C CE2 1 
ATOM   7837  C  CE3 . TRP   C  1 125 ? 16.141  43.705  -83.414  1.00 41.96  ? 426  TRP   C CE3 1 
ATOM   7838  C  CZ2 . TRP   C  1 125 ? 14.947  46.016  -82.305  1.00 46.93  ? 426  TRP   C CZ2 1 
ATOM   7839  C  CZ3 . TRP   C  1 125 ? 14.932  44.195  -83.879  1.00 50.91  ? 426  TRP   C CZ3 1 
ATOM   7840  C  CH2 . TRP   C  1 125 ? 14.349  45.338  -83.327  1.00 47.80  ? 426  TRP   C CH2 1 
ATOM   7841  N  N   . SER   C  1 126 ? 19.023  45.236  -84.236  1.00 50.71  ? 427  SER   C N   1 
ATOM   7842  C  CA  . SER   C  1 126 ? 18.345  45.765  -85.413  1.00 43.19  ? 427  SER   C CA  1 
ATOM   7843  C  C   . SER   C  1 126 ? 19.289  45.988  -86.596  1.00 55.34  ? 427  SER   C C   1 
ATOM   7844  O  O   . SER   C  1 126 ? 18.838  46.367  -87.687  1.00 63.18  ? 427  SER   C O   1 
ATOM   7845  C  CB  . SER   C  1 126 ? 17.651  47.074  -85.063  1.00 48.07  ? 427  SER   C CB  1 
ATOM   7846  O  OG  . SER   C  1 126 ? 18.569  48.146  -85.177  1.00 51.26  ? 427  SER   C OG  1 
ATOM   7847  N  N   . LYS   C  1 127 ? 20.582  45.761  -86.402  1.00 54.62  ? 428  LYS   C N   1 
ATOM   7848  C  CA  . LYS   C  1 127 ? 21.602  46.027  -87.397  1.00 50.65  ? 428  LYS   C CA  1 
ATOM   7849  C  C   . LYS   C  1 127 ? 22.201  44.688  -87.813  1.00 54.04  ? 428  LYS   C C   1 
ATOM   7850  O  O   . LYS   C  1 127 ? 23.340  44.362  -87.486  1.00 72.83  ? 428  LYS   C O   1 
ATOM   7851  C  CB  . LYS   C  1 127 ? 22.659  46.979  -86.816  1.00 46.78  ? 428  LYS   C CB  1 
ATOM   7852  C  CG  . LYS   C  1 127 ? 23.583  47.560  -87.843  1.00 70.38  ? 428  LYS   C CG  1 
ATOM   7853  C  CD  . LYS   C  1 127 ? 25.021  47.588  -87.345  1.00 79.50  ? 428  LYS   C CD  1 
ATOM   7854  C  CE  . LYS   C  1 127 ? 26.011  47.800  -88.507  1.00 83.49  ? 428  LYS   C CE  1 
ATOM   7855  N  NZ  . LYS   C  1 127 ? 25.757  49.044  -89.305  1.00 79.16  ? 428  LYS   C NZ  1 
ATOM   7856  N  N   . LEU   C  1 128 ? 21.394  43.888  -88.488  1.00 44.73  ? 429  LEU   C N   1 
ATOM   7857  C  CA  . LEU   C  1 128 ? 21.730  42.526  -88.874  1.00 43.17  ? 429  LEU   C CA  1 
ATOM   7858  C  C   . LEU   C  1 128 ? 21.454  42.372  -90.360  1.00 54.32  ? 429  LEU   C C   1 
ATOM   7859  O  O   . LEU   C  1 128 ? 20.434  42.852  -90.852  1.00 62.23  ? 429  LEU   C O   1 
ATOM   7860  C  CB  . LEU   C  1 128 ? 20.898  41.524  -88.099  1.00 27.60  ? 429  LEU   C CB  1 
ATOM   7861  C  CG  . LEU   C  1 128 ? 20.817  40.094  -88.613  1.00 27.06  ? 429  LEU   C CG  1 
ATOM   7862  C  CD1 . LEU   C  1 128 ? 22.067  39.350  -88.255  1.00 28.87  ? 429  LEU   C CD1 1 
ATOM   7863  C  CD2 . LEU   C  1 128 ? 19.610  39.396  -88.039  1.00 33.94  ? 429  LEU   C CD2 1 
ATOM   7864  N  N   . GLN   C  1 129 ? 22.358  41.712  -91.071  1.00 47.63  ? 430  GLN   C N   1 
ATOM   7865  C  CA  . GLN   C  1 129 ? 22.244  41.537  -92.510  1.00 43.80  ? 430  GLN   C CA  1 
ATOM   7866  C  C   . GLN   C  1 129 ? 21.685  40.147  -92.805  1.00 51.25  ? 430  GLN   C C   1 
ATOM   7867  O  O   . GLN   C  1 129 ? 22.227  39.150  -92.323  1.00 65.70  ? 430  GLN   C O   1 
ATOM   7868  C  CB  . GLN   C  1 129 ? 23.617  41.739  -93.155  1.00 45.03  ? 430  GLN   C CB  1 
ATOM   7869  C  CG  . GLN   C  1 129 ? 23.648  41.557  -94.662  1.00 53.79  ? 430  GLN   C CG  1 
ATOM   7870  C  CD  . GLN   C  1 129 ? 22.722  42.504  -95.363  1.00 57.60  ? 430  GLN   C CD  1 
ATOM   7871  O  OE1 . GLN   C  1 129 ? 22.656  43.688  -95.030  1.00 62.70  ? 430  GLN   C OE1 1 
ATOM   7872  N  NE2 . GLN   C  1 129 ? 21.978  41.989  -96.325  1.00 65.30  ? 430  GLN   C NE2 1 
ATOM   7873  N  N   . VAL   C  1 130 ? 20.595  40.076  -93.578  1.00 50.93  ? 431  VAL   C N   1 
ATOM   7874  C  CA  . VAL   C  1 130 ? 19.877  38.820  -93.826  1.00 38.81  ? 431  VAL   C CA  1 
ATOM   7875  C  C   . VAL   C  1 130 ? 20.079  38.396  -95.279  1.00 43.72  ? 431  VAL   C C   1 
ATOM   7876  O  O   . VAL   C  1 130 ? 19.707  39.129  -96.204  1.00 54.54  ? 431  VAL   C O   1 
ATOM   7877  C  CB  . VAL   C  1 130 ? 18.376  38.946  -93.517  1.00 36.27  ? 431  VAL   C CB  1 
ATOM   7878  C  CG1 . VAL   C  1 130 ? 17.677  37.581  -93.641  1.00 31.35  ? 431  VAL   C CG1 1 
ATOM   7879  C  CG2 . VAL   C  1 130 ? 18.165  39.531  -92.148  1.00 45.98  ? 431  VAL   C CG2 1 
ATOM   7880  N  N   . PHE   C  1 131 ? 20.646  37.202  -95.472  1.00 36.25  ? 432  PHE   C N   1 
ATOM   7881  C  CA  . PHE   C  1 131 ? 20.823  36.588  -96.779  1.00 30.80  ? 432  PHE   C CA  1 
ATOM   7882  C  C   . PHE   C  1 131 ? 19.769  35.498  -96.929  1.00 45.59  ? 432  PHE   C C   1 
ATOM   7883  O  O   . PHE   C  1 131 ? 19.831  34.470  -96.244  1.00 47.26  ? 432  PHE   C O   1 
ATOM   7884  C  CB  . PHE   C  1 131 ? 22.236  36.036  -96.944  1.00 34.83  ? 432  PHE   C CB  1 
ATOM   7885  C  CG  . PHE   C  1 131 ? 23.286  37.079  -96.781  1.00 43.18  ? 432  PHE   C CG  1 
ATOM   7886  C  CD1 . PHE   C  1 131 ? 23.276  38.199  -97.590  1.00 28.63  ? 432  PHE   C CD1 1 
ATOM   7887  C  CD2 . PHE   C  1 131 ? 24.261  36.969  -95.809  1.00 39.29  ? 432  PHE   C CD2 1 
ATOM   7888  C  CE1 . PHE   C  1 131 ? 24.212  39.183  -97.439  1.00 34.65  ? 432  PHE   C CE1 1 
ATOM   7889  C  CE2 . PHE   C  1 131 ? 25.226  37.957  -95.670  1.00 37.98  ? 432  PHE   C CE2 1 
ATOM   7890  C  CZ  . PHE   C  1 131 ? 25.199  39.063  -96.477  1.00 36.06  ? 432  PHE   C CZ  1 
ATOM   7891  N  N   . ASP   C  1 132 ? 18.799  35.745  -97.815  1.00 39.70  ? 433  ASP   C N   1 
ATOM   7892  C  CA  . ASP   C  1 132 ? 17.720  34.811  -98.128  1.00 45.08  ? 433  ASP   C CA  1 
ATOM   7893  C  C   . ASP   C  1 132 ? 18.276  33.718  -99.026  1.00 42.55  ? 433  ASP   C C   1 
ATOM   7894  O  O   . ASP   C  1 132 ? 18.542  33.948  -100.206 1.00 60.31  ? 433  ASP   C O   1 
ATOM   7895  C  CB  . ASP   C  1 132 ? 16.580  35.543  -98.825  1.00 30.00  ? 433  ASP   C CB  1 
ATOM   7896  C  CG  . ASP   C  1 132 ? 15.296  34.752  -98.846  1.00 52.21  ? 433  ASP   C CG  1 
ATOM   7897  O  OD1 . ASP   C  1 132 ? 14.245  35.417  -98.941  1.00 54.58  ? 433  ASP   C OD1 1 
ATOM   7898  O  OD2 . ASP   C  1 132 ? 15.326  33.490  -98.767  1.00 36.05  ? 433  ASP   C OD2 1 
ATOM   7899  N  N   . ALA   C  1 133 ? 18.504  32.546  -98.461  1.00 40.24  ? 434  ALA   C N   1 
ATOM   7900  C  CA  . ALA   C  1 133 ? 19.015  31.404  -99.203  1.00 39.59  ? 434  ALA   C CA  1 
ATOM   7901  C  C   . ALA   C  1 133 ? 17.933  30.365  -99.422  1.00 37.46  ? 434  ALA   C C   1 
ATOM   7902  O  O   . ALA   C  1 133 ? 18.233  29.171  -99.539  1.00 32.91  ? 434  ALA   C O   1 
ATOM   7903  C  CB  . ALA   C  1 133 ? 20.213  30.787  -98.473  1.00 41.49  ? 434  ALA   C CB  1 
ATOM   7904  N  N   . ARG   C  1 134 ? 16.669  30.793  -99.438  1.00 30.45  ? 435  ARG   C N   1 
ATOM   7905  C  CA  . ARG   C  1 134 ? 15.576  29.836  -99.500  1.00 39.42  ? 435  ARG   C CA  1 
ATOM   7906  C  C   . ARG   C  1 134 ? 15.436  29.199  -100.871 1.00 45.17  ? 435  ARG   C C   1 
ATOM   7907  O  O   . ARG   C  1 134 ? 14.737  28.190  -101.002 1.00 58.57  ? 435  ARG   C O   1 
ATOM   7908  C  CB  . ARG   C  1 134 ? 14.278  30.520  -99.114  1.00 41.63  ? 435  ARG   C CB  1 
ATOM   7909  C  CG  . ARG   C  1 134 ? 14.155  30.791  -97.637  1.00 40.41  ? 435  ARG   C CG  1 
ATOM   7910  C  CD  . ARG   C  1 134 ? 12.823  31.457  -97.348  1.00 32.89  ? 435  ARG   C CD  1 
ATOM   7911  N  NE  . ARG   C  1 134 ? 12.840  32.856  -97.754  1.00 34.07  ? 435  ARG   C NE  1 
ATOM   7912  C  CZ  . ARG   C  1 134 ? 11.748  33.610  -97.805  1.00 38.54  ? 435  ARG   C CZ  1 
ATOM   7913  N  NH1 . ARG   C  1 134 ? 10.569  33.068  -97.495  1.00 34.95  ? 435  ARG   C NH1 1 
ATOM   7914  N  NH2 . ARG   C  1 134 ? 11.827  34.885  -98.168  1.00 41.09  ? 435  ARG   C NH2 1 
ATOM   7915  N  N   . ASP   C  1 135 ? 16.059  29.770  -101.896 1.00 39.75  ? 436  ASP   C N   1 
ATOM   7916  C  CA  . ASP   C  1 135 ? 16.009  29.162  -103.215 1.00 38.34  ? 436  ASP   C CA  1 
ATOM   7917  C  C   . ASP   C  1 135 ? 17.013  28.036  -103.339 1.00 49.29  ? 436  ASP   C C   1 
ATOM   7918  O  O   . ASP   C  1 135 ? 17.073  27.384  -104.393 1.00 56.21  ? 436  ASP   C O   1 
ATOM   7919  C  CB  . ASP   C  1 135 ? 16.262  30.217  -104.288 1.00 43.93  ? 436  ASP   C CB  1 
ATOM   7920  C  CG  . ASP   C  1 135 ? 17.667  30.779  -104.231 1.00 51.72  ? 436  ASP   C CG  1 
ATOM   7921  O  OD1 . ASP   C  1 135 ? 18.096  31.484  -105.171 1.00 50.24  ? 436  ASP   C OD1 1 
ATOM   7922  O  OD2 . ASP   C  1 135 ? 18.352  30.518  -103.226 1.00 61.03  ? 436  ASP   C OD2 1 
ATOM   7923  N  N   . CYS   C  1 136 ? 17.788  27.797  -102.281 1.00 38.73  ? 437  CYS   C N   1 
ATOM   7924  C  CA  . CYS   C  1 136 ? 18.844  26.792  -102.306 1.00 42.47  ? 437  CYS   C CA  1 
ATOM   7925  C  C   . CYS   C  1 136 ? 18.254  25.390  -102.449 1.00 45.93  ? 437  CYS   C C   1 
ATOM   7926  O  O   . CYS   C  1 136 ? 17.107  25.130  -102.063 1.00 45.30  ? 437  CYS   C O   1 
ATOM   7927  C  CB  . CYS   C  1 136 ? 19.694  26.893  -101.039 1.00 38.69  ? 437  CYS   C CB  1 
ATOM   7928  S  SG  . CYS   C  1 136 ? 21.214  25.960  -101.097 1.00 51.46  ? 437  CYS   C SG  1 
ATOM   7929  N  N   . THR   C  1 137 ? 19.031  24.496  -103.075 1.00 45.39  ? 438  THR   C N   1 
ATOM   7930  C  CA  . THR   C  1 137 ? 18.559  23.140  -103.355 1.00 37.48  ? 438  THR   C CA  1 
ATOM   7931  C  C   . THR   C  1 137 ? 19.599  22.046  -103.144 1.00 37.27  ? 438  THR   C C   1 
ATOM   7932  O  O   . THR   C  1 137 ? 19.194  20.893  -102.982 1.00 36.51  ? 438  THR   C O   1 
ATOM   7933  C  CB  . THR   C  1 137 ? 18.035  23.027  -104.798 1.00 45.68  ? 438  THR   C CB  1 
ATOM   7934  O  OG1 . THR   C  1 137 ? 19.142  22.976  -105.711 1.00 43.79  ? 438  THR   C OG1 1 
ATOM   7935  C  CG2 . THR   C  1 137 ? 17.126  24.205  -105.177 1.00 38.10  ? 438  THR   C CG2 1 
ATOM   7936  N  N   . THR   C  1 138 ? 20.912  22.332  -103.161 1.00 43.26  ? 439  THR   C N   1 
ATOM   7937  C  CA  . THR   C  1 138 ? 21.942  21.310  -102.972 1.00 45.53  ? 439  THR   C CA  1 
ATOM   7938  C  C   . THR   C  1 138 ? 22.975  21.713  -101.926 1.00 52.45  ? 439  THR   C C   1 
ATOM   7939  O  O   . THR   C  1 138 ? 23.174  22.894  -101.617 1.00 44.21  ? 439  THR   C O   1 
ATOM   7940  C  CB  . THR   C  1 138 ? 22.732  21.016  -104.237 1.00 54.74  ? 439  THR   C CB  1 
ATOM   7941  O  OG1 . THR   C  1 138 ? 23.288  22.244  -104.731 1.00 66.09  ? 439  THR   C OG1 1 
ATOM   7942  C  CG2 . THR   C  1 138 ? 21.856  20.361  -105.283 1.00 53.74  ? 439  THR   C CG2 1 
ATOM   7943  N  N   . ALA   C  1 139 ? 23.677  20.685  -101.434 1.00 55.08  ? 440  ALA   C N   1 
ATOM   7944  C  CA  . ALA   C  1 139 ? 24.832  20.889  -100.569 1.00 49.48  ? 440  ALA   C CA  1 
ATOM   7945  C  C   . ALA   C  1 139 ? 25.874  21.798  -101.210 1.00 50.90  ? 440  ALA   C C   1 
ATOM   7946  O  O   . ALA   C  1 139 ? 26.583  22.527  -100.497 1.00 56.26  ? 440  ALA   C O   1 
ATOM   7947  C  CB  . ALA   C  1 139 ? 25.449  19.536  -100.214 1.00 53.65  ? 440  ALA   C CB  1 
ATOM   7948  N  N   . HIS   C  1 140 ? 26.000  21.757  -102.544 1.00 48.67  ? 441  HIS   C N   1 
ATOM   7949  C  CA  . HIS   C  1 140 ? 26.905  22.675  -103.236 1.00 40.56  ? 441  HIS   C CA  1 
ATOM   7950  C  C   . HIS   C  1 140 ? 26.364  24.091  -103.201 1.00 35.96  ? 441  HIS   C C   1 
ATOM   7951  O  O   . HIS   C  1 140 ? 27.119  25.043  -102.999 1.00 39.97  ? 441  HIS   C O   1 
ATOM   7952  C  CB  . HIS   C  1 140 ? 27.126  22.239  -104.681 1.00 47.61  ? 441  HIS   C CB  1 
ATOM   7953  C  CG  . HIS   C  1 140 ? 28.130  21.136  -104.844 1.00 48.01  ? 441  HIS   C CG  1 
ATOM   7954  N  ND1 . HIS   C  1 140 ? 29.480  21.376  -105.002 1.00 44.08  ? 441  HIS   C ND1 1 
ATOM   7955  C  CD2 . HIS   C  1 140 ? 27.977  19.791  -104.910 1.00 46.19  ? 441  HIS   C CD2 1 
ATOM   7956  C  CE1 . HIS   C  1 140 ? 30.118  20.227  -105.149 1.00 41.36  ? 441  HIS   C CE1 1 
ATOM   7957  N  NE2 . HIS   C  1 140 ? 29.229  19.251  -105.097 1.00 47.66  ? 441  HIS   C NE2 1 
ATOM   7958  N  N   . GLY   C  1 141 ? 25.060  24.257  -103.402 1.00 43.44  ? 442  GLY   C N   1 
ATOM   7959  C  CA  . GLY   C  1 141 ? 24.470  25.569  -103.208 1.00 43.88  ? 442  GLY   C CA  1 
ATOM   7960  C  C   . GLY   C  1 141 ? 24.724  26.103  -101.812 1.00 53.30  ? 442  GLY   C C   1 
ATOM   7961  O  O   . GLY   C  1 141 ? 25.079  27.271  -101.638 1.00 60.34  ? 442  GLY   C O   1 
ATOM   7962  N  N   . MET   C  1 142 ? 24.564  25.247  -100.798 1.00 51.33  ? 443  MET   C N   1 
ATOM   7963  C  CA  . MET   C  1 142 ? 24.779  25.674  -99.417  1.00 42.99  ? 443  MET   C CA  1 
ATOM   7964  C  C   . MET   C  1 142 ? 26.207  26.164  -99.200  1.00 42.24  ? 443  MET   C C   1 
ATOM   7965  O  O   . MET   C  1 142 ? 26.424  27.181  -98.534  1.00 52.96  ? 443  MET   C O   1 
ATOM   7966  C  CB  . MET   C  1 142 ? 24.447  24.530  -98.463  1.00 36.92  ? 443  MET   C CB  1 
ATOM   7967  C  CG  . MET   C  1 142 ? 22.965  24.294  -98.262  1.00 33.24  ? 443  MET   C CG  1 
ATOM   7968  S  SD  . MET   C  1 142 ? 22.666  22.703  -97.453  1.00 50.12  ? 443  MET   C SD  1 
ATOM   7969  C  CE  . MET   C  1 142 ? 23.035  23.107  -95.742  1.00 45.36  ? 443  MET   C CE  1 
ATOM   7970  N  N   . PHE   C  1 143 ? 27.190  25.475  -99.782  1.00 45.52  ? 444  PHE   C N   1 
ATOM   7971  C  CA  . PHE   C  1 143 ? 28.576  25.918  -99.669  1.00 31.57  ? 444  PHE   C CA  1 
ATOM   7972  C  C   . PHE   C  1 143 ? 28.761  27.318  -100.245 1.00 41.76  ? 444  PHE   C C   1 
ATOM   7973  O  O   . PHE   C  1 143 ? 29.409  28.172  -99.630  1.00 45.42  ? 444  PHE   C O   1 
ATOM   7974  C  CB  . PHE   C  1 143 ? 29.476  24.892  -100.359 1.00 56.18  ? 444  PHE   C CB  1 
ATOM   7975  C  CG  . PHE   C  1 143 ? 30.924  25.288  -100.438 1.00 53.49  ? 444  PHE   C CG  1 
ATOM   7976  C  CD1 . PHE   C  1 143 ? 31.527  25.503  -101.665 1.00 51.99  ? 444  PHE   C CD1 1 
ATOM   7977  C  CD2 . PHE   C  1 143 ? 31.686  25.429  -99.297  1.00 44.50  ? 444  PHE   C CD2 1 
ATOM   7978  C  CE1 . PHE   C  1 143 ? 32.860  25.862  -101.745 1.00 53.12  ? 444  PHE   C CE1 1 
ATOM   7979  C  CE2 . PHE   C  1 143 ? 33.018  25.782  -99.376  1.00 50.84  ? 444  PHE   C CE2 1 
ATOM   7980  C  CZ  . PHE   C  1 143 ? 33.604  26.006  -100.596 1.00 53.49  ? 444  PHE   C CZ  1 
ATOM   7981  N  N   . ASN   C  1 144 ? 28.189  27.573  -101.423 1.00 44.62  ? 445  ASN   C N   1 
ATOM   7982  C  CA  . ASN   C  1 144 ? 28.301  28.882  -102.069 1.00 48.35  ? 445  ASN   C CA  1 
ATOM   7983  C  C   . ASN   C  1 144 ? 27.666  29.966  -101.198 1.00 44.83  ? 445  ASN   C C   1 
ATOM   7984  O  O   . ASN   C  1 144 ? 28.267  31.022  -100.953 1.00 47.43  ? 445  ASN   C O   1 
ATOM   7985  C  CB  . ASN   C  1 144 ? 27.660  28.786  -103.477 1.00 47.72  ? 445  ASN   C CB  1 
ATOM   7986  C  CG  . ASN   C  1 144 ? 27.680  30.099  -104.279 1.00 52.31  ? 445  ASN   C CG  1 
ATOM   7987  O  OD1 . ASN   C  1 144 ? 26.623  30.617  -104.693 1.00 52.25  ? 445  ASN   C OD1 1 
ATOM   7988  N  ND2 . ASN   C  1 144 ? 28.871  30.605  -104.550 1.00 55.20  ? 445  ASN   C ND2 1 
ATOM   7989  N  N   . TYR   C  1 145 ? 26.461  29.697  -100.686 1.00 47.56  ? 446  TYR   C N   1 
ATOM   7990  C  CA  . TYR   C  1 145 ? 25.771  30.649  -99.819  1.00 57.30  ? 446  TYR   C CA  1 
ATOM   7991  C  C   . TYR   C  1 145 ? 26.519  30.881  -98.506  1.00 54.03  ? 446  TYR   C C   1 
ATOM   7992  O  O   . TYR   C  1 145 ? 26.482  31.993  -97.951  1.00 42.72  ? 446  TYR   C O   1 
ATOM   7993  C  CB  . TYR   C  1 145 ? 24.365  30.139  -99.528  1.00 52.12  ? 446  TYR   C CB  1 
ATOM   7994  C  CG  . TYR   C  1 145 ? 23.287  30.711  -100.413 1.00 42.33  ? 446  TYR   C CG  1 
ATOM   7995  C  CD1 . TYR   C  1 145 ? 22.576  29.898  -101.288 1.00 43.67  ? 446  TYR   C CD1 1 
ATOM   7996  C  CD2 . TYR   C  1 145 ? 22.940  32.054  -100.342 1.00 30.65  ? 446  TYR   C CD2 1 
ATOM   7997  C  CE1 . TYR   C  1 145 ? 21.565  30.415  -102.070 1.00 34.37  ? 446  TYR   C CE1 1 
ATOM   7998  C  CE2 . TYR   C  1 145 ? 21.931  32.575  -101.135 1.00 34.44  ? 446  TYR   C CE2 1 
ATOM   7999  C  CZ  . TYR   C  1 145 ? 21.256  31.755  -101.992 1.00 39.28  ? 446  TYR   C CZ  1 
ATOM   8000  O  OH  . TYR   C  1 145 ? 20.256  32.288  -102.773 1.00 58.65  ? 446  TYR   C OH  1 
ATOM   8001  N  N   . ILE   C  1 146 ? 27.188  29.842  -97.996  1.00 48.05  ? 447  ILE   C N   1 
ATOM   8002  C  CA  . ILE   C  1 146 ? 27.916  29.928  -96.735  1.00 42.38  ? 447  ILE   C CA  1 
ATOM   8003  C  C   . ILE   C  1 146 ? 29.241  30.666  -96.911  1.00 48.12  ? 447  ILE   C C   1 
ATOM   8004  O  O   . ILE   C  1 146 ? 29.631  31.469  -96.050  1.00 44.33  ? 447  ILE   C O   1 
ATOM   8005  C  CB  . ILE   C  1 146 ? 28.117  28.518  -96.162  1.00 35.22  ? 447  ILE   C CB  1 
ATOM   8006  C  CG1 . ILE   C  1 146 ? 26.835  28.044  -95.464  1.00 35.10  ? 447  ILE   C CG1 1 
ATOM   8007  C  CG2 . ILE   C  1 146 ? 29.270  28.520  -95.212  1.00 30.46  ? 447  ILE   C CG2 1 
ATOM   8008  C  CD1 . ILE   C  1 146 ? 26.902  26.628  -94.892  1.00 34.78  ? 447  ILE   C CD1 1 
ATOM   8009  N  N   . CYS   C  1 147 ? 29.941  30.416  -98.029  1.00 45.70  ? 448  CYS   C N   1 
ATOM   8010  C  CA  . CYS   C  1 147 ? 31.181  31.126  -98.325  1.00 33.78  ? 448  CYS   C CA  1 
ATOM   8011  C  C   . CYS   C  1 147 ? 30.941  32.619  -98.456  1.00 40.64  ? 448  CYS   C C   1 
ATOM   8012  O  O   . CYS   C  1 147 ? 31.744  33.432  -97.984  1.00 47.25  ? 448  CYS   C O   1 
ATOM   8013  C  CB  . CYS   C  1 147 ? 31.801  30.592  -99.614  1.00 43.28  ? 448  CYS   C CB  1 
ATOM   8014  S  SG  . CYS   C  1 147 ? 32.774  29.077  -99.483  1.00 50.40  ? 448  CYS   C SG  1 
ATOM   8015  N  N   . ASN   C  1 148 ? 29.864  33.009  -99.134  1.00 55.04  ? 449  ASN   C N   1 
ATOM   8016  C  CA  . ASN   C  1 148 ? 29.571  34.433  -99.236  1.00 45.62  ? 449  ASN   C CA  1 
ATOM   8017  C  C   . ASN   C  1 148 ? 29.255  35.003  -97.862  1.00 38.96  ? 449  ASN   C C   1 
ATOM   8018  O  O   . ASN   C  1 148 ? 29.678  36.114  -97.531  1.00 38.57  ? 449  ASN   C O   1 
ATOM   8019  C  CB  . ASN   C  1 148 ? 28.421  34.671  -100.214 1.00 37.11  ? 449  ASN   C CB  1 
ATOM   8020  C  CG  . ASN   C  1 148 ? 28.687  34.088  -101.591 1.00 41.83  ? 449  ASN   C CG  1 
ATOM   8021  O  OD1 . ASN   C  1 148 ? 29.827  34.049  -102.063 1.00 41.58  ? 449  ASN   C OD1 1 
ATOM   8022  N  ND2 . ASN   C  1 148 ? 27.620  33.644  -102.254 1.00 39.13  ? 449  ASN   C ND2 1 
ATOM   8023  N  N   . HIS   C  1 149 ? 28.548  34.239  -97.030  1.00 40.93  ? 450  HIS   C N   1 
ATOM   8024  C  CA  . HIS   C  1 149 ? 28.313  34.671  -95.656  1.00 38.27  ? 450  HIS   C CA  1 
ATOM   8025  C  C   . HIS   C  1 149 ? 29.631  34.976  -94.955  1.00 37.93  ? 450  HIS   C C   1 
ATOM   8026  O  O   . HIS   C  1 149 ? 29.853  36.094  -94.470  1.00 33.41  ? 450  HIS   C O   1 
ATOM   8027  C  CB  . HIS   C  1 149 ? 27.526  33.599  -94.896  1.00 40.88  ? 450  HIS   C CB  1 
ATOM   8028  C  CG  . HIS   C  1 149 ? 27.194  33.968  -93.476  1.00 36.80  ? 450  HIS   C CG  1 
ATOM   8029  N  ND1 . HIS   C  1 149 ? 26.026  33.569  -92.864  1.00 35.33  ? 450  HIS   C ND1 1 
ATOM   8030  C  CD2 . HIS   C  1 149 ? 27.873  34.693  -92.552  1.00 36.00  ? 450  HIS   C CD2 1 
ATOM   8031  C  CE1 . HIS   C  1 149 ? 26.001  34.032  -91.624  1.00 40.13  ? 450  HIS   C CE1 1 
ATOM   8032  N  NE2 . HIS   C  1 149 ? 27.108  34.721  -91.413  1.00 37.48  ? 450  HIS   C NE2 1 
ATOM   8033  N  N   . VAL   C  1 150 ? 30.515  33.977  -94.888  1.00 28.31  ? 451  VAL   C N   1 
ATOM   8034  C  CA  . VAL   C  1 150 ? 31.808  34.157  -94.236  1.00 28.68  ? 451  VAL   C CA  1 
ATOM   8035  C  C   . VAL   C  1 150 ? 32.502  35.415  -94.741  1.00 46.66  ? 451  VAL   C C   1 
ATOM   8036  O  O   . VAL   C  1 150 ? 33.002  36.226  -93.951  1.00 48.04  ? 451  VAL   C O   1 
ATOM   8037  C  CB  . VAL   C  1 150 ? 32.687  32.913  -94.447  1.00 29.24  ? 451  VAL   C CB  1 
ATOM   8038  C  CG1 . VAL   C  1 150 ? 34.109  33.215  -94.076  1.00 29.91  ? 451  VAL   C CG1 1 
ATOM   8039  C  CG2 . VAL   C  1 150 ? 32.182  31.776  -93.592  1.00 28.90  ? 451  VAL   C CG2 1 
ATOM   8040  N  N   . LYS   C  1 151 ? 32.532  35.604  -96.068  1.00 44.92  ? 452  LYS   C N   1 
ATOM   8041  C  CA  . LYS   C  1 151 ? 33.342  36.673  -96.645  1.00 35.90  ? 452  LYS   C CA  1 
ATOM   8042  C  C   . LYS   C  1 151 ? 32.729  38.036  -96.385  1.00 34.90  ? 452  LYS   C C   1 
ATOM   8043  O  O   . LYS   C  1 151 ? 33.451  38.994  -96.099  1.00 38.13  ? 452  LYS   C O   1 
ATOM   8044  C  CB  . LYS   C  1 151 ? 33.530  36.458  -98.140  1.00 30.95  ? 452  LYS   C CB  1 
ATOM   8045  C  CG  . LYS   C  1 151 ? 34.462  37.479  -98.806  1.00 36.71  ? 452  LYS   C CG  1 
ATOM   8046  C  CD  . LYS   C  1 151 ? 34.625  37.151  -100.335 1.00 37.58  ? 452  LYS   C CD  1 
ATOM   8047  C  CE  . LYS   C  1 151 ? 35.743  37.951  -101.020 1.00 33.75  ? 452  LYS   C CE  1 
ATOM   8048  N  NZ  . LYS   C  1 151 ? 35.941  37.627  -102.510 1.00 46.66  ? 452  LYS   C NZ  1 
ATOM   8049  N  N   . TYR   C  1 152 ? 31.404  38.147  -96.480  1.00 38.10  ? 453  TYR   C N   1 
ATOM   8050  C  CA  . TYR   C  1 152 ? 30.746  39.399  -96.115  1.00 41.51  ? 453  TYR   C CA  1 
ATOM   8051  C  C   . TYR   C  1 152 ? 30.922  39.698  -94.630  1.00 47.01  ? 453  TYR   C C   1 
ATOM   8052  O  O   . TYR   C  1 152 ? 31.233  40.835  -94.243  1.00 48.66  ? 453  TYR   C O   1 
ATOM   8053  C  CB  . TYR   C  1 152 ? 29.258  39.346  -96.467  1.00 33.44  ? 453  TYR   C CB  1 
ATOM   8054  C  CG  . TYR   C  1 152 ? 28.475  40.512  -95.899  1.00 46.49  ? 453  TYR   C CG  1 
ATOM   8055  C  CD1 . TYR   C  1 152 ? 28.279  41.653  -96.647  1.00 48.08  ? 453  TYR   C CD1 1 
ATOM   8056  C  CD2 . TYR   C  1 152 ? 27.959  40.485  -94.604  1.00 46.62  ? 453  TYR   C CD2 1 
ATOM   8057  C  CE1 . TYR   C  1 152 ? 27.585  42.719  -96.151  1.00 48.26  ? 453  TYR   C CE1 1 
ATOM   8058  C  CE2 . TYR   C  1 152 ? 27.263  41.568  -94.095  1.00 47.63  ? 453  TYR   C CE2 1 
ATOM   8059  C  CZ  . TYR   C  1 152 ? 27.077  42.678  -94.889  1.00 50.61  ? 453  TYR   C CZ  1 
ATOM   8060  O  OH  . TYR   C  1 152 ? 26.385  43.773  -94.435  1.00 57.46  ? 453  TYR   C OH  1 
ATOM   8061  N  N   . ALA   C  1 153 ? 30.692  38.689  -93.781  1.00 41.98  ? 454  ALA   C N   1 
ATOM   8062  C  CA  . ALA   C  1 153 ? 30.736  38.887  -92.330  1.00 39.92  ? 454  ALA   C CA  1 
ATOM   8063  C  C   . ALA   C  1 153 ? 32.146  39.209  -91.850  1.00 36.88  ? 454  ALA   C C   1 
ATOM   8064  O  O   . ALA   C  1 153 ? 32.333  40.034  -90.944  1.00 45.20  ? 454  ALA   C O   1 
ATOM   8065  C  CB  . ALA   C  1 153 ? 30.200  37.640  -91.617  1.00 29.16  ? 454  ALA   C CB  1 
ATOM   8066  N  N   . THR   C  1 154 ? 33.151  38.565  -92.440  1.00 33.83  ? 455  THR   C N   1 
ATOM   8067  C  CA  . THR   C  1 154 ? 34.524  38.798  -92.012  1.00 32.97  ? 455  THR   C CA  1 
ATOM   8068  C  C   . THR   C  1 154 ? 34.990  40.202  -92.407  1.00 41.78  ? 455  THR   C C   1 
ATOM   8069  O  O   . THR   C  1 154 ? 35.644  40.888  -91.615  1.00 41.44  ? 455  THR   C O   1 
ATOM   8070  C  CB  . THR   C  1 154 ? 35.419  37.703  -92.597  1.00 39.83  ? 455  THR   C CB  1 
ATOM   8071  O  OG1 . THR   C  1 154 ? 34.947  36.414  -92.163  1.00 36.82  ? 455  THR   C OG1 1 
ATOM   8072  C  CG2 . THR   C  1 154 ? 36.843  37.888  -92.146  1.00 31.63  ? 455  THR   C CG2 1 
ATOM   8073  N  N   . ASN   C  1 155 ? 34.652  40.645  -93.624  1.00 49.55  ? 456  ASN   C N   1 
ATOM   8074  C  CA  . ASN   C  1 155 ? 34.846  42.033  -94.091  1.00 47.92  ? 456  ASN   C CA  1 
ATOM   8075  C  C   . ASN   C  1 155 ? 36.234  42.581  -93.745  1.00 47.10  ? 456  ASN   C C   1 
ATOM   8076  O  O   . ASN   C  1 155 ? 36.388  43.723  -93.302  1.00 45.69  ? 456  ASN   C O   1 
ATOM   8077  C  CB  . ASN   C  1 155 ? 33.738  42.952  -93.558  1.00 43.01  ? 456  ASN   C CB  1 
ATOM   8078  C  CG  . ASN   C  1 155 ? 33.759  44.337  -94.202  1.00 58.32  ? 456  ASN   C CG  1 
ATOM   8079  O  OD1 . ASN   C  1 155 ? 34.084  44.484  -95.386  1.00 70.43  ? 456  ASN   C OD1 1 
ATOM   8080  N  ND2 . ASN   C  1 155 ? 33.424  45.360  -93.421  1.00 50.28  ? 456  ASN   C ND2 1 
ATOM   8081  N  N   . LYS   C  1 156 ? 37.262  41.766  -93.984  1.00 47.96  ? 457  LYS   C N   1 
ATOM   8082  C  CA  . LYS   C  1 156 ? 38.653  42.180  -93.807  1.00 50.50  ? 457  LYS   C CA  1 
ATOM   8083  C  C   . LYS   C  1 156 ? 38.954  42.537  -92.360  1.00 55.71  ? 457  LYS   C C   1 
ATOM   8084  O  O   . LYS   C  1 156 ? 39.817  43.374  -92.091  1.00 62.98  ? 457  LYS   C O   1 
ATOM   8085  C  CB  . LYS   C  1 156 ? 39.015  43.361  -94.714  1.00 58.07  ? 457  LYS   C CB  1 
ATOM   8086  C  CG  . LYS   C  1 156 ? 39.087  43.052  -96.216  1.00 57.28  ? 457  LYS   C CG  1 
ATOM   8087  C  CD  . LYS   C  1 156 ? 39.195  44.344  -97.030  1.00 68.20  ? 457  LYS   C CD  1 
ATOM   8088  C  CE  . LYS   C  1 156 ? 39.359  44.096  -98.531  1.00 70.92  ? 457  LYS   C CE  1 
ATOM   8089  N  NZ  . LYS   C  1 156 ? 40.579  43.289  -98.811  1.00 74.36  ? 457  LYS   C NZ  1 
ATOM   8090  N  N   . GLY   C  1 157 ? 38.243  41.912  -91.417  1.00 63.52  ? 458  GLY   C N   1 
ATOM   8091  C  CA  . GLY   C  1 157 ? 38.453  42.141  -90.003  1.00 58.95  ? 458  GLY   C CA  1 
ATOM   8092  C  C   . GLY   C  1 157 ? 37.516  43.143  -89.361  1.00 57.96  ? 458  GLY   C C   1 
ATOM   8093  O  O   . GLY   C  1 157 ? 37.457  43.199  -88.126  1.00 60.46  ? 458  GLY   C O   1 
ATOM   8094  N  N   . ASN   C  1 158 ? 36.799  43.949  -90.148  1.00 46.51  ? 459  ASN   C N   1 
ATOM   8095  C  CA  . ASN   C  1 158 ? 35.794  44.857  -89.597  1.00 41.37  ? 459  ASN   C CA  1 
ATOM   8096  C  C   . ASN   C  1 158 ? 34.453  44.136  -89.655  1.00 50.36  ? 459  ASN   C C   1 
ATOM   8097  O  O   . ASN   C  1 158 ? 33.627  44.362  -90.540  1.00 52.50  ? 459  ASN   C O   1 
ATOM   8098  C  CB  . ASN   C  1 158 ? 35.776  46.171  -90.359  1.00 42.00  ? 459  ASN   C CB  1 
ATOM   8099  C  CG  . ASN   C  1 158 ? 34.594  47.057  -89.979  1.00 59.67  ? 459  ASN   C CG  1 
ATOM   8100  O  OD1 . ASN   C  1 158 ? 34.166  47.082  -88.824  1.00 72.49  ? 459  ASN   C OD1 1 
ATOM   8101  N  ND2 . ASN   C  1 158 ? 34.058  47.789  -90.959  1.00 56.32  ? 459  ASN   C ND2 1 
ATOM   8102  N  N   . LEU   C  1 159 ? 34.235  43.265  -88.667  1.00 51.02  ? 460  LEU   C N   1 
ATOM   8103  C  CA  . LEU   C  1 159 ? 33.199  42.249  -88.762  1.00 43.73  ? 460  LEU   C CA  1 
ATOM   8104  C  C   . LEU   C  1 159 ? 31.808  42.868  -88.857  1.00 48.53  ? 460  LEU   C C   1 
ATOM   8105  O  O   . LEU   C  1 159 ? 31.553  43.976  -88.368  1.00 43.78  ? 460  LEU   C O   1 
ATOM   8106  C  CB  . LEU   C  1 159 ? 33.246  41.310  -87.556  1.00 31.40  ? 460  LEU   C CB  1 
ATOM   8107  C  CG  . LEU   C  1 159 ? 34.521  40.509  -87.258  1.00 42.84  ? 460  LEU   C CG  1 
ATOM   8108  C  CD1 . LEU   C  1 159 ? 34.161  39.136  -86.719  1.00 40.39  ? 460  LEU   C CD1 1 
ATOM   8109  C  CD2 . LEU   C  1 159 ? 35.448  40.360  -88.437  1.00 44.52  ? 460  LEU   C CD2 1 
ATOM   8110  N  N   . ARG   C  1 160 ? 30.901  42.122  -89.493  1.00 34.02  ? 461  ARG   C N   1 
ATOM   8111  C  CA  . ARG   C  1 160 ? 29.500  42.488  -89.580  1.00 32.45  ? 461  ARG   C CA  1 
ATOM   8112  C  C   . ARG   C  1 160 ? 28.632  41.308  -89.182  1.00 38.32  ? 461  ARG   C C   1 
ATOM   8113  O  O   . ARG   C  1 160 ? 28.977  40.146  -89.419  1.00 46.97  ? 461  ARG   C O   1 
ATOM   8114  C  CB  . ARG   C  1 160 ? 29.152  42.951  -90.985  1.00 38.40  ? 461  ARG   C CB  1 
ATOM   8115  C  CG  . ARG   C  1 160 ? 29.871  44.233  -91.349  1.00 52.71  ? 461  ARG   C CG  1 
ATOM   8116  C  CD  . ARG   C  1 160 ? 29.599  44.659  -92.776  1.00 57.89  ? 461  ARG   C CD  1 
ATOM   8117  N  NE  . ARG   C  1 160 ? 30.350  43.866  -93.737  1.00 55.50  ? 461  ARG   C NE  1 
ATOM   8118  C  CZ  . ARG   C  1 160 ? 30.431  44.179  -95.018  1.00 53.61  ? 461  ARG   C CZ  1 
ATOM   8119  N  NH1 . ARG   C  1 160 ? 29.805  45.260  -95.469  1.00 57.59  ? 461  ARG   C NH1 1 
ATOM   8120  N  NH2 . ARG   C  1 160 ? 31.129  43.419  -95.840  1.00 52.58  ? 461  ARG   C NH2 1 
ATOM   8121  N  N   . SER   C  1 161 ? 27.509  41.613  -88.553  1.00 40.10  ? 462  SER   C N   1 
ATOM   8122  C  CA  . SER   C  1 161 ? 26.609  40.546  -88.161  1.00 47.42  ? 462  SER   C CA  1 
ATOM   8123  C  C   . SER   C  1 161 ? 25.781  40.126  -89.368  1.00 44.78  ? 462  SER   C C   1 
ATOM   8124  O  O   . SER   C  1 161 ? 25.453  40.947  -90.234  1.00 40.12  ? 462  SER   C O   1 
ATOM   8125  C  CB  . SER   C  1 161 ? 25.706  40.976  -86.994  1.00 48.53  ? 462  SER   C CB  1 
ATOM   8126  O  OG  . SER   C  1 161 ? 25.771  42.374  -86.750  1.00 57.72  ? 462  SER   C OG  1 
ATOM   8127  N  N   . ALA   C  1 162 ? 25.436  38.838  -89.414  1.00 29.93  ? 463  ALA   C N   1 
ATOM   8128  C  CA  . ALA   C  1 162 ? 24.762  38.309  -90.584  1.00 26.55  ? 463  ALA   C CA  1 
ATOM   8129  C  C   . ALA   C  1 162 ? 24.186  36.945  -90.273  1.00 33.05  ? 463  ALA   C C   1 
ATOM   8130  O  O   . ALA   C  1 162 ? 24.761  36.172  -89.511  1.00 30.99  ? 463  ALA   C O   1 
ATOM   8131  C  CB  . ALA   C  1 162 ? 25.714  38.187  -91.774  1.00 34.18  ? 463  ALA   C CB  1 
ATOM   8132  N  N   . ILE   C  1 163 ? 23.077  36.644  -90.939  1.00 46.58  ? 464  ILE   C N   1 
ATOM   8133  C  CA  . ILE   C  1 163 ? 22.422  35.346  -90.890  1.00 38.83  ? 464  ILE   C CA  1 
ATOM   8134  C  C   . ILE   C  1 163 ? 22.083  34.965  -92.327  1.00 49.85  ? 464  ILE   C C   1 
ATOM   8135  O  O   . ILE   C  1 163 ? 21.763  35.830  -93.155  1.00 45.41  ? 464  ILE   C O   1 
ATOM   8136  C  CB  . ILE   C  1 163 ? 21.170  35.392  -89.976  1.00 35.18  ? 464  ILE   C CB  1 
ATOM   8137  C  CG1 . ILE   C  1 163 ? 20.614  33.992  -89.699  1.00 36.69  ? 464  ILE   C CG1 1 
ATOM   8138  C  CG2 . ILE   C  1 163 ? 20.109  36.363  -90.518  1.00 29.75  ? 464  ILE   C CG2 1 
ATOM   8139  C  CD1 . ILE   C  1 163 ? 19.436  33.972  -88.691  1.00 26.20  ? 464  ILE   C CD1 1 
ATOM   8140  N  N   . THR   C  1 164 ? 22.226  33.682  -92.638  1.00 43.78  ? 465  THR   C N   1 
ATOM   8141  C  CA  . THR   C  1 164 ? 21.904  33.133  -93.940  1.00 48.54  ? 465  THR   C CA  1 
ATOM   8142  C  C   . THR   C  1 164 ? 20.840  32.083  -93.691  1.00 39.52  ? 465  THR   C C   1 
ATOM   8143  O  O   . THR   C  1 164 ? 21.067  31.174  -92.888  1.00 39.35  ? 465  THR   C O   1 
ATOM   8144  C  CB  . THR   C  1 164 ? 23.149  32.519  -94.624  1.00 44.40  ? 465  THR   C CB  1 
ATOM   8145  O  OG1 . THR   C  1 164 ? 23.989  33.553  -95.172  1.00 36.50  ? 465  THR   C OG1 1 
ATOM   8146  C  CG2 . THR   C  1 164 ? 22.726  31.561  -95.721  1.00 43.28  ? 465  THR   C CG2 1 
ATOM   8147  N  N   . ILE   C  1 165 ? 19.687  32.208  -94.358  1.00 36.79  ? 466  ILE   C N   1 
ATOM   8148  C  CA  . ILE   C  1 165 ? 18.493  31.438  -94.013  1.00 38.37  ? 466  ILE   C CA  1 
ATOM   8149  C  C   . ILE   C  1 165 ? 18.115  30.503  -95.164  1.00 39.96  ? 466  ILE   C C   1 
ATOM   8150  O  O   . ILE   C  1 165 ? 17.631  30.940  -96.214  1.00 37.59  ? 466  ILE   C O   1 
ATOM   8151  C  CB  . ILE   C  1 165 ? 17.316  32.344  -93.638  1.00 44.37  ? 466  ILE   C CB  1 
ATOM   8152  C  CG1 . ILE   C  1 165 ? 17.651  33.191  -92.414  1.00 33.87  ? 466  ILE   C CG1 1 
ATOM   8153  C  CG2 . ILE   C  1 165 ? 16.108  31.501  -93.305  1.00 52.30  ? 466  ILE   C CG2 1 
ATOM   8154  C  CD1 . ILE   C  1 165 ? 16.547  34.156  -92.051  1.00 27.81  ? 466  ILE   C CD1 1 
ATOM   8155  N  N   . PHE   C  1 166 ? 18.261  29.224  -94.932  1.00 43.21  ? 467  PHE   C N   1 
ATOM   8156  C  CA  . PHE   C  1 166 ? 18.061  28.168  -95.901  1.00 29.40  ? 467  PHE   C CA  1 
ATOM   8157  C  C   . PHE   C  1 166 ? 16.609  27.722  -95.886  1.00 41.01  ? 467  PHE   C C   1 
ATOM   8158  O  O   . PHE   C  1 166 ? 15.827  28.253  -95.094  1.00 52.21  ? 467  PHE   C O   1 
ATOM   8159  C  CB  . PHE   C  1 166 ? 19.019  27.026  -95.575  1.00 33.70  ? 467  PHE   C CB  1 
ATOM   8160  C  CG  . PHE   C  1 166 ? 20.430  27.313  -95.968  1.00 40.58  ? 467  PHE   C CG  1 
ATOM   8161  C  CD1 . PHE   C  1 166 ? 20.763  27.474  -97.306  1.00 39.85  ? 467  PHE   C CD1 1 
ATOM   8162  C  CD2 . PHE   C  1 166 ? 21.426  27.418  -95.013  1.00 34.76  ? 467  PHE   C CD2 1 
ATOM   8163  C  CE1 . PHE   C  1 166 ? 22.058  27.726  -97.688  1.00 39.38  ? 467  PHE   C CE1 1 
ATOM   8164  C  CE2 . PHE   C  1 166 ? 22.736  27.682  -95.389  1.00 39.82  ? 467  PHE   C CE2 1 
ATOM   8165  C  CZ  . PHE   C  1 166 ? 23.048  27.843  -96.723  1.00 49.33  ? 467  PHE   C CZ  1 
ATOM   8166  N  N   . PRO   C  1 167 ? 16.193  26.789  -96.748  1.00 48.15  ? 468  PRO   C N   1 
ATOM   8167  C  CA  . PRO   C  1 167 ? 14.769  26.455  -96.820  1.00 44.19  ? 468  PRO   C CA  1 
ATOM   8168  C  C   . PRO   C  1 167 ? 14.230  25.954  -95.491  1.00 42.74  ? 468  PRO   C C   1 
ATOM   8169  O  O   . PRO   C  1 167 ? 14.901  25.230  -94.756  1.00 53.04  ? 468  PRO   C O   1 
ATOM   8170  C  CB  . PRO   C  1 167 ? 14.726  25.356  -97.880  1.00 47.47  ? 468  PRO   C CB  1 
ATOM   8171  C  CG  . PRO   C  1 167 ? 15.867  25.655  -98.748  1.00 46.33  ? 468  PRO   C CG  1 
ATOM   8172  C  CD  . PRO   C  1 167 ? 16.942  26.089  -97.808  1.00 49.03  ? 468  PRO   C CD  1 
ATOM   8173  N  N   . GLN   C  1 168 ? 12.990  26.325  -95.204  1.00 51.49  ? 469  GLN   C N   1 
ATOM   8174  C  CA  . GLN   C  1 168 ? 12.345  25.861  -93.994  1.00 53.45  ? 469  GLN   C CA  1 
ATOM   8175  C  C   . GLN   C  1 168 ? 12.092  24.362  -94.062  1.00 60.15  ? 469  GLN   C C   1 
ATOM   8176  O  O   . GLN   C  1 168 ? 12.096  23.744  -95.135  1.00 58.50  ? 469  GLN   C O   1 
ATOM   8177  C  CB  . GLN   C  1 168 ? 11.031  26.591  -93.776  1.00 52.29  ? 469  GLN   C CB  1 
ATOM   8178  C  CG  . GLN   C  1 168 ? 10.074  26.439  -94.899  1.00 34.30  ? 469  GLN   C CG  1 
ATOM   8179  C  CD  . GLN   C  1 168 ? 9.185   27.645  -95.021  1.00 46.72  ? 469  GLN   C CD  1 
ATOM   8180  O  OE1 . GLN   C  1 168 ? 9.666   28.776  -95.172  1.00 44.64  ? 469  GLN   C OE1 1 
ATOM   8181  N  NE2 . GLN   C  1 168 ? 7.876   27.422  -94.952  1.00 41.79  ? 469  GLN   C NE2 1 
ATOM   8182  N  N   . ARG   C  1 169 ? 11.887  23.783  -92.880  1.00 64.32  ? 470  ARG   C N   1 
ATOM   8183  C  CA  . ARG   C  1 169 ? 11.536  22.374  -92.762  1.00 61.57  ? 470  ARG   C CA  1 
ATOM   8184  C  C   . ARG   C  1 169 ? 10.120  22.156  -93.272  1.00 58.59  ? 470  ARG   C C   1 
ATOM   8185  O  O   . ARG   C  1 169 ? 9.232   22.991  -93.069  1.00 56.94  ? 470  ARG   C O   1 
ATOM   8186  C  CB  . ARG   C  1 169 ? 11.665  21.917  -91.306  1.00 58.88  ? 470  ARG   C CB  1 
ATOM   8187  C  CG  . ARG   C  1 169 ? 11.272  20.473  -91.075  1.00 58.81  ? 470  ARG   C CG  1 
ATOM   8188  C  CD  . ARG   C  1 169 ? 11.361  20.101  -89.608  1.00 54.95  ? 470  ARG   C CD  1 
ATOM   8189  N  NE  . ARG   C  1 169 ? 12.739  19.994  -89.157  1.00 55.29  ? 470  ARG   C NE  1 
ATOM   8190  C  CZ  . ARG   C  1 169 ? 13.126  20.260  -87.917  1.00 67.19  ? 470  ARG   C CZ  1 
ATOM   8191  N  NH1 . ARG   C  1 169 ? 12.227  20.656  -87.027  1.00 74.77  ? 470  ARG   C NH1 1 
ATOM   8192  N  NH2 . ARG   C  1 169 ? 14.405  20.155  -87.568  1.00 66.25  ? 470  ARG   C NH2 1 
ATOM   8193  N  N   . THR   C  1 170 ? 9.908   21.038  -93.960  1.00 52.02  ? 471  THR   C N   1 
ATOM   8194  C  CA  . THR   C  1 170 ? 8.586   20.747  -94.508  1.00 56.36  ? 471  THR   C CA  1 
ATOM   8195  C  C   . THR   C  1 170 ? 8.000   19.491  -93.876  1.00 63.05  ? 471  THR   C C   1 
ATOM   8196  O  O   . THR   C  1 170 ? 7.002   19.588  -93.159  1.00 63.84  ? 471  THR   C O   1 
ATOM   8197  C  CB  . THR   C  1 170 ? 8.656   20.657  -96.038  1.00 59.08  ? 471  THR   C CB  1 
ATOM   8198  O  OG1 . THR   C  1 170 ? 9.455   19.531  -96.437  1.00 60.12  ? 471  THR   C OG1 1 
ATOM   8199  C  CG2 . THR   C  1 170 ? 9.256   21.952  -96.611  1.00 55.16  ? 471  THR   C CG2 1 
ATOM   8200  N  N   . ASP   C  1 171 ? 8.579   18.315  -94.112  1.00 66.53  ? 472  ASP   C N   1 
ATOM   8201  C  CA  . ASP   C  1 171 ? 8.065   17.090  -93.511  1.00 69.89  ? 472  ASP   C CA  1 
ATOM   8202  C  C   . ASP   C  1 171 ? 9.084   16.435  -92.587  1.00 70.70  ? 472  ASP   C C   1 
ATOM   8203  O  O   . ASP   C  1 171 ? 8.885   15.287  -92.174  1.00 73.59  ? 472  ASP   C O   1 
ATOM   8204  C  CB  . ASP   C  1 171 ? 7.603   16.104  -94.596  1.00 74.37  ? 472  ASP   C CB  1 
ATOM   8205  C  CG  . ASP   C  1 171 ? 8.759   15.493  -95.382  1.00 76.37  ? 472  ASP   C CG  1 
ATOM   8206  O  OD1 . ASP   C  1 171 ? 9.909   15.963  -95.267  1.00 81.34  ? 472  ASP   C OD1 1 
ATOM   8207  O  OD2 . ASP   C  1 171 ? 8.517   14.526  -96.125  1.00 76.83  ? 472  ASP   C OD2 1 
ATOM   8208  N  N   . GLY   C  1 172 ? 10.162  17.131  -92.246  1.00 68.28  ? 473  GLY   C N   1 
ATOM   8209  C  CA  . GLY   C  1 172 ? 11.204  16.597  -91.385  1.00 72.71  ? 473  GLY   C CA  1 
ATOM   8210  C  C   . GLY   C  1 172 ? 12.224  15.726  -92.097  1.00 82.75  ? 473  GLY   C C   1 
ATOM   8211  O  O   . GLY   C  1 172 ? 13.410  15.756  -91.763  1.00 93.22  ? 473  GLY   C O   1 
ATOM   8212  N  N   . LYS   C  1 173 ? 11.777  14.940  -93.068  1.00 82.73  ? 474  LYS   C N   1 
ATOM   8213  C  CA  . LYS   C  1 173 ? 12.675  14.085  -93.828  1.00 80.19  ? 474  LYS   C CA  1 
ATOM   8214  C  C   . LYS   C  1 173 ? 13.378  14.822  -94.964  1.00 78.28  ? 474  LYS   C C   1 
ATOM   8215  O  O   . LYS   C  1 173 ? 14.145  14.201  -95.706  1.00 73.36  ? 474  LYS   C O   1 
ATOM   8216  C  CB  . LYS   C  1 173 ? 11.898  12.887  -94.376  1.00 77.64  ? 474  LYS   C CB  1 
ATOM   8217  C  CG  . LYS   C  1 173 ? 11.572  11.811  -93.343  1.00 77.06  ? 474  LYS   C CG  1 
ATOM   8218  C  CD  . LYS   C  1 173 ? 10.406  10.943  -93.815  1.00 84.68  ? 474  LYS   C CD  1 
ATOM   8219  C  CE  . LYS   C  1 173 ? 10.372  9.579   -93.131  1.00 88.72  ? 474  LYS   C CE  1 
ATOM   8220  N  NZ  . LYS   C  1 173 ? 9.184   8.755   -93.540  1.00 87.29  ? 474  LYS   C NZ  1 
ATOM   8221  N  N   . HIS   C  1 174 ? 13.128  16.115  -95.133  1.00 76.34  ? 475  HIS   C N   1 
ATOM   8222  C  CA  . HIS   C  1 174 ? 13.782  16.918  -96.156  1.00 75.09  ? 475  HIS   C CA  1 
ATOM   8223  C  C   . HIS   C  1 174 ? 14.528  18.073  -95.510  1.00 68.89  ? 475  HIS   C C   1 
ATOM   8224  O  O   . HIS   C  1 174 ? 14.575  19.185  -96.039  1.00 66.86  ? 475  HIS   C O   1 
ATOM   8225  C  CB  . HIS   C  1 174 ? 12.777  17.445  -97.180  1.00 77.43  ? 475  HIS   C CB  1 
ATOM   8226  C  CG  . HIS   C  1 174 ? 12.161  16.388  -98.043  1.00 71.09  ? 475  HIS   C CG  1 
ATOM   8227  N  ND1 . HIS   C  1 174 ? 12.198  15.046  -97.732  1.00 71.21  ? 475  HIS   C ND1 1 
ATOM   8228  C  CD2 . HIS   C  1 174 ? 11.470  16.485  -99.201  1.00 64.56  ? 475  HIS   C CD2 1 
ATOM   8229  C  CE1 . HIS   C  1 174 ? 11.566  14.360  -98.665  1.00 70.24  ? 475  HIS   C CE1 1 
ATOM   8230  N  NE2 . HIS   C  1 174 ? 11.114  15.210  -99.568  1.00 72.57  ? 475  HIS   C NE2 1 
ATOM   8231  N  N   . ASP   C  1 175 ? 15.102  17.824  -94.339  1.00 65.17  ? 476  ASP   C N   1 
ATOM   8232  C  CA  . ASP   C  1 175 ? 15.756  18.887  -93.593  1.00 59.46  ? 476  ASP   C CA  1 
ATOM   8233  C  C   . ASP   C  1 175 ? 16.980  19.392  -94.335  1.00 55.31  ? 476  ASP   C C   1 
ATOM   8234  O  O   . ASP   C  1 175 ? 17.712  18.615  -94.948  1.00 62.82  ? 476  ASP   C O   1 
ATOM   8235  C  CB  . ASP   C  1 175 ? 16.185  18.387  -92.212  1.00 64.21  ? 476  ASP   C CB  1 
ATOM   8236  C  CG  . ASP   C  1 175 ? 15.095  18.499  -91.189  1.00 61.43  ? 476  ASP   C CG  1 
ATOM   8237  O  OD1 . ASP   C  1 175 ? 13.953  18.777  -91.599  1.00 68.90  ? 476  ASP   C OD1 1 
ATOM   8238  O  OD2 . ASP   C  1 175 ? 15.382  18.326  -89.984  1.00 61.01  ? 476  ASP   C OD2 1 
ATOM   8239  N  N   . PHE   C  1 176 ? 17.199  20.702  -94.278  1.00 49.43  ? 477  PHE   C N   1 
ATOM   8240  C  CA  . PHE   C  1 176 ? 18.510  21.272  -94.535  1.00 45.63  ? 477  PHE   C CA  1 
ATOM   8241  C  C   . PHE   C  1 176 ? 19.243  21.388  -93.210  1.00 50.57  ? 477  PHE   C C   1 
ATOM   8242  O  O   . PHE   C  1 176 ? 18.635  21.732  -92.197  1.00 62.77  ? 477  PHE   C O   1 
ATOM   8243  C  CB  . PHE   C  1 176 ? 18.390  22.643  -95.188  1.00 44.30  ? 477  PHE   C CB  1 
ATOM   8244  C  CG  . PHE   C  1 176 ? 18.042  22.587  -96.647  1.00 50.58  ? 477  PHE   C CG  1 
ATOM   8245  C  CD1 . PHE   C  1 176 ? 16.780  22.208  -97.056  1.00 51.70  ? 477  PHE   C CD1 1 
ATOM   8246  C  CD2 . PHE   C  1 176 ? 18.983  22.908  -97.604  1.00 47.24  ? 477  PHE   C CD2 1 
ATOM   8247  C  CE1 . PHE   C  1 176 ? 16.467  22.140  -98.388  1.00 56.20  ? 477  PHE   C CE1 1 
ATOM   8248  C  CE2 . PHE   C  1 176 ? 18.679  22.847  -98.937  1.00 51.48  ? 477  PHE   C CE2 1 
ATOM   8249  C  CZ  . PHE   C  1 176 ? 17.421  22.466  -99.332  1.00 52.68  ? 477  PHE   C CZ  1 
ATOM   8250  N  N   . ARG   C  1 177 ? 20.548  21.105  -93.215  1.00 50.32  ? 478  ARG   C N   1 
ATOM   8251  C  CA  . ARG   C  1 177 ? 21.318  21.073  -91.970  1.00 55.88  ? 478  ARG   C CA  1 
ATOM   8252  C  C   . ARG   C  1 177 ? 22.784  21.387  -92.224  1.00 53.11  ? 478  ARG   C C   1 
ATOM   8253  O  O   . ARG   C  1 177 ? 23.451  20.683  -92.987  1.00 61.69  ? 478  ARG   C O   1 
ATOM   8254  C  CB  . ARG   C  1 177 ? 21.211  19.701  -91.285  1.00 54.95  ? 478  ARG   C CB  1 
ATOM   8255  C  CG  . ARG   C  1 177 ? 19.900  19.401  -90.570  1.00 61.83  ? 478  ARG   C CG  1 
ATOM   8256  C  CD  . ARG   C  1 177 ? 19.521  20.500  -89.587  1.00 57.94  ? 478  ARG   C CD  1 
ATOM   8257  N  NE  . ARG   C  1 177 ? 20.342  20.514  -88.381  1.00 57.76  ? 478  ARG   C NE  1 
ATOM   8258  C  CZ  . ARG   C  1 177 ? 20.134  19.732  -87.329  1.00 59.45  ? 478  ARG   C CZ  1 
ATOM   8259  N  NH1 . ARG   C  1 177 ? 19.143  18.853  -87.337  1.00 56.58  ? 478  ARG   C NH1 1 
ATOM   8260  N  NH2 . ARG   C  1 177 ? 20.919  19.824  -86.272  1.00 59.93  ? 478  ARG   C NH2 1 
ATOM   8261  N  N   . VAL   C  1 178 ? 23.302  22.409  -91.557  1.00 44.94  ? 479  VAL   C N   1 
ATOM   8262  C  CA  . VAL   C  1 178 ? 24.739  22.490  -91.329  1.00 47.01  ? 479  VAL   C CA  1 
ATOM   8263  C  C   . VAL   C  1 178 ? 25.059  21.525  -90.199  1.00 58.22  ? 479  VAL   C C   1 
ATOM   8264  O  O   . VAL   C  1 178 ? 24.534  21.667  -89.089  1.00 55.29  ? 479  VAL   C O   1 
ATOM   8265  C  CB  . VAL   C  1 178 ? 25.181  23.914  -90.969  1.00 38.37  ? 479  VAL   C CB  1 
ATOM   8266  C  CG1 . VAL   C  1 178 ? 26.688  23.955  -90.822  1.00 34.53  ? 479  VAL   C CG1 1 
ATOM   8267  C  CG2 . VAL   C  1 178 ? 24.721  24.906  -92.015  1.00 41.67  ? 479  VAL   C CG2 1 
ATOM   8268  N  N   . TRP   C  1 179 ? 25.891  20.521  -90.485  1.00 59.65  ? 480  TRP   C N   1 
ATOM   8269  C  CA  . TRP   C  1 179 ? 26.243  19.539  -89.462  1.00 50.31  ? 480  TRP   C CA  1 
ATOM   8270  C  C   . TRP   C  1 179 ? 27.306  20.057  -88.509  1.00 50.01  ? 480  TRP   C C   1 
ATOM   8271  O  O   . TRP   C  1 179 ? 27.400  19.565  -87.381  1.00 51.55  ? 480  TRP   C O   1 
ATOM   8272  C  CB  . TRP   C  1 179 ? 26.716  18.235  -90.109  1.00 42.26  ? 480  TRP   C CB  1 
ATOM   8273  C  CG  . TRP   C  1 179 ? 25.589  17.395  -90.579  1.00 48.98  ? 480  TRP   C CG  1 
ATOM   8274  C  CD1 . TRP   C  1 179 ? 24.431  17.827  -91.171  1.00 56.30  ? 480  TRP   C CD1 1 
ATOM   8275  C  CD2 . TRP   C  1 179 ? 25.484  15.975  -90.486  1.00 45.04  ? 480  TRP   C CD2 1 
ATOM   8276  N  NE1 . TRP   C  1 179 ? 23.615  16.756  -91.454  1.00 50.46  ? 480  TRP   C NE1 1 
ATOM   8277  C  CE2 . TRP   C  1 179 ? 24.238  15.609  -91.038  1.00 49.66  ? 480  TRP   C CE2 1 
ATOM   8278  C  CE3 . TRP   C  1 179 ? 26.328  14.974  -90.010  1.00 45.73  ? 480  TRP   C CE3 1 
ATOM   8279  C  CZ2 . TRP   C  1 179 ? 23.814  14.285  -91.109  1.00 54.08  ? 480  TRP   C CZ2 1 
ATOM   8280  C  CZ3 . TRP   C  1 179 ? 25.901  13.659  -90.080  1.00 50.47  ? 480  TRP   C CZ3 1 
ATOM   8281  C  CH2 . TRP   C  1 179 ? 24.657  13.327  -90.627  1.00 53.15  ? 480  TRP   C CH2 1 
ATOM   8282  N  N   . ASN   C  1 180 ? 28.112  21.024  -88.947  1.00 46.76  ? 481  ASN   C N   1 
ATOM   8283  C  CA  . ASN   C  1 180 ? 29.051  21.677  -88.058  1.00 41.51  ? 481  ASN   C CA  1 
ATOM   8284  C  C   . ASN   C  1 180 ? 28.287  22.437  -86.996  1.00 55.41  ? 481  ASN   C C   1 
ATOM   8285  O  O   . ASN   C  1 180 ? 27.221  22.996  -87.262  1.00 66.88  ? 481  ASN   C O   1 
ATOM   8286  C  CB  . ASN   C  1 180 ? 29.925  22.653  -88.826  1.00 35.28  ? 481  ASN   C CB  1 
ATOM   8287  C  CG  . ASN   C  1 180 ? 30.642  22.006  -89.988  1.00 44.43  ? 481  ASN   C CG  1 
ATOM   8288  O  OD1 . ASN   C  1 180 ? 30.045  21.288  -90.797  1.00 48.74  ? 481  ASN   C OD1 1 
ATOM   8289  N  ND2 . ASN   C  1 180 ? 31.940  22.271  -90.088  1.00 44.43  ? 481  ASN   C ND2 1 
ATOM   8290  N  N   . SER   C  1 181 ? 28.841  22.467  -85.778  1.00 50.86  ? 482  SER   C N   1 
ATOM   8291  C  CA  . SER   C  1 181 ? 28.218  23.264  -84.724  1.00 35.87  ? 482  SER   C CA  1 
ATOM   8292  C  C   . SER   C  1 181 ? 28.536  24.746  -84.899  1.00 32.20  ? 482  SER   C C   1 
ATOM   8293  O  O   . SER   C  1 181 ? 27.677  25.601  -84.662  1.00 43.16  ? 482  SER   C O   1 
ATOM   8294  C  CB  . SER   C  1 181 ? 28.668  22.762  -83.366  1.00 41.86  ? 482  SER   C CB  1 
ATOM   8295  O  OG  . SER   C  1 181 ? 30.051  22.455  -83.418  1.00 58.54  ? 482  SER   C OG  1 
ATOM   8296  N  N   . GLN   C  1 182 ? 29.752  25.071  -85.329  1.00 36.35  ? 483  GLN   C N   1 
ATOM   8297  C  CA  . GLN   C  1 182 ? 30.043  26.380  -85.903  1.00 46.43  ? 483  GLN   C CA  1 
ATOM   8298  C  C   . GLN   C  1 182 ? 30.677  26.200  -87.278  1.00 49.48  ? 483  GLN   C C   1 
ATOM   8299  O  O   . GLN   C  1 182 ? 31.242  25.148  -87.589  1.00 62.88  ? 483  GLN   C O   1 
ATOM   8300  C  CB  . GLN   C  1 182 ? 30.973  27.213  -85.029  1.00 44.93  ? 483  GLN   C CB  1 
ATOM   8301  C  CG  . GLN   C  1 182 ? 30.391  27.656  -83.705  1.00 44.34  ? 483  GLN   C CG  1 
ATOM   8302  C  CD  . GLN   C  1 182 ? 31.492  27.968  -82.692  1.00 50.32  ? 483  GLN   C CD  1 
ATOM   8303  O  OE1 . GLN   C  1 182 ? 32.392  28.785  -82.952  1.00 51.50  ? 483  GLN   C OE1 1 
ATOM   8304  N  NE2 . GLN   C  1 182 ? 31.449  27.286  -81.550  1.00 44.47  ? 483  GLN   C NE2 1 
ATOM   8305  N  N   . LEU   C  1 183 ? 30.591  27.251  -88.098  1.00 42.92  ? 484  LEU   C N   1 
ATOM   8306  C  CA  . LEU   C  1 183 ? 31.153  27.179  -89.447  1.00 44.22  ? 484  LEU   C CA  1 
ATOM   8307  C  C   . LEU   C  1 183 ? 32.660  26.948  -89.407  1.00 50.89  ? 484  LEU   C C   1 
ATOM   8308  O  O   . LEU   C  1 183 ? 33.194  26.118  -90.155  1.00 50.54  ? 484  LEU   C O   1 
ATOM   8309  C  CB  . LEU   C  1 183 ? 30.816  28.454  -90.221  1.00 32.40  ? 484  LEU   C CB  1 
ATOM   8310  C  CG  . LEU   C  1 183 ? 29.318  28.711  -90.425  1.00 31.66  ? 484  LEU   C CG  1 
ATOM   8311  C  CD1 . LEU   C  1 183 ? 29.068  29.850  -91.397  1.00 31.22  ? 484  LEU   C CD1 1 
ATOM   8312  C  CD2 . LEU   C  1 183 ? 28.656  27.418  -90.899  1.00 33.29  ? 484  LEU   C CD2 1 
ATOM   8313  N  N   . ILE   C  1 184 ? 33.356  27.640  -88.516  1.00 51.86  ? 485  ILE   C N   1 
ATOM   8314  C  CA  . ILE   C  1 184 ? 34.803  27.540  -88.383  1.00 52.22  ? 485  ILE   C CA  1 
ATOM   8315  C  C   . ILE   C  1 184 ? 35.089  27.055  -86.967  1.00 58.38  ? 485  ILE   C C   1 
ATOM   8316  O  O   . ILE   C  1 184 ? 34.884  27.800  -86.000  1.00 60.57  ? 485  ILE   C O   1 
ATOM   8317  C  CB  . ILE   C  1 184 ? 35.490  28.884  -88.670  1.00 45.27  ? 485  ILE   C CB  1 
ATOM   8318  C  CG1 . ILE   C  1 184 ? 34.987  29.454  -89.998  1.00 44.89  ? 485  ILE   C CG1 1 
ATOM   8319  C  CG2 . ILE   C  1 184 ? 36.996  28.736  -88.735  1.00 36.79  ? 485  ILE   C CG2 1 
ATOM   8320  C  CD1 . ILE   C  1 184 ? 35.202  30.928  -90.116  1.00 43.14  ? 485  ILE   C CD1 1 
ATOM   8321  N  N   . ARG   C  1 185 ? 35.522  25.796  -86.842  1.00 48.55  ? 486  ARG   C N   1 
ATOM   8322  C  CA  . ARG   C  1 185 ? 35.989  25.214  -85.587  1.00 46.07  ? 486  ARG   C CA  1 
ATOM   8323  C  C   . ARG   C  1 185 ? 37.246  24.401  -85.874  1.00 52.83  ? 486  ARG   C C   1 
ATOM   8324  O  O   . ARG   C  1 185 ? 37.429  23.901  -86.986  1.00 43.70  ? 486  ARG   C O   1 
ATOM   8325  C  CB  . ARG   C  1 185 ? 34.961  24.273  -84.942  1.00 44.15  ? 486  ARG   C CB  1 
ATOM   8326  C  CG  . ARG   C  1 185 ? 33.646  24.876  -84.492  1.00 49.79  ? 486  ARG   C CG  1 
ATOM   8327  C  CD  . ARG   C  1 185 ? 33.756  25.523  -83.129  1.00 68.83  ? 486  ARG   C CD  1 
ATOM   8328  N  NE  . ARG   C  1 185 ? 34.074  24.593  -82.039  1.00 76.95  ? 486  ARG   C NE  1 
ATOM   8329  C  CZ  . ARG   C  1 185 ? 33.169  23.993  -81.264  1.00 66.23  ? 486  ARG   C CZ  1 
ATOM   8330  N  NH1 . ARG   C  1 185 ? 31.874  24.198  -81.454  1.00 59.62  ? 486  ARG   C NH1 1 
ATOM   8331  N  NH2 . ARG   C  1 185 ? 33.557  23.183  -80.297  1.00 63.90  ? 486  ARG   C NH2 1 
ATOM   8332  N  N   . TYR   C  1 186 ? 38.095  24.224  -84.869  1.00 48.91  ? 487  TYR   C N   1 
ATOM   8333  C  CA  . TYR   C  1 186 ? 39.262  23.392  -85.111  1.00 47.77  ? 487  TYR   C CA  1 
ATOM   8334  C  C   . TYR   C  1 186 ? 38.974  21.926  -84.783  1.00 56.67  ? 487  TYR   C C   1 
ATOM   8335  O  O   . TYR   C  1 186 ? 38.066  21.595  -84.022  1.00 67.23  ? 487  TYR   C O   1 
ATOM   8336  C  CB  . TYR   C  1 186 ? 40.464  23.889  -84.314  1.00 45.43  ? 487  TYR   C CB  1 
ATOM   8337  C  CG  . TYR   C  1 186 ? 40.892  25.307  -84.638  1.00 46.78  ? 487  TYR   C CG  1 
ATOM   8338  C  CD1 . TYR   C  1 186 ? 40.679  26.320  -83.737  1.00 52.95  ? 487  TYR   C CD1 1 
ATOM   8339  C  CD2 . TYR   C  1 186 ? 41.501  25.631  -85.834  1.00 49.65  ? 487  TYR   C CD2 1 
ATOM   8340  C  CE1 . TYR   C  1 186 ? 41.065  27.613  -83.999  1.00 52.34  ? 487  TYR   C CE1 1 
ATOM   8341  C  CE2 . TYR   C  1 186 ? 41.899  26.938  -86.102  1.00 55.81  ? 487  TYR   C CE2 1 
ATOM   8342  C  CZ  . TYR   C  1 186 ? 41.674  27.926  -85.164  1.00 52.40  ? 487  TYR   C CZ  1 
ATOM   8343  O  OH  . TYR   C  1 186 ? 42.040  29.245  -85.378  1.00 52.90  ? 487  TYR   C OH  1 
ATOM   8344  N  N   . ALA   C  1 187 ? 39.771  21.045  -85.381  1.00 61.69  ? 488  ALA   C N   1 
ATOM   8345  C  CA  . ALA   C  1 187 ? 39.578  19.612  -85.269  1.00 55.51  ? 488  ALA   C CA  1 
ATOM   8346  C  C   . ALA   C  1 187 ? 40.134  19.087  -83.953  1.00 65.95  ? 488  ALA   C C   1 
ATOM   8347  O  O   . ALA   C  1 187 ? 41.009  19.693  -83.329  1.00 71.35  ? 488  ALA   C O   1 
ATOM   8348  C  CB  . ALA   C  1 187 ? 40.252  18.893  -86.431  1.00 55.89  ? 488  ALA   C CB  1 
ATOM   8349  N  N   . GLY   C  1 188 ? 39.618  17.929  -83.543  1.00 62.07  ? 489  GLY   C N   1 
ATOM   8350  C  CA  . GLY   C  1 188 ? 40.088  17.247  -82.353  1.00 59.79  ? 489  GLY   C CA  1 
ATOM   8351  C  C   . GLY   C  1 188 ? 40.444  15.796  -82.611  1.00 65.48  ? 489  GLY   C C   1 
ATOM   8352  O  O   . GLY   C  1 188 ? 39.661  15.046  -83.206  1.00 70.28  ? 489  GLY   C O   1 
ATOM   8353  N  N   . TYR   C  1 189 ? 41.620  15.381  -82.152  1.00 60.92  ? 490  TYR   C N   1 
ATOM   8354  C  CA  . TYR   C  1 189 ? 42.188  14.094  -82.514  1.00 59.67  ? 490  TYR   C CA  1 
ATOM   8355  C  C   . TYR   C  1 189 ? 42.472  13.292  -81.256  1.00 68.50  ? 490  TYR   C C   1 
ATOM   8356  O  O   . TYR   C  1 189 ? 43.136  13.787  -80.339  1.00 78.74  ? 490  TYR   C O   1 
ATOM   8357  C  CB  . TYR   C  1 189 ? 43.465  14.284  -83.336  1.00 61.88  ? 490  TYR   C CB  1 
ATOM   8358  C  CG  . TYR   C  1 189 ? 43.275  15.072  -84.624  1.00 63.99  ? 490  TYR   C CG  1 
ATOM   8359  C  CD1 . TYR   C  1 189 ? 43.843  16.331  -84.776  1.00 65.86  ? 490  TYR   C CD1 1 
ATOM   8360  C  CD2 . TYR   C  1 189 ? 42.528  14.557  -85.682  1.00 60.88  ? 490  TYR   C CD2 1 
ATOM   8361  C  CE1 . TYR   C  1 189 ? 43.673  17.061  -85.942  1.00 68.99  ? 490  TYR   C CE1 1 
ATOM   8362  C  CE2 . TYR   C  1 189 ? 42.357  15.279  -86.861  1.00 66.42  ? 490  TYR   C CE2 1 
ATOM   8363  C  CZ  . TYR   C  1 189 ? 42.940  16.531  -86.986  1.00 70.79  ? 490  TYR   C CZ  1 
ATOM   8364  O  OH  . TYR   C  1 189 ? 42.779  17.268  -88.147  1.00 68.56  ? 490  TYR   C OH  1 
ATOM   8365  N  N   . LYS   C  1 190 ? 41.962  12.059  -81.217  1.00 66.63  ? 491  LYS   C N   1 
ATOM   8366  C  CA  . LYS   C  1 190 ? 42.108  11.171  -80.066  1.00 66.04  ? 491  LYS   C CA  1 
ATOM   8367  C  C   . LYS   C  1 190 ? 43.398  10.372  -80.237  1.00 79.50  ? 491  LYS   C C   1 
ATOM   8368  O  O   . LYS   C  1 190 ? 43.498  9.532   -81.135  1.00 86.31  ? 491  LYS   C O   1 
ATOM   8369  C  CB  . LYS   C  1 190 ? 40.894  10.253  -79.953  1.00 74.04  ? 491  LYS   C CB  1 
ATOM   8370  C  CG  . LYS   C  1 190 ? 40.713  9.599   -78.588  1.00 87.06  ? 491  LYS   C CG  1 
ATOM   8371  C  CD  . LYS   C  1 190 ? 39.511  10.170  -77.821  1.00 88.90  ? 491  LYS   C CD  1 
ATOM   8372  C  CE  . LYS   C  1 190 ? 39.870  11.393  -76.971  1.00 83.78  ? 491  LYS   C CE  1 
ATOM   8373  N  NZ  . LYS   C  1 190 ? 40.844  11.054  -75.884  1.00 83.15  ? 491  LYS   C NZ  1 
ATOM   8374  N  N   . GLN   C  1 191 ? 44.371  10.617  -79.361  1.00 92.19  ? 492  GLN   C N   1 
ATOM   8375  C  CA  . GLN   C  1 191 ? 45.753  10.202  -79.575  1.00 98.04  ? 492  GLN   C CA  1 
ATOM   8376  C  C   . GLN   C  1 191 ? 45.977  8.739   -79.210  1.00 95.17  ? 492  GLN   C C   1 
ATOM   8377  O  O   . GLN   C  1 191 ? 45.139  8.103   -78.567  1.00 90.96  ? 492  GLN   C O   1 
ATOM   8378  C  CB  . GLN   C  1 191 ? 46.698  11.097  -78.771  1.00 100.28 ? 492  GLN   C CB  1 
ATOM   8379  C  CG  . GLN   C  1 191 ? 46.798  12.536  -79.261  1.00 98.18  ? 492  GLN   C CG  1 
ATOM   8380  C  CD  . GLN   C  1 191 ? 47.552  12.693  -80.575  1.00 94.01  ? 492  GLN   C CD  1 
ATOM   8381  O  OE1 . GLN   C  1 191 ? 47.540  11.813  -81.433  1.00 90.70  ? 492  GLN   C OE1 1 
ATOM   8382  N  NE2 . GLN   C  1 191 ? 48.211  13.832  -80.735  1.00 95.22  ? 492  GLN   C NE2 1 
ATOM   8383  N  N   . PRO   C  1 192 ? 47.124  8.163   -79.641  1.00 93.64  ? 493  PRO   C N   1 
ATOM   8384  C  CA  . PRO   C  1 192 ? 47.460  6.795   -79.236  1.00 92.74  ? 493  PRO   C CA  1 
ATOM   8385  C  C   . PRO   C  1 192 ? 47.409  6.582   -77.728  1.00 98.83  ? 493  PRO   C C   1 
ATOM   8386  O  O   . PRO   C  1 192 ? 46.712  5.675   -77.250  1.00 95.97  ? 493  PRO   C O   1 
ATOM   8387  C  CB  . PRO   C  1 192 ? 48.877  6.612   -79.783  1.00 83.97  ? 493  PRO   C CB  1 
ATOM   8388  C  CG  . PRO   C  1 192 ? 48.942  7.490   -80.967  1.00 80.99  ? 493  PRO   C CG  1 
ATOM   8389  C  CD  . PRO   C  1 192 ? 48.036  8.663   -80.686  1.00 84.10  ? 493  PRO   C CD  1 
ATOM   8390  N  N   . ASP   C  1 193 ? 48.133  7.411   -76.967  1.00 101.91 ? 494  ASP   C N   1 
ATOM   8391  C  CA  . ASP   C  1 193 ? 48.222  7.205   -75.521  1.00 94.96  ? 494  ASP   C CA  1 
ATOM   8392  C  C   . ASP   C  1 193 ? 46.858  7.337   -74.859  1.00 93.40  ? 494  ASP   C C   1 
ATOM   8393  O  O   . ASP   C  1 193 ? 46.474  6.507   -74.027  1.00 100.28 ? 494  ASP   C O   1 
ATOM   8394  C  CB  . ASP   C  1 193 ? 49.222  8.181   -74.884  1.00 87.91  ? 494  ASP   C CB  1 
ATOM   8395  C  CG  . ASP   C  1 193 ? 49.112  9.594   -75.431  1.00 84.19  ? 494  ASP   C CG  1 
ATOM   8396  O  OD1 . ASP   C  1 193 ? 50.131  10.127  -75.933  1.00 83.74  ? 494  ASP   C OD1 1 
ATOM   8397  O  OD2 . ASP   C  1 193 ? 48.011  10.176  -75.366  1.00 85.67  ? 494  ASP   C OD2 1 
ATOM   8398  N  N   . GLY   C  1 194 ? 46.111  8.372   -75.218  1.00 87.74  ? 495  GLY   C N   1 
ATOM   8399  C  CA  . GLY   C  1 194 ? 44.826  8.598   -74.594  1.00 82.84  ? 495  GLY   C CA  1 
ATOM   8400  C  C   . GLY   C  1 194 ? 44.457  10.063  -74.538  1.00 88.68  ? 495  GLY   C C   1 
ATOM   8401  O  O   . GLY   C  1 194 ? 43.271  10.406  -74.528  1.00 95.34  ? 495  GLY   C O   1 
ATOM   8402  N  N   . SER   C  1 195 ? 45.456  10.939  -74.515  1.00 91.46  ? 496  SER   C N   1 
ATOM   8403  C  CA  . SER   C  1 195 ? 45.198  12.373  -74.488  1.00 93.55  ? 496  SER   C CA  1 
ATOM   8404  C  C   . SER   C  1 195 ? 44.684  12.813  -75.863  1.00 90.48  ? 496  SER   C C   1 
ATOM   8405  O  O   . SER   C  1 195 ? 44.328  11.998  -76.718  1.00 97.71  ? 496  SER   C O   1 
ATOM   8406  C  CB  . SER   C  1 195 ? 46.445  13.138  -74.052  1.00 97.28  ? 496  SER   C CB  1 
ATOM   8407  O  OG  . SER   C  1 195 ? 47.037  13.824  -75.138  1.00 95.36  ? 496  SER   C OG  1 
ATOM   8408  N  N   . THR   C  1 196 ? 44.638  14.121  -76.094  1.00 77.12  ? 497  THR   C N   1 
ATOM   8409  C  CA  . THR   C  1 196 ? 43.845  14.636  -77.196  1.00 70.83  ? 497  THR   C CA  1 
ATOM   8410  C  C   . THR   C  1 196 ? 44.507  15.850  -77.820  1.00 75.20  ? 497  THR   C C   1 
ATOM   8411  O  O   . THR   C  1 196 ? 44.886  16.784  -77.113  1.00 78.69  ? 497  THR   C O   1 
ATOM   8412  C  CB  . THR   C  1 196 ? 42.444  14.999  -76.711  1.00 70.71  ? 497  THR   C CB  1 
ATOM   8413  O  OG1 . THR   C  1 196 ? 41.863  13.872  -76.034  1.00 78.52  ? 497  THR   C OG1 1 
ATOM   8414  C  CG2 . THR   C  1 196 ? 41.579  15.398  -77.890  1.00 63.97  ? 497  THR   C CG2 1 
ATOM   8415  N  N   . LEU   C  1 197 ? 44.613  15.838  -79.145  1.00 77.86  ? 498  LEU   C N   1 
ATOM   8416  C  CA  . LEU   C  1 197 ? 45.206  16.924  -79.911  1.00 81.89  ? 498  LEU   C CA  1 
ATOM   8417  C  C   . LEU   C  1 197 ? 44.112  17.772  -80.546  1.00 73.58  ? 498  LEU   C C   1 
ATOM   8418  O  O   . LEU   C  1 197 ? 43.119  17.239  -81.052  1.00 71.39  ? 498  LEU   C O   1 
ATOM   8419  C  CB  . LEU   C  1 197 ? 46.141  16.373  -80.994  1.00 83.36  ? 498  LEU   C CB  1 
ATOM   8420  C  CG  . LEU   C  1 197 ? 46.599  17.318  -82.111  1.00 82.55  ? 498  LEU   C CG  1 
ATOM   8421  C  CD1 . LEU   C  1 197 ? 47.331  18.544  -81.581  1.00 81.56  ? 498  LEU   C CD1 1 
ATOM   8422  C  CD2 . LEU   C  1 197 ? 47.473  16.580  -83.105  1.00 87.09  ? 498  LEU   C CD2 1 
ATOM   8423  N  N   . GLY   C  1 198 ? 44.304  19.094  -80.518  1.00 66.49  ? 499  GLY   C N   1 
ATOM   8424  C  CA  . GLY   C  1 198 ? 43.344  20.035  -81.061  1.00 65.04  ? 499  GLY   C CA  1 
ATOM   8425  C  C   . GLY   C  1 198 ? 42.292  20.481  -80.064  1.00 71.33  ? 499  GLY   C C   1 
ATOM   8426  O  O   . GLY   C  1 198 ? 42.598  20.767  -78.902  1.00 79.51  ? 499  GLY   C O   1 
ATOM   8427  N  N   . ASP   C  1 199 ? 41.041  20.551  -80.508  1.00 68.58  ? 500  ASP   C N   1 
ATOM   8428  C  CA  . ASP   C  1 199 ? 39.936  20.957  -79.655  1.00 65.33  ? 500  ASP   C CA  1 
ATOM   8429  C  C   . ASP   C  1 199 ? 39.172  19.714  -79.230  1.00 64.18  ? 500  ASP   C C   1 
ATOM   8430  O  O   . ASP   C  1 199 ? 38.541  19.069  -80.080  1.00 60.69  ? 500  ASP   C O   1 
ATOM   8431  C  CB  . ASP   C  1 199 ? 39.019  21.923  -80.405  1.00 74.07  ? 500  ASP   C CB  1 
ATOM   8432  C  CG  . ASP   C  1 199 ? 37.947  22.537  -79.522  1.00 77.74  ? 500  ASP   C CG  1 
ATOM   8433  O  OD1 . ASP   C  1 199 ? 37.260  21.793  -78.782  1.00 75.02  ? 500  ASP   C OD1 1 
ATOM   8434  O  OD2 . ASP   C  1 199 ? 37.793  23.780  -79.587  1.00 79.71  ? 500  ASP   C OD2 1 
ATOM   8435  N  N   . PRO   C  1 200 ? 39.191  19.336  -77.949  1.00 64.15  ? 501  PRO   C N   1 
ATOM   8436  C  CA  . PRO   C  1 200 ? 38.550  18.068  -77.553  1.00 61.48  ? 501  PRO   C CA  1 
ATOM   8437  C  C   . PRO   C  1 200 ? 37.053  18.038  -77.797  1.00 61.41  ? 501  PRO   C C   1 
ATOM   8438  O  O   . PRO   C  1 200 ? 36.480  16.943  -77.885  1.00 56.42  ? 501  PRO   C O   1 
ATOM   8439  C  CB  . PRO   C  1 200 ? 38.879  17.957  -76.059  1.00 54.30  ? 501  PRO   C CB  1 
ATOM   8440  C  CG  . PRO   C  1 200 ? 40.082  18.815  -75.881  1.00 51.55  ? 501  PRO   C CG  1 
ATOM   8441  C  CD  . PRO   C  1 200 ? 39.938  19.951  -76.844  1.00 49.55  ? 501  PRO   C CD  1 
ATOM   8442  N  N   . ALA   C  1 201 ? 36.409  19.205  -77.929  1.00 60.39  ? 502  ALA   C N   1 
ATOM   8443  C  CA  . ALA   C  1 201 ? 34.957  19.256  -78.078  1.00 62.36  ? 502  ALA   C CA  1 
ATOM   8444  C  C   . ALA   C  1 201 ? 34.496  18.616  -79.374  1.00 65.63  ? 502  ALA   C C   1 
ATOM   8445  O  O   . ALA   C  1 201 ? 33.386  18.074  -79.446  1.00 55.72  ? 502  ALA   C O   1 
ATOM   8446  C  CB  . ALA   C  1 201 ? 34.475  20.703  -78.024  1.00 60.39  ? 502  ALA   C CB  1 
ATOM   8447  N  N   . ASN   C  1 202 ? 35.329  18.674  -80.403  1.00 70.87  ? 503  ASN   C N   1 
ATOM   8448  C  CA  . ASN   C  1 202 ? 34.946  18.281  -81.742  1.00 63.10  ? 503  ASN   C CA  1 
ATOM   8449  C  C   . ASN   C  1 202 ? 35.430  16.891  -82.102  1.00 69.03  ? 503  ASN   C C   1 
ATOM   8450  O  O   . ASN   C  1 202 ? 35.295  16.486  -83.258  1.00 84.25  ? 503  ASN   C O   1 
ATOM   8451  C  CB  . ASN   C  1 202 ? 35.481  19.310  -82.726  1.00 59.94  ? 503  ASN   C CB  1 
ATOM   8452  C  CG  . ASN   C  1 202 ? 34.992  20.697  -82.398  1.00 60.66  ? 503  ASN   C CG  1 
ATOM   8453  O  OD1 . ASN   C  1 202 ? 33.821  20.874  -82.041  1.00 64.88  ? 503  ASN   C OD1 1 
ATOM   8454  N  ND2 . ASN   C  1 202 ? 35.881  21.690  -82.491  1.00 53.85  ? 503  ASN   C ND2 1 
ATOM   8455  N  N   . VAL   C  1 203 ? 35.988  16.153  -81.139  1.00 67.95  ? 504  VAL   C N   1 
ATOM   8456  C  CA  . VAL   C  1 203 ? 36.533  14.834  -81.440  1.00 68.20  ? 504  VAL   C CA  1 
ATOM   8457  C  C   . VAL   C  1 203 ? 35.490  13.979  -82.147  1.00 72.41  ? 504  VAL   C C   1 
ATOM   8458  O  O   . VAL   C  1 203 ? 35.781  13.316  -83.151  1.00 80.12  ? 504  VAL   C O   1 
ATOM   8459  C  CB  . VAL   C  1 203 ? 37.049  14.157  -80.160  1.00 67.39  ? 504  VAL   C CB  1 
ATOM   8460  C  CG1 . VAL   C  1 203 ? 37.271  12.670  -80.408  1.00 62.74  ? 504  VAL   C CG1 1 
ATOM   8461  C  CG2 . VAL   C  1 203 ? 38.335  14.828  -79.690  1.00 71.30  ? 504  VAL   C CG2 1 
ATOM   8462  N  N   . GLN   C  1 204 ? 34.248  14.007  -81.656  1.00 62.48  ? 505  GLN   C N   1 
ATOM   8463  C  CA  . GLN   C  1 204 ? 33.231  13.191  -82.304  1.00 63.98  ? 505  GLN   C CA  1 
ATOM   8464  C  C   . GLN   C  1 204 ? 32.951  13.698  -83.710  1.00 74.91  ? 505  GLN   C C   1 
ATOM   8465  O  O   . GLN   C  1 204 ? 32.800  12.903  -84.648  1.00 77.65  ? 505  GLN   C O   1 
ATOM   8466  C  CB  . GLN   C  1 204 ? 31.943  13.154  -81.485  1.00 65.06  ? 505  GLN   C CB  1 
ATOM   8467  C  CG  . GLN   C  1 204 ? 31.249  11.798  -81.621  1.00 74.13  ? 505  GLN   C CG  1 
ATOM   8468  C  CD  . GLN   C  1 204 ? 29.742  11.851  -81.442  1.00 79.86  ? 505  GLN   C CD  1 
ATOM   8469  O  OE1 . GLN   C  1 204 ? 29.151  12.925  -81.313  1.00 78.45  ? 505  GLN   C OE1 1 
ATOM   8470  N  NE2 . GLN   C  1 204 ? 29.109  10.678  -81.440  1.00 77.08  ? 505  GLN   C NE2 1 
ATOM   8471  N  N   . PHE   C  1 205 ? 32.901  15.017  -83.883  1.00 66.67  ? 506  PHE   C N   1 
ATOM   8472  C  CA  . PHE   C  1 205 ? 32.671  15.556  -85.214  1.00 56.64  ? 506  PHE   C CA  1 
ATOM   8473  C  C   . PHE   C  1 205 ? 33.862  15.279  -86.123  1.00 66.85  ? 506  PHE   C C   1 
ATOM   8474  O  O   . PHE   C  1 205 ? 33.695  14.771  -87.241  1.00 72.14  ? 506  PHE   C O   1 
ATOM   8475  C  CB  . PHE   C  1 205 ? 32.380  17.051  -85.142  1.00 45.24  ? 506  PHE   C CB  1 
ATOM   8476  C  CG  . PHE   C  1 205 ? 31.931  17.639  -86.453  1.00 46.66  ? 506  PHE   C CG  1 
ATOM   8477  C  CD1 . PHE   C  1 205 ? 30.642  17.420  -86.915  1.00 41.98  ? 506  PHE   C CD1 1 
ATOM   8478  C  CD2 . PHE   C  1 205 ? 32.792  18.416  -87.220  1.00 50.78  ? 506  PHE   C CD2 1 
ATOM   8479  C  CE1 . PHE   C  1 205 ? 30.211  17.972  -88.114  1.00 54.67  ? 506  PHE   C CE1 1 
ATOM   8480  C  CE2 . PHE   C  1 205 ? 32.368  18.972  -88.426  1.00 59.31  ? 506  PHE   C CE2 1 
ATOM   8481  C  CZ  . PHE   C  1 205 ? 31.075  18.745  -88.875  1.00 55.87  ? 506  PHE   C CZ  1 
ATOM   8482  N  N   . THR   C  1 206 ? 35.077  15.602  -85.657  1.00 57.43  ? 507  THR   C N   1 
ATOM   8483  C  CA  . THR   C  1 206 ? 36.276  15.283  -86.426  1.00 55.28  ? 507  THR   C CA  1 
ATOM   8484  C  C   . THR   C  1 206 ? 36.328  13.808  -86.799  1.00 56.72  ? 507  THR   C C   1 
ATOM   8485  O  O   . THR   C  1 206 ? 36.910  13.448  -87.824  1.00 64.46  ? 507  THR   C O   1 
ATOM   8486  C  CB  . THR   C  1 206 ? 37.537  15.667  -85.645  1.00 51.59  ? 507  THR   C CB  1 
ATOM   8487  O  OG1 . THR   C  1 206 ? 37.548  17.080  -85.411  1.00 51.96  ? 507  THR   C OG1 1 
ATOM   8488  C  CG2 . THR   C  1 206 ? 38.797  15.272  -86.413  1.00 43.92  ? 507  THR   C CG2 1 
ATOM   8489  N  N   . GLU   C  1 207 ? 35.698  12.939  -86.012  1.00 60.98  ? 508  GLU   C N   1 
ATOM   8490  C  CA  . GLU   C  1 207 ? 35.678  11.535  -86.405  1.00 70.99  ? 508  GLU   C CA  1 
ATOM   8491  C  C   . GLU   C  1 207 ? 34.699  11.294  -87.553  1.00 73.02  ? 508  GLU   C C   1 
ATOM   8492  O  O   . GLU   C  1 207 ? 35.000  10.522  -88.466  1.00 75.78  ? 508  GLU   C O   1 
ATOM   8493  C  CB  . GLU   C  1 207 ? 35.369  10.649  -85.200  1.00 81.94  ? 508  GLU   C CB  1 
ATOM   8494  C  CG  . GLU   C  1 207 ? 36.591  9.886   -84.710  1.00 101.44 ? 508  GLU   C CG  1 
ATOM   8495  C  CD  . GLU   C  1 207 ? 36.553  9.609   -83.216  1.00 118.96 ? 508  GLU   C CD  1 
ATOM   8496  O  OE1 . GLU   C  1 207 ? 35.450  9.693   -82.629  1.00 124.85 ? 508  GLU   C OE1 1 
ATOM   8497  O  OE2 . GLU   C  1 207 ? 37.626  9.318   -82.631  1.00 120.95 ? 508  GLU   C OE2 1 
ATOM   8498  N  N   . ILE   C  1 208 ? 33.542  11.968  -87.549  1.00 72.24  ? 509  ILE   C N   1 
ATOM   8499  C  CA  . ILE   C  1 208 ? 32.571  11.786  -88.630  1.00 65.62  ? 509  ILE   C CA  1 
ATOM   8500  C  C   . ILE   C  1 208 ? 33.149  12.275  -89.947  1.00 71.29  ? 509  ILE   C C   1 
ATOM   8501  O  O   . ILE   C  1 208 ? 33.002  11.625  -90.990  1.00 68.75  ? 509  ILE   C O   1 
ATOM   8502  C  CB  . ILE   C  1 208 ? 31.257  12.518  -88.318  1.00 59.15  ? 509  ILE   C CB  1 
ATOM   8503  C  CG1 . ILE   C  1 208 ? 30.667  12.071  -86.981  1.00 58.39  ? 509  ILE   C CG1 1 
ATOM   8504  C  CG2 . ILE   C  1 208 ? 30.274  12.312  -89.460  1.00 58.64  ? 509  ILE   C CG2 1 
ATOM   8505  C  CD1 . ILE   C  1 208 ? 29.500  12.933  -86.515  1.00 55.17  ? 509  ILE   C CD1 1 
ATOM   8506  N  N   . CYS   C  1 209 ? 33.791  13.442  -89.919  1.00 67.47  ? 510  CYS   C N   1 
ATOM   8507  C  CA  . CYS   C  1 209 ? 34.477  13.953  -91.095  1.00 63.23  ? 510  CYS   C CA  1 
ATOM   8508  C  C   . CYS   C  1 209 ? 35.494  12.948  -91.626  1.00 70.42  ? 510  CYS   C C   1 
ATOM   8509  O  O   . CYS   C  1 209 ? 35.460  12.589  -92.810  1.00 70.98  ? 510  CYS   C O   1 
ATOM   8510  C  CB  . CYS   C  1 209 ? 35.142  15.284  -90.754  1.00 63.68  ? 510  CYS   C CB  1 
ATOM   8511  S  SG  . CYS   C  1 209 ? 33.957  16.565  -90.251  1.00 69.00  ? 510  CYS   C SG  1 
ATOM   8512  N  N   . ILE   C  1 210 ? 36.412  12.476  -90.773  1.00 71.21  ? 511  ILE   C N   1 
ATOM   8513  C  CA  . ILE   C  1 210 ? 37.413  11.531  -91.270  1.00 77.77  ? 511  ILE   C CA  1 
ATOM   8514  C  C   . ILE   C  1 210 ? 36.736  10.244  -91.715  1.00 76.86  ? 511  ILE   C C   1 
ATOM   8515  O  O   . ILE   C  1 210 ? 37.090  9.661   -92.746  1.00 74.65  ? 511  ILE   C O   1 
ATOM   8516  C  CB  . ILE   C  1 210 ? 38.508  11.253  -90.223  1.00 73.22  ? 511  ILE   C CB  1 
ATOM   8517  C  CG1 . ILE   C  1 210 ? 39.053  12.540  -89.621  1.00 72.24  ? 511  ILE   C CG1 1 
ATOM   8518  C  CG2 . ILE   C  1 210 ? 39.675  10.578  -90.887  1.00 76.47  ? 511  ILE   C CG2 1 
ATOM   8519  C  CD1 . ILE   C  1 210 ? 39.894  12.304  -88.374  1.00 71.85  ? 511  ILE   C CD1 1 
ATOM   8520  N  N   . GLN   C  1 211 ? 35.738  9.796   -90.954  1.00 78.68  ? 512  GLN   C N   1 
ATOM   8521  C  CA  . GLN   C  1 211 ? 34.904  8.661   -91.329  1.00 83.18  ? 512  GLN   C CA  1 
ATOM   8522  C  C   . GLN   C  1 211 ? 34.056  8.948   -92.569  1.00 84.57  ? 512  GLN   C C   1 
ATOM   8523  O  O   . GLN   C  1 211 ? 33.489  8.015   -93.147  1.00 90.04  ? 512  GLN   C O   1 
ATOM   8524  C  CB  . GLN   C  1 211 ? 34.041  8.269   -90.116  1.00 89.33  ? 512  GLN   C CB  1 
ATOM   8525  C  CG  . GLN   C  1 211 ? 33.111  7.091   -90.280  1.00 99.75  ? 512  GLN   C CG  1 
ATOM   8526  C  CD  . GLN   C  1 211 ? 31.714  7.521   -90.689  1.00 108.40 ? 512  GLN   C CD  1 
ATOM   8527  O  OE1 . GLN   C  1 211 ? 31.226  8.580   -90.272  1.00 109.22 ? 512  GLN   C OE1 1 
ATOM   8528  N  NE2 . GLN   C  1 211 ? 31.063  6.706   -91.516  1.00 110.49 ? 512  GLN   C NE2 1 
ATOM   8529  N  N   . GLN   C  1 212 ? 33.970  10.204  -93.004  1.00 79.68  ? 513  GLN   C N   1 
ATOM   8530  C  CA  . GLN   C  1 212 ? 33.341  10.562  -94.268  1.00 73.45  ? 513  GLN   C CA  1 
ATOM   8531  C  C   . GLN   C  1 212 ? 34.360  10.817  -95.365  1.00 73.24  ? 513  GLN   C C   1 
ATOM   8532  O  O   . GLN   C  1 212 ? 34.014  11.388  -96.402  1.00 74.66  ? 513  GLN   C O   1 
ATOM   8533  C  CB  . GLN   C  1 212 ? 32.458  11.798  -94.092  1.00 78.04  ? 513  GLN   C CB  1 
ATOM   8534  C  CG  . GLN   C  1 212 ? 31.057  11.497  -93.621  1.00 76.96  ? 513  GLN   C CG  1 
ATOM   8535  C  CD  . GLN   C  1 212 ? 30.299  10.663  -94.620  1.00 79.09  ? 513  GLN   C CD  1 
ATOM   8536  O  OE1 . GLN   C  1 212 ? 30.198  9.448   -94.477  1.00 80.54  ? 513  GLN   C OE1 1 
ATOM   8537  N  NE2 . GLN   C  1 212 ? 29.767  11.311  -95.649  1.00 81.66  ? 513  GLN   C NE2 1 
ATOM   8538  N  N   . GLY   C  1 213 ? 35.608  10.428  -95.156  1.00 79.67  ? 514  GLY   C N   1 
ATOM   8539  C  CA  . GLY   C  1 213 ? 36.630  10.612  -96.160  1.00 75.85  ? 514  GLY   C CA  1 
ATOM   8540  C  C   . GLY   C  1 213 ? 37.419  11.898  -96.067  1.00 71.68  ? 514  GLY   C C   1 
ATOM   8541  O  O   . GLY   C  1 213 ? 38.220  12.167  -96.969  1.00 67.93  ? 514  GLY   C O   1 
ATOM   8542  N  N   . TRP   C  1 214 ? 37.220  12.706  -95.022  1.00 65.81  ? 515  TRP   C N   1 
ATOM   8543  C  CA  . TRP   C  1 214 ? 38.062  13.883  -94.841  1.00 61.16  ? 515  TRP   C CA  1 
ATOM   8544  C  C   . TRP   C  1 214 ? 39.501  13.449  -94.592  1.00 73.74  ? 515  TRP   C C   1 
ATOM   8545  O  O   . TRP   C  1 214 ? 39.759  12.471  -93.881  1.00 73.96  ? 515  TRP   C O   1 
ATOM   8546  C  CB  . TRP   C  1 214 ? 37.564  14.754  -93.679  1.00 58.05  ? 515  TRP   C CB  1 
ATOM   8547  C  CG  . TRP   C  1 214 ? 38.315  16.073  -93.558  1.00 63.55  ? 515  TRP   C CG  1 
ATOM   8548  C  CD1 . TRP   C  1 214 ? 38.466  17.015  -94.536  1.00 65.52  ? 515  TRP   C CD1 1 
ATOM   8549  C  CD2 . TRP   C  1 214 ? 39.006  16.585  -92.403  1.00 66.22  ? 515  TRP   C CD2 1 
ATOM   8550  N  NE1 . TRP   C  1 214 ? 39.210  18.073  -94.069  1.00 66.28  ? 515  TRP   C NE1 1 
ATOM   8551  C  CE2 . TRP   C  1 214 ? 39.554  17.835  -92.764  1.00 63.57  ? 515  TRP   C CE2 1 
ATOM   8552  C  CE3 . TRP   C  1 214 ? 39.218  16.107  -91.104  1.00 70.50  ? 515  TRP   C CE3 1 
ATOM   8553  C  CZ2 . TRP   C  1 214 ? 40.302  18.609  -91.879  1.00 64.30  ? 515  TRP   C CZ2 1 
ATOM   8554  C  CZ3 . TRP   C  1 214 ? 39.963  16.883  -90.220  1.00 74.45  ? 515  TRP   C CZ3 1 
ATOM   8555  C  CH2 . TRP   C  1 214 ? 40.497  18.116  -90.615  1.00 74.62  ? 515  TRP   C CH2 1 
ATOM   8556  N  N   . LYS   C  1 215 ? 40.441  14.174  -95.209  1.00 79.50  ? 516  LYS   C N   1 
ATOM   8557  C  CA  . LYS   C  1 215 ? 41.868  13.942  -95.027  1.00 84.79  ? 516  LYS   C CA  1 
ATOM   8558  C  C   . LYS   C  1 215 ? 42.382  14.829  -93.904  1.00 85.82  ? 516  LYS   C C   1 
ATOM   8559  O  O   . LYS   C  1 215 ? 42.602  16.029  -94.102  1.00 90.40  ? 516  LYS   C O   1 
ATOM   8560  C  CB  . LYS   C  1 215 ? 42.642  14.219  -96.309  1.00 87.42  ? 516  LYS   C CB  1 
ATOM   8561  C  CG  . LYS   C  1 215 ? 43.261  12.983  -96.914  1.00 99.16  ? 516  LYS   C CG  1 
ATOM   8562  C  CD  . LYS   C  1 215 ? 44.105  12.216  -95.903  1.00 104.66 ? 516  LYS   C CD  1 
ATOM   8563  C  CE  . LYS   C  1 215 ? 45.104  11.312  -96.627  1.00 110.15 ? 516  LYS   C CE  1 
ATOM   8564  N  NZ  . LYS   C  1 215 ? 44.495  10.610  -97.801  1.00 109.26 ? 516  LYS   C NZ  1 
ATOM   8565  N  N   . PRO   C  1 216 ? 42.580  14.280  -92.716  1.00 75.86  ? 517  PRO   C N   1 
ATOM   8566  C  CA  . PRO   C  1 216 ? 42.978  15.098  -91.586  1.00 71.54  ? 517  PRO   C CA  1 
ATOM   8567  C  C   . PRO   C  1 216 ? 44.470  15.376  -91.612  1.00 75.16  ? 517  PRO   C C   1 
ATOM   8568  O  O   . PRO   C  1 216 ? 45.283  14.439  -91.609  1.00 82.60  ? 517  PRO   C O   1 
ATOM   8569  C  CB  . PRO   C  1 216 ? 42.597  14.225  -90.384  1.00 81.43  ? 517  PRO   C CB  1 
ATOM   8570  C  CG  . PRO   C  1 216 ? 42.754  12.814  -90.900  1.00 81.37  ? 517  PRO   C CG  1 
ATOM   8571  C  CD  . PRO   C  1 216 ? 42.409  12.858  -92.359  1.00 74.72  ? 517  PRO   C CD  1 
ATOM   8572  N  N   . PRO   C  1 217 ? 44.878  16.650  -91.642  1.00 69.17  ? 518  PRO   C N   1 
ATOM   8573  C  CA  . PRO   C  1 217 ? 46.305  16.965  -91.438  1.00 68.62  ? 518  PRO   C CA  1 
ATOM   8574  C  C   . PRO   C  1 217 ? 46.808  16.669  -90.012  1.00 66.09  ? 518  PRO   C C   1 
ATOM   8575  O  O   . PRO   C  1 217 ? 48.029  16.646  -89.785  1.00 63.54  ? 518  PRO   C O   1 
ATOM   8576  C  CB  . PRO   C  1 217 ? 46.387  18.463  -91.781  1.00 65.23  ? 518  PRO   C CB  1 
ATOM   8577  C  CG  . PRO   C  1 217 ? 44.976  18.982  -91.658  1.00 54.82  ? 518  PRO   C CG  1 
ATOM   8578  C  CD  . PRO   C  1 217 ? 44.084  17.832  -92.018  1.00 57.02  ? 518  PRO   C CD  1 
ATOM   8579  N  N   . ARG   C  1 218 ? 45.912  16.428  -89.059  1.00 64.71  ? 519  ARG   C N   1 
ATOM   8580  C  CA  . ARG   C  1 218 ? 46.263  15.992  -87.708  1.00 76.12  ? 519  ARG   C CA  1 
ATOM   8581  C  C   . ARG   C  1 218 ? 47.226  16.972  -87.027  1.00 84.31  ? 519  ARG   C C   1 
ATOM   8582  O  O   . ARG   C  1 218 ? 48.421  16.718  -86.868  1.00 81.63  ? 519  ARG   C O   1 
ATOM   8583  C  CB  . ARG   C  1 218 ? 46.830  14.568  -87.720  1.00 73.91  ? 519  ARG   C CB  1 
ATOM   8584  C  CG  . ARG   C  1 218 ? 45.776  13.541  -88.084  1.00 78.28  ? 519  ARG   C CG  1 
ATOM   8585  C  CD  . ARG   C  1 218 ? 46.116  12.137  -87.610  1.00 87.36  ? 519  ARG   C CD  1 
ATOM   8586  N  NE  . ARG   C  1 218 ? 45.005  11.217  -87.858  1.00 94.77  ? 519  ARG   C NE  1 
ATOM   8587  C  CZ  . ARG   C  1 218 ? 44.169  10.767  -86.922  1.00 97.68  ? 519  ARG   C CZ  1 
ATOM   8588  N  NH1 . ARG   C  1 218 ? 43.181  9.943   -87.261  1.00 103.04 ? 519  ARG   C NH1 1 
ATOM   8589  N  NH2 . ARG   C  1 218 ? 44.322  11.123  -85.649  1.00 84.97  ? 519  ARG   C NH2 1 
ATOM   8590  N  N   . GLY   C  1 219 ? 46.651  18.096  -86.602  1.00 89.91  ? 520  GLY   C N   1 
ATOM   8591  C  CA  . GLY   C  1 219 ? 47.361  19.084  -85.809  1.00 92.79  ? 520  GLY   C CA  1 
ATOM   8592  C  C   . GLY   C  1 219 ? 46.473  19.719  -84.753  1.00 93.29  ? 520  GLY   C C   1 
ATOM   8593  O  O   . GLY   C  1 219 ? 45.379  19.221  -84.471  1.00 92.11  ? 520  GLY   C O   1 
ATOM   8594  N  N   . ARG   C  1 220 ? 46.931  20.811  -84.144  1.00 91.07  ? 521  ARG   C N   1 
ATOM   8595  C  CA  . ARG   C  1 220 ? 46.093  21.542  -83.203  1.00 81.15  ? 521  ARG   C CA  1 
ATOM   8596  C  C   . ARG   C  1 220 ? 44.999  22.269  -83.971  1.00 77.30  ? 521  ARG   C C   1 
ATOM   8597  O  O   . ARG   C  1 220 ? 43.819  21.912  -83.890  1.00 81.19  ? 521  ARG   C O   1 
ATOM   8598  C  CB  . ARG   C  1 220 ? 46.932  22.531  -82.384  1.00 79.93  ? 521  ARG   C CB  1 
ATOM   8599  C  CG  . ARG   C  1 220 ? 46.510  22.689  -80.927  1.00 83.67  ? 521  ARG   C CG  1 
ATOM   8600  C  CD  . ARG   C  1 220 ? 47.328  21.777  -79.999  1.00 91.93  ? 521  ARG   C CD  1 
ATOM   8601  N  NE  . ARG   C  1 220 ? 46.850  21.791  -78.615  1.00 87.34  ? 521  ARG   C NE  1 
ATOM   8602  C  CZ  . ARG   C  1 220 ? 47.322  22.587  -77.661  1.00 82.88  ? 521  ARG   C CZ  1 
ATOM   8603  N  NH1 . ARG   C  1 220 ? 48.306  23.444  -77.928  1.00 81.48  ? 521  ARG   C NH1 1 
ATOM   8604  N  NH2 . ARG   C  1 220 ? 46.805  22.526  -76.440  1.00 77.12  ? 521  ARG   C NH2 1 
ATOM   8605  N  N   . PHE   C  1 221 ? 45.396  23.241  -84.782  1.00 73.42  ? 522  PHE   C N   1 
ATOM   8606  C  CA  . PHE   C  1 221 ? 44.464  24.198  -85.372  1.00 75.37  ? 522  PHE   C CA  1 
ATOM   8607  C  C   . PHE   C  1 221 ? 44.166  23.875  -86.842  1.00 79.63  ? 522  PHE   C C   1 
ATOM   8608  O  O   . PHE   C  1 221 ? 44.408  24.662  -87.768  1.00 80.81  ? 522  PHE   C O   1 
ATOM   8609  C  CB  . PHE   C  1 221 ? 45.013  25.608  -85.191  1.00 77.22  ? 522  PHE   C CB  1 
ATOM   8610  C  CG  . PHE   C  1 221 ? 45.317  25.943  -83.753  1.00 78.79  ? 522  PHE   C CG  1 
ATOM   8611  C  CD1 . PHE   C  1 221 ? 46.396  26.737  -83.420  1.00 76.11  ? 522  PHE   C CD1 1 
ATOM   8612  C  CD2 . PHE   C  1 221 ? 44.514  25.455  -82.731  1.00 78.64  ? 522  PHE   C CD2 1 
ATOM   8613  C  CE1 . PHE   C  1 221 ? 46.673  27.030  -82.101  1.00 75.29  ? 522  PHE   C CE1 1 
ATOM   8614  C  CE2 . PHE   C  1 221 ? 44.786  25.752  -81.413  1.00 75.83  ? 522  PHE   C CE2 1 
ATOM   8615  C  CZ  . PHE   C  1 221 ? 45.867  26.534  -81.096  1.00 73.23  ? 522  PHE   C CZ  1 
ATOM   8616  N  N   . ASP   C  1 222 ? 43.592  22.689  -87.042  1.00 73.48  ? 523  ASP   C N   1 
ATOM   8617  C  CA  . ASP   C  1 222 ? 43.110  22.251  -88.347  1.00 64.54  ? 523  ASP   C CA  1 
ATOM   8618  C  C   . ASP   C  1 222 ? 41.664  22.698  -88.497  1.00 61.19  ? 523  ASP   C C   1 
ATOM   8619  O  O   . ASP   C  1 222 ? 40.783  22.208  -87.783  1.00 63.38  ? 523  ASP   C O   1 
ATOM   8620  C  CB  . ASP   C  1 222 ? 43.203  20.734  -88.483  1.00 71.75  ? 523  ASP   C CB  1 
ATOM   8621  C  CG  . ASP   C  1 222 ? 44.630  20.229  -88.496  1.00 80.84  ? 523  ASP   C CG  1 
ATOM   8622  O  OD1 . ASP   C  1 222 ? 45.554  21.057  -88.654  1.00 87.42  ? 523  ASP   C OD1 1 
ATOM   8623  O  OD2 . ASP   C  1 222 ? 44.825  19.001  -88.348  1.00 77.47  ? 523  ASP   C OD2 1 
ATOM   8624  N  N   . VAL   C  1 223 ? 41.408  23.605  -89.435  1.00 51.66  ? 524  VAL   C N   1 
ATOM   8625  C  CA  . VAL   C  1 223 ? 40.037  24.044  -89.665  1.00 39.29  ? 524  VAL   C CA  1 
ATOM   8626  C  C   . VAL   C  1 223 ? 39.241  22.875  -90.219  1.00 40.86  ? 524  VAL   C C   1 
ATOM   8627  O  O   . VAL   C  1 223 ? 39.617  22.275  -91.231  1.00 45.69  ? 524  VAL   C O   1 
ATOM   8628  C  CB  . VAL   C  1 223 ? 39.996  25.245  -90.613  1.00 41.89  ? 524  VAL   C CB  1 
ATOM   8629  C  CG1 . VAL   C  1 223 ? 38.560  25.638  -90.893  1.00 38.86  ? 524  VAL   C CG1 1 
ATOM   8630  C  CG2 . VAL   C  1 223 ? 40.791  26.415  -90.017  1.00 36.92  ? 524  VAL   C CG2 1 
ATOM   8631  N  N   . LEU   C  1 224 ? 38.146  22.542  -89.555  1.00 36.41  ? 525  LEU   C N   1 
ATOM   8632  C  CA  . LEU   C  1 224 ? 37.323  21.425  -89.979  1.00 55.48  ? 525  LEU   C CA  1 
ATOM   8633  C  C   . LEU   C  1 224 ? 36.611  21.767  -91.284  1.00 54.09  ? 525  LEU   C C   1 
ATOM   8634  O  O   . LEU   C  1 224 ? 36.367  22.939  -91.573  1.00 60.50  ? 525  LEU   C O   1 
ATOM   8635  C  CB  . LEU   C  1 224 ? 36.294  21.076  -88.904  1.00 54.74  ? 525  LEU   C CB  1 
ATOM   8636  C  CG  . LEU   C  1 224 ? 36.808  20.314  -87.675  1.00 60.90  ? 525  LEU   C CG  1 
ATOM   8637  C  CD1 . LEU   C  1 224 ? 35.955  20.637  -86.449  1.00 52.08  ? 525  LEU   C CD1 1 
ATOM   8638  C  CD2 . LEU   C  1 224 ? 36.803  18.822  -87.962  1.00 65.05  ? 525  LEU   C CD2 1 
ATOM   8639  N  N   . PRO   C  1 225 ? 36.276  20.763  -92.094  1.00 43.13  ? 526  PRO   C N   1 
ATOM   8640  C  CA  . PRO   C  1 225 ? 35.491  21.021  -93.300  1.00 37.08  ? 526  PRO   C CA  1 
ATOM   8641  C  C   . PRO   C  1 225 ? 34.052  21.308  -92.936  1.00 50.37  ? 526  PRO   C C   1 
ATOM   8642  O  O   . PRO   C  1 225 ? 33.615  21.091  -91.806  1.00 66.10  ? 526  PRO   C O   1 
ATOM   8643  C  CB  . PRO   C  1 225 ? 35.599  19.711  -94.074  1.00 45.00  ? 526  PRO   C CB  1 
ATOM   8644  C  CG  . PRO   C  1 225 ? 35.719  18.688  -93.021  1.00 53.63  ? 526  PRO   C CG  1 
ATOM   8645  C  CD  . PRO   C  1 225 ? 36.526  19.324  -91.913  1.00 50.36  ? 526  PRO   C CD  1 
ATOM   8646  N  N   . LEU   C  1 226 ? 33.310  21.808  -93.917  1.00 48.23  ? 527  LEU   C N   1 
ATOM   8647  C  CA  . LEU   C  1 226 ? 31.863  21.892  -93.796  1.00 52.67  ? 527  LEU   C CA  1 
ATOM   8648  C  C   . LEU   C  1 226 ? 31.251  20.539  -94.137  1.00 59.59  ? 527  LEU   C C   1 
ATOM   8649  O  O   . LEU   C  1 226 ? 31.727  19.848  -95.036  1.00 70.98  ? 527  LEU   C O   1 
ATOM   8650  C  CB  . LEU   C  1 226 ? 31.318  22.975  -94.734  1.00 51.79  ? 527  LEU   C CB  1 
ATOM   8651  C  CG  . LEU   C  1 226 ? 31.698  24.387  -94.286  1.00 46.81  ? 527  LEU   C CG  1 
ATOM   8652  C  CD1 . LEU   C  1 226 ? 31.204  25.440  -95.257  1.00 32.02  ? 527  LEU   C CD1 1 
ATOM   8653  C  CD2 . LEU   C  1 226 ? 31.167  24.669  -92.866  1.00 33.48  ? 527  LEU   C CD2 1 
ATOM   8654  N  N   . LEU   C  1 227 ? 30.224  20.141  -93.392  1.00 57.88  ? 528  LEU   C N   1 
ATOM   8655  C  CA  . LEU   C  1 227 ? 29.445  18.943  -93.703  1.00 51.97  ? 528  LEU   C CA  1 
ATOM   8656  C  C   . LEU   C  1 227 ? 28.026  19.426  -93.965  1.00 53.46  ? 528  LEU   C C   1 
ATOM   8657  O  O   . LEU   C  1 227 ? 27.185  19.417  -93.068  1.00 50.23  ? 528  LEU   C O   1 
ATOM   8658  C  CB  . LEU   C  1 227 ? 29.473  17.911  -92.575  1.00 48.59  ? 528  LEU   C CB  1 
ATOM   8659  C  CG  . LEU   C  1 227 ? 29.897  16.449  -92.771  1.00 49.26  ? 528  LEU   C CG  1 
ATOM   8660  C  CD1 . LEU   C  1 227 ? 29.438  15.617  -91.569  1.00 47.15  ? 528  LEU   C CD1 1 
ATOM   8661  C  CD2 . LEU   C  1 227 ? 29.395  15.852  -94.068  1.00 48.15  ? 528  LEU   C CD2 1 
ATOM   8662  N  N   . LEU   C  1 228 ? 27.753  19.841  -95.195  1.00 58.12  ? 529  LEU   C N   1 
ATOM   8663  C  CA  . LEU   C  1 228 ? 26.478  20.461  -95.514  1.00 49.54  ? 529  LEU   C CA  1 
ATOM   8664  C  C   . LEU   C  1 228 ? 25.480  19.422  -96.005  1.00 48.04  ? 529  LEU   C C   1 
ATOM   8665  O  O   . LEU   C  1 228 ? 25.855  18.465  -96.689  1.00 42.17  ? 529  LEU   C O   1 
ATOM   8666  C  CB  . LEU   C  1 228 ? 26.696  21.560  -96.546  1.00 43.75  ? 529  LEU   C CB  1 
ATOM   8667  C  CG  . LEU   C  1 228 ? 27.802  22.470  -95.985  1.00 40.68  ? 529  LEU   C CG  1 
ATOM   8668  C  CD1 . LEU   C  1 228 ? 28.083  23.596  -96.899  1.00 31.82  ? 529  LEU   C CD1 1 
ATOM   8669  C  CD2 . LEU   C  1 228 ? 27.425  23.031  -94.621  1.00 33.01  ? 529  LEU   C CD2 1 
ATOM   8670  N  N   . GLN   C  1 229 ? 24.215  19.588  -95.595  1.00 50.29  ? 530  GLN   C N   1 
ATOM   8671  C  CA  . GLN   C  1 229 ? 23.126  18.662  -95.913  1.00 44.63  ? 530  GLN   C CA  1 
ATOM   8672  C  C   . GLN   C  1 229 ? 21.932  19.425  -96.467  1.00 51.67  ? 530  GLN   C C   1 
ATOM   8673  O  O   . GLN   C  1 229 ? 21.365  20.281  -95.779  1.00 46.62  ? 530  GLN   C O   1 
ATOM   8674  C  CB  . GLN   C  1 229 ? 22.673  17.863  -94.693  1.00 49.75  ? 530  GLN   C CB  1 
ATOM   8675  C  CG  . GLN   C  1 229 ? 21.269  17.308  -94.885  1.00 56.00  ? 530  GLN   C CG  1 
ATOM   8676  C  CD  . GLN   C  1 229 ? 20.802  16.413  -93.757  1.00 58.90  ? 530  GLN   C CD  1 
ATOM   8677  O  OE1 . GLN   C  1 229 ? 21.092  16.653  -92.584  1.00 52.68  ? 530  GLN   C OE1 1 
ATOM   8678  N  NE2 . GLN   C  1 229 ? 20.070  15.362  -94.115  1.00 63.22  ? 530  GLN   C NE2 1 
ATOM   8679  N  N   . ALA   C  1 230 ? 21.524  19.076  -97.688  1.00 55.70  ? 531  ALA   C N   1 
ATOM   8680  C  CA  . ALA   C  1 230 ? 20.400  19.698  -98.369  1.00 43.69  ? 531  ALA   C CA  1 
ATOM   8681  C  C   . ALA   C  1 230 ? 19.268  18.699  -98.550  1.00 48.12  ? 531  ALA   C C   1 
ATOM   8682  O  O   . ALA   C  1 230 ? 19.497  17.494  -98.708  1.00 44.16  ? 531  ALA   C O   1 
ATOM   8683  C  CB  . ALA   C  1 230 ? 20.819  20.238  -99.733  1.00 46.11  ? 531  ALA   C CB  1 
ATOM   8684  N  N   . ASN   C  1 231 ? 18.044  19.228  -98.522  1.00 52.23  ? 532  ASN   C N   1 
ATOM   8685  C  CA  . ASN   C  1 231 ? 16.810  18.475  -98.724  1.00 55.38  ? 532  ASN   C CA  1 
ATOM   8686  C  C   . ASN   C  1 231 ? 16.866  17.023  -98.256  1.00 55.68  ? 532  ASN   C C   1 
ATOM   8687  O  O   . ASN   C  1 231 ? 16.733  16.106  -99.074  1.00 61.22  ? 532  ASN   C O   1 
ATOM   8688  C  CB  . ASN   C  1 231 ? 16.419  18.519  -100.199 1.00 61.51  ? 532  ASN   C CB  1 
ATOM   8689  C  CG  . ASN   C  1 231 ? 14.957  18.273  -100.394 1.00 71.45  ? 532  ASN   C CG  1 
ATOM   8690  O  OD1 . ASN   C  1 231 ? 14.139  18.657  -99.555  1.00 84.62  ? 532  ASN   C OD1 1 
ATOM   8691  N  ND2 . ASN   C  1 231 ? 14.610  17.619  -101.478 1.00 67.68  ? 532  ASN   C ND2 1 
ATOM   8692  N  N   . GLY   C  1 232 ? 17.083  16.805  -96.958  1.00 51.40  ? 533  GLY   C N   1 
ATOM   8693  C  CA  . GLY   C  1 232 ? 17.146  15.476  -96.371  1.00 56.27  ? 533  GLY   C CA  1 
ATOM   8694  C  C   . GLY   C  1 232 ? 18.261  14.559  -96.859  1.00 62.73  ? 533  GLY   C C   1 
ATOM   8695  O  O   . GLY   C  1 232 ? 18.406  13.446  -96.321  1.00 55.04  ? 533  GLY   C O   1 
ATOM   8696  N  N   . ASN   C  1 233 ? 19.058  14.983  -97.836  1.00 58.14  ? 534  ASN   C N   1 
ATOM   8697  C  CA  . ASN   C  1 233 ? 20.018  14.079  -98.452  1.00 58.60  ? 534  ASN   C CA  1 
ATOM   8698  C  C   . ASN   C  1 233 ? 21.233  13.851  -97.548  1.00 56.10  ? 534  ASN   C C   1 
ATOM   8699  O  O   . ASN   C  1 233 ? 21.423  14.525  -96.531  1.00 59.82  ? 534  ASN   C O   1 
ATOM   8700  C  CB  . ASN   C  1 233 ? 20.426  14.617  -99.829  1.00 64.46  ? 534  ASN   C CB  1 
ATOM   8701  C  CG  . ASN   C  1 233 ? 19.278  14.558  -100.836 1.00 64.96  ? 534  ASN   C CG  1 
ATOM   8702  O  OD1 . ASN   C  1 233 ? 18.641  13.513  -101.010 1.00 68.78  ? 534  ASN   C OD1 1 
ATOM   8703  N  ND2 . ASN   C  1 233 ? 18.991  15.683  -101.476 1.00 59.27  ? 534  ASN   C ND2 1 
ATOM   8704  N  N   . ASP   C  1 234 ? 22.041  12.856  -97.914  1.00 52.21  ? 535  ASP   C N   1 
ATOM   8705  C  CA  . ASP   C  1 234 ? 23.293  12.615  -97.206  1.00 48.48  ? 535  ASP   C CA  1 
ATOM   8706  C  C   . ASP   C  1 234 ? 24.176  13.864  -97.255  1.00 53.24  ? 535  ASP   C C   1 
ATOM   8707  O  O   . ASP   C  1 234 ? 24.216  14.559  -98.279  1.00 67.68  ? 535  ASP   C O   1 
ATOM   8708  C  CB  . ASP   C  1 234 ? 24.054  11.432  -97.807  1.00 51.13  ? 535  ASP   C CB  1 
ATOM   8709  C  CG  . ASP   C  1 234 ? 23.414  10.097  -97.494  1.00 59.26  ? 535  ASP   C CG  1 
ATOM   8710  O  OD1 . ASP   C  1 234 ? 24.020  9.065   -97.852  1.00 66.74  ? 535  ASP   C OD1 1 
ATOM   8711  O  OD2 . ASP   C  1 234 ? 22.310  10.073  -96.915  1.00 60.90  ? 535  ASP   C OD2 1 
ATOM   8712  N  N   . PRO   C  1 235 ? 24.886  14.180  -96.175  1.00 54.59  ? 536  PRO   C N   1 
ATOM   8713  C  CA  . PRO   C  1 235 ? 25.708  15.391  -96.161  1.00 56.14  ? 536  PRO   C CA  1 
ATOM   8714  C  C   . PRO   C  1 235 ? 26.979  15.240  -96.984  1.00 50.54  ? 536  PRO   C C   1 
ATOM   8715  O  O   . PRO   C  1 235 ? 27.447  14.137  -97.281  1.00 58.46  ? 536  PRO   C O   1 
ATOM   8716  C  CB  . PRO   C  1 235 ? 26.023  15.584  -94.672  1.00 50.71  ? 536  PRO   C CB  1 
ATOM   8717  C  CG  . PRO   C  1 235 ? 25.912  14.232  -94.095  1.00 39.96  ? 536  PRO   C CG  1 
ATOM   8718  C  CD  . PRO   C  1 235 ? 24.801  13.565  -94.839  1.00 42.83  ? 536  PRO   C CD  1 
ATOM   8719  N  N   . GLU   C  1 236 ? 27.551  16.391  -97.332  1.00 44.69  ? 537  GLU   C N   1 
ATOM   8720  C  CA  . GLU   C  1 236 ? 28.657  16.478  -98.275  1.00 48.12  ? 537  GLU   C CA  1 
ATOM   8721  C  C   . GLU   C  1 236 ? 29.761  17.357  -97.707  1.00 51.91  ? 537  GLU   C C   1 
ATOM   8722  O  O   . GLU   C  1 236 ? 29.490  18.463  -97.229  1.00 50.92  ? 537  GLU   C O   1 
ATOM   8723  C  CB  . GLU   C  1 236 ? 28.155  17.029  -99.616  1.00 47.10  ? 537  GLU   C CB  1 
ATOM   8724  C  CG  . GLU   C  1 236 ? 27.080  16.135  -100.203 1.00 54.19  ? 537  GLU   C CG  1 
ATOM   8725  C  CD  . GLU   C  1 236 ? 26.643  16.521  -101.601 1.00 58.15  ? 537  GLU   C CD  1 
ATOM   8726  O  OE1 . GLU   C  1 236 ? 27.463  17.061  -102.389 1.00 54.96  ? 537  GLU   C OE1 1 
ATOM   8727  O  OE2 . GLU   C  1 236 ? 25.457  16.264  -101.905 1.00 60.47  ? 537  GLU   C OE2 1 
ATOM   8728  N  N   . LEU   C  1 237 ? 31.001  16.868  -97.759  1.00 44.66  ? 538  LEU   C N   1 
ATOM   8729  C  CA  . LEU   C  1 237 ? 32.131  17.629  -97.236  1.00 41.71  ? 538  LEU   C CA  1 
ATOM   8730  C  C   . LEU   C  1 237 ? 32.531  18.760  -98.183  1.00 52.83  ? 538  LEU   C C   1 
ATOM   8731  O  O   . LEU   C  1 237 ? 32.491  18.607  -99.403  1.00 50.95  ? 538  LEU   C O   1 
ATOM   8732  C  CB  . LEU   C  1 237 ? 33.329  16.705  -97.001  1.00 43.52  ? 538  LEU   C CB  1 
ATOM   8733  C  CG  . LEU   C  1 237 ? 33.287  15.747  -95.800  1.00 57.32  ? 538  LEU   C CG  1 
ATOM   8734  C  CD1 . LEU   C  1 237 ? 34.492  14.822  -95.798  1.00 61.56  ? 538  LEU   C CD1 1 
ATOM   8735  C  CD2 . LEU   C  1 237 ? 33.173  16.484  -94.456  1.00 53.17  ? 538  LEU   C CD2 1 
ATOM   8736  N  N   . PHE   C  1 238 ? 32.914  19.905  -97.617  1.00 55.30  ? 539  PHE   C N   1 
ATOM   8737  C  CA  . PHE   C  1 238 ? 33.548  20.977  -98.379  1.00 52.49  ? 539  PHE   C CA  1 
ATOM   8738  C  C   . PHE   C  1 238 ? 34.615  21.642  -97.519  1.00 52.94  ? 539  PHE   C C   1 
ATOM   8739  O  O   . PHE   C  1 238 ? 34.375  21.940  -96.345  1.00 47.84  ? 539  PHE   C O   1 
ATOM   8740  C  CB  . PHE   C  1 238 ? 32.549  22.056  -98.829  1.00 55.07  ? 539  PHE   C CB  1 
ATOM   8741  C  CG  . PHE   C  1 238 ? 31.424  21.537  -99.650  1.00 56.63  ? 539  PHE   C CG  1 
ATOM   8742  C  CD1 . PHE   C  1 238 ? 30.333  20.926  -99.054  1.00 64.69  ? 539  PHE   C CD1 1 
ATOM   8743  C  CD2 . PHE   C  1 238 ? 31.441  21.668  -101.023 1.00 48.09  ? 539  PHE   C CD2 1 
ATOM   8744  C  CE1 . PHE   C  1 238 ? 29.289  20.442  -99.823  1.00 67.26  ? 539  PHE   C CE1 1 
ATOM   8745  C  CE2 . PHE   C  1 238 ? 30.396  21.183  -101.800 1.00 46.89  ? 539  PHE   C CE2 1 
ATOM   8746  C  CZ  . PHE   C  1 238 ? 29.321  20.576  -101.203 1.00 54.77  ? 539  PHE   C CZ  1 
ATOM   8747  N  N   . GLN   C  1 239 ? 35.782  21.892  -98.105  1.00 51.42  ? 540  GLN   C N   1 
ATOM   8748  C  CA  . GLN   C  1 239 ? 36.845  22.615  -97.419  1.00 54.19  ? 540  GLN   C CA  1 
ATOM   8749  C  C   . GLN   C  1 239 ? 36.682  24.111  -97.676  1.00 49.43  ? 540  GLN   C C   1 
ATOM   8750  O  O   . GLN   C  1 239 ? 36.764  24.552  -98.821  1.00 37.50  ? 540  GLN   C O   1 
ATOM   8751  C  CB  . GLN   C  1 239 ? 38.218  22.145  -97.891  1.00 52.53  ? 540  GLN   C CB  1 
ATOM   8752  C  CG  . GLN   C  1 239 ? 39.340  23.006  -97.347  1.00 59.99  ? 540  GLN   C CG  1 
ATOM   8753  C  CD  . GLN   C  1 239 ? 40.509  23.114  -98.297  1.00 72.09  ? 540  GLN   C CD  1 
ATOM   8754  O  OE1 . GLN   C  1 239 ? 40.541  22.444  -99.324  1.00 85.01  ? 540  GLN   C OE1 1 
ATOM   8755  N  NE2 . GLN   C  1 239 ? 41.473  23.972  -97.969  1.00 71.71  ? 540  GLN   C NE2 1 
ATOM   8756  N  N   . ILE   C  1 240 ? 36.444  24.882  -96.619  1.00 49.10  ? 541  ILE   C N   1 
ATOM   8757  C  CA  . ILE   C  1 240 ? 36.317  26.339  -96.781  1.00 47.94  ? 541  ILE   C CA  1 
ATOM   8758  C  C   . ILE   C  1 240 ? 37.641  26.900  -97.282  1.00 49.99  ? 541  ILE   C C   1 
ATOM   8759  O  O   . ILE   C  1 240 ? 38.692  26.639  -96.661  1.00 51.85  ? 541  ILE   C O   1 
ATOM   8760  C  CB  . ILE   C  1 240 ? 35.934  27.006  -95.448  1.00 47.88  ? 541  ILE   C CB  1 
ATOM   8761  C  CG1 . ILE   C  1 240 ? 34.634  26.426  -94.911  1.00 49.19  ? 541  ILE   C CG1 1 
ATOM   8762  C  CG2 . ILE   C  1 240 ? 35.770  28.494  -95.629  1.00 44.25  ? 541  ILE   C CG2 1 
ATOM   8763  C  CD1 . ILE   C  1 240 ? 34.130  27.119  -93.688  1.00 48.20  ? 541  ILE   C CD1 1 
ATOM   8764  N  N   . PRO   C  1 241 ? 37.670  27.651  -98.385  1.00 46.77  ? 542  PRO   C N   1 
ATOM   8765  C  CA  . PRO   C  1 241 ? 38.939  28.189  -98.877  1.00 42.38  ? 542  PRO   C CA  1 
ATOM   8766  C  C   . PRO   C  1 241 ? 39.636  29.007  -97.805  1.00 44.72  ? 542  PRO   C C   1 
ATOM   8767  O  O   . PRO   C  1 241 ? 39.034  29.912  -97.197  1.00 35.48  ? 542  PRO   C O   1 
ATOM   8768  C  CB  . PRO   C  1 241 ? 38.537  29.058  -100.089 1.00 51.95  ? 542  PRO   C CB  1 
ATOM   8769  C  CG  . PRO   C  1 241 ? 37.061  29.036  -100.173 1.00 46.67  ? 542  PRO   C CG  1 
ATOM   8770  C  CD  . PRO   C  1 241 ? 36.565  27.877  -99.333  1.00 54.35  ? 542  PRO   C CD  1 
ATOM   8771  N  N   . PRO   C  1 242 ? 40.895  28.664  -97.519  1.00 46.04  ? 543  PRO   C N   1 
ATOM   8772  C  CA  . PRO   C  1 242 ? 41.654  29.341  -96.462  1.00 45.77  ? 543  PRO   C CA  1 
ATOM   8773  C  C   . PRO   C  1 242 ? 41.602  30.849  -96.524  1.00 54.12  ? 543  PRO   C C   1 
ATOM   8774  O  O   . PRO   C  1 242 ? 41.495  31.503  -95.477  1.00 58.00  ? 543  PRO   C O   1 
ATOM   8775  C  CB  . PRO   C  1 242 ? 43.070  28.823  -96.713  1.00 45.49  ? 543  PRO   C CB  1 
ATOM   8776  C  CG  . PRO   C  1 242 ? 42.839  27.430  -97.196  1.00 43.68  ? 543  PRO   C CG  1 
ATOM   8777  C  CD  . PRO   C  1 242 ? 41.592  27.464  -98.005  1.00 49.20  ? 543  PRO   C CD  1 
ATOM   8778  N  N   . GLU   C  1 243 ? 41.673  31.420  -97.728  1.00 49.99  ? 544  GLU   C N   1 
ATOM   8779  C  CA  . GLU   C  1 243 ? 41.694  32.870  -97.852  1.00 48.63  ? 544  GLU   C CA  1 
ATOM   8780  C  C   . GLU   C  1 243 ? 40.463  33.499  -97.244  1.00 49.59  ? 544  GLU   C C   1 
ATOM   8781  O  O   . GLU   C  1 243 ? 40.429  34.721  -97.079  1.00 57.68  ? 544  GLU   C O   1 
ATOM   8782  C  CB  . GLU   C  1 243 ? 41.827  33.299  -99.325  1.00 49.07  ? 544  GLU   C CB  1 
ATOM   8783  C  CG  . GLU   C  1 243 ? 40.692  32.839  -100.235 1.00 44.10  ? 544  GLU   C CG  1 
ATOM   8784  C  CD  . GLU   C  1 243 ? 41.009  31.539  -100.948 1.00 55.94  ? 544  GLU   C CD  1 
ATOM   8785  O  OE1 . GLU   C  1 243 ? 41.935  30.844  -100.471 1.00 40.95  ? 544  GLU   C OE1 1 
ATOM   8786  O  OE2 . GLU   C  1 243 ? 40.359  31.232  -101.995 1.00 69.41  ? 544  GLU   C OE2 1 
ATOM   8787  N  N   . LEU   C  1 244 ? 39.464  32.697  -96.890  1.00 41.69  ? 545  LEU   C N   1 
ATOM   8788  C  CA  . LEU   C  1 244 ? 38.254  33.212  -96.283  1.00 39.57  ? 545  LEU   C CA  1 
ATOM   8789  C  C   . LEU   C  1 244 ? 38.194  33.029  -94.770  1.00 37.41  ? 545  LEU   C C   1 
ATOM   8790  O  O   . LEU   C  1 244 ? 37.272  33.561  -94.147  1.00 44.65  ? 545  LEU   C O   1 
ATOM   8791  C  CB  . LEU   C  1 244 ? 37.035  32.547  -96.911  1.00 37.43  ? 545  LEU   C CB  1 
ATOM   8792  C  CG  . LEU   C  1 244 ? 36.723  32.785  -98.382  1.00 43.19  ? 545  LEU   C CG  1 
ATOM   8793  C  CD1 . LEU   C  1 244 ? 35.578  31.887  -98.749  1.00 32.52  ? 545  LEU   C CD1 1 
ATOM   8794  C  CD2 . LEU   C  1 244 ? 36.368  34.244  -98.643  1.00 32.84  ? 545  LEU   C CD2 1 
ATOM   8795  N  N   . VAL   C  1 245 ? 39.114  32.287  -94.162  1.00 47.13  ? 546  VAL   C N   1 
ATOM   8796  C  CA  . VAL   C  1 245 ? 39.072  32.037  -92.713  1.00 51.07  ? 546  VAL   C CA  1 
ATOM   8797  C  C   . VAL   C  1 245 ? 40.112  32.953  -92.081  1.00 46.28  ? 546  VAL   C C   1 
ATOM   8798  O  O   . VAL   C  1 245 ? 41.302  32.627  -92.010  1.00 47.12  ? 546  VAL   C O   1 
ATOM   8799  C  CB  . VAL   C  1 245 ? 39.320  30.570  -92.370  1.00 50.80  ? 546  VAL   C CB  1 
ATOM   8800  C  CG1 . VAL   C  1 245 ? 39.392  30.392  -90.871  1.00 54.87  ? 546  VAL   C CG1 1 
ATOM   8801  C  CG2 . VAL   C  1 245 ? 38.220  29.692  -92.964  1.00 50.56  ? 546  VAL   C CG2 1 
ATOM   8802  N  N   . LEU   C  1 246 ? 39.661  34.124  -91.630  1.00 41.73  ? 547  LEU   C N   1 
ATOM   8803  C  CA  . LEU   C  1 246 ? 40.549  35.049  -90.930  1.00 42.60  ? 547  LEU   C CA  1 
ATOM   8804  C  C   . LEU   C  1 246 ? 40.943  34.461  -89.577  1.00 40.20  ? 547  LEU   C C   1 
ATOM   8805  O  O   . LEU   C  1 246 ? 40.109  33.906  -88.861  1.00 39.23  ? 547  LEU   C O   1 
ATOM   8806  C  CB  . LEU   C  1 246 ? 39.871  36.404  -90.759  1.00 39.12  ? 547  LEU   C CB  1 
ATOM   8807  C  CG  . LEU   C  1 246 ? 40.707  37.473  -90.059  1.00 41.64  ? 547  LEU   C CG  1 
ATOM   8808  C  CD1 . LEU   C  1 246 ? 42.072  37.587  -90.715  1.00 36.99  ? 547  LEU   C CD1 1 
ATOM   8809  C  CD2 . LEU   C  1 246 ? 39.961  38.795  -90.147  1.00 34.88  ? 547  LEU   C CD2 1 
ATOM   8810  N  N   . GLU   C  1 247 ? 42.236  34.534  -89.258  1.00 35.69  ? 548  GLU   C N   1 
ATOM   8811  C  CA  . GLU   C  1 247 ? 42.800  33.897  -88.076  1.00 38.01  ? 548  GLU   C CA  1 
ATOM   8812  C  C   . GLU   C  1 247 ? 43.799  34.841  -87.421  1.00 48.38  ? 548  GLU   C C   1 
ATOM   8813  O  O   . GLU   C  1 247 ? 44.571  35.519  -88.111  1.00 49.15  ? 548  GLU   C O   1 
ATOM   8814  C  CB  . GLU   C  1 247 ? 43.494  32.586  -88.426  1.00 41.82  ? 548  GLU   C CB  1 
ATOM   8815  C  CG  . GLU   C  1 247 ? 42.591  31.434  -88.808  1.00 36.37  ? 548  GLU   C CG  1 
ATOM   8816  C  CD  . GLU   C  1 247 ? 43.389  30.131  -88.839  1.00 50.76  ? 548  GLU   C CD  1 
ATOM   8817  O  OE1 . GLU   C  1 247 ? 44.429  30.098  -89.516  1.00 59.17  ? 548  GLU   C OE1 1 
ATOM   8818  O  OE2 . GLU   C  1 247 ? 43.019  29.150  -88.168  1.00 59.13  ? 548  GLU   C OE2 1 
ATOM   8819  N  N   . VAL   C  1 248 ? 43.793  34.880  -86.095  1.00 46.01  ? 549  VAL   C N   1 
ATOM   8820  C  CA  . VAL   C  1 248 ? 44.626  35.819  -85.354  1.00 50.31  ? 549  VAL   C CA  1 
ATOM   8821  C  C   . VAL   C  1 248 ? 45.651  35.015  -84.565  1.00 61.14  ? 549  VAL   C C   1 
ATOM   8822  O  O   . VAL   C  1 248 ? 45.269  34.138  -83.778  1.00 67.02  ? 549  VAL   C O   1 
ATOM   8823  C  CB  . VAL   C  1 248 ? 43.796  36.717  -84.425  1.00 53.15  ? 549  VAL   C CB  1 
ATOM   8824  C  CG1 . VAL   C  1 248 ? 44.704  37.689  -83.687  1.00 63.00  ? 549  VAL   C CG1 1 
ATOM   8825  C  CG2 . VAL   C  1 248 ? 42.743  37.471  -85.210  1.00 48.42  ? 549  VAL   C CG2 1 
ATOM   8826  N  N   . PRO   C  1 249 ? 46.949  35.252  -84.758  1.00 61.18  ? 550  PRO   C N   1 
ATOM   8827  C  CA  . PRO   C  1 249 ? 47.948  34.607  -83.895  1.00 57.19  ? 550  PRO   C CA  1 
ATOM   8828  C  C   . PRO   C  1 249 ? 47.994  35.332  -82.558  1.00 66.92  ? 550  PRO   C C   1 
ATOM   8829  O  O   . PRO   C  1 249 ? 48.017  36.566  -82.511  1.00 75.40  ? 550  PRO   C O   1 
ATOM   8830  C  CB  . PRO   C  1 249 ? 49.256  34.766  -84.676  1.00 56.22  ? 550  PRO   C CB  1 
ATOM   8831  C  CG  . PRO   C  1 249 ? 49.029  35.995  -85.536  1.00 60.09  ? 550  PRO   C CG  1 
ATOM   8832  C  CD  . PRO   C  1 249 ? 47.559  36.065  -85.833  1.00 55.95  ? 550  PRO   C CD  1 
ATOM   8833  N  N   . ILE   C  1 250 ? 47.984  34.567  -81.471  1.00 63.55  ? 551  ILE   C N   1 
ATOM   8834  C  CA  . ILE   C  1 250 ? 47.908  35.139  -80.129  1.00 60.66  ? 551  ILE   C CA  1 
ATOM   8835  C  C   . ILE   C  1 250 ? 49.313  35.463  -79.647  1.00 61.73  ? 551  ILE   C C   1 
ATOM   8836  O  O   . ILE   C  1 250 ? 50.139  34.563  -79.457  1.00 56.68  ? 551  ILE   C O   1 
ATOM   8837  C  CB  . ILE   C  1 250 ? 47.203  34.195  -79.146  1.00 54.95  ? 551  ILE   C CB  1 
ATOM   8838  C  CG1 . ILE   C  1 250 ? 45.948  33.589  -79.783  1.00 46.52  ? 551  ILE   C CG1 1 
ATOM   8839  C  CG2 . ILE   C  1 250 ? 46.867  34.951  -77.852  1.00 53.80  ? 551  ILE   C CG2 1 
ATOM   8840  C  CD1 . ILE   C  1 250 ? 44.896  34.584  -80.063  1.00 38.48  ? 551  ILE   C CD1 1 
ATOM   8841  N  N   . ARG   C  1 251 ? 49.581  36.748  -79.434  1.00 66.53  ? 552  ARG   C N   1 
ATOM   8842  C  CA  . ARG   C  1 251 ? 50.793  37.178  -78.753  1.00 68.05  ? 552  ARG   C CA  1 
ATOM   8843  C  C   . ARG   C  1 251 ? 50.425  38.119  -77.607  1.00 61.84  ? 552  ARG   C C   1 
ATOM   8844  O  O   . ARG   C  1 251 ? 49.323  38.680  -77.563  1.00 58.04  ? 552  ARG   C O   1 
ATOM   8845  C  CB  . ARG   C  1 251 ? 51.764  37.852  -79.717  1.00 57.33  ? 552  ARG   C CB  1 
ATOM   8846  C  CG  . ARG   C  1 251 ? 51.165  39.025  -80.422  1.00 66.70  ? 552  ARG   C CG  1 
ATOM   8847  C  CD  . ARG   C  1 251 ? 50.548  38.628  -81.776  1.00 65.62  ? 552  ARG   C CD  1 
ATOM   8848  N  NE  . ARG   C  1 251 ? 50.050  39.808  -82.465  1.00 55.05  ? 552  ARG   C NE  1 
ATOM   8849  C  CZ  . ARG   C  1 251 ? 49.075  39.800  -83.362  1.00 60.67  ? 552  ARG   C CZ  1 
ATOM   8850  N  NH1 . ARG   C  1 251 ? 48.698  40.945  -83.901  1.00 64.90  ? 552  ARG   C NH1 1 
ATOM   8851  N  NH2 . ARG   C  1 251 ? 48.480  38.662  -83.715  1.00 56.22  ? 552  ARG   C NH2 1 
ATOM   8852  N  N   . HIS   C  1 252 ? 51.368  38.275  -76.662  1.00 64.06  ? 553  HIS   C N   1 
ATOM   8853  C  CA  . HIS   C  1 252 ? 51.152  38.994  -75.413  1.00 55.58  ? 553  HIS   C CA  1 
ATOM   8854  C  C   . HIS   C  1 252 ? 51.971  40.275  -75.382  1.00 59.72  ? 553  HIS   C C   1 
ATOM   8855  O  O   . HIS   C  1 252 ? 53.127  40.284  -75.818  1.00 63.56  ? 553  HIS   C O   1 
ATOM   8856  C  CB  . HIS   C  1 252 ? 51.531  38.129  -74.212  1.00 59.34  ? 553  HIS   C CB  1 
ATOM   8857  C  CG  . HIS   C  1 252 ? 51.055  38.669  -72.899  1.00 59.63  ? 553  HIS   C CG  1 
ATOM   8858  N  ND1 . HIS   C  1 252 ? 51.786  39.572  -72.156  1.00 62.16  ? 553  HIS   C ND1 1 
ATOM   8859  C  CD2 . HIS   C  1 252 ? 49.923  38.429  -72.197  1.00 50.56  ? 553  HIS   C CD2 1 
ATOM   8860  C  CE1 . HIS   C  1 252 ? 51.123  39.867  -71.052  1.00 57.30  ? 553  HIS   C CE1 1 
ATOM   8861  N  NE2 . HIS   C  1 252 ? 49.987  39.193  -71.057  1.00 60.30  ? 553  HIS   C NE2 1 
ATOM   8862  N  N   . PRO   C  1 253 ? 51.401  41.362  -74.859  1.00 61.77  ? 554  PRO   C N   1 
ATOM   8863  C  CA  . PRO   C  1 253 ? 52.090  42.662  -74.928  1.00 59.17  ? 554  PRO   C CA  1 
ATOM   8864  C  C   . PRO   C  1 253 ? 53.291  42.791  -74.020  1.00 67.48  ? 554  PRO   C C   1 
ATOM   8865  O  O   . PRO   C  1 253 ? 54.102  43.698  -74.238  1.00 68.57  ? 554  PRO   C O   1 
ATOM   8866  C  CB  . PRO   C  1 253 ? 50.998  43.663  -74.529  1.00 55.83  ? 554  PRO   C CB  1 
ATOM   8867  C  CG  . PRO   C  1 253 ? 49.987  42.862  -73.806  1.00 56.00  ? 554  PRO   C CG  1 
ATOM   8868  C  CD  . PRO   C  1 253 ? 50.006  41.497  -74.416  1.00 55.66  ? 554  PRO   C CD  1 
ATOM   8869  N  N   . LYS   C  1 254 ? 53.432  41.956  -73.002  1.00 71.85  ? 555  LYS   C N   1 
ATOM   8870  C  CA  . LYS   C  1 254 ? 54.630  42.003  -72.173  1.00 73.80  ? 555  LYS   C CA  1 
ATOM   8871  C  C   . LYS   C  1 254 ? 55.446  40.724  -72.236  1.00 72.11  ? 555  LYS   C C   1 
ATOM   8872  O  O   . LYS   C  1 254 ? 56.678  40.783  -72.300  1.00 73.59  ? 555  LYS   C O   1 
ATOM   8873  C  CB  . LYS   C  1 254 ? 54.260  42.307  -70.714  1.00 86.65  ? 555  LYS   C CB  1 
ATOM   8874  C  CG  . LYS   C  1 254 ? 53.827  43.748  -70.474  1.00 97.04  ? 555  LYS   C CG  1 
ATOM   8875  C  CD  . LYS   C  1 254 ? 54.859  44.743  -71.015  1.00 104.10 ? 555  LYS   C CD  1 
ATOM   8876  C  CE  . LYS   C  1 254 ? 54.415  46.193  -70.833  1.00 102.67 ? 555  LYS   C CE  1 
ATOM   8877  N  NZ  . LYS   C  1 254 ? 54.271  46.562  -69.389  1.00 99.30  ? 555  LYS   C NZ  1 
ATOM   8878  N  N   . PHE   C  1 255 ? 54.790  39.569  -72.243  1.00 75.71  ? 556  PHE   C N   1 
ATOM   8879  C  CA  . PHE   C  1 255 ? 55.473  38.279  -72.277  1.00 77.40  ? 556  PHE   C CA  1 
ATOM   8880  C  C   . PHE   C  1 255 ? 55.891  37.987  -73.711  1.00 72.42  ? 556  PHE   C C   1 
ATOM   8881  O  O   . PHE   C  1 255 ? 55.105  37.482  -74.513  1.00 68.24  ? 556  PHE   C O   1 
ATOM   8882  C  CB  . PHE   C  1 255 ? 54.564  37.189  -71.727  1.00 79.99  ? 556  PHE   C CB  1 
ATOM   8883  C  CG  . PHE   C  1 255 ? 54.069  37.463  -70.334  1.00 81.78  ? 556  PHE   C CG  1 
ATOM   8884  C  CD1 . PHE   C  1 255 ? 52.840  36.995  -69.914  1.00 76.94  ? 556  PHE   C CD1 1 
ATOM   8885  C  CD2 . PHE   C  1 255 ? 54.842  38.186  -69.446  1.00 75.14  ? 556  PHE   C CD2 1 
ATOM   8886  C  CE1 . PHE   C  1 255 ? 52.400  37.246  -68.635  1.00 80.01  ? 556  PHE   C CE1 1 
ATOM   8887  C  CE2 . PHE   C  1 255 ? 54.402  38.439  -68.181  1.00 73.75  ? 556  PHE   C CE2 1 
ATOM   8888  C  CZ  . PHE   C  1 255 ? 53.183  37.966  -67.770  1.00 76.49  ? 556  PHE   C CZ  1 
ATOM   8889  N  N   . GLU   C  1 256 ? 57.140  38.312  -74.039  1.00 71.81  ? 557  GLU   C N   1 
ATOM   8890  C  CA  . GLU   C  1 256 ? 57.660  37.986  -75.359  1.00 83.07  ? 557  GLU   C CA  1 
ATOM   8891  C  C   . GLU   C  1 256 ? 57.550  36.493  -75.645  1.00 84.70  ? 557  GLU   C C   1 
ATOM   8892  O  O   . GLU   C  1 256 ? 57.410  36.090  -76.805  1.00 98.15  ? 557  GLU   C O   1 
ATOM   8893  C  CB  . GLU   C  1 256 ? 59.112  38.456  -75.471  1.00 93.74  ? 557  GLU   C CB  1 
ATOM   8894  C  CG  . GLU   C  1 256 ? 59.307  39.943  -75.226  1.00 101.97 ? 557  GLU   C CG  1 
ATOM   8895  C  CD  . GLU   C  1 256 ? 59.428  40.736  -76.515  1.00 116.83 ? 557  GLU   C CD  1 
ATOM   8896  O  OE1 . GLU   C  1 256 ? 60.146  41.759  -76.500  1.00 121.53 ? 557  GLU   C OE1 1 
ATOM   8897  O  OE2 . GLU   C  1 256 ? 58.818  40.338  -77.539  1.00 118.78 ? 557  GLU   C OE2 1 
ATOM   8898  N  N   . TRP   C  1 257 ? 57.586  35.665  -74.605  1.00 76.90  ? 558  TRP   C N   1 
ATOM   8899  C  CA  . TRP   C  1 257 ? 57.557  34.219  -74.766  1.00 78.95  ? 558  TRP   C CA  1 
ATOM   8900  C  C   . TRP   C  1 257 ? 56.166  33.686  -75.034  1.00 77.58  ? 558  TRP   C C   1 
ATOM   8901  O  O   . TRP   C  1 257 ? 56.008  32.472  -75.196  1.00 85.57  ? 558  TRP   C O   1 
ATOM   8902  C  CB  . TRP   C  1 257 ? 58.112  33.535  -73.516  1.00 86.96  ? 558  TRP   C CB  1 
ATOM   8903  C  CG  . TRP   C  1 257 ? 57.475  34.021  -72.260  1.00 83.88  ? 558  TRP   C CG  1 
ATOM   8904  C  CD1 . TRP   C  1 257 ? 57.985  34.936  -71.392  1.00 91.78  ? 558  TRP   C CD1 1 
ATOM   8905  C  CD2 . TRP   C  1 257 ? 56.209  33.627  -71.728  1.00 72.58  ? 558  TRP   C CD2 1 
ATOM   8906  N  NE1 . TRP   C  1 257 ? 57.120  35.133  -70.350  1.00 85.96  ? 558  TRP   C NE1 1 
ATOM   8907  C  CE2 . TRP   C  1 257 ? 56.018  34.343  -70.537  1.00 75.21  ? 558  TRP   C CE2 1 
ATOM   8908  C  CE3 . TRP   C  1 257 ? 55.221  32.734  -72.140  1.00 75.22  ? 558  TRP   C CE3 1 
ATOM   8909  C  CZ2 . TRP   C  1 257 ? 54.881  34.200  -69.758  1.00 77.43  ? 558  TRP   C CZ2 1 
ATOM   8910  C  CZ3 . TRP   C  1 257 ? 54.082  32.606  -71.371  1.00 77.70  ? 558  TRP   C CZ3 1 
ATOM   8911  C  CH2 . TRP   C  1 257 ? 53.926  33.325  -70.192  1.00 79.15  ? 558  TRP   C CH2 1 
ATOM   8912  N  N   . PHE   C  1 258 ? 55.150  34.545  -75.035  1.00 71.57  ? 559  PHE   C N   1 
ATOM   8913  C  CA  . PHE   C  1 258 ? 53.799  34.049  -75.251  1.00 71.98  ? 559  PHE   C CA  1 
ATOM   8914  C  C   . PHE   C  1 258 ? 53.633  33.546  -76.672  1.00 67.73  ? 559  PHE   C C   1 
ATOM   8915  O  O   . PHE   C  1 258 ? 53.074  32.466  -76.891  1.00 70.78  ? 559  PHE   C O   1 
ATOM   8916  C  CB  . PHE   C  1 258 ? 52.771  35.131  -74.956  1.00 63.71  ? 559  PHE   C CB  1 
ATOM   8917  C  CG  . PHE   C  1 258 ? 51.425  34.587  -74.621  1.00 65.86  ? 559  PHE   C CG  1 
ATOM   8918  C  CD1 . PHE   C  1 258 ? 50.944  34.657  -73.327  1.00 62.34  ? 559  PHE   C CD1 1 
ATOM   8919  C  CD2 . PHE   C  1 258 ? 50.647  33.971  -75.587  1.00 63.86  ? 559  PHE   C CD2 1 
ATOM   8920  C  CE1 . PHE   C  1 258 ? 49.708  34.142  -73.006  1.00 56.07  ? 559  PHE   C CE1 1 
ATOM   8921  C  CE2 . PHE   C  1 258 ? 49.411  33.453  -75.272  1.00 55.86  ? 559  PHE   C CE2 1 
ATOM   8922  C  CZ  . PHE   C  1 258 ? 48.941  33.542  -73.978  1.00 50.15  ? 559  PHE   C CZ  1 
ATOM   8923  N  N   . LYS   C  1 259 ? 54.120  34.316  -77.651  1.00 62.30  ? 560  LYS   C N   1 
ATOM   8924  C  CA  . LYS   C  1 259 ? 53.938  33.938  -79.049  1.00 66.37  ? 560  LYS   C CA  1 
ATOM   8925  C  C   . LYS   C  1 259 ? 54.447  32.529  -79.313  1.00 72.33  ? 560  LYS   C C   1 
ATOM   8926  O  O   . LYS   C  1 259 ? 53.847  31.791  -80.102  1.00 65.88  ? 560  LYS   C O   1 
ATOM   8927  C  CB  . LYS   C  1 259 ? 54.627  34.949  -79.978  1.00 63.86  ? 560  LYS   C CB  1 
ATOM   8928  C  CG  . LYS   C  1 259 ? 56.053  35.354  -79.610  1.00 64.81  ? 560  LYS   C CG  1 
ATOM   8929  C  CD  . LYS   C  1 259 ? 56.550  36.421  -80.575  1.00 64.98  ? 560  LYS   C CD  1 
ATOM   8930  C  CE  . LYS   C  1 259 ? 58.022  36.768  -80.377  1.00 70.35  ? 560  LYS   C CE  1 
ATOM   8931  N  NZ  . LYS   C  1 259 ? 58.280  37.686  -79.221  1.00 79.10  ? 560  LYS   C NZ  1 
ATOM   8932  N  N   . ASP   C  1 260 ? 55.511  32.119  -78.619  1.00 76.87  ? 561  ASP   C N   1 
ATOM   8933  C  CA  . ASP   C  1 260 ? 56.073  30.788  -78.806  1.00 74.99  ? 561  ASP   C CA  1 
ATOM   8934  C  C   . ASP   C  1 260 ? 55.159  29.683  -78.285  1.00 67.18  ? 561  ASP   C C   1 
ATOM   8935  O  O   . ASP   C  1 260 ? 55.483  28.507  -78.473  1.00 70.67  ? 561  ASP   C O   1 
ATOM   8936  C  CB  . ASP   C  1 260 ? 57.444  30.693  -78.130  1.00 86.65  ? 561  ASP   C CB  1 
ATOM   8937  C  CG  . ASP   C  1 260 ? 58.336  31.889  -78.434  1.00 95.01  ? 561  ASP   C CG  1 
ATOM   8938  O  OD1 . ASP   C  1 260 ? 58.162  32.505  -79.510  1.00 96.97  ? 561  ASP   C OD1 1 
ATOM   8939  O  OD2 . ASP   C  1 260 ? 59.213  32.207  -77.592  1.00 95.26  ? 561  ASP   C OD2 1 
ATOM   8940  N  N   . LEU   C  1 261 ? 54.038  30.008  -77.637  1.00 64.89  ? 562  LEU   C N   1 
ATOM   8941  C  CA  . LEU   C  1 261 ? 53.087  28.965  -77.263  1.00 67.58  ? 562  LEU   C CA  1 
ATOM   8942  C  C   . LEU   C  1 261 ? 52.405  28.345  -78.478  1.00 82.79  ? 562  LEU   C C   1 
ATOM   8943  O  O   . LEU   C  1 261 ? 51.767  27.294  -78.345  1.00 90.25  ? 562  LEU   C O   1 
ATOM   8944  C  CB  . LEU   C  1 261 ? 52.033  29.521  -76.309  1.00 50.21  ? 562  LEU   C CB  1 
ATOM   8945  C  CG  . LEU   C  1 261 ? 52.420  29.758  -74.847  1.00 63.44  ? 562  LEU   C CG  1 
ATOM   8946  C  CD1 . LEU   C  1 261 ? 51.412  30.675  -74.154  1.00 58.04  ? 562  LEU   C CD1 1 
ATOM   8947  C  CD2 . LEU   C  1 261 ? 52.488  28.442  -74.116  1.00 64.09  ? 562  LEU   C CD2 1 
ATOM   8948  N  N   . GLY   C  1 262 ? 52.521  28.972  -79.644  1.00 82.17  ? 563  GLY   C N   1 
ATOM   8949  C  CA  . GLY   C  1 262 ? 52.005  28.414  -80.881  1.00 83.21  ? 563  GLY   C CA  1 
ATOM   8950  C  C   . GLY   C  1 262 ? 50.499  28.387  -80.962  1.00 77.02  ? 563  GLY   C C   1 
ATOM   8951  O  O   . GLY   C  1 262 ? 49.926  27.421  -81.477  1.00 75.06  ? 563  GLY   C O   1 
ATOM   8952  N  N   . LEU   C  1 263 ? 49.843  29.420  -80.457  1.00 71.13  ? 564  LEU   C N   1 
ATOM   8953  C  CA  . LEU   C  1 263 ? 48.396  29.459  -80.369  1.00 65.00  ? 564  LEU   C CA  1 
ATOM   8954  C  C   . LEU   C  1 263 ? 47.840  30.491  -81.343  1.00 59.59  ? 564  LEU   C C   1 
ATOM   8955  O  O   . LEU   C  1 263 ? 48.427  31.562  -81.531  1.00 51.99  ? 564  LEU   C O   1 
ATOM   8956  C  CB  . LEU   C  1 263 ? 47.954  29.784  -78.935  1.00 66.06  ? 564  LEU   C CB  1 
ATOM   8957  C  CG  . LEU   C  1 263 ? 48.476  28.929  -77.772  1.00 74.59  ? 564  LEU   C CG  1 
ATOM   8958  C  CD1 . LEU   C  1 263 ? 48.373  29.711  -76.466  1.00 74.76  ? 564  LEU   C CD1 1 
ATOM   8959  C  CD2 . LEU   C  1 263 ? 47.742  27.599  -77.638  1.00 69.36  ? 564  LEU   C CD2 1 
ATOM   8960  N  N   . LYS   C  1 264 ? 46.709  30.159  -81.966  1.00 64.78  ? 565  LYS   C N   1 
ATOM   8961  C  CA  . LYS   C  1 264 ? 45.959  31.089  -82.806  1.00 59.95  ? 565  LYS   C CA  1 
ATOM   8962  C  C   . LYS   C  1 264 ? 44.487  30.742  -82.685  1.00 52.92  ? 565  LYS   C C   1 
ATOM   8963  O  O   . LYS   C  1 264 ? 44.124  29.610  -82.351  1.00 59.46  ? 565  LYS   C O   1 
ATOM   8964  C  CB  . LYS   C  1 264 ? 46.406  31.049  -84.286  1.00 60.11  ? 565  LYS   C CB  1 
ATOM   8965  C  CG  . LYS   C  1 264 ? 45.919  29.832  -85.093  1.00 60.19  ? 565  LYS   C CG  1 
ATOM   8966  C  CD  . LYS   C  1 264 ? 46.755  29.583  -86.358  1.00 64.21  ? 565  LYS   C CD  1 
ATOM   8967  C  CE  . LYS   C  1 264 ? 46.148  28.469  -87.212  1.00 77.78  ? 565  LYS   C CE  1 
ATOM   8968  N  NZ  . LYS   C  1 264 ? 47.196  27.590  -87.835  1.00 90.12  ? 565  LYS   C NZ  1 
ATOM   8969  N  N   . TRP   C  1 265 ? 43.637  31.734  -82.919  1.00 42.97  ? 566  TRP   C N   1 
ATOM   8970  C  CA  . TRP   C  1 265 ? 42.199  31.502  -82.974  1.00 39.73  ? 566  TRP   C CA  1 
ATOM   8971  C  C   . TRP   C  1 265 ? 41.642  32.166  -84.228  1.00 53.67  ? 566  TRP   C C   1 
ATOM   8972  O  O   . TRP   C  1 265 ? 42.306  32.994  -84.863  1.00 57.22  ? 566  TRP   C O   1 
ATOM   8973  C  CB  . TRP   C  1 265 ? 41.474  32.016  -81.723  1.00 37.32  ? 566  TRP   C CB  1 
ATOM   8974  C  CG  . TRP   C  1 265 ? 40.204  31.262  -81.451  1.00 37.66  ? 566  TRP   C CG  1 
ATOM   8975  C  CD1 . TRP   C  1 265 ? 38.940  31.739  -81.575  1.00 39.74  ? 566  TRP   C CD1 1 
ATOM   8976  C  CD2 . TRP   C  1 265 ? 40.077  29.886  -81.028  1.00 45.30  ? 566  TRP   C CD2 1 
ATOM   8977  N  NE1 . TRP   C  1 265 ? 38.027  30.756  -81.257  1.00 47.56  ? 566  TRP   C NE1 1 
ATOM   8978  C  CE2 . TRP   C  1 265 ? 38.700  29.611  -80.919  1.00 41.38  ? 566  TRP   C CE2 1 
ATOM   8979  C  CE3 . TRP   C  1 265 ? 40.998  28.868  -80.724  1.00 43.97  ? 566  TRP   C CE3 1 
ATOM   8980  C  CZ2 . TRP   C  1 265 ? 38.215  28.365  -80.524  1.00 40.64  ? 566  TRP   C CZ2 1 
ATOM   8981  C  CZ3 . TRP   C  1 265 ? 40.516  27.625  -80.336  1.00 36.63  ? 566  TRP   C CZ3 1 
ATOM   8982  C  CH2 . TRP   C  1 265 ? 39.138  27.386  -80.238  1.00 45.86  ? 566  TRP   C CH2 1 
ATOM   8983  N  N   . TYR   C  1 266 ? 40.419  31.780  -84.589  1.00 46.28  ? 567  TYR   C N   1 
ATOM   8984  C  CA  . TYR   C  1 266 ? 39.738  32.358  -85.732  1.00 41.82  ? 567  TYR   C CA  1 
ATOM   8985  C  C   . TYR   C  1 266 ? 38.951  33.601  -85.329  1.00 46.87  ? 567  TYR   C C   1 
ATOM   8986  O  O   . TYR   C  1 266 ? 38.757  33.894  -84.149  1.00 54.30  ? 567  TYR   C O   1 
ATOM   8987  C  CB  . TYR   C  1 266 ? 38.833  31.327  -86.398  1.00 38.91  ? 567  TYR   C CB  1 
ATOM   8988  C  CG  . TYR   C  1 266 ? 37.928  30.570  -85.471  1.00 40.98  ? 567  TYR   C CG  1 
ATOM   8989  C  CD1 . TYR   C  1 266 ? 36.638  30.995  -85.250  1.00 53.11  ? 567  TYR   C CD1 1 
ATOM   8990  C  CD2 . TYR   C  1 266 ? 38.350  29.410  -84.848  1.00 37.02  ? 567  TYR   C CD2 1 
ATOM   8991  C  CE1 . TYR   C  1 266 ? 35.789  30.306  -84.421  1.00 54.58  ? 567  TYR   C CE1 1 
ATOM   8992  C  CE2 . TYR   C  1 266 ? 37.499  28.699  -84.017  1.00 38.71  ? 567  TYR   C CE2 1 
ATOM   8993  C  CZ  . TYR   C  1 266 ? 36.222  29.164  -83.790  1.00 49.44  ? 567  TYR   C CZ  1 
ATOM   8994  O  OH  . TYR   C  1 266 ? 35.359  28.477  -82.958  1.00 51.83  ? 567  TYR   C OH  1 
ATOM   8995  N  N   . GLY   C  1 267 ? 38.503  34.349  -86.339  1.00 42.37  ? 568  GLY   C N   1 
ATOM   8996  C  CA  . GLY   C  1 267 ? 37.982  35.684  -86.102  1.00 34.32  ? 568  GLY   C CA  1 
ATOM   8997  C  C   . GLY   C  1 267 ? 36.476  35.749  -86.056  1.00 39.89  ? 568  GLY   C C   1 
ATOM   8998  O  O   . GLY   C  1 267 ? 35.897  36.669  -85.474  1.00 48.55  ? 568  GLY   C O   1 
ATOM   8999  N  N   . LEU   C  1 268 ? 35.828  34.751  -86.637  1.00 37.67  ? 569  LEU   C N   1 
ATOM   9000  C  CA  . LEU   C  1 268 ? 34.400  34.826  -86.896  1.00 38.30  ? 569  LEU   C CA  1 
ATOM   9001  C  C   . LEU   C  1 268 ? 33.684  33.742  -86.109  1.00 45.63  ? 569  LEU   C C   1 
ATOM   9002  O  O   . LEU   C  1 268 ? 33.839  32.546  -86.414  1.00 38.97  ? 569  LEU   C O   1 
ATOM   9003  C  CB  . LEU   C  1 268 ? 34.121  34.684  -88.398  1.00 33.82  ? 569  LEU   C CB  1 
ATOM   9004  C  CG  . LEU   C  1 268 ? 32.648  34.817  -88.765  1.00 38.46  ? 569  LEU   C CG  1 
ATOM   9005  C  CD1 . LEU   C  1 268 ? 32.237  36.279  -88.741  1.00 42.24  ? 569  LEU   C CD1 1 
ATOM   9006  C  CD2 . LEU   C  1 268 ? 32.331  34.162  -90.119  1.00 46.70  ? 569  LEU   C CD2 1 
ATOM   9007  N  N   . PRO   C  1 269 ? 32.934  34.103  -85.071  1.00 44.19  ? 570  PRO   C N   1 
ATOM   9008  C  CA  . PRO   C  1 269 ? 32.036  33.136  -84.448  1.00 33.10  ? 570  PRO   C CA  1 
ATOM   9009  C  C   . PRO   C  1 269 ? 30.779  33.042  -85.290  1.00 36.60  ? 570  PRO   C C   1 
ATOM   9010  O  O   . PRO   C  1 269 ? 30.171  34.059  -85.632  1.00 37.74  ? 570  PRO   C O   1 
ATOM   9011  C  CB  . PRO   C  1 269 ? 31.745  33.753  -83.081  1.00 27.13  ? 570  PRO   C CB  1 
ATOM   9012  C  CG  . PRO   C  1 269 ? 31.857  35.247  -83.321  1.00 37.11  ? 570  PRO   C CG  1 
ATOM   9013  C  CD  . PRO   C  1 269 ? 32.899  35.419  -84.399  1.00 45.09  ? 570  PRO   C CD  1 
ATOM   9014  N  N   . ALA   C  1 270 ? 30.377  31.818  -85.605  1.00 34.80  ? 571  ALA   C N   1 
ATOM   9015  C  CA  . ALA   C  1 270 ? 29.291  31.639  -86.554  1.00 31.85  ? 571  ALA   C CA  1 
ATOM   9016  C  C   . ALA   C  1 270 ? 28.540  30.368  -86.177  1.00 26.53  ? 571  ALA   C C   1 
ATOM   9017  O  O   . ALA   C  1 270 ? 28.977  29.265  -86.511  1.00 48.03  ? 571  ALA   C O   1 
ATOM   9018  C  CB  . ALA   C  1 270 ? 29.847  31.583  -87.971  1.00 36.92  ? 571  ALA   C CB  1 
ATOM   9019  N  N   . VAL   C  1 271 ? 27.425  30.526  -85.481  1.00 31.22  ? 572  VAL   C N   1 
ATOM   9020  C  CA  . VAL   C  1 271 ? 26.701  29.379  -84.936  1.00 36.50  ? 572  VAL   C CA  1 
ATOM   9021  C  C   . VAL   C  1 271 ? 25.836  28.784  -86.029  1.00 43.08  ? 572  VAL   C C   1 
ATOM   9022  O  O   . VAL   C  1 271 ? 25.159  29.515  -86.761  1.00 50.39  ? 572  VAL   C O   1 
ATOM   9023  C  CB  . VAL   C  1 271 ? 25.842  29.797  -83.732  1.00 29.42  ? 572  VAL   C CB  1 
ATOM   9024  C  CG1 . VAL   C  1 271 ? 25.110  28.596  -83.180  1.00 26.30  ? 572  VAL   C CG1 1 
ATOM   9025  C  CG2 . VAL   C  1 271 ? 26.698  30.410  -82.701  1.00 29.90  ? 572  VAL   C CG2 1 
ATOM   9026  N  N   . SER   C  1 272 ? 25.820  27.453  -86.130  1.00 34.39  ? 573  SER   C N   1 
ATOM   9027  C  CA  . SER   C  1 272 ? 25.209  26.818  -87.288  1.00 42.35  ? 573  SER   C CA  1 
ATOM   9028  C  C   . SER   C  1 272 ? 24.326  25.627  -86.962  1.00 46.38  ? 573  SER   C C   1 
ATOM   9029  O  O   . SER   C  1 272 ? 23.752  25.037  -87.888  1.00 42.44  ? 573  SER   C O   1 
ATOM   9030  C  CB  . SER   C  1 272 ? 26.292  26.384  -88.291  1.00 36.87  ? 573  SER   C CB  1 
ATOM   9031  O  OG  . SER   C  1 272 ? 27.193  25.451  -87.709  1.00 43.43  ? 573  SER   C OG  1 
ATOM   9032  N  N   . ASN   C  1 273 ? 24.192  25.257  -85.692  1.00 44.79  ? 574  ASN   C N   1 
ATOM   9033  C  CA  . ASN   C  1 273 ? 23.411  24.087  -85.313  1.00 41.09  ? 574  ASN   C CA  1 
ATOM   9034  C  C   . ASN   C  1 273 ? 22.046  24.432  -84.736  1.00 42.70  ? 574  ASN   C C   1 
ATOM   9035  O  O   . ASN   C  1 273 ? 21.340  23.525  -84.285  1.00 51.91  ? 574  ASN   C O   1 
ATOM   9036  C  CB  . ASN   C  1 273 ? 24.191  23.228  -84.310  1.00 50.87  ? 574  ASN   C CB  1 
ATOM   9037  C  CG  . ASN   C  1 273 ? 24.636  24.005  -83.060  1.00 49.38  ? 574  ASN   C CG  1 
ATOM   9038  O  OD1 . ASN   C  1 273 ? 24.283  25.166  -82.850  1.00 49.89  ? 574  ASN   C OD1 1 
ATOM   9039  N  ND2 . ASN   C  1 273 ? 25.424  23.347  -82.228  1.00 47.81  ? 574  ASN   C ND2 1 
ATOM   9040  N  N   . MET   C  1 274 ? 21.653  25.706  -84.738  1.00 39.45  ? 575  MET   C N   1 
ATOM   9041  C  CA  . MET   C  1 274 ? 20.422  26.136  -84.085  1.00 34.43  ? 575  MET   C CA  1 
ATOM   9042  C  C   . MET   C  1 274 ? 19.266  26.263  -85.078  1.00 44.62  ? 575  MET   C C   1 
ATOM   9043  O  O   . MET   C  1 274 ? 19.429  26.134  -86.296  1.00 37.50  ? 575  MET   C O   1 
ATOM   9044  C  CB  . MET   C  1 274 ? 20.648  27.445  -83.338  1.00 26.93  ? 575  MET   C CB  1 
ATOM   9045  C  CG  . MET   C  1 274 ? 21.365  27.180  -82.005  1.00 35.83  ? 575  MET   C CG  1 
ATOM   9046  S  SD  . MET   C  1 274 ? 21.494  28.579  -80.887  1.00 50.03  ? 575  MET   C SD  1 
ATOM   9047  C  CE  . MET   C  1 274 ? 19.924  28.519  -80.024  1.00 45.31  ? 575  MET   C CE  1 
ATOM   9048  N  N   . LEU   C  1 275 ? 18.077  26.516  -84.536  1.00 36.60  ? 576  LEU   C N   1 
ATOM   9049  C  CA  . LEU   C  1 275 ? 16.838  26.424  -85.294  1.00 32.94  ? 576  LEU   C CA  1 
ATOM   9050  C  C   . LEU   C  1 275 ? 16.123  27.755  -85.202  1.00 39.47  ? 576  LEU   C C   1 
ATOM   9051  O  O   . LEU   C  1 275 ? 15.800  28.198  -84.105  1.00 41.65  ? 576  LEU   C O   1 
ATOM   9052  C  CB  . LEU   C  1 275 ? 15.951  25.308  -84.737  1.00 36.58  ? 576  LEU   C CB  1 
ATOM   9053  C  CG  . LEU   C  1 275 ? 14.658  25.066  -85.506  1.00 42.18  ? 576  LEU   C CG  1 
ATOM   9054  C  CD1 . LEU   C  1 275 ? 14.349  23.588  -85.568  1.00 35.24  ? 576  LEU   C CD1 1 
ATOM   9055  C  CD2 . LEU   C  1 275 ? 13.518  25.798  -84.871  1.00 45.35  ? 576  LEU   C CD2 1 
ATOM   9056  N  N   . LEU   C  1 276 ? 15.858  28.387  -86.339  1.00 46.70  ? 577  LEU   C N   1 
ATOM   9057  C  CA  . LEU   C  1 276 ? 15.151  29.661  -86.355  1.00 40.18  ? 577  LEU   C CA  1 
ATOM   9058  C  C   . LEU   C  1 276 ? 13.664  29.396  -86.547  1.00 41.86  ? 577  LEU   C C   1 
ATOM   9059  O  O   . LEU   C  1 276 ? 13.260  28.859  -87.580  1.00 54.04  ? 577  LEU   C O   1 
ATOM   9060  C  CB  . LEU   C  1 276 ? 15.690  30.581  -87.450  1.00 41.80  ? 577  LEU   C CB  1 
ATOM   9061  C  CG  . LEU   C  1 276 ? 14.989  31.928  -87.622  1.00 45.54  ? 577  LEU   C CG  1 
ATOM   9062  C  CD1 . LEU   C  1 276 ? 14.879  32.598  -86.319  1.00 47.63  ? 577  LEU   C CD1 1 
ATOM   9063  C  CD2 . LEU   C  1 276 ? 15.749  32.827  -88.586  1.00 58.92  ? 577  LEU   C CD2 1 
ATOM   9064  N  N   . GLU   C  1 277 ? 12.863  29.777  -85.554  1.00 41.78  ? 578  GLU   C N   1 
ATOM   9065  C  CA  . GLU   C  1 277 ? 11.419  29.567  -85.544  1.00 35.64  ? 578  GLU   C CA  1 
ATOM   9066  C  C   . GLU   C  1 277 ? 10.730  30.916  -85.710  1.00 45.70  ? 578  GLU   C C   1 
ATOM   9067  O  O   . GLU   C  1 277 ? 10.979  31.844  -84.925  1.00 44.01  ? 578  GLU   C O   1 
ATOM   9068  C  CB  . GLU   C  1 277 ? 10.981  28.895  -84.243  1.00 50.98  ? 578  GLU   C CB  1 
ATOM   9069  C  CG  . GLU   C  1 277 ? 9.603   28.276  -84.284  1.00 61.97  ? 578  GLU   C CG  1 
ATOM   9070  C  CD  . GLU   C  1 277 ? 8.569   29.162  -83.642  1.00 71.76  ? 578  GLU   C CD  1 
ATOM   9071  O  OE1 . GLU   C  1 277 ? 7.376   29.042  -83.985  1.00 74.15  ? 578  GLU   C OE1 1 
ATOM   9072  O  OE2 . GLU   C  1 277 ? 8.953   29.983  -82.787  1.00 78.10  ? 578  GLU   C OE2 1 
ATOM   9073  N  N   . ILE   C  1 278 ? 9.894   31.026  -86.752  1.00 45.75  ? 579  ILE   C N   1 
ATOM   9074  C  CA  . ILE   C  1 278 ? 9.095   32.212  -87.054  1.00 39.17  ? 579  ILE   C CA  1 
ATOM   9075  C  C   . ILE   C  1 278 ? 7.707   31.765  -87.486  1.00 45.01  ? 579  ILE   C C   1 
ATOM   9076  O  O   . ILE   C  1 278 ? 7.571   30.878  -88.336  1.00 42.40  ? 579  ILE   C O   1 
ATOM   9077  C  CB  . ILE   C  1 278 ? 9.713   33.078  -88.162  1.00 35.15  ? 579  ILE   C CB  1 
ATOM   9078  C  CG1 . ILE   C  1 278 ? 11.097  33.547  -87.759  1.00 30.79  ? 579  ILE   C CG1 1 
ATOM   9079  C  CG2 . ILE   C  1 278 ? 8.816   34.260  -88.428  1.00 36.19  ? 579  ILE   C CG2 1 
ATOM   9080  C  CD1 . ILE   C  1 278 ? 11.903  34.144  -88.865  1.00 36.41  ? 579  ILE   C CD1 1 
ATOM   9081  N  N   . GLY   C  1 279 ? 6.685   32.401  -86.919  1.00 45.14  ? 580  GLY   C N   1 
ATOM   9082  C  CA  . GLY   C  1 279 ? 5.294   32.088  -87.160  1.00 39.35  ? 580  GLY   C CA  1 
ATOM   9083  C  C   . GLY   C  1 279 ? 5.029   30.662  -87.569  1.00 47.76  ? 580  GLY   C C   1 
ATOM   9084  O  O   . GLY   C  1 279 ? 4.434   30.409  -88.619  1.00 64.60  ? 580  GLY   C O   1 
ATOM   9085  N  N   . GLY   C  1 280 ? 5.488   29.720  -86.768  1.00 42.88  ? 581  GLY   C N   1 
ATOM   9086  C  CA  . GLY   C  1 280 ? 5.187   28.328  -86.999  1.00 48.85  ? 581  GLY   C CA  1 
ATOM   9087  C  C   . GLY   C  1 280 ? 6.178   27.605  -87.876  1.00 49.68  ? 581  GLY   C C   1 
ATOM   9088  O  O   . GLY   C  1 280 ? 6.176   26.367  -87.888  1.00 58.15  ? 581  GLY   C O   1 
ATOM   9089  N  N   . LEU   C  1 281 ? 7.035   28.345  -88.586  1.00 45.50  ? 582  LEU   C N   1 
ATOM   9090  C  CA  . LEU   C  1 281 ? 7.977   27.807  -89.559  1.00 47.60  ? 582  LEU   C CA  1 
ATOM   9091  C  C   . LEU   C  1 281 ? 9.344   27.582  -88.933  1.00 42.44  ? 582  LEU   C C   1 
ATOM   9092  O  O   . LEU   C  1 281 ? 9.819   28.403  -88.149  1.00 49.67  ? 582  LEU   C O   1 
ATOM   9093  C  CB  . LEU   C  1 281 ? 8.125   28.754  -90.753  1.00 45.51  ? 582  LEU   C CB  1 
ATOM   9094  C  CG  . LEU   C  1 281 ? 6.780   29.183  -91.308  1.00 42.09  ? 582  LEU   C CG  1 
ATOM   9095  C  CD1 . LEU   C  1 281 ? 6.946   30.359  -92.249  1.00 39.36  ? 582  LEU   C CD1 1 
ATOM   9096  C  CD2 . LEU   C  1 281 ? 6.139   27.992  -91.981  1.00 36.43  ? 582  LEU   C CD2 1 
ATOM   9097  N  N   . GLU   C  1 282 ? 10.001  26.500  -89.337  1.00 44.04  ? 583  GLU   C N   1 
ATOM   9098  C  CA  . GLU   C  1 282 ? 11.240  26.048  -88.712  1.00 45.00  ? 583  GLU   C CA  1 
ATOM   9099  C  C   . GLU   C  1 282 ? 12.377  26.007  -89.730  1.00 48.52  ? 583  GLU   C C   1 
ATOM   9100  O  O   . GLU   C  1 282 ? 12.462  25.085  -90.549  1.00 52.89  ? 583  GLU   C O   1 
ATOM   9101  C  CB  . GLU   C  1 282 ? 11.030  24.680  -88.073  1.00 53.79  ? 583  GLU   C CB  1 
ATOM   9102  C  CG  . GLU   C  1 282 ? 9.939   24.654  -87.036  1.00 49.57  ? 583  GLU   C CG  1 
ATOM   9103  C  CD  . GLU   C  1 282 ? 9.870   23.324  -86.341  1.00 62.63  ? 583  GLU   C CD  1 
ATOM   9104  O  OE1 . GLU   C  1 282 ? 10.086  22.309  -87.029  1.00 55.03  ? 583  GLU   C OE1 1 
ATOM   9105  O  OE2 . GLU   C  1 282 ? 9.623   23.298  -85.110  1.00 80.37  ? 583  GLU   C OE2 1 
ATOM   9106  N  N   . PHE   C  1 283 ? 13.278  26.981  -89.628  1.00 43.74  ? 584  PHE   C N   1 
ATOM   9107  C  CA  . PHE   C  1 283 ? 14.476  27.065  -90.458  1.00 37.22  ? 584  PHE   C CA  1 
ATOM   9108  C  C   . PHE   C  1 283 ? 15.631  26.351  -89.753  1.00 40.94  ? 584  PHE   C C   1 
ATOM   9109  O  O   . PHE   C  1 283 ? 16.369  26.935  -88.960  1.00 51.29  ? 584  PHE   C O   1 
ATOM   9110  C  CB  . PHE   C  1 283 ? 14.791  28.526  -90.735  1.00 30.91  ? 584  PHE   C CB  1 
ATOM   9111  C  CG  . PHE   C  1 283 ? 13.686  29.255  -91.453  1.00 38.02  ? 584  PHE   C CG  1 
ATOM   9112  C  CD1 . PHE   C  1 283 ? 12.749  29.998  -90.744  1.00 41.85  ? 584  PHE   C CD1 1 
ATOM   9113  C  CD2 . PHE   C  1 283 ? 13.584  29.201  -92.843  1.00 44.94  ? 584  PHE   C CD2 1 
ATOM   9114  C  CE1 . PHE   C  1 283 ? 11.728  30.687  -91.397  1.00 45.54  ? 584  PHE   C CE1 1 
ATOM   9115  C  CE2 . PHE   C  1 283 ? 12.564  29.897  -93.521  1.00 42.57  ? 584  PHE   C CE2 1 
ATOM   9116  C  CZ  . PHE   C  1 283 ? 11.633  30.637  -92.794  1.00 53.57  ? 584  PHE   C CZ  1 
ATOM   9117  N  N   . SER   C  1 284 ? 15.808  25.070  -90.055  1.00 41.25  ? 585  SER   C N   1 
ATOM   9118  C  CA  . SER   C  1 284 ? 16.811  24.261  -89.374  1.00 33.83  ? 585  SER   C CA  1 
ATOM   9119  C  C   . SER   C  1 284 ? 18.238  24.520  -89.817  1.00 36.06  ? 585  SER   C C   1 
ATOM   9120  O  O   . SER   C  1 284 ? 19.152  23.907  -89.265  1.00 41.58  ? 585  SER   C O   1 
ATOM   9121  C  CB  . SER   C  1 284 ? 16.514  22.793  -89.603  1.00 49.22  ? 585  SER   C CB  1 
ATOM   9122  O  OG  . SER   C  1 284 ? 16.237  22.582  -90.970  1.00 49.39  ? 585  SER   C OG  1 
ATOM   9123  N  N   . ALA   C  1 285 ? 18.466  25.340  -90.835  1.00 42.70  ? 586  ALA   C N   1 
ATOM   9124  C  CA  . ALA   C  1 285 ? 19.822  25.719  -91.223  1.00 36.57  ? 586  ALA   C CA  1 
ATOM   9125  C  C   . ALA   C  1 285 ? 19.816  27.229  -91.359  1.00 41.34  ? 586  ALA   C C   1 
ATOM   9126  O  O   . ALA   C  1 285 ? 19.247  27.755  -92.318  1.00 42.80  ? 586  ALA   C O   1 
ATOM   9127  C  CB  . ALA   C  1 285 ? 20.254  25.050  -92.516  1.00 34.88  ? 586  ALA   C CB  1 
ATOM   9128  N  N   . CYS   C  1 286 ? 20.423  27.911  -90.386  1.00 38.43  ? 587  CYS   C N   1 
ATOM   9129  C  CA  . CYS   C  1 286 ? 20.379  29.361  -90.326  1.00 36.96  ? 587  CYS   C CA  1 
ATOM   9130  C  C   . CYS   C  1 286 ? 21.644  29.944  -89.715  1.00 48.36  ? 587  CYS   C C   1 
ATOM   9131  O  O   . CYS   C  1 286 ? 21.551  30.735  -88.768  1.00 54.18  ? 587  CYS   C O   1 
ATOM   9132  C  CB  . CYS   C  1 286 ? 19.185  29.818  -89.502  1.00 44.83  ? 587  CYS   C CB  1 
ATOM   9133  S  SG  . CYS   C  1 286 ? 19.168  29.051  -87.881  1.00 43.16  ? 587  CYS   C SG  1 
ATOM   9134  N  N   . PRO   C  1 287 ? 22.824  29.628  -90.247  1.00 52.18  ? 588  PRO   C N   1 
ATOM   9135  C  CA  . PRO   C  1 287 ? 24.062  30.092  -89.613  1.00 43.85  ? 588  PRO   C CA  1 
ATOM   9136  C  C   . PRO   C  1 287 ? 24.045  31.594  -89.382  1.00 48.18  ? 588  PRO   C C   1 
ATOM   9137  O  O   . PRO   C  1 287 ? 23.707  32.375  -90.281  1.00 51.01  ? 588  PRO   C O   1 
ATOM   9138  C  CB  . PRO   C  1 287 ? 25.144  29.683  -90.620  1.00 47.08  ? 588  PRO   C CB  1 
ATOM   9139  C  CG  . PRO   C  1 287 ? 24.417  29.360  -91.894  1.00 41.98  ? 588  PRO   C CG  1 
ATOM   9140  C  CD  . PRO   C  1 287 ? 23.094  28.854  -91.472  1.00 44.63  ? 588  PRO   C CD  1 
ATOM   9141  N  N   . PHE   C  1 288 ? 24.377  32.001  -88.152  1.00 40.63  ? 589  PHE   C N   1 
ATOM   9142  C  CA  . PHE   C  1 288 ? 24.526  33.417  -87.826  1.00 31.33  ? 589  PHE   C CA  1 
ATOM   9143  C  C   . PHE   C  1 288 ? 25.886  33.686  -87.210  1.00 33.17  ? 589  PHE   C C   1 
ATOM   9144  O  O   . PHE   C  1 288 ? 26.553  32.796  -86.678  1.00 31.40  ? 589  PHE   C O   1 
ATOM   9145  C  CB  . PHE   C  1 288 ? 23.434  33.935  -86.886  1.00 26.74  ? 589  PHE   C CB  1 
ATOM   9146  C  CG  . PHE   C  1 288 ? 23.220  33.088  -85.667  1.00 39.50  ? 589  PHE   C CG  1 
ATOM   9147  C  CD1 . PHE   C  1 288 ? 23.928  33.334  -84.487  1.00 40.56  ? 589  PHE   C CD1 1 
ATOM   9148  C  CD2 . PHE   C  1 288 ? 22.287  32.058  -85.689  1.00 37.70  ? 589  PHE   C CD2 1 
ATOM   9149  C  CE1 . PHE   C  1 288 ? 23.718  32.553  -83.362  1.00 34.18  ? 589  PHE   C CE1 1 
ATOM   9150  C  CE2 . PHE   C  1 288 ? 22.068  31.272  -84.570  1.00 45.17  ? 589  PHE   C CE2 1 
ATOM   9151  C  CZ  . PHE   C  1 288 ? 22.792  31.519  -83.403  1.00 38.26  ? 589  PHE   C CZ  1 
ATOM   9152  N  N   . SER   C  1 289 ? 26.283  34.946  -87.299  1.00 28.32  ? 590  SER   C N   1 
ATOM   9153  C  CA  . SER   C  1 289 ? 27.656  35.342  -87.055  1.00 28.50  ? 590  SER   C CA  1 
ATOM   9154  C  C   . SER   C  1 289 ? 27.644  36.746  -86.453  1.00 32.10  ? 590  SER   C C   1 
ATOM   9155  O  O   . SER   C  1 289 ? 26.813  37.579  -86.820  1.00 41.20  ? 590  SER   C O   1 
ATOM   9156  C  CB  . SER   C  1 289 ? 28.460  35.305  -88.372  1.00 26.60  ? 590  SER   C CB  1 
ATOM   9157  O  OG  . SER   C  1 289 ? 29.125  36.551  -88.603  1.00 42.88  ? 590  SER   C OG  1 
ATOM   9158  N  N   . GLY   C  1 290 ? 28.535  36.996  -85.506  1.00 33.65  ? 591  GLY   C N   1 
ATOM   9159  C  CA  . GLY   C  1 290 ? 28.733  38.351  -85.044  1.00 30.63  ? 591  GLY   C CA  1 
ATOM   9160  C  C   . GLY   C  1 290 ? 30.209  38.568  -84.809  1.00 46.98  ? 591  GLY   C C   1 
ATOM   9161  O  O   . GLY   C  1 290 ? 31.003  38.471  -85.748  1.00 57.28  ? 591  GLY   C O   1 
ATOM   9162  N  N   . TRP   C  1 291 ? 30.603  38.830  -83.562  1.00 44.50  ? 592  TRP   C N   1 
ATOM   9163  C  CA  . TRP   C  1 291 ? 32.014  38.897  -83.236  1.00 44.27  ? 592  TRP   C CA  1 
ATOM   9164  C  C   . TRP   C  1 291 ? 32.214  38.519  -81.767  1.00 46.25  ? 592  TRP   C C   1 
ATOM   9165  O  O   . TRP   C  1 291 ? 31.285  38.512  -80.956  1.00 49.44  ? 592  TRP   C O   1 
ATOM   9166  C  CB  . TRP   C  1 291 ? 32.587  40.282  -83.574  1.00 40.88  ? 592  TRP   C CB  1 
ATOM   9167  C  CG  . TRP   C  1 291 ? 31.833  41.382  -82.941  1.00 48.24  ? 592  TRP   C CG  1 
ATOM   9168  C  CD1 . TRP   C  1 291 ? 31.877  41.753  -81.630  1.00 45.76  ? 592  TRP   C CD1 1 
ATOM   9169  C  CD2 . TRP   C  1 291 ? 30.892  42.254  -83.572  1.00 51.54  ? 592  TRP   C CD2 1 
ATOM   9170  N  NE1 . TRP   C  1 291 ? 31.019  42.802  -81.405  1.00 49.26  ? 592  TRP   C NE1 1 
ATOM   9171  C  CE2 . TRP   C  1 291 ? 30.403  43.127  -82.584  1.00 46.34  ? 592  TRP   C CE2 1 
ATOM   9172  C  CE3 . TRP   C  1 291 ? 30.410  42.380  -84.872  1.00 58.14  ? 592  TRP   C CE3 1 
ATOM   9173  C  CZ2 . TRP   C  1 291 ? 29.464  44.110  -82.857  1.00 48.05  ? 592  TRP   C CZ2 1 
ATOM   9174  C  CZ3 . TRP   C  1 291 ? 29.475  43.371  -85.140  1.00 54.67  ? 592  TRP   C CZ3 1 
ATOM   9175  C  CH2 . TRP   C  1 291 ? 29.017  44.219  -84.141  1.00 53.31  ? 592  TRP   C CH2 1 
ATOM   9176  N  N   . TYR   C  1 292 ? 33.446  38.185  -81.443  1.00 37.86  ? 593  TYR   C N   1 
ATOM   9177  C  CA  . TYR   C  1 292 ? 33.757  37.528  -80.192  1.00 38.25  ? 593  TYR   C CA  1 
ATOM   9178  C  C   . TYR   C  1 292 ? 33.818  38.521  -79.036  1.00 41.37  ? 593  TYR   C C   1 
ATOM   9179  O  O   . TYR   C  1 292 ? 34.249  39.673  -79.185  1.00 37.56  ? 593  TYR   C O   1 
ATOM   9180  C  CB  . TYR   C  1 292 ? 35.106  36.830  -80.296  1.00 34.43  ? 593  TYR   C CB  1 
ATOM   9181  C  CG  . TYR   C  1 292 ? 35.076  35.406  -80.770  1.00 38.76  ? 593  TYR   C CG  1 
ATOM   9182  C  CD1 . TYR   C  1 292 ? 35.937  34.961  -81.782  1.00 39.94  ? 593  TYR   C CD1 1 
ATOM   9183  C  CD2 . TYR   C  1 292 ? 34.229  34.492  -80.185  1.00 35.66  ? 593  TYR   C CD2 1 
ATOM   9184  C  CE1 . TYR   C  1 292 ? 35.945  33.626  -82.178  1.00 43.28  ? 593  TYR   C CE1 1 
ATOM   9185  C  CE2 . TYR   C  1 292 ? 34.217  33.173  -80.579  1.00 40.70  ? 593  TYR   C CE2 1 
ATOM   9186  C  CZ  . TYR   C  1 292 ? 35.072  32.742  -81.563  1.00 49.80  ? 593  TYR   C CZ  1 
ATOM   9187  O  OH  . TYR   C  1 292 ? 35.030  31.417  -81.912  1.00 64.47  ? 593  TYR   C OH  1 
ATOM   9188  N  N   . MET   C  1 293 ? 33.387  38.054  -77.872  1.00 40.66  ? 594  MET   C N   1 
ATOM   9189  C  CA  . MET   C  1 293 ? 33.820  38.619  -76.602  1.00 35.79  ? 594  MET   C CA  1 
ATOM   9190  C  C   . MET   C  1 293 ? 35.083  37.880  -76.190  1.00 36.49  ? 594  MET   C C   1 
ATOM   9191  O  O   . MET   C  1 293 ? 35.115  36.646  -76.221  1.00 41.59  ? 594  MET   C O   1 
ATOM   9192  C  CB  . MET   C  1 293 ? 32.725  38.476  -75.553  1.00 31.10  ? 594  MET   C CB  1 
ATOM   9193  C  CG  . MET   C  1 293 ? 33.083  39.097  -74.211  1.00 47.45  ? 594  MET   C CG  1 
ATOM   9194  S  SD  . MET   C  1 293 ? 31.580  39.446  -73.332  1.00 43.36  ? 594  MET   C SD  1 
ATOM   9195  C  CE  . MET   C  1 293 ? 31.075  37.784  -72.894  1.00 43.80  ? 594  MET   C CE  1 
ATOM   9196  N  N   . GLY   C  1 294 ? 36.135  38.631  -75.860  1.00 34.50  ? 595  GLY   C N   1 
ATOM   9197  C  CA  . GLY   C  1 294 ? 37.431  38.034  -75.577  1.00 31.85  ? 595  GLY   C CA  1 
ATOM   9198  C  C   . GLY   C  1 294 ? 37.378  36.813  -74.685  1.00 44.24  ? 595  GLY   C C   1 
ATOM   9199  O  O   . GLY   C  1 294 ? 38.119  35.848  -74.907  1.00 55.18  ? 595  GLY   C O   1 
ATOM   9200  N  N   . THR   C  1 295 ? 36.477  36.824  -73.694  1.00 40.36  ? 596  THR   C N   1 
ATOM   9201  C  CA  . THR   C  1 295 ? 36.358  35.705  -72.756  1.00 43.45  ? 596  THR   C CA  1 
ATOM   9202  C  C   . THR   C  1 295 ? 35.985  34.389  -73.425  1.00 37.76  ? 596  THR   C C   1 
ATOM   9203  O  O   . THR   C  1 295 ? 36.322  33.329  -72.890  1.00 49.60  ? 596  THR   C O   1 
ATOM   9204  C  CB  . THR   C  1 295 ? 35.316  36.001  -71.678  1.00 43.38  ? 596  THR   C CB  1 
ATOM   9205  O  OG1 . THR   C  1 295 ? 34.052  36.269  -72.305  1.00 40.25  ? 596  THR   C OG1 1 
ATOM   9206  C  CG2 . THR   C  1 295 ? 35.743  37.195  -70.796  1.00 36.61  ? 596  THR   C CG2 1 
ATOM   9207  N  N   . GLU   C  1 296 ? 35.280  34.417  -74.563  1.00 44.86  ? 597  GLU   C N   1 
ATOM   9208  C  CA  . GLU   C  1 296 ? 34.838  33.166  -75.181  1.00 38.65  ? 597  GLU   C CA  1 
ATOM   9209  C  C   . GLU   C  1 296 ? 36.028  32.345  -75.639  1.00 45.05  ? 597  GLU   C C   1 
ATOM   9210  O  O   . GLU   C  1 296 ? 36.029  31.117  -75.503  1.00 50.09  ? 597  GLU   C O   1 
ATOM   9211  C  CB  . GLU   C  1 296 ? 33.903  33.437  -76.360  1.00 48.93  ? 597  GLU   C CB  1 
ATOM   9212  C  CG  . GLU   C  1 296 ? 32.783  34.394  -76.036  1.00 51.02  ? 597  GLU   C CG  1 
ATOM   9213  C  CD  . GLU   C  1 296 ? 31.870  34.669  -77.217  1.00 48.15  ? 597  GLU   C CD  1 
ATOM   9214  O  OE1 . GLU   C  1 296 ? 31.194  33.706  -77.666  1.00 36.99  ? 597  GLU   C OE1 1 
ATOM   9215  O  OE2 . GLU   C  1 296 ? 31.825  35.853  -77.661  1.00 35.73  ? 597  GLU   C OE2 1 
ATOM   9216  N  N   . ILE   C  1 297 ? 37.049  33.018  -76.169  1.00 45.78  ? 598  ILE   C N   1 
ATOM   9217  C  CA  . ILE   C  1 297 ? 38.279  32.352  -76.579  1.00 42.85  ? 598  ILE   C CA  1 
ATOM   9218  C  C   . ILE   C  1 297 ? 39.163  32.059  -75.376  1.00 53.04  ? 598  ILE   C C   1 
ATOM   9219  O  O   . ILE   C  1 297 ? 39.566  30.908  -75.161  1.00 59.93  ? 598  ILE   C O   1 
ATOM   9220  C  CB  . ILE   C  1 297 ? 39.042  33.230  -77.578  1.00 40.41  ? 598  ILE   C CB  1 
ATOM   9221  C  CG1 . ILE   C  1 297 ? 38.160  33.544  -78.777  1.00 43.23  ? 598  ILE   C CG1 1 
ATOM   9222  C  CG2 . ILE   C  1 297 ? 40.332  32.555  -77.967  1.00 41.79  ? 598  ILE   C CG2 1 
ATOM   9223  C  CD1 . ILE   C  1 297 ? 38.552  34.801  -79.466  1.00 40.10  ? 598  ILE   C CD1 1 
ATOM   9224  N  N   . GLY   C  1 298 ? 39.517  33.118  -74.620  1.00 57.43  ? 599  GLY   C N   1 
ATOM   9225  C  CA  . GLY   C  1 298 ? 40.531  33.010  -73.574  1.00 60.31  ? 599  GLY   C CA  1 
ATOM   9226  C  C   . GLY   C  1 298 ? 40.055  32.318  -72.307  1.00 55.38  ? 599  GLY   C C   1 
ATOM   9227  O  O   . GLY   C  1 298 ? 40.792  31.532  -71.700  1.00 48.67  ? 599  GLY   C O   1 
ATOM   9228  N  N   . VAL   C  1 299 ? 38.825  32.578  -71.895  1.00 56.35  ? 600  VAL   C N   1 
ATOM   9229  C  CA  . VAL   C  1 299 ? 38.346  31.922  -70.689  1.00 59.02  ? 600  VAL   C CA  1 
ATOM   9230  C  C   . VAL   C  1 299 ? 37.854  30.515  -71.003  1.00 65.36  ? 600  VAL   C C   1 
ATOM   9231  O  O   . VAL   C  1 299 ? 38.293  29.539  -70.377  1.00 63.46  ? 600  VAL   C O   1 
ATOM   9232  C  CB  . VAL   C  1 299 ? 37.262  32.768  -70.003  1.00 59.63  ? 600  VAL   C CB  1 
ATOM   9233  C  CG1 . VAL   C  1 299 ? 36.792  32.074  -68.750  1.00 58.65  ? 600  VAL   C CG1 1 
ATOM   9234  C  CG2 . VAL   C  1 299 ? 37.797  34.161  -69.677  1.00 59.27  ? 600  VAL   C CG2 1 
ATOM   9235  N  N   . ARG   C  1 300 ? 36.952  30.387  -71.990  1.00 62.91  ? 601  ARG   C N   1 
ATOM   9236  C  CA  . ARG   C  1 300 ? 36.272  29.118  -72.262  1.00 53.96  ? 601  ARG   C CA  1 
ATOM   9237  C  C   . ARG   C  1 300 ? 37.035  28.232  -73.244  1.00 61.12  ? 601  ARG   C C   1 
ATOM   9238  O  O   . ARG   C  1 300 ? 37.291  27.059  -72.946  1.00 65.26  ? 601  ARG   C O   1 
ATOM   9239  C  CB  . ARG   C  1 300 ? 34.854  29.357  -72.799  1.00 39.88  ? 601  ARG   C CB  1 
ATOM   9240  C  CG  . ARG   C  1 300 ? 33.936  30.184  -71.921  1.00 42.46  ? 601  ARG   C CG  1 
ATOM   9241  C  CD  . ARG   C  1 300 ? 33.758  29.562  -70.537  1.00 54.59  ? 601  ARG   C CD  1 
ATOM   9242  N  NE  . ARG   C  1 300 ? 33.250  28.192  -70.561  1.00 53.40  ? 601  ARG   C NE  1 
ATOM   9243  C  CZ  . ARG   C  1 300 ? 31.982  27.881  -70.800  1.00 47.97  ? 601  ARG   C CZ  1 
ATOM   9244  N  NH1 . ARG   C  1 300 ? 31.096  28.844  -71.051  1.00 46.32  ? 601  ARG   C NH1 1 
ATOM   9245  N  NH2 . ARG   C  1 300 ? 31.599  26.611  -70.787  1.00 48.13  ? 601  ARG   C NH2 1 
ATOM   9246  N  N   . ASP   C  1 301 ? 37.390  28.771  -74.418  1.00 63.21  ? 602  ASP   C N   1 
ATOM   9247  C  CA  . ASP   C  1 301 ? 38.037  27.965  -75.454  1.00 61.41  ? 602  ASP   C CA  1 
ATOM   9248  C  C   . ASP   C  1 301 ? 39.410  27.457  -75.001  1.00 63.80  ? 602  ASP   C C   1 
ATOM   9249  O  O   . ASP   C  1 301 ? 39.732  26.272  -75.149  1.00 64.59  ? 602  ASP   C O   1 
ATOM   9250  C  CB  . ASP   C  1 301 ? 38.147  28.779  -76.747  1.00 60.86  ? 602  ASP   C CB  1 
ATOM   9251  C  CG  . ASP   C  1 301 ? 36.805  28.932  -77.465  1.00 62.33  ? 602  ASP   C CG  1 
ATOM   9252  O  OD1 . ASP   C  1 301 ? 36.069  27.923  -77.592  1.00 49.08  ? 602  ASP   C OD1 1 
ATOM   9253  O  OD2 . ASP   C  1 301 ? 36.485  30.066  -77.899  1.00 63.82  ? 602  ASP   C OD2 1 
ATOM   9254  N  N   . TYR   C  1 302 ? 40.228  28.333  -74.425  1.00 60.37  ? 603  TYR   C N   1 
ATOM   9255  C  CA  . TYR   C  1 302 ? 41.565  27.919  -74.019  1.00 58.73  ? 603  TYR   C CA  1 
ATOM   9256  C  C   . TYR   C  1 302 ? 41.613  27.248  -72.646  1.00 60.66  ? 603  TYR   C C   1 
ATOM   9257  O  O   . TYR   C  1 302 ? 42.507  26.427  -72.404  1.00 59.86  ? 603  TYR   C O   1 
ATOM   9258  C  CB  . TYR   C  1 302 ? 42.489  29.127  -74.037  1.00 62.29  ? 603  TYR   C CB  1 
ATOM   9259  C  CG  . TYR   C  1 302 ? 42.912  29.524  -75.427  1.00 66.98  ? 603  TYR   C CG  1 
ATOM   9260  C  CD1 . TYR   C  1 302 ? 43.096  30.858  -75.761  1.00 66.15  ? 603  TYR   C CD1 1 
ATOM   9261  C  CD2 . TYR   C  1 302 ? 43.162  28.567  -76.395  1.00 63.11  ? 603  TYR   C CD2 1 
ATOM   9262  C  CE1 . TYR   C  1 302 ? 43.503  31.231  -77.020  1.00 61.85  ? 603  TYR   C CE1 1 
ATOM   9263  C  CE2 . TYR   C  1 302 ? 43.559  28.931  -77.651  1.00 69.03  ? 603  TYR   C CE2 1 
ATOM   9264  C  CZ  . TYR   C  1 302 ? 43.727  30.267  -77.961  1.00 69.22  ? 603  TYR   C CZ  1 
ATOM   9265  O  OH  . TYR   C  1 302 ? 44.126  30.648  -79.223  1.00 85.11  ? 603  TYR   C OH  1 
ATOM   9266  N  N   . CYS   C  1 303 ? 40.676  27.558  -71.741  1.00 58.71  ? 604  CYS   C N   1 
ATOM   9267  C  CA  . CYS   C  1 303 ? 40.886  27.275  -70.328  1.00 64.41  ? 604  CYS   C CA  1 
ATOM   9268  C  C   . CYS   C  1 303 ? 39.878  26.348  -69.661  1.00 64.83  ? 604  CYS   C C   1 
ATOM   9269  O  O   . CYS   C  1 303 ? 40.156  25.892  -68.549  1.00 67.86  ? 604  CYS   C O   1 
ATOM   9270  C  CB  . CYS   C  1 303 ? 40.945  28.582  -69.534  1.00 68.18  ? 604  CYS   C CB  1 
ATOM   9271  S  SG  . CYS   C  1 303 ? 42.462  29.479  -69.813  1.00 75.97  ? 604  CYS   C SG  1 
ATOM   9272  N  N   . ASP   C  1 304 ? 38.737  26.041  -70.278  1.00 67.48  ? 605  ASP   C N   1 
ATOM   9273  C  CA  . ASP   C  1 304 ? 37.932  24.929  -69.779  1.00 71.67  ? 605  ASP   C CA  1 
ATOM   9274  C  C   . ASP   C  1 304 ? 38.774  23.651  -69.728  1.00 84.34  ? 605  ASP   C C   1 
ATOM   9275  O  O   . ASP   C  1 304 ? 39.818  23.539  -70.376  1.00 95.38  ? 605  ASP   C O   1 
ATOM   9276  C  CB  . ASP   C  1 304 ? 36.704  24.692  -70.659  1.00 65.67  ? 605  ASP   C CB  1 
ATOM   9277  C  CG  . ASP   C  1 304 ? 35.526  25.561  -70.277  1.00 63.64  ? 605  ASP   C CG  1 
ATOM   9278  O  OD1 . ASP   C  1 304 ? 35.713  26.562  -69.546  1.00 63.26  ? 605  ASP   C OD1 1 
ATOM   9279  O  OD2 . ASP   C  1 304 ? 34.403  25.235  -70.722  1.00 66.68  ? 605  ASP   C OD2 1 
ATOM   9280  N  N   . ASN   C  1 305 ? 38.313  22.674  -68.939  1.00 78.48  ? 606  ASN   C N   1 
ATOM   9281  C  CA  . ASN   C  1 305 ? 39.059  21.422  -68.811  1.00 68.92  ? 606  ASN   C CA  1 
ATOM   9282  C  C   . ASN   C  1 305 ? 38.880  20.526  -70.036  1.00 75.19  ? 606  ASN   C C   1 
ATOM   9283  O  O   . ASN   C  1 305 ? 39.852  19.923  -70.514  1.00 76.41  ? 606  ASN   C O   1 
ATOM   9284  C  CB  . ASN   C  1 305 ? 38.634  20.678  -67.544  1.00 65.42  ? 606  ASN   C CB  1 
ATOM   9285  C  CG  . ASN   C  1 305 ? 39.455  21.064  -66.343  1.00 66.67  ? 606  ASN   C CG  1 
ATOM   9286  O  OD1 . ASN   C  1 305 ? 39.041  21.884  -65.525  1.00 58.78  ? 606  ASN   C OD1 1 
ATOM   9287  N  ND2 . ASN   C  1 305 ? 40.639  20.481  -66.233  1.00 72.72  ? 606  ASN   C ND2 1 
ATOM   9288  N  N   . SER   C  1 306 ? 37.648  20.422  -70.552  1.00 73.39  ? 607  SER   C N   1 
ATOM   9289  C  CA  . SER   C  1 306 ? 37.340  19.619  -71.730  1.00 72.49  ? 607  SER   C CA  1 
ATOM   9290  C  C   . SER   C  1 306 ? 37.565  20.385  -73.028  1.00 74.83  ? 607  SER   C C   1 
ATOM   9291  O  O   . SER   C  1 306 ? 36.976  20.043  -74.063  1.00 74.08  ? 607  SER   C O   1 
ATOM   9292  C  CB  . SER   C  1 306 ? 35.898  19.117  -71.664  1.00 72.81  ? 607  SER   C CB  1 
ATOM   9293  O  OG  . SER   C  1 306 ? 35.434  19.079  -70.330  1.00 79.50  ? 607  SER   C OG  1 
ATOM   9294  N  N   . ARG   C  1 307 ? 38.387  21.427  -72.982  1.00 73.06  ? 608  ARG   C N   1 
ATOM   9295  C  CA  . ARG   C  1 307 ? 38.743  22.198  -74.159  1.00 65.98  ? 608  ARG   C CA  1 
ATOM   9296  C  C   . ARG   C  1 307 ? 40.266  22.286  -74.265  1.00 69.55  ? 608  ARG   C C   1 
ATOM   9297  O  O   . ARG   C  1 307 ? 40.954  21.281  -74.044  1.00 75.40  ? 608  ARG   C O   1 
ATOM   9298  C  CB  . ARG   C  1 307 ? 38.070  23.569  -74.102  1.00 53.94  ? 608  ARG   C CB  1 
ATOM   9299  C  CG  . ARG   C  1 307 ? 36.540  23.488  -74.140  1.00 52.04  ? 608  ARG   C CG  1 
ATOM   9300  C  CD  . ARG   C  1 307 ? 35.977  22.833  -75.419  1.00 53.91  ? 608  ARG   C CD  1 
ATOM   9301  N  NE  . ARG   C  1 307 ? 36.386  23.537  -76.637  1.00 58.43  ? 608  ARG   C NE  1 
ATOM   9302  C  CZ  . ARG   C  1 307 ? 35.972  24.760  -76.968  1.00 62.40  ? 608  ARG   C CZ  1 
ATOM   9303  N  NH1 . ARG   C  1 307 ? 35.132  25.423  -76.176  1.00 65.52  ? 608  ARG   C NH1 1 
ATOM   9304  N  NH2 . ARG   C  1 307 ? 36.399  25.331  -78.086  1.00 53.62  ? 608  ARG   C NH2 1 
ATOM   9305  N  N   . TYR   C  1 308 ? 40.817  23.461  -74.588  1.00 59.98  ? 609  TYR   C N   1 
ATOM   9306  C  CA  . TYR   C  1 308 ? 42.241  23.500  -74.902  1.00 63.66  ? 609  TYR   C CA  1 
ATOM   9307  C  C   . TYR   C  1 308 ? 43.124  23.386  -73.669  1.00 64.63  ? 609  TYR   C C   1 
ATOM   9308  O  O   . TYR   C  1 308 ? 44.261  22.916  -73.791  1.00 80.49  ? 609  TYR   C O   1 
ATOM   9309  C  CB  . TYR   C  1 308 ? 42.578  24.753  -75.707  1.00 70.47  ? 609  TYR   C CB  1 
ATOM   9310  C  CG  . TYR   C  1 308 ? 42.557  24.428  -77.178  1.00 78.12  ? 609  TYR   C CG  1 
ATOM   9311  C  CD1 . TYR   C  1 308 ? 41.371  24.488  -77.913  1.00 69.86  ? 609  TYR   C CD1 1 
ATOM   9312  C  CD2 . TYR   C  1 308 ? 43.707  23.994  -77.822  1.00 83.19  ? 609  TYR   C CD2 1 
ATOM   9313  C  CE1 . TYR   C  1 308 ? 41.346  24.168  -79.251  1.00 68.29  ? 609  TYR   C CE1 1 
ATOM   9314  C  CE2 . TYR   C  1 308 ? 43.692  23.670  -79.159  1.00 79.94  ? 609  TYR   C CE2 1 
ATOM   9315  C  CZ  . TYR   C  1 308 ? 42.513  23.756  -79.870  1.00 74.74  ? 609  TYR   C CZ  1 
ATOM   9316  O  OH  . TYR   C  1 308 ? 42.516  23.428  -81.208  1.00 71.04  ? 609  TYR   C OH  1 
ATOM   9317  N  N   . ASN   C  1 309 ? 42.630  23.798  -72.492  1.00 58.72  ? 610  ASN   C N   1 
ATOM   9318  C  CA  . ASN   C  1 309 ? 43.214  23.415  -71.190  1.00 65.05  ? 610  ASN   C CA  1 
ATOM   9319  C  C   . ASN   C  1 309 ? 44.686  23.820  -71.063  1.00 62.03  ? 610  ASN   C C   1 
ATOM   9320  O  O   . ASN   C  1 309 ? 45.518  23.064  -70.549  1.00 57.24  ? 610  ASN   C O   1 
ATOM   9321  C  CB  . ASN   C  1 309 ? 43.037  21.908  -70.943  1.00 69.46  ? 610  ASN   C CB  1 
ATOM   9322  C  CG  . ASN   C  1 309 ? 43.264  21.500  -69.479  1.00 75.38  ? 610  ASN   C CG  1 
ATOM   9323  O  OD1 . ASN   C  1 309 ? 43.207  22.328  -68.562  1.00 76.39  ? 610  ASN   C OD1 1 
ATOM   9324  N  ND2 . ASN   C  1 309 ? 43.511  20.208  -69.262  1.00 71.55  ? 610  ASN   C ND2 1 
ATOM   9325  N  N   . ILE   C  1 310 ? 45.015  25.032  -71.508  1.00 67.97  ? 611  ILE   C N   1 
ATOM   9326  C  CA  . ILE   C  1 310 ? 46.406  25.473  -71.572  1.00 74.40  ? 611  ILE   C CA  1 
ATOM   9327  C  C   . ILE   C  1 310 ? 46.806  26.290  -70.340  1.00 70.66  ? 611  ILE   C C   1 
ATOM   9328  O  O   . ILE   C  1 310 ? 47.782  27.040  -70.396  1.00 67.20  ? 611  ILE   C O   1 
ATOM   9329  C  CB  . ILE   C  1 310 ? 46.695  26.251  -72.862  1.00 74.80  ? 611  ILE   C CB  1 
ATOM   9330  C  CG1 . ILE   C  1 310 ? 45.958  27.583  -72.837  1.00 70.84  ? 611  ILE   C CG1 1 
ATOM   9331  C  CG2 . ILE   C  1 310 ? 46.292  25.441  -74.086  1.00 85.89  ? 611  ILE   C CG2 1 
ATOM   9332  C  CD1 . ILE   C  1 310 ? 46.630  28.601  -73.668  1.00 74.63  ? 611  ILE   C CD1 1 
ATOM   9333  N  N   . LEU   C  1 311 ? 46.064  26.163  -69.230  1.00 67.48  ? 612  LEU   C N   1 
ATOM   9334  C  CA  . LEU   C  1 311 ? 46.410  26.899  -68.011  1.00 61.70  ? 612  LEU   C CA  1 
ATOM   9335  C  C   . LEU   C  1 311 ? 47.750  26.440  -67.438  1.00 64.30  ? 612  LEU   C C   1 
ATOM   9336  O  O   . LEU   C  1 311 ? 48.601  27.274  -67.108  1.00 71.45  ? 612  LEU   C O   1 
ATOM   9337  C  CB  . LEU   C  1 311 ? 45.308  26.764  -66.962  1.00 45.71  ? 612  LEU   C CB  1 
ATOM   9338  C  CG  . LEU   C  1 311 ? 44.140  27.745  -67.086  1.00 46.21  ? 612  LEU   C CG  1 
ATOM   9339  C  CD1 . LEU   C  1 311 ? 43.028  27.385  -66.142  1.00 41.43  ? 612  LEU   C CD1 1 
ATOM   9340  C  CD2 . LEU   C  1 311 ? 44.591  29.174  -66.848  1.00 42.28  ? 612  LEU   C CD2 1 
ATOM   9341  N  N   . GLU   C  1 312 ? 47.957  25.119  -67.314  1.00 63.94  ? 613  GLU   C N   1 
ATOM   9342  C  CA  . GLU   C  1 312 ? 49.222  24.597  -66.785  1.00 72.36  ? 613  GLU   C CA  1 
ATOM   9343  C  C   . GLU   C  1 312 ? 50.416  25.161  -67.541  1.00 76.86  ? 613  GLU   C C   1 
ATOM   9344  O  O   . GLU   C  1 312 ? 51.385  25.636  -66.938  1.00 73.32  ? 613  GLU   C O   1 
ATOM   9345  C  CB  . GLU   C  1 312 ? 49.263  23.067  -66.862  1.00 76.63  ? 613  GLU   C CB  1 
ATOM   9346  C  CG  . GLU   C  1 312 ? 48.104  22.341  -66.228  1.00 84.30  ? 613  GLU   C CG  1 
ATOM   9347  C  CD  . GLU   C  1 312 ? 46.966  22.078  -67.214  1.00 86.52  ? 613  GLU   C CD  1 
ATOM   9348  O  OE1 . GLU   C  1 312 ? 46.535  23.021  -67.924  1.00 72.68  ? 613  GLU   C OE1 1 
ATOM   9349  O  OE2 . GLU   C  1 312 ? 46.502  20.917  -67.272  1.00 93.65  ? 613  GLU   C OE2 1 
ATOM   9350  N  N   . GLU   C  1 313 ? 50.364  25.103  -68.873  1.00 85.05  ? 614  GLU   C N   1 
ATOM   9351  C  CA  . GLU   C  1 313 ? 51.515  25.491  -69.680  1.00 87.61  ? 614  GLU   C CA  1 
ATOM   9352  C  C   . GLU   C  1 313 ? 51.786  26.984  -69.582  1.00 81.56  ? 614  GLU   C C   1 
ATOM   9353  O  O   . GLU   C  1 313 ? 52.949  27.407  -69.549  1.00 81.39  ? 614  GLU   C O   1 
ATOM   9354  C  CB  . GLU   C  1 313 ? 51.292  25.081  -71.129  1.00 91.64  ? 614  GLU   C CB  1 
ATOM   9355  C  CG  . GLU   C  1 313 ? 52.303  25.663  -72.087  1.00 93.54  ? 614  GLU   C CG  1 
ATOM   9356  C  CD  . GLU   C  1 313 ? 52.660  24.700  -73.188  1.00 97.33  ? 614  GLU   C CD  1 
ATOM   9357  O  OE1 . GLU   C  1 313 ? 53.850  24.313  -73.278  1.00 94.12  ? 614  GLU   C OE1 1 
ATOM   9358  O  OE2 . GLU   C  1 313 ? 51.743  24.315  -73.947  1.00 99.69  ? 614  GLU   C OE2 1 
ATOM   9359  N  N   . VAL   C  1 314 ? 50.727  27.797  -69.542  1.00 72.37  ? 615  VAL   C N   1 
ATOM   9360  C  CA  . VAL   C  1 314 ? 50.921  29.228  -69.346  1.00 64.38  ? 615  VAL   C CA  1 
ATOM   9361  C  C   . VAL   C  1 314 ? 51.374  29.526  -67.925  1.00 66.06  ? 615  VAL   C C   1 
ATOM   9362  O  O   . VAL   C  1 314 ? 52.166  30.448  -67.702  1.00 75.26  ? 615  VAL   C O   1 
ATOM   9363  C  CB  . VAL   C  1 314 ? 49.641  29.991  -69.703  1.00 59.84  ? 615  VAL   C CB  1 
ATOM   9364  C  CG1 . VAL   C  1 314 ? 49.759  31.442  -69.278  1.00 55.66  ? 615  VAL   C CG1 1 
ATOM   9365  C  CG2 . VAL   C  1 314 ? 49.389  29.891  -71.195  1.00 59.45  ? 615  VAL   C CG2 1 
ATOM   9366  N  N   . ALA   C  1 315 ? 50.907  28.756  -66.943  1.00 68.10  ? 616  ALA   C N   1 
ATOM   9367  C  CA  . ALA   C  1 315 ? 51.396  28.944  -65.578  1.00 66.60  ? 616  ALA   C CA  1 
ATOM   9368  C  C   . ALA   C  1 315 ? 52.879  28.610  -65.485  1.00 61.15  ? 616  ALA   C C   1 
ATOM   9369  O  O   . ALA   C  1 315 ? 53.662  29.394  -64.943  1.00 63.57  ? 616  ALA   C O   1 
ATOM   9370  C  CB  . ALA   C  1 315 ? 50.584  28.101  -64.594  1.00 64.09  ? 616  ALA   C CB  1 
ATOM   9371  N  N   . LYS   C  1 316 ? 53.283  27.457  -66.034  1.00 65.00  ? 617  LYS   C N   1 
ATOM   9372  C  CA  . LYS   C  1 316 ? 54.690  27.063  -66.056  1.00 70.98  ? 617  LYS   C CA  1 
ATOM   9373  C  C   . LYS   C  1 316 ? 55.565  28.192  -66.581  1.00 72.84  ? 617  LYS   C C   1 
ATOM   9374  O  O   . LYS   C  1 316 ? 56.527  28.610  -65.928  1.00 68.59  ? 617  LYS   C O   1 
ATOM   9375  C  CB  . LYS   C  1 316 ? 54.888  25.817  -66.927  1.00 76.38  ? 617  LYS   C CB  1 
ATOM   9376  C  CG  . LYS   C  1 316 ? 54.356  24.499  -66.387  1.00 81.60  ? 617  LYS   C CG  1 
ATOM   9377  C  CD  . LYS   C  1 316 ? 54.520  23.407  -67.451  1.00 91.97  ? 617  LYS   C CD  1 
ATOM   9378  C  CE  . LYS   C  1 316 ? 55.059  22.093  -66.888  1.00 94.29  ? 617  LYS   C CE  1 
ATOM   9379  N  NZ  . LYS   C  1 316 ? 53.992  21.298  -66.217  1.00 93.43  ? 617  LYS   C NZ  1 
ATOM   9380  N  N   . LYS   C  1 317 ? 55.232  28.699  -67.771  1.00 78.06  ? 618  LYS   C N   1 
ATOM   9381  C  CA  . LYS   C  1 317 ? 55.999  29.783  -68.370  1.00 80.39  ? 618  LYS   C CA  1 
ATOM   9382  C  C   . LYS   C  1 317 ? 55.984  31.047  -67.514  1.00 83.70  ? 618  LYS   C C   1 
ATOM   9383  O  O   . LYS   C  1 317 ? 56.910  31.862  -67.612  1.00 86.83  ? 618  LYS   C O   1 
ATOM   9384  C  CB  . LYS   C  1 317 ? 55.467  30.078  -69.774  1.00 74.22  ? 618  LYS   C CB  1 
ATOM   9385  C  CG  . LYS   C  1 317 ? 56.087  29.241  -70.893  1.00 79.86  ? 618  LYS   C CG  1 
ATOM   9386  C  CD  . LYS   C  1 317 ? 57.497  29.724  -71.212  1.00 88.70  ? 618  LYS   C CD  1 
ATOM   9387  C  CE  . LYS   C  1 317 ? 58.273  28.698  -72.016  1.00 93.98  ? 618  LYS   C CE  1 
ATOM   9388  N  NZ  . LYS   C  1 317 ? 58.407  27.413  -71.271  1.00 97.04  ? 618  LYS   C NZ  1 
ATOM   9389  N  N   . MET   C  1 318 ? 54.966  31.228  -66.670  1.00 77.33  ? 619  MET   C N   1 
ATOM   9390  C  CA  . MET   C  1 318 ? 54.942  32.367  -65.761  1.00 71.42  ? 619  MET   C CA  1 
ATOM   9391  C  C   . MET   C  1 318 ? 55.716  32.108  -64.478  1.00 79.24  ? 619  MET   C C   1 
ATOM   9392  O  O   . MET   C  1 318 ? 55.935  33.053  -63.714  1.00 82.40  ? 619  MET   C O   1 
ATOM   9393  C  CB  . MET   C  1 318 ? 53.493  32.765  -65.433  1.00 64.65  ? 619  MET   C CB  1 
ATOM   9394  C  CG  . MET   C  1 318 ? 52.787  33.488  -66.589  1.00 53.52  ? 619  MET   C CG  1 
ATOM   9395  S  SD  . MET   C  1 318 ? 51.076  33.992  -66.303  1.00 61.39  ? 619  MET   C SD  1 
ATOM   9396  C  CE  . MET   C  1 318 ? 51.215  34.861  -64.732  1.00 66.63  ? 619  MET   C CE  1 
ATOM   9397  N  N   . ASN   C  1 319 ? 56.155  30.866  -64.247  1.00 83.41  ? 620  ASN   C N   1 
ATOM   9398  C  CA  . ASN   C  1 319 ? 56.871  30.465  -63.033  1.00 83.58  ? 620  ASN   C CA  1 
ATOM   9399  C  C   . ASN   C  1 319 ? 56.016  30.704  -61.793  1.00 78.31  ? 620  ASN   C C   1 
ATOM   9400  O  O   . ASN   C  1 319 ? 56.398  31.416  -60.864  1.00 84.10  ? 620  ASN   C O   1 
ATOM   9401  C  CB  . ASN   C  1 319 ? 58.213  31.188  -62.915  1.00 91.19  ? 620  ASN   C CB  1 
ATOM   9402  C  CG  . ASN   C  1 319 ? 59.289  30.540  -63.746  1.00 99.33  ? 620  ASN   C CG  1 
ATOM   9403  O  OD1 . ASN   C  1 319 ? 59.547  30.954  -64.879  1.00 97.42  ? 620  ASN   C OD1 1 
ATOM   9404  N  ND2 . ASN   C  1 319 ? 59.931  29.512  -63.188  1.00 104.38 ? 620  ASN   C ND2 1 
ATOM   9405  N  N   . LEU   C  1 320 ? 54.841  30.093  -61.795  1.00 71.52  ? 621  LEU   C N   1 
ATOM   9406  C  CA  . LEU   C  1 320 ? 53.867  30.329  -60.745  1.00 61.31  ? 621  LEU   C CA  1 
ATOM   9407  C  C   . LEU   C  1 320 ? 53.904  29.201  -59.727  1.00 79.17  ? 621  LEU   C C   1 
ATOM   9408  O  O   . LEU   C  1 320 ? 54.239  28.054  -60.042  1.00 74.94  ? 621  LEU   C O   1 
ATOM   9409  C  CB  . LEU   C  1 320 ? 52.455  30.476  -61.326  1.00 56.04  ? 621  LEU   C CB  1 
ATOM   9410  C  CG  . LEU   C  1 320 ? 52.142  31.780  -62.074  1.00 63.54  ? 621  LEU   C CG  1 
ATOM   9411  C  CD1 . LEU   C  1 320 ? 50.719  31.783  -62.627  1.00 55.48  ? 621  LEU   C CD1 1 
ATOM   9412  C  CD2 . LEU   C  1 320 ? 52.352  32.979  -61.167  1.00 65.50  ? 621  LEU   C CD2 1 
ATOM   9413  N  N   . ASP   C  1 321 ? 53.587  29.559  -58.484  1.00 89.59  ? 622  ASP   C N   1 
ATOM   9414  C  CA  . ASP   C  1 321 ? 53.410  28.611  -57.395  1.00 98.98  ? 622  ASP   C CA  1 
ATOM   9415  C  C   . ASP   C  1 321 ? 52.272  27.656  -57.736  1.00 94.06  ? 622  ASP   C C   1 
ATOM   9416  O  O   . ASP   C  1 321 ? 51.124  27.905  -57.365  1.00 97.77  ? 622  ASP   C O   1 
ATOM   9417  C  CB  . ASP   C  1 321 ? 53.119  29.381  -56.096  1.00 109.51 ? 622  ASP   C CB  1 
ATOM   9418  C  CG  . ASP   C  1 321 ? 53.062  28.492  -54.864  1.00 118.21 ? 622  ASP   C CG  1 
ATOM   9419  O  OD1 . ASP   C  1 321 ? 52.745  29.023  -53.769  1.00 113.82 ? 622  ASP   C OD1 1 
ATOM   9420  O  OD2 . ASP   C  1 321 ? 53.355  27.280  -54.981  1.00 125.98 ? 622  ASP   C OD2 1 
ATOM   9421  N  N   . MET   C  1 322 ? 52.559  26.568  -58.447  1.00 82.22  ? 623  MET   C N   1 
ATOM   9422  C  CA  . MET   C  1 322 ? 51.516  25.610  -58.795  1.00 81.23  ? 623  MET   C CA  1 
ATOM   9423  C  C   . MET   C  1 322 ? 51.345  24.514  -57.751  1.00 88.16  ? 623  MET   C C   1 
ATOM   9424  O  O   . MET   C  1 322 ? 50.659  23.525  -58.025  1.00 89.69  ? 623  MET   C O   1 
ATOM   9425  C  CB  . MET   C  1 322 ? 51.792  24.992  -60.163  1.00 70.12  ? 623  MET   C CB  1 
ATOM   9426  C  CG  . MET   C  1 322 ? 51.727  26.007  -61.292  1.00 77.83  ? 623  MET   C CG  1 
ATOM   9427  S  SD  . MET   C  1 322 ? 52.037  25.281  -62.921  1.00 88.36  ? 623  MET   C SD  1 
ATOM   9428  C  CE  . MET   C  1 322 ? 50.828  23.956  -62.921  1.00 89.60  ? 623  MET   C CE  1 
ATOM   9429  N  N   . ARG   C  1 323 ? 51.945  24.679  -56.566  1.00 91.54  ? 624  ARG   C N   1 
ATOM   9430  C  CA  . ARG   C  1 323 ? 51.815  23.754  -55.441  1.00 87.95  ? 624  ARG   C CA  1 
ATOM   9431  C  C   . ARG   C  1 323 ? 50.371  23.466  -55.051  1.00 76.66  ? 624  ARG   C C   1 
ATOM   9432  O  O   . ARG   C  1 323 ? 49.920  22.321  -55.146  1.00 65.21  ? 624  ARG   C O   1 
ATOM   9433  C  CB  . ARG   C  1 323 ? 52.544  24.310  -54.221  1.00 95.95  ? 624  ARG   C CB  1 
ATOM   9434  C  CG  . ARG   C  1 323 ? 54.046  24.204  -54.266  1.00 104.43 ? 624  ARG   C CG  1 
ATOM   9435  C  CD  . ARG   C  1 323 ? 54.538  23.049  -53.400  1.00 109.52 ? 624  ARG   C CD  1 
ATOM   9436  N  NE  . ARG   C  1 323 ? 53.666  22.753  -52.260  1.00 108.38 ? 624  ARG   C NE  1 
ATOM   9437  C  CZ  . ARG   C  1 323 ? 53.726  23.362  -51.076  1.00 106.35 ? 624  ARG   C CZ  1 
ATOM   9438  N  NH1 . ARG   C  1 323 ? 54.610  24.327  -50.864  1.00 104.76 ? 624  ARG   C NH1 1 
ATOM   9439  N  NH2 . ARG   C  1 323 ? 52.893  23.008  -50.104  1.00 106.15 ? 624  ARG   C NH2 1 
ATOM   9440  N  N   . LYS   C  1 324 ? 49.656  24.490  -54.578  1.00 78.15  ? 625  LYS   C N   1 
ATOM   9441  C  CA  . LYS   C  1 324 ? 48.264  24.391  -54.142  1.00 87.13  ? 625  LYS   C CA  1 
ATOM   9442  C  C   . LYS   C  1 324 ? 47.413  25.433  -54.875  1.00 83.76  ? 625  LYS   C C   1 
ATOM   9443  O  O   . LYS   C  1 324 ? 47.931  26.313  -55.569  1.00 93.22  ? 625  LYS   C O   1 
ATOM   9444  C  CB  . LYS   C  1 324 ? 48.158  24.566  -52.614  1.00 92.32  ? 625  LYS   C CB  1 
ATOM   9445  C  CG  . LYS   C  1 324 ? 48.719  25.892  -52.110  1.00 97.54  ? 625  LYS   C CG  1 
ATOM   9446  C  CD  . LYS   C  1 324 ? 49.936  25.699  -51.198  1.00 103.02 ? 625  LYS   C CD  1 
ATOM   9447  C  CE  . LYS   C  1 324 ? 50.991  26.787  -51.423  1.00 101.51 ? 625  LYS   C CE  1 
ATOM   9448  N  NZ  . LYS   C  1 324 ? 50.415  28.164  -51.536  1.00 94.24  ? 625  LYS   C NZ  1 
ATOM   9449  N  N   . THR   C  1 325 ? 46.086  25.348  -54.731  1.00 66.58  ? 626  THR   C N   1 
ATOM   9450  C  CA  . THR   C  1 325 ? 45.242  26.318  -55.428  1.00 59.46  ? 626  THR   C CA  1 
ATOM   9451  C  C   . THR   C  1 325 ? 45.211  27.683  -54.756  1.00 57.46  ? 626  THR   C C   1 
ATOM   9452  O  O   . THR   C  1 325 ? 44.895  28.671  -55.427  1.00 55.49  ? 626  THR   C O   1 
ATOM   9453  C  CB  . THR   C  1 325 ? 43.796  25.817  -55.582  1.00 49.52  ? 626  THR   C CB  1 
ATOM   9454  O  OG1 . THR   C  1 325 ? 43.388  25.093  -54.419  1.00 59.85  ? 626  THR   C OG1 1 
ATOM   9455  C  CG2 . THR   C  1 325 ? 43.648  24.943  -56.840  1.00 61.69  ? 626  THR   C CG2 1 
ATOM   9456  N  N   . SER   C  1 326 ? 45.541  27.763  -53.463  1.00 54.91  ? 627  SER   C N   1 
ATOM   9457  C  CA  . SER   C  1 326 ? 45.471  29.024  -52.734  1.00 56.76  ? 627  SER   C CA  1 
ATOM   9458  C  C   . SER   C  1 326 ? 46.344  30.110  -53.351  1.00 61.36  ? 627  SER   C C   1 
ATOM   9459  O  O   . SER   C  1 326 ? 46.073  31.295  -53.140  1.00 58.07  ? 627  SER   C O   1 
ATOM   9460  C  CB  . SER   C  1 326 ? 45.869  28.814  -51.271  1.00 55.56  ? 627  SER   C CB  1 
ATOM   9461  O  OG  . SER   C  1 326 ? 45.829  27.438  -50.921  1.00 64.52  ? 627  SER   C OG  1 
ATOM   9462  N  N   . SER   C  1 327 ? 47.391  29.740  -54.094  1.00 62.31  ? 628  SER   C N   1 
ATOM   9463  C  CA  . SER   C  1 327 ? 48.209  30.724  -54.796  1.00 59.46  ? 628  SER   C CA  1 
ATOM   9464  C  C   . SER   C  1 327 ? 47.462  31.417  -55.916  1.00 61.64  ? 628  SER   C C   1 
ATOM   9465  O  O   . SER   C  1 327 ? 47.935  32.443  -56.412  1.00 64.67  ? 628  SER   C O   1 
ATOM   9466  C  CB  . SER   C  1 327 ? 49.443  30.065  -55.384  1.00 57.03  ? 628  SER   C CB  1 
ATOM   9467  O  OG  . SER   C  1 327 ? 49.044  29.164  -56.391  1.00 57.61  ? 628  SER   C OG  1 
ATOM   9468  N  N   . LEU   C  1 328 ? 46.328  30.872  -56.341  1.00 62.27  ? 629  LEU   C N   1 
ATOM   9469  C  CA  . LEU   C  1 328 ? 45.528  31.485  -57.392  1.00 60.71  ? 629  LEU   C CA  1 
ATOM   9470  C  C   . LEU   C  1 328 ? 46.303  31.522  -58.707  1.00 64.36  ? 629  LEU   C C   1 
ATOM   9471  O  O   . LEU   C  1 328 ? 46.211  32.483  -59.476  1.00 58.06  ? 629  LEU   C O   1 
ATOM   9472  C  CB  . LEU   C  1 328 ? 45.069  32.884  -56.980  1.00 55.78  ? 629  LEU   C CB  1 
ATOM   9473  C  CG  . LEU   C  1 328 ? 44.204  32.976  -55.730  1.00 52.66  ? 629  LEU   C CG  1 
ATOM   9474  C  CD1 . LEU   C  1 328 ? 43.360  34.230  -55.777  1.00 45.80  ? 629  LEU   C CD1 1 
ATOM   9475  C  CD2 . LEU   C  1 328 ? 43.304  31.755  -55.597  1.00 48.68  ? 629  LEU   C CD2 1 
ATOM   9476  N  N   . TRP   C  1 329 ? 47.079  30.458  -58.961  1.00 54.65  ? 630  TRP   C N   1 
ATOM   9477  C  CA  . TRP   C  1 329 ? 47.913  30.415  -60.155  1.00 54.50  ? 630  TRP   C CA  1 
ATOM   9478  C  C   . TRP   C  1 329 ? 47.062  30.294  -61.418  1.00 59.84  ? 630  TRP   C C   1 
ATOM   9479  O  O   . TRP   C  1 329 ? 47.340  30.954  -62.425  1.00 53.14  ? 630  TRP   C O   1 
ATOM   9480  C  CB  . TRP   C  1 329 ? 48.926  29.274  -60.052  1.00 60.29  ? 630  TRP   C CB  1 
ATOM   9481  C  CG  . TRP   C  1 329 ? 48.332  27.894  -60.001  1.00 63.91  ? 630  TRP   C CG  1 
ATOM   9482  C  CD1 . TRP   C  1 329 ? 48.036  27.168  -58.884  1.00 65.71  ? 630  TRP   C CD1 1 
ATOM   9483  C  CD2 . TRP   C  1 329 ? 47.985  27.065  -61.120  1.00 66.31  ? 630  TRP   C CD2 1 
ATOM   9484  N  NE1 . TRP   C  1 329 ? 47.514  25.943  -59.237  1.00 67.79  ? 630  TRP   C NE1 1 
ATOM   9485  C  CE2 . TRP   C  1 329 ? 47.476  25.856  -60.605  1.00 69.47  ? 630  TRP   C CE2 1 
ATOM   9486  C  CE3 . TRP   C  1 329 ? 48.048  27.230  -62.507  1.00 63.04  ? 630  TRP   C CE3 1 
ATOM   9487  C  CZ2 . TRP   C  1 329 ? 47.039  24.816  -61.430  1.00 64.70  ? 630  TRP   C CZ2 1 
ATOM   9488  C  CZ3 . TRP   C  1 329 ? 47.609  26.192  -63.325  1.00 57.67  ? 630  TRP   C CZ3 1 
ATOM   9489  C  CH2 . TRP   C  1 329 ? 47.112  25.006  -62.785  1.00 59.77  ? 630  TRP   C CH2 1 
ATOM   9490  N  N   . LYS   C  1 330 ? 46.007  29.474  -61.374  1.00 54.45  ? 631  LYS   C N   1 
ATOM   9491  C  CA  . LYS   C  1 330 ? 45.045  29.438  -62.463  1.00 46.82  ? 631  LYS   C CA  1 
ATOM   9492  C  C   . LYS   C  1 330 ? 44.467  30.818  -62.725  1.00 58.03  ? 631  LYS   C C   1 
ATOM   9493  O  O   . LYS   C  1 330 ? 44.334  31.247  -63.879  1.00 54.68  ? 631  LYS   C O   1 
ATOM   9494  C  CB  . LYS   C  1 330 ? 43.917  28.458  -62.146  1.00 52.31  ? 631  LYS   C CB  1 
ATOM   9495  C  CG  . LYS   C  1 330 ? 44.241  26.995  -62.374  1.00 56.21  ? 631  LYS   C CG  1 
ATOM   9496  C  CD  . LYS   C  1 330 ? 42.989  26.133  -62.231  1.00 53.01  ? 631  LYS   C CD  1 
ATOM   9497  C  CE  . LYS   C  1 330 ? 43.362  24.673  -62.086  1.00 55.45  ? 631  LYS   C CE  1 
ATOM   9498  N  NZ  . LYS   C  1 330 ? 42.307  23.899  -61.397  1.00 60.11  ? 631  LYS   C NZ  1 
ATOM   9499  N  N   . ASP   C  1 331 ? 44.085  31.518  -61.657  1.00 61.95  ? 632  ASP   C N   1 
ATOM   9500  C  CA  . ASP   C  1 331 ? 43.498  32.843  -61.814  1.00 62.25  ? 632  ASP   C CA  1 
ATOM   9501  C  C   . ASP   C  1 331 ? 44.468  33.788  -62.503  1.00 60.82  ? 632  ASP   C C   1 
ATOM   9502  O  O   . ASP   C  1 331 ? 44.087  34.542  -63.409  1.00 55.60  ? 632  ASP   C O   1 
ATOM   9503  C  CB  . ASP   C  1 331 ? 43.091  33.392  -60.445  1.00 52.24  ? 632  ASP   C CB  1 
ATOM   9504  C  CG  . ASP   C  1 331 ? 42.144  32.478  -59.722  1.00 53.76  ? 632  ASP   C CG  1 
ATOM   9505  O  OD1 . ASP   C  1 331 ? 42.611  31.446  -59.214  1.00 65.95  ? 632  ASP   C OD1 1 
ATOM   9506  O  OD2 . ASP   C  1 331 ? 40.937  32.776  -59.648  1.00 53.99  ? 632  ASP   C OD2 1 
ATOM   9507  N  N   . GLN   C  1 332 ? 45.736  33.734  -62.099  1.00 62.63  ? 633  GLN   C N   1 
ATOM   9508  C  CA  . GLN   C  1 332 ? 46.728  34.657  -62.629  1.00 62.47  ? 633  GLN   C CA  1 
ATOM   9509  C  C   . GLN   C  1 332 ? 46.970  34.413  -64.110  1.00 56.72  ? 633  GLN   C C   1 
ATOM   9510  O  O   . GLN   C  1 332 ? 47.021  35.358  -64.899  1.00 45.32  ? 633  GLN   C O   1 
ATOM   9511  C  CB  . GLN   C  1 332 ? 48.027  34.521  -61.846  1.00 62.25  ? 633  GLN   C CB  1 
ATOM   9512  C  CG  . GLN   C  1 332 ? 48.739  35.816  -61.641  1.00 68.90  ? 633  GLN   C CG  1 
ATOM   9513  C  CD  . GLN   C  1 332 ? 49.561  35.797  -60.378  1.00 71.13  ? 633  GLN   C CD  1 
ATOM   9514  O  OE1 . GLN   C  1 332 ? 49.826  34.734  -59.804  1.00 69.74  ? 633  GLN   C OE1 1 
ATOM   9515  N  NE2 . GLN   C  1 332 ? 49.965  36.974  -59.929  1.00 76.25  ? 633  GLN   C NE2 1 
ATOM   9516  N  N   . ALA   C  1 333 ? 47.137  33.144  -64.499  1.00 51.78  ? 634  ALA   C N   1 
ATOM   9517  C  CA  . ALA   C  1 333 ? 47.419  32.822  -65.893  1.00 53.97  ? 634  ALA   C CA  1 
ATOM   9518  C  C   . ALA   C  1 333 ? 46.227  33.151  -66.775  1.00 54.10  ? 634  ALA   C C   1 
ATOM   9519  O  O   . ALA   C  1 333 ? 46.388  33.732  -67.857  1.00 54.93  ? 634  ALA   C O   1 
ATOM   9520  C  CB  . ALA   C  1 333 ? 47.800  31.345  -66.025  1.00 52.53  ? 634  ALA   C CB  1 
ATOM   9521  N  N   . LEU   C  1 334 ? 45.023  32.808  -66.305  1.00 54.72  ? 635  LEU   C N   1 
ATOM   9522  C  CA  . LEU   C  1 334 ? 43.804  33.079  -67.052  1.00 49.63  ? 635  LEU   C CA  1 
ATOM   9523  C  C   . LEU   C  1 334 ? 43.634  34.569  -67.324  1.00 57.36  ? 635  LEU   C C   1 
ATOM   9524  O  O   . LEU   C  1 334 ? 43.140  34.948  -68.389  1.00 59.92  ? 635  LEU   C O   1 
ATOM   9525  C  CB  . LEU   C  1 334 ? 42.595  32.521  -66.299  1.00 40.74  ? 635  LEU   C CB  1 
ATOM   9526  C  CG  . LEU   C  1 334 ? 41.242  33.062  -66.765  1.00 40.05  ? 635  LEU   C CG  1 
ATOM   9527  C  CD1 . LEU   C  1 334 ? 40.896  32.486  -68.134  1.00 41.44  ? 635  LEU   C CD1 1 
ATOM   9528  C  CD2 . LEU   C  1 334 ? 40.133  32.793  -65.739  1.00 40.99  ? 635  LEU   C CD2 1 
ATOM   9529  N  N   . VAL   C  1 335 ? 44.048  35.437  -66.400  1.00 59.65  ? 636  VAL   C N   1 
ATOM   9530  C  CA  . VAL   C  1 335 ? 43.972  36.860  -66.711  1.00 61.73  ? 636  VAL   C CA  1 
ATOM   9531  C  C   . VAL   C  1 335 ? 44.936  37.203  -67.842  1.00 64.07  ? 636  VAL   C C   1 
ATOM   9532  O  O   . VAL   C  1 335 ? 44.599  37.969  -68.755  1.00 62.77  ? 636  VAL   C O   1 
ATOM   9533  C  CB  . VAL   C  1 335 ? 44.234  37.711  -65.458  1.00 50.78  ? 636  VAL   C CB  1 
ATOM   9534  C  CG1 . VAL   C  1 335 ? 44.488  39.142  -65.862  1.00 43.89  ? 636  VAL   C CG1 1 
ATOM   9535  C  CG2 . VAL   C  1 335 ? 43.035  37.653  -64.523  1.00 57.81  ? 636  VAL   C CG2 1 
ATOM   9536  N  N   . GLU   C  1 336 ? 46.134  36.614  -67.820  1.00 50.89  ? 637  GLU   C N   1 
ATOM   9537  C  CA  . GLU   C  1 336 ? 47.130  36.933  -68.831  1.00 45.01  ? 637  GLU   C CA  1 
ATOM   9538  C  C   . GLU   C  1 336 ? 46.706  36.445  -70.214  1.00 56.43  ? 637  GLU   C C   1 
ATOM   9539  O  O   . GLU   C  1 336 ? 46.899  37.146  -71.215  1.00 47.79  ? 637  GLU   C O   1 
ATOM   9540  C  CB  . GLU   C  1 336 ? 48.469  36.338  -68.425  1.00 45.99  ? 637  GLU   C CB  1 
ATOM   9541  C  CG  . GLU   C  1 336 ? 49.078  37.019  -67.199  1.00 56.01  ? 637  GLU   C CG  1 
ATOM   9542  C  CD  . GLU   C  1 336 ? 49.551  38.460  -67.420  1.00 56.45  ? 637  GLU   C CD  1 
ATOM   9543  O  OE1 . GLU   C  1 336 ? 49.282  39.055  -68.471  1.00 65.19  ? 637  GLU   C OE1 1 
ATOM   9544  O  OE2 . GLU   C  1 336 ? 50.220  39.008  -66.533  1.00 62.56  ? 637  GLU   C OE2 1 
ATOM   9545  N  N   . ILE   C  1 337 ? 46.117  35.251  -70.284  1.00 58.81  ? 638  ILE   C N   1 
ATOM   9546  C  CA  . ILE   C  1 337 ? 45.660  34.716  -71.560  1.00 51.03  ? 638  ILE   C CA  1 
ATOM   9547  C  C   . ILE   C  1 337 ? 44.706  35.690  -72.229  1.00 56.35  ? 638  ILE   C C   1 
ATOM   9548  O  O   . ILE   C  1 337 ? 44.847  36.018  -73.410  1.00 58.30  ? 638  ILE   C O   1 
ATOM   9549  C  CB  . ILE   C  1 337 ? 44.996  33.346  -71.356  1.00 40.30  ? 638  ILE   C CB  1 
ATOM   9550  C  CG1 . ILE   C  1 337 ? 45.979  32.393  -70.684  1.00 47.82  ? 638  ILE   C CG1 1 
ATOM   9551  C  CG2 . ILE   C  1 337 ? 44.469  32.830  -72.700  1.00 39.37  ? 638  ILE   C CG2 1 
ATOM   9552  C  CD1 . ILE   C  1 337 ? 46.077  31.062  -71.318  1.00 54.24  ? 638  ILE   C CD1 1 
ATOM   9553  N  N   . ASN   C  1 338 ? 43.729  36.179  -71.474  1.00 59.56  ? 639  ASN   C N   1 
ATOM   9554  C  CA  . ASN   C  1 338 ? 42.712  37.055  -72.037  1.00 53.95  ? 639  ASN   C CA  1 
ATOM   9555  C  C   . ASN   C  1 338 ? 43.277  38.409  -72.437  1.00 58.14  ? 639  ASN   C C   1 
ATOM   9556  O  O   . ASN   C  1 338 ? 42.825  38.994  -73.427  1.00 67.66  ? 639  ASN   C O   1 
ATOM   9557  C  CB  . ASN   C  1 338 ? 41.576  37.219  -71.036  1.00 53.72  ? 639  ASN   C CB  1 
ATOM   9558  C  CG  . ASN   C  1 338 ? 40.664  36.024  -71.021  1.00 52.84  ? 639  ASN   C CG  1 
ATOM   9559  O  OD1 . ASN   C  1 338 ? 39.598  36.043  -71.622  1.00 59.15  ? 639  ASN   C OD1 1 
ATOM   9560  N  ND2 . ASN   C  1 338 ? 41.092  34.962  -70.365  1.00 45.56  ? 639  ASN   C ND2 1 
ATOM   9561  N  N   . ILE   C  1 339 ? 44.245  38.933  -71.682  1.00 58.60  ? 640  ILE   C N   1 
ATOM   9562  C  CA  . ILE   C  1 339 ? 44.921  40.149  -72.119  1.00 58.24  ? 640  ILE   C CA  1 
ATOM   9563  C  C   . ILE   C  1 339 ? 45.564  39.924  -73.479  1.00 62.03  ? 640  ILE   C C   1 
ATOM   9564  O  O   . ILE   C  1 339 ? 45.538  40.799  -74.351  1.00 63.22  ? 640  ILE   C O   1 
ATOM   9565  C  CB  . ILE   C  1 339 ? 45.954  40.594  -71.068  1.00 48.02  ? 640  ILE   C CB  1 
ATOM   9566  C  CG1 . ILE   C  1 339 ? 45.250  41.245  -69.889  1.00 55.47  ? 640  ILE   C CG1 1 
ATOM   9567  C  CG2 . ILE   C  1 339 ? 46.976  41.557  -71.655  1.00 44.25  ? 640  ILE   C CG2 1 
ATOM   9568  C  CD1 . ILE   C  1 339 ? 46.160  41.537  -68.785  1.00 44.08  ? 640  ILE   C CD1 1 
ATOM   9569  N  N   . ALA   C  1 340 ? 46.138  38.741  -73.680  1.00 56.53  ? 641  ALA   C N   1 
ATOM   9570  C  CA  . ALA   C  1 340 ? 46.855  38.471  -74.912  1.00 45.57  ? 641  ALA   C CA  1 
ATOM   9571  C  C   . ALA   C  1 340 ? 45.892  38.331  -76.075  1.00 51.30  ? 641  ALA   C C   1 
ATOM   9572  O  O   . ALA   C  1 340 ? 46.170  38.812  -77.178  1.00 59.79  ? 641  ALA   C O   1 
ATOM   9573  C  CB  . ALA   C  1 340 ? 47.697  37.209  -74.754  1.00 53.03  ? 641  ALA   C CB  1 
ATOM   9574  N  N   . VAL   C  1 341 ? 44.752  37.681  -75.841  1.00 48.63  ? 642  VAL   C N   1 
ATOM   9575  C  CA  . VAL   C  1 341 ? 43.753  37.518  -76.893  1.00 47.26  ? 642  VAL   C CA  1 
ATOM   9576  C  C   . VAL   C  1 341 ? 43.260  38.883  -77.371  1.00 55.68  ? 642  VAL   C C   1 
ATOM   9577  O  O   . VAL   C  1 341 ? 43.316  39.201  -78.565  1.00 45.92  ? 642  VAL   C O   1 
ATOM   9578  C  CB  . VAL   C  1 341 ? 42.602  36.626  -76.392  1.00 40.11  ? 642  VAL   C CB  1 
ATOM   9579  C  CG1 . VAL   C  1 341 ? 41.413  36.740  -77.295  1.00 38.16  ? 642  VAL   C CG1 1 
ATOM   9580  C  CG2 . VAL   C  1 341 ? 43.053  35.169  -76.314  1.00 36.78  ? 642  VAL   C CG2 1 
ATOM   9581  N  N   . LEU   C  1 342 ? 42.802  39.724  -76.437  1.00 60.03  ? 643  LEU   C N   1 
ATOM   9582  C  CA  . LEU   C  1 342 ? 42.314  41.051  -76.808  1.00 53.88  ? 643  LEU   C CA  1 
ATOM   9583  C  C   . LEU   C  1 342 ? 43.386  41.859  -77.532  1.00 62.33  ? 643  LEU   C C   1 
ATOM   9584  O  O   . LEU   C  1 342 ? 43.112  42.534  -78.533  1.00 54.61  ? 643  LEU   C O   1 
ATOM   9585  C  CB  . LEU   C  1 342 ? 41.847  41.804  -75.568  1.00 38.21  ? 643  LEU   C CB  1 
ATOM   9586  C  CG  . LEU   C  1 342 ? 40.637  41.239  -74.845  1.00 42.08  ? 643  LEU   C CG  1 
ATOM   9587  C  CD1 . LEU   C  1 342 ? 40.529  41.821  -73.440  1.00 37.07  ? 643  LEU   C CD1 1 
ATOM   9588  C  CD2 . LEU   C  1 342 ? 39.393  41.529  -75.675  1.00 34.70  ? 643  LEU   C CD2 1 
ATOM   9589  N  N   . TYR   C  1 343 ? 44.612  41.830  -77.015  1.00 63.89  ? 644  TYR   C N   1 
ATOM   9590  C  CA  . TYR   C  1 343 ? 45.688  42.584  -77.643  1.00 63.87  ? 644  TYR   C CA  1 
ATOM   9591  C  C   . TYR   C  1 343 ? 45.938  42.087  -79.062  1.00 67.62  ? 644  TYR   C C   1 
ATOM   9592  O  O   . TYR   C  1 343 ? 46.042  42.883  -80.004  1.00 68.08  ? 644  TYR   C O   1 
ATOM   9593  C  CB  . TYR   C  1 343 ? 46.932  42.473  -76.771  1.00 43.47  ? 644  TYR   C CB  1 
ATOM   9594  C  CG  . TYR   C  1 343 ? 48.225  42.891  -77.376  1.00 45.38  ? 644  TYR   C CG  1 
ATOM   9595  C  CD1 . TYR   C  1 343 ? 48.560  44.232  -77.479  1.00 46.61  ? 644  TYR   C CD1 1 
ATOM   9596  C  CD2 . TYR   C  1 343 ? 49.146  41.943  -77.795  1.00 47.36  ? 644  TYR   C CD2 1 
ATOM   9597  C  CE1 . TYR   C  1 343 ? 49.761  44.620  -78.022  1.00 53.40  ? 644  TYR   C CE1 1 
ATOM   9598  C  CE2 . TYR   C  1 343 ? 50.359  42.315  -78.341  1.00 55.53  ? 644  TYR   C CE2 1 
ATOM   9599  C  CZ  . TYR   C  1 343 ? 50.661  43.660  -78.455  1.00 62.60  ? 644  TYR   C CZ  1 
ATOM   9600  O  OH  . TYR   C  1 343 ? 51.866  44.050  -79.003  1.00 65.84  ? 644  TYR   C OH  1 
ATOM   9601  N  N   . SER   C  1 344 ? 45.986  40.767  -79.236  1.00 63.72  ? 645  SER   C N   1 
ATOM   9602  C  CA  . SER   C  1 344 ? 46.265  40.201  -80.545  1.00 56.19  ? 645  SER   C CA  1 
ATOM   9603  C  C   . SER   C  1 344 ? 45.178  40.571  -81.544  1.00 57.47  ? 645  SER   C C   1 
ATOM   9604  O  O   . SER   C  1 344 ? 45.467  41.007  -82.663  1.00 69.64  ? 645  SER   C O   1 
ATOM   9605  C  CB  . SER   C  1 344 ? 46.401  38.688  -80.417  1.00 57.78  ? 645  SER   C CB  1 
ATOM   9606  O  OG  . SER   C  1 344 ? 47.538  38.348  -79.636  1.00 60.66  ? 645  SER   C OG  1 
ATOM   9607  N  N   . PHE   C  1 345 ? 43.916  40.402  -81.154  1.00 54.32  ? 646  PHE   C N   1 
ATOM   9608  C  CA  . PHE   C  1 345 ? 42.814  40.770  -82.036  1.00 51.12  ? 646  PHE   C CA  1 
ATOM   9609  C  C   . PHE   C  1 345 ? 42.831  42.258  -82.358  1.00 59.83  ? 646  PHE   C C   1 
ATOM   9610  O  O   . PHE   C  1 345 ? 42.594  42.653  -83.499  1.00 63.89  ? 646  PHE   C O   1 
ATOM   9611  C  CB  . PHE   C  1 345 ? 41.485  40.390  -81.397  1.00 36.58  ? 646  PHE   C CB  1 
ATOM   9612  C  CG  . PHE   C  1 345 ? 40.955  39.055  -81.835  1.00 43.03  ? 646  PHE   C CG  1 
ATOM   9613  C  CD1 . PHE   C  1 345 ? 41.568  37.881  -81.430  1.00 43.70  ? 646  PHE   C CD1 1 
ATOM   9614  C  CD2 . PHE   C  1 345 ? 39.831  38.971  -82.646  1.00 37.93  ? 646  PHE   C CD2 1 
ATOM   9615  C  CE1 . PHE   C  1 345 ? 41.069  36.640  -81.830  1.00 46.10  ? 646  PHE   C CE1 1 
ATOM   9616  C  CE2 . PHE   C  1 345 ? 39.324  37.744  -83.039  1.00 41.23  ? 646  PHE   C CE2 1 
ATOM   9617  C  CZ  . PHE   C  1 345 ? 39.945  36.574  -82.634  1.00 43.70  ? 646  PHE   C CZ  1 
ATOM   9618  N  N   . GLN   C  1 346 ? 43.095  43.104  -81.367  1.00 65.54  ? 647  GLN   C N   1 
ATOM   9619  C  CA  . GLN   C  1 346 ? 43.092  44.536  -81.633  1.00 64.69  ? 647  GLN   C CA  1 
ATOM   9620  C  C   . GLN   C  1 346 ? 44.245  44.936  -82.528  1.00 57.75  ? 647  GLN   C C   1 
ATOM   9621  O  O   . GLN   C  1 346 ? 44.115  45.882  -83.307  1.00 58.72  ? 647  GLN   C O   1 
ATOM   9622  C  CB  . GLN   C  1 346 ? 43.161  45.317  -80.324  1.00 65.94  ? 647  GLN   C CB  1 
ATOM   9623  C  CG  . GLN   C  1 346 ? 41.807  45.674  -79.784  1.00 63.94  ? 647  GLN   C CG  1 
ATOM   9624  C  CD  . GLN   C  1 346 ? 41.811  45.752  -78.299  1.00 56.42  ? 647  GLN   C CD  1 
ATOM   9625  O  OE1 . GLN   C  1 346 ? 42.864  45.909  -77.687  1.00 53.50  ? 647  GLN   C OE1 1 
ATOM   9626  N  NE2 . GLN   C  1 346 ? 40.634  45.626  -77.697  1.00 54.22  ? 647  GLN   C NE2 1 
ATOM   9627  N  N   . SER   C  1 347 ? 45.373  44.232  -82.417  1.00 56.96  ? 648  SER   C N   1 
ATOM   9628  C  CA  . SER   C  1 347 ? 46.563  44.565  -83.187  1.00 50.23  ? 648  SER   C CA  1 
ATOM   9629  C  C   . SER   C  1 347 ? 46.397  44.223  -84.659  1.00 57.47  ? 648  SER   C C   1 
ATOM   9630  O  O   . SER   C  1 347 ? 47.044  44.836  -85.519  1.00 68.02  ? 648  SER   C O   1 
ATOM   9631  C  CB  . SER   C  1 347 ? 47.772  43.830  -82.608  1.00 50.30  ? 648  SER   C CB  1 
ATOM   9632  O  OG  . SER   C  1 347 ? 48.060  44.303  -81.302  1.00 59.10  ? 648  SER   C OG  1 
ATOM   9633  N  N   . ASP   C  1 348 ? 45.562  43.236  -84.967  1.00 48.29  ? 649  ASP   C N   1 
ATOM   9634  C  CA  . ASP   C  1 348 ? 45.253  42.880  -86.342  1.00 45.37  ? 649  ASP   C CA  1 
ATOM   9635  C  C   . ASP   C  1 348 ? 43.965  43.541  -86.822  1.00 52.14  ? 649  ASP   C C   1 
ATOM   9636  O  O   . ASP   C  1 348 ? 43.367  43.089  -87.802  1.00 49.46  ? 649  ASP   C O   1 
ATOM   9637  C  CB  . ASP   C  1 348 ? 45.179  41.359  -86.475  1.00 40.25  ? 649  ASP   C CB  1 
ATOM   9638  C  CG  . ASP   C  1 348 ? 46.521  40.699  -86.244  1.00 50.08  ? 649  ASP   C CG  1 
ATOM   9639  O  OD1 . ASP   C  1 348 ? 47.531  41.429  -86.156  1.00 43.34  ? 649  ASP   C OD1 1 
ATOM   9640  O  OD2 . ASP   C  1 348 ? 46.574  39.458  -86.156  1.00 53.52  ? 649  ASP   C OD2 1 
ATOM   9641  N  N   . LYS   C  1 349 ? 43.546  44.615  -86.148  1.00 55.51  ? 650  LYS   C N   1 
ATOM   9642  C  CA  . LYS   C  1 349 ? 42.299  45.333  -86.394  1.00 55.70  ? 650  LYS   C CA  1 
ATOM   9643  C  C   . LYS   C  1 349 ? 41.127  44.397  -86.683  1.00 58.67  ? 650  LYS   C C   1 
ATOM   9644  O  O   . LYS   C  1 349 ? 40.251  44.721  -87.489  1.00 63.76  ? 650  LYS   C O   1 
ATOM   9645  C  CB  . LYS   C  1 349 ? 42.492  46.338  -87.527  1.00 54.50  ? 650  LYS   C CB  1 
ATOM   9646  C  CG  . LYS   C  1 349 ? 43.065  47.686  -87.082  1.00 66.91  ? 650  LYS   C CG  1 
ATOM   9647  C  CD  . LYS   C  1 349 ? 44.002  48.292  -88.150  1.00 81.08  ? 650  LYS   C CD  1 
ATOM   9648  C  CE  . LYS   C  1 349 ? 43.571  49.703  -88.593  1.00 84.95  ? 650  LYS   C CE  1 
ATOM   9649  N  NZ  . LYS   C  1 349 ? 43.407  50.652  -87.447  1.00 87.79  ? 650  LYS   C NZ  1 
ATOM   9650  N  N   . VAL   C  1 350 ? 41.097  43.244  -86.014  1.00 47.74  ? 651  VAL   C N   1 
ATOM   9651  C  CA  . VAL   C  1 350 ? 39.975  42.311  -86.076  1.00 43.89  ? 651  VAL   C CA  1 
ATOM   9652  C  C   . VAL   C  1 350 ? 39.017  42.618  -84.928  1.00 55.20  ? 651  VAL   C C   1 
ATOM   9653  O  O   . VAL   C  1 350 ? 39.428  42.709  -83.759  1.00 58.43  ? 651  VAL   C O   1 
ATOM   9654  C  CB  . VAL   C  1 350 ? 40.473  40.856  -86.018  1.00 34.81  ? 651  VAL   C CB  1 
ATOM   9655  C  CG1 . VAL   C  1 350 ? 39.332  39.877  -86.191  1.00 36.45  ? 651  VAL   C CG1 1 
ATOM   9656  C  CG2 . VAL   C  1 350 ? 41.558  40.614  -87.074  1.00 35.88  ? 651  VAL   C CG2 1 
ATOM   9657  N  N   . THR   C  1 351 ? 37.738  42.782  -85.256  1.00 50.71  ? 652  THR   C N   1 
ATOM   9658  C  CA  . THR   C  1 351 ? 36.780  43.261  -84.271  1.00 43.00  ? 652  THR   C CA  1 
ATOM   9659  C  C   . THR   C  1 351 ? 36.705  42.318  -83.081  1.00 48.69  ? 652  THR   C C   1 
ATOM   9660  O  O   . THR   C  1 351 ? 36.636  41.096  -83.234  1.00 57.46  ? 652  THR   C O   1 
ATOM   9661  C  CB  . THR   C  1 351 ? 35.400  43.429  -84.897  1.00 41.31  ? 652  THR   C CB  1 
ATOM   9662  O  OG1 . THR   C  1 351 ? 35.469  44.444  -85.900  1.00 60.85  ? 652  THR   C OG1 1 
ATOM   9663  C  CG2 . THR   C  1 351 ? 34.372  43.880  -83.849  1.00 42.16  ? 652  THR   C CG2 1 
ATOM   9664  N  N   . ILE   C  1 352 ? 36.721  42.899  -81.886  1.00 43.46  ? 653  ILE   C N   1 
ATOM   9665  C  CA  . ILE   C  1 352 ? 36.593  42.130  -80.653  1.00 38.07  ? 653  ILE   C CA  1 
ATOM   9666  C  C   . ILE   C  1 352 ? 36.095  43.082  -79.585  1.00 39.79  ? 653  ILE   C C   1 
ATOM   9667  O  O   . ILE   C  1 352 ? 36.213  44.302  -79.717  1.00 39.22  ? 653  ILE   C O   1 
ATOM   9668  C  CB  . ILE   C  1 352 ? 37.941  41.479  -80.267  1.00 35.23  ? 653  ILE   C CB  1 
ATOM   9669  C  CG1 . ILE   C  1 352 ? 37.718  40.293  -79.345  1.00 35.25  ? 653  ILE   C CG1 1 
ATOM   9670  C  CG2 . ILE   C  1 352 ? 38.859  42.506  -79.713  1.00 34.15  ? 653  ILE   C CG2 1 
ATOM   9671  C  CD1 . ILE   C  1 352 ? 39.003  39.536  -79.041  1.00 35.00  ? 653  ILE   C CD1 1 
ATOM   9672  N  N   . VAL   C  1 353 ? 35.511  42.531  -78.526  1.00 39.42  ? 654  VAL   C N   1 
ATOM   9673  C  CA  . VAL   C  1 353 ? 34.981  43.346  -77.443  1.00 40.92  ? 654  VAL   C CA  1 
ATOM   9674  C  C   . VAL   C  1 353 ? 35.348  42.674  -76.120  1.00 46.38  ? 654  VAL   C C   1 
ATOM   9675  O  O   . VAL   C  1 353 ? 35.190  41.458  -75.971  1.00 44.23  ? 654  VAL   C O   1 
ATOM   9676  C  CB  . VAL   C  1 353 ? 33.458  43.565  -77.620  1.00 47.49  ? 654  VAL   C CB  1 
ATOM   9677  C  CG1 . VAL   C  1 353 ? 32.693  42.247  -77.638  1.00 42.65  ? 654  VAL   C CG1 1 
ATOM   9678  C  CG2 . VAL   C  1 353 ? 32.895  44.522  -76.594  1.00 50.99  ? 654  VAL   C CG2 1 
ATOM   9679  N  N   . ASP   C  1 354 ? 35.921  43.442  -75.189  1.00 36.03  ? 655  ASP   C N   1 
ATOM   9680  C  CA  . ASP   C  1 354 ? 36.208  42.878  -73.873  1.00 41.92  ? 655  ASP   C CA  1 
ATOM   9681  C  C   . ASP   C  1 354 ? 34.911  42.707  -73.096  1.00 45.57  ? 655  ASP   C C   1 
ATOM   9682  O  O   . ASP   C  1 354 ? 33.832  43.137  -73.524  1.00 49.52  ? 655  ASP   C O   1 
ATOM   9683  C  CB  . ASP   C  1 354 ? 37.211  43.733  -73.099  1.00 39.02  ? 655  ASP   C CB  1 
ATOM   9684  C  CG  . ASP   C  1 354 ? 36.675  45.115  -72.744  1.00 53.59  ? 655  ASP   C CG  1 
ATOM   9685  O  OD1 . ASP   C  1 354 ? 37.280  46.122  -73.169  1.00 67.53  ? 655  ASP   C OD1 1 
ATOM   9686  O  OD2 . ASP   C  1 354 ? 35.664  45.208  -72.027  1.00 60.48  ? 655  ASP   C OD2 1 
ATOM   9687  N  N   . HIS   C  1 355 ? 35.008  42.078  -71.930  1.00 47.94  ? 656  HIS   C N   1 
ATOM   9688  C  CA  . HIS   C  1 355 ? 33.791  41.780  -71.193  1.00 40.12  ? 656  HIS   C CA  1 
ATOM   9689  C  C   . HIS   C  1 355 ? 33.312  42.942  -70.338  1.00 47.89  ? 656  HIS   C C   1 
ATOM   9690  O  O   . HIS   C  1 355 ? 32.133  42.971  -69.965  1.00 55.92  ? 656  HIS   C O   1 
ATOM   9691  C  CB  . HIS   C  1 355 ? 33.995  40.536  -70.343  1.00 38.79  ? 656  HIS   C CB  1 
ATOM   9692  C  CG  . HIS   C  1 355 ? 35.253  40.568  -69.545  1.00 48.31  ? 656  HIS   C CG  1 
ATOM   9693  N  ND1 . HIS   C  1 355 ? 36.493  40.423  -70.122  1.00 44.66  ? 656  HIS   C ND1 1 
ATOM   9694  C  CD2 . HIS   C  1 355 ? 35.465  40.734  -68.218  1.00 42.48  ? 656  HIS   C CD2 1 
ATOM   9695  C  CE1 . HIS   C  1 355 ? 37.420  40.502  -69.182  1.00 54.00  ? 656  HIS   C CE1 1 
ATOM   9696  N  NE2 . HIS   C  1 355 ? 36.822  40.688  -68.019  1.00 48.08  ? 656  HIS   C NE2 1 
ATOM   9697  N  N   . HIS   C  1 356 ? 34.175  43.920  -70.059  1.00 49.58  ? 657  HIS   C N   1 
ATOM   9698  C  CA  . HIS   C  1 356 ? 33.705  45.130  -69.394  1.00 49.53  ? 657  HIS   C CA  1 
ATOM   9699  C  C   . HIS   C  1 356 ? 32.842  45.956  -70.330  1.00 52.41  ? 657  HIS   C C   1 
ATOM   9700  O  O   . HIS   C  1 356 ? 31.715  46.333  -69.987  1.00 56.39  ? 657  HIS   C O   1 
ATOM   9701  C  CB  . HIS   C  1 356 ? 34.894  45.935  -68.883  1.00 47.22  ? 657  HIS   C CB  1 
ATOM   9702  C  CG  . HIS   C  1 356 ? 35.810  45.127  -68.029  1.00 52.24  ? 657  HIS   C CG  1 
ATOM   9703  N  ND1 . HIS   C  1 356 ? 35.485  44.761  -66.742  1.00 52.36  ? 657  HIS   C ND1 1 
ATOM   9704  C  CD2 . HIS   C  1 356 ? 37.008  44.558  -68.296  1.00 53.24  ? 657  HIS   C CD2 1 
ATOM   9705  C  CE1 . HIS   C  1 356 ? 36.456  44.019  -66.246  1.00 54.42  ? 657  HIS   C CE1 1 
ATOM   9706  N  NE2 . HIS   C  1 356 ? 37.395  43.887  -67.166  1.00 50.97  ? 657  HIS   C NE2 1 
ATOM   9707  N  N   . SER   C  1 357 ? 33.349  46.212  -71.534  1.00 56.15  ? 658  SER   C N   1 
ATOM   9708  C  CA  A SER   C  1 357 ? 32.596  46.977  -72.522  0.38 50.98  ? 658  SER   C CA  1 
ATOM   9709  C  CA  B SER   C  1 357 ? 32.589  46.984  -72.506  0.62 51.07  ? 658  SER   C CA  1 
ATOM   9710  C  C   . SER   C  1 357 ? 31.325  46.248  -72.934  1.00 48.81  ? 658  SER   C C   1 
ATOM   9711  O  O   . SER   C  1 357 ? 30.260  46.868  -73.080  1.00 36.93  ? 658  SER   C O   1 
ATOM   9712  C  CB  A SER   C  1 357 ? 33.473  47.250  -73.746  0.38 48.77  ? 658  SER   C CB  1 
ATOM   9713  C  CB  B SER   C  1 357 ? 33.473  47.302  -73.709  0.62 48.73  ? 658  SER   C CB  1 
ATOM   9714  O  OG  A SER   C  1 357 ? 32.689  47.688  -74.839  0.38 45.94  ? 658  SER   C OG  1 
ATOM   9715  O  OG  B SER   C  1 357 ? 34.624  48.007  -73.279  0.62 49.96  ? 658  SER   C OG  1 
ATOM   9716  N  N   . ALA   C  1 358 ? 31.417  44.929  -73.126  1.00 43.45  ? 659  ALA   C N   1 
ATOM   9717  C  CA  . ALA   C  1 358 ? 30.266  44.162  -73.600  1.00 35.94  ? 659  ALA   C CA  1 
ATOM   9718  C  C   . ALA   C  1 358 ? 29.121  44.224  -72.611  1.00 51.08  ? 659  ALA   C C   1 
ATOM   9719  O  O   . ALA   C  1 358 ? 27.974  44.508  -72.983  1.00 50.46  ? 659  ALA   C O   1 
ATOM   9720  C  CB  . ALA   C  1 358 ? 30.654  42.705  -73.824  1.00 35.28  ? 659  ALA   C CB  1 
ATOM   9721  N  N   . THR   C  1 359 ? 29.420  43.932  -71.337  1.00 53.48  ? 660  THR   C N   1 
ATOM   9722  C  CA  . THR   C  1 359 ? 28.386  43.890  -70.316  1.00 30.87  ? 660  THR   C CA  1 
ATOM   9723  C  C   . THR   C  1 359 ? 27.844  45.285  -70.035  1.00 34.72  ? 660  THR   C C   1 
ATOM   9724  O  O   . THR   C  1 359 ? 26.640  45.453  -69.813  1.00 42.23  ? 660  THR   C O   1 
ATOM   9725  C  CB  . THR   C  1 359 ? 28.940  43.238  -69.048  1.00 42.77  ? 660  THR   C CB  1 
ATOM   9726  O  OG1 . THR   C  1 359 ? 30.130  43.912  -68.629  1.00 47.30  ? 660  THR   C OG1 1 
ATOM   9727  C  CG2 . THR   C  1 359 ? 29.278  41.811  -69.319  1.00 42.42  ? 660  THR   C CG2 1 
ATOM   9728  N  N   . GLU   C  1 360 ? 28.717  46.298  -70.047  1.00 34.74  ? 661  GLU   C N   1 
ATOM   9729  C  CA  . GLU   C  1 360 ? 28.269  47.674  -69.860  1.00 33.72  ? 661  GLU   C CA  1 
ATOM   9730  C  C   . GLU   C  1 360 ? 27.245  48.060  -70.920  1.00 47.53  ? 661  GLU   C C   1 
ATOM   9731  O  O   . GLU   C  1 360 ? 26.253  48.738  -70.628  1.00 56.29  ? 661  GLU   C O   1 
ATOM   9732  C  CB  . GLU   C  1 360 ? 29.482  48.607  -69.900  1.00 40.14  ? 661  GLU   C CB  1 
ATOM   9733  C  CG  . GLU   C  1 360 ? 29.175  50.107  -69.887  1.00 59.97  ? 661  GLU   C CG  1 
ATOM   9734  C  CD  . GLU   C  1 360 ? 30.434  50.970  -70.080  1.00 74.55  ? 661  GLU   C CD  1 
ATOM   9735  O  OE1 . GLU   C  1 360 ? 31.491  50.430  -70.481  1.00 72.91  ? 661  GLU   C OE1 1 
ATOM   9736  O  OE2 . GLU   C  1 360 ? 30.368  52.194  -69.826  1.00 79.46  ? 661  GLU   C OE2 1 
ATOM   9737  N  N   . SER   C  1 361 ? 27.469  47.623  -72.161  1.00 48.92  ? 662  SER   C N   1 
ATOM   9738  C  CA  . SER   C  1 361 ? 26.542  47.950  -73.234  1.00 46.47  ? 662  SER   C CA  1 
ATOM   9739  C  C   . SER   C  1 361 ? 25.223  47.227  -73.048  1.00 44.58  ? 662  SER   C C   1 
ATOM   9740  O  O   . SER   C  1 361 ? 24.158  47.801  -73.295  1.00 58.00  ? 662  SER   C O   1 
ATOM   9741  C  CB  . SER   C  1 361 ? 27.162  47.608  -74.577  1.00 56.03  ? 662  SER   C CB  1 
ATOM   9742  O  OG  . SER   C  1 361 ? 28.221  48.505  -74.856  1.00 74.18  ? 662  SER   C OG  1 
ATOM   9743  N  N   . PHE   C  1 362 ? 25.263  45.978  -72.582  1.00 43.45  ? 663  PHE   C N   1 
ATOM   9744  C  CA  . PHE   C  1 362 ? 24.010  45.261  -72.366  1.00 42.89  ? 663  PHE   C CA  1 
ATOM   9745  C  C   . PHE   C  1 362 ? 23.136  45.968  -71.327  1.00 46.40  ? 663  PHE   C C   1 
ATOM   9746  O  O   . PHE   C  1 362 ? 21.916  46.068  -71.499  1.00 53.95  ? 663  PHE   C O   1 
ATOM   9747  C  CB  . PHE   C  1 362 ? 24.275  43.808  -71.969  1.00 37.12  ? 663  PHE   C CB  1 
ATOM   9748  C  CG  . PHE   C  1 362 ? 23.015  42.996  -71.822  1.00 39.14  ? 663  PHE   C CG  1 
ATOM   9749  C  CD1 . PHE   C  1 362 ? 22.328  42.535  -72.948  1.00 29.76  ? 663  PHE   C CD1 1 
ATOM   9750  C  CD2 . PHE   C  1 362 ? 22.483  42.738  -70.563  1.00 37.49  ? 663  PHE   C CD2 1 
ATOM   9751  C  CE1 . PHE   C  1 362 ? 21.142  41.793  -72.810  1.00 28.54  ? 663  PHE   C CE1 1 
ATOM   9752  C  CE2 . PHE   C  1 362 ? 21.305  42.008  -70.414  1.00 40.16  ? 663  PHE   C CE2 1 
ATOM   9753  C  CZ  . PHE   C  1 362 ? 20.637  41.532  -71.529  1.00 45.53  ? 663  PHE   C CZ  1 
ATOM   9754  N  N   . ILE   C  1 363 ? 23.736  46.471  -70.246  1.00 48.32  ? 664  ILE   C N   1 
ATOM   9755  C  CA  . ILE   C  1 363 ? 22.965  47.245  -69.272  1.00 45.94  ? 664  ILE   C CA  1 
ATOM   9756  C  C   . ILE   C  1 363 ? 22.284  48.424  -69.966  1.00 48.14  ? 664  ILE   C C   1 
ATOM   9757  O  O   . ILE   C  1 363 ? 21.077  48.644  -69.809  1.00 49.02  ? 664  ILE   C O   1 
ATOM   9758  C  CB  . ILE   C  1 363 ? 23.863  47.698  -68.100  1.00 52.01  ? 664  ILE   C CB  1 
ATOM   9759  C  CG1 . ILE   C  1 363 ? 24.418  46.492  -67.328  1.00 38.39  ? 664  ILE   C CG1 1 
ATOM   9760  C  CG2 . ILE   C  1 363 ? 23.112  48.653  -67.171  1.00 35.00  ? 664  ILE   C CG2 1 
ATOM   9761  C  CD1 . ILE   C  1 363 ? 23.419  45.849  -66.356  1.00 40.18  ? 664  ILE   C CD1 1 
ATOM   9762  N  N   . LYS   C  1 364 ? 23.042  49.166  -70.785  1.00 55.75  ? 665  LYS   C N   1 
ATOM   9763  C  CA  . LYS   C  1 364 ? 22.468  50.192  -71.666  1.00 54.39  ? 665  LYS   C CA  1 
ATOM   9764  C  C   . LYS   C  1 364 ? 21.345  49.639  -72.544  1.00 52.98  ? 665  LYS   C C   1 
ATOM   9765  O  O   . LYS   C  1 364 ? 20.299  50.282  -72.704  1.00 61.95  ? 665  LYS   C O   1 
ATOM   9766  C  CB  . LYS   C  1 364 ? 23.575  50.791  -72.536  1.00 45.46  ? 665  LYS   C CB  1 
ATOM   9767  C  CG  . LYS   C  1 364 ? 23.160  51.836  -73.537  1.00 68.38  ? 665  LYS   C CG  1 
ATOM   9768  C  CD  . LYS   C  1 364 ? 24.130  51.793  -74.735  1.00 84.93  ? 665  LYS   C CD  1 
ATOM   9769  C  CE  . LYS   C  1 364 ? 23.927  52.934  -75.732  1.00 96.01  ? 665  LYS   C CE  1 
ATOM   9770  N  NZ  . LYS   C  1 364 ? 24.731  54.149  -75.375  1.00 98.65  ? 665  LYS   C NZ  1 
ATOM   9771  N  N   . HIS   C  1 365 ? 21.540  48.450  -73.128  1.00 43.33  ? 666  HIS   C N   1 
ATOM   9772  C  CA  . HIS   C  1 365 ? 20.486  47.857  -73.955  1.00 43.64  ? 666  HIS   C CA  1 
ATOM   9773  C  C   . HIS   C  1 365 ? 19.244  47.572  -73.119  1.00 52.54  ? 666  HIS   C C   1 
ATOM   9774  O  O   . HIS   C  1 365 ? 18.111  47.780  -73.574  1.00 59.12  ? 666  HIS   C O   1 
ATOM   9775  C  CB  . HIS   C  1 365 ? 20.989  46.572  -74.630  1.00 35.62  ? 666  HIS   C CB  1 
ATOM   9776  C  CG  . HIS   C  1 365 ? 19.948  45.849  -75.440  1.00 46.85  ? 666  HIS   C CG  1 
ATOM   9777  N  ND1 . HIS   C  1 365 ? 19.398  46.372  -76.592  1.00 46.98  ? 666  HIS   C ND1 1 
ATOM   9778  C  CD2 . HIS   C  1 365 ? 19.375  44.630  -75.275  1.00 46.36  ? 666  HIS   C CD2 1 
ATOM   9779  C  CE1 . HIS   C  1 365 ? 18.518  45.518  -77.088  1.00 43.46  ? 666  HIS   C CE1 1 
ATOM   9780  N  NE2 . HIS   C  1 365 ? 18.488  44.451  -76.310  1.00 38.73  ? 666  HIS   C NE2 1 
ATOM   9781  N  N   . MET   C  1 366 ? 19.448  47.100  -71.888  1.00 47.51  ? 667  MET   C N   1 
ATOM   9782  C  CA  . MET   C  1 366 ? 18.332  46.793  -71.007  1.00 39.83  ? 667  MET   C CA  1 
ATOM   9783  C  C   . MET   C  1 366 ? 17.477  48.032  -70.771  1.00 40.70  ? 667  MET   C C   1 
ATOM   9784  O  O   . MET   C  1 366 ? 16.247  47.976  -70.861  1.00 36.14  ? 667  MET   C O   1 
ATOM   9785  C  CB  . MET   C  1 366 ? 18.859  46.233  -69.680  1.00 41.08  ? 667  MET   C CB  1 
ATOM   9786  C  CG  . MET   C  1 366 ? 19.014  44.714  -69.615  1.00 47.53  ? 667  MET   C CG  1 
ATOM   9787  S  SD  . MET   C  1 366 ? 19.181  44.112  -67.897  1.00 50.10  ? 667  MET   C SD  1 
ATOM   9788  C  CE  . MET   C  1 366 ? 17.514  43.628  -67.460  1.00 46.57  ? 667  MET   C CE  1 
ATOM   9789  N  N   . GLU   C  1 367 ? 18.113  49.158  -70.443  1.00 47.82  ? 668  GLU   C N   1 
ATOM   9790  C  CA  . GLU   C  1 367 ? 17.376  50.400  -70.246  1.00 52.91  ? 668  GLU   C CA  1 
ATOM   9791  C  C   . GLU   C  1 367 ? 16.475  50.688  -71.440  1.00 56.81  ? 668  GLU   C C   1 
ATOM   9792  O  O   . GLU   C  1 367 ? 15.249  50.805  -71.300  1.00 49.87  ? 668  GLU   C O   1 
ATOM   9793  C  CB  . GLU   C  1 367 ? 18.360  51.546  -70.011  1.00 61.52  ? 668  GLU   C CB  1 
ATOM   9794  C  CG  . GLU   C  1 367 ? 18.984  51.521  -68.621  1.00 76.32  ? 668  GLU   C CG  1 
ATOM   9795  C  CD  . GLU   C  1 367 ? 20.208  52.402  -68.532  1.00 79.41  ? 668  GLU   C CD  1 
ATOM   9796  O  OE1 . GLU   C  1 367 ? 20.415  53.204  -69.479  1.00 84.27  ? 668  GLU   C OE1 1 
ATOM   9797  O  OE2 . GLU   C  1 367 ? 20.964  52.270  -67.535  1.00 67.06  ? 668  GLU   C OE2 1 
ATOM   9798  N  N   . ASN   C  1 368 ? 17.086  50.769  -72.630  1.00 56.84  ? 669  ASN   C N   1 
ATOM   9799  C  CA  . ASN   C  1 368 ? 16.366  50.992  -73.883  1.00 46.41  ? 669  ASN   C CA  1 
ATOM   9800  C  C   . ASN   C  1 368 ? 15.143  50.096  -74.010  1.00 52.12  ? 669  ASN   C C   1 
ATOM   9801  O  O   . ASN   C  1 368 ? 14.019  50.576  -74.209  1.00 54.20  ? 669  ASN   C O   1 
ATOM   9802  C  CB  . ASN   C  1 368 ? 17.307  50.732  -75.055  1.00 46.39  ? 669  ASN   C CB  1 
ATOM   9803  C  CG  . ASN   C  1 368 ? 18.429  51.736  -75.134  1.00 56.16  ? 669  ASN   C CG  1 
ATOM   9804  O  OD1 . ASN   C  1 368 ? 18.315  52.868  -74.627  1.00 49.86  ? 669  ASN   C OD1 1 
ATOM   9805  N  ND2 . ASN   C  1 368 ? 19.528  51.338  -75.791  1.00 56.04  ? 669  ASN   C ND2 1 
ATOM   9806  N  N   . GLU   C  1 369 ? 15.358  48.778  -73.915  1.00 44.72  ? 670  GLU   C N   1 
ATOM   9807  C  CA  . GLU   C  1 369 ? 14.272  47.822  -74.094  1.00 41.30  ? 670  GLU   C CA  1 
ATOM   9808  C  C   . GLU   C  1 369 ? 13.132  48.064  -73.109  1.00 58.15  ? 670  GLU   C C   1 
ATOM   9809  O  O   . GLU   C  1 369 ? 11.956  48.005  -73.491  1.00 61.91  ? 670  GLU   C O   1 
ATOM   9810  C  CB  . GLU   C  1 369 ? 14.817  46.399  -73.959  1.00 35.43  ? 670  GLU   C CB  1 
ATOM   9811  C  CG  . GLU   C  1 369 ? 15.814  45.988  -75.059  1.00 44.46  ? 670  GLU   C CG  1 
ATOM   9812  C  CD  . GLU   C  1 369 ? 15.126  45.736  -76.420  1.00 47.39  ? 670  GLU   C CD  1 
ATOM   9813  O  OE1 . GLU   C  1 369 ? 15.177  44.592  -76.949  1.00 32.14  ? 670  GLU   C OE1 1 
ATOM   9814  O  OE2 . GLU   C  1 369 ? 14.503  46.681  -76.933  1.00 33.32  ? 670  GLU   C OE2 1 
ATOM   9815  N  N   . TYR   C  1 370 ? 13.454  48.322  -71.830  1.00 53.99  ? 671  TYR   C N   1 
ATOM   9816  C  CA  . TYR   C  1 370 ? 12.398  48.538  -70.848  1.00 47.27  ? 671  TYR   C CA  1 
ATOM   9817  C  C   . TYR   C  1 370 ? 11.676  49.846  -71.125  1.00 54.72  ? 671  TYR   C C   1 
ATOM   9818  O  O   . TYR   C  1 370 ? 10.454  49.940  -70.956  1.00 67.79  ? 671  TYR   C O   1 
ATOM   9819  C  CB  . TYR   C  1 370 ? 12.971  48.514  -69.416  1.00 43.83  ? 671  TYR   C CB  1 
ATOM   9820  C  CG  . TYR   C  1 370 ? 12.984  47.130  -68.801  1.00 40.86  ? 671  TYR   C CG  1 
ATOM   9821  C  CD1 . TYR   C  1 370 ? 14.067  46.287  -68.965  1.00 41.78  ? 671  TYR   C CD1 1 
ATOM   9822  C  CD2 . TYR   C  1 370 ? 11.898  46.654  -68.089  1.00 51.54  ? 671  TYR   C CD2 1 
ATOM   9823  C  CE1 . TYR   C  1 370 ? 14.079  45.015  -68.422  1.00 45.34  ? 671  TYR   C CE1 1 
ATOM   9824  C  CE2 . TYR   C  1 370 ? 11.903  45.381  -67.539  1.00 51.12  ? 671  TYR   C CE2 1 
ATOM   9825  C  CZ  . TYR   C  1 370 ? 12.993  44.563  -67.712  1.00 50.77  ? 671  TYR   C CZ  1 
ATOM   9826  O  OH  . TYR   C  1 370 ? 12.990  43.290  -67.173  1.00 50.11  ? 671  TYR   C OH  1 
ATOM   9827  N  N   . ARG   C  1 371 ? 12.420  50.860  -71.573  1.00 48.78  ? 672  ARG   C N   1 
ATOM   9828  C  CA  . ARG   C  1 371 ? 11.837  52.175  -71.829  1.00 57.99  ? 672  ARG   C CA  1 
ATOM   9829  C  C   . ARG   C  1 371 ? 10.906  52.158  -73.044  1.00 61.91  ? 672  ARG   C C   1 
ATOM   9830  O  O   . ARG   C  1 371 ? 9.856   52.813  -73.029  1.00 62.35  ? 672  ARG   C O   1 
ATOM   9831  C  CB  . ARG   C  1 371 ? 12.967  53.200  -71.999  1.00 65.34  ? 672  ARG   C CB  1 
ATOM   9832  C  CG  . ARG   C  1 371 ? 12.611  54.493  -72.717  1.00 77.35  ? 672  ARG   C CG  1 
ATOM   9833  C  CD  . ARG   C  1 371 ? 13.452  54.694  -73.998  1.00 92.62  ? 672  ARG   C CD  1 
ATOM   9834  N  NE  . ARG   C  1 371 ? 14.858  54.326  -73.834  1.00 99.36  ? 672  ARG   C NE  1 
ATOM   9835  C  CZ  . ARG   C  1 371 ? 15.760  55.071  -73.202  1.00 107.41 ? 672  ARG   C CZ  1 
ATOM   9836  N  NH1 . ARG   C  1 371 ? 15.407  56.231  -72.662  1.00 107.56 ? 672  ARG   C NH1 1 
ATOM   9837  N  NH2 . ARG   C  1 371 ? 17.016  54.654  -73.102  1.00 112.60 ? 672  ARG   C NH2 1 
ATOM   9838  N  N   . CYS   C  1 372 ? 11.253  51.398  -74.095  1.00 56.87  ? 673  CYS   C N   1 
ATOM   9839  C  CA  A CYS   C  1 372 ? 10.457  51.411  -75.314  0.51 59.73  ? 673  CYS   C CA  1 
ATOM   9840  C  CA  B CYS   C  1 372 ? 10.497  51.392  -75.345  0.49 59.77  ? 673  CYS   C CA  1 
ATOM   9841  C  C   . CYS   C  1 372 ? 9.609   50.165  -75.530  1.00 64.57  ? 673  CYS   C C   1 
ATOM   9842  O  O   . CYS   C  1 372 ? 8.649   50.228  -76.294  1.00 85.26  ? 673  CYS   C O   1 
ATOM   9843  C  CB  A CYS   C  1 372 ? 11.356  51.602  -76.545  0.51 58.66  ? 673  CYS   C CB  1 
ATOM   9844  C  CB  B CYS   C  1 372 ? 11.449  51.483  -76.552  0.49 58.29  ? 673  CYS   C CB  1 
ATOM   9845  S  SG  A CYS   C  1 372 ? 12.051  50.068  -77.141  0.51 53.47  ? 673  CYS   C SG  1 
ATOM   9846  S  SG  B CYS   C  1 372 ? 12.234  53.099  -76.844  0.49 61.24  ? 673  CYS   C SG  1 
ATOM   9847  N  N   . ARG   C  1 373 ? 9.911   49.047  -74.882  1.00 61.92  ? 674  ARG   C N   1 
ATOM   9848  C  CA  . ARG   C  1 373 ? 9.193   47.805  -75.149  1.00 59.18  ? 674  ARG   C CA  1 
ATOM   9849  C  C   . ARG   C  1 373 ? 8.458   47.247  -73.941  1.00 63.93  ? 674  ARG   C C   1 
ATOM   9850  O  O   . ARG   C  1 373 ? 7.615   46.360  -74.108  1.00 57.65  ? 674  ARG   C O   1 
ATOM   9851  C  CB  . ARG   C  1 373 ? 10.175  46.740  -75.674  1.00 58.22  ? 674  ARG   C CB  1 
ATOM   9852  C  CG  . ARG   C  1 373 ? 9.614   45.675  -76.607  1.00 52.03  ? 674  ARG   C CG  1 
ATOM   9853  C  CD  . ARG   C  1 373 ? 10.716  44.681  -76.958  1.00 46.62  ? 674  ARG   C CD  1 
ATOM   9854  N  NE  . ARG   C  1 373 ? 10.214  43.458  -77.582  1.00 54.01  ? 674  ARG   C NE  1 
ATOM   9855  C  CZ  . ARG   C  1 373 ? 10.947  42.358  -77.749  1.00 54.65  ? 674  ARG   C CZ  1 
ATOM   9856  N  NH1 . ARG   C  1 373 ? 12.203  42.330  -77.334  1.00 60.57  ? 674  ARG   C NH1 1 
ATOM   9857  N  NH2 . ARG   C  1 373 ? 10.424  41.278  -78.311  1.00 49.38  ? 674  ARG   C NH2 1 
ATOM   9858  N  N   . GLY   C  1 374 ? 8.757   47.728  -72.736  1.00 70.35  ? 675  GLY   C N   1 
ATOM   9859  C  CA  . GLY   C  1 374 ? 8.182   47.169  -71.530  1.00 67.55  ? 675  GLY   C CA  1 
ATOM   9860  C  C   . GLY   C  1 374 ? 8.884   45.945  -70.985  1.00 60.86  ? 675  GLY   C C   1 
ATOM   9861  O  O   . GLY   C  1 374 ? 8.274   45.192  -70.218  1.00 59.89  ? 675  GLY   C O   1 
ATOM   9862  N  N   . GLY   C  1 375 ? 10.135  45.707  -71.358  1.00 48.67  ? 676  GLY   C N   1 
ATOM   9863  C  CA  . GLY   C  1 375 ? 10.836  44.546  -70.847  1.00 49.79  ? 676  GLY   C CA  1 
ATOM   9864  C  C   . GLY   C  1 375 ? 11.972  44.124  -71.749  1.00 58.01  ? 676  GLY   C C   1 
ATOM   9865  O  O   . GLY   C  1 375 ? 12.151  44.635  -72.860  1.00 65.52  ? 676  GLY   C O   1 
ATOM   9866  N  N   . CYS   C  1 376 ? 12.751  43.147  -71.246  1.00 48.08  ? 677  CYS   C N   1 
ATOM   9867  C  CA  . CYS   C  1 376 ? 13.844  42.553  -72.005  1.00 42.06  ? 677  CYS   C CA  1 
ATOM   9868  C  C   . CYS   C  1 376 ? 14.263  41.222  -71.395  1.00 46.56  ? 677  CYS   C C   1 
ATOM   9869  O  O   . CYS   C  1 376 ? 14.894  41.213  -70.331  1.00 48.26  ? 677  CYS   C O   1 
ATOM   9870  C  CB  . CYS   C  1 376 ? 15.039  43.503  -72.052  1.00 31.95  ? 677  CYS   C CB  1 
ATOM   9871  S  SG  . CYS   C  1 376 ? 16.472  42.770  -72.815  1.00 42.09  ? 677  CYS   C SG  1 
ATOM   9872  N  N   . PRO   C  1 377 ? 13.966  40.088  -72.040  1.00 41.02  ? 678  PRO   C N   1 
ATOM   9873  C  CA  . PRO   C  1 377 ? 14.317  38.787  -71.447  1.00 33.99  ? 678  PRO   C CA  1 
ATOM   9874  C  C   . PRO   C  1 377 ? 15.825  38.584  -71.402  1.00 36.26  ? 678  PRO   C C   1 
ATOM   9875  O  O   . PRO   C  1 377 ? 16.520  38.759  -72.404  1.00 46.30  ? 678  PRO   C O   1 
ATOM   9876  C  CB  . PRO   C  1 377 ? 13.636  37.775  -72.378  1.00 38.56  ? 678  PRO   C CB  1 
ATOM   9877  C  CG  . PRO   C  1 377 ? 13.625  38.464  -73.715  1.00 42.66  ? 678  PRO   C CG  1 
ATOM   9878  C  CD  . PRO   C  1 377 ? 13.402  39.938  -73.396  1.00 47.69  ? 678  PRO   C CD  1 
ATOM   9879  N  N   . ALA   C  1 378 ? 16.337  38.230  -70.223  1.00 48.32  ? 679  ALA   C N   1 
ATOM   9880  C  CA  . ALA   C  1 378 ? 17.768  38.012  -70.054  1.00 48.68  ? 679  ALA   C CA  1 
ATOM   9881  C  C   . ALA   C  1 378 ? 18.006  36.800  -69.165  1.00 44.25  ? 679  ALA   C C   1 
ATOM   9882  O  O   . ALA   C  1 378 ? 17.204  36.506  -68.276  1.00 53.19  ? 679  ALA   C O   1 
ATOM   9883  C  CB  . ALA   C  1 378 ? 18.450  39.250  -69.471  1.00 48.72  ? 679  ALA   C CB  1 
ATOM   9884  N  N   . ASP   C  1 379 ? 19.107  36.086  -69.430  1.00 39.96  ? 680  ASP   C N   1 
ATOM   9885  C  CA  . ASP   C  1 379 ? 19.495  34.872  -68.700  1.00 39.36  ? 680  ASP   C CA  1 
ATOM   9886  C  C   . ASP   C  1 379 ? 20.776  35.202  -67.925  1.00 44.08  ? 680  ASP   C C   1 
ATOM   9887  O  O   . ASP   C  1 379 ? 21.873  35.204  -68.496  1.00 39.31  ? 680  ASP   C O   1 
ATOM   9888  C  CB  . ASP   C  1 379 ? 19.679  33.693  -69.671  1.00 36.96  ? 680  ASP   C CB  1 
ATOM   9889  C  CG  . ASP   C  1 379 ? 19.937  32.338  -68.962  1.00 42.68  ? 680  ASP   C CG  1 
ATOM   9890  O  OD1 . ASP   C  1 379 ? 19.254  31.340  -69.272  1.00 44.95  ? 680  ASP   C OD1 1 
ATOM   9891  O  OD2 . ASP   C  1 379 ? 20.835  32.244  -68.102  1.00 53.12  ? 680  ASP   C OD2 1 
ATOM   9892  N  N   . TRP   C  1 380 ? 20.624  35.493  -66.619  1.00 47.34  ? 681  TRP   C N   1 
ATOM   9893  C  CA  . TRP   C  1 380 ? 21.761  35.885  -65.781  1.00 36.80  ? 681  TRP   C CA  1 
ATOM   9894  C  C   . TRP   C  1 380 ? 22.916  34.901  -65.894  1.00 30.33  ? 681  TRP   C C   1 
ATOM   9895  O  O   . TRP   C  1 380 ? 24.081  35.303  -65.956  1.00 30.06  ? 681  TRP   C O   1 
ATOM   9896  C  CB  . TRP   C  1 380 ? 21.316  35.987  -64.315  1.00 45.52  ? 681  TRP   C CB  1 
ATOM   9897  C  CG  . TRP   C  1 380 ? 22.237  36.789  -63.443  1.00 45.50  ? 681  TRP   C CG  1 
ATOM   9898  C  CD1 . TRP   C  1 380 ? 22.140  38.123  -63.157  1.00 44.11  ? 681  TRP   C CD1 1 
ATOM   9899  C  CD2 . TRP   C  1 380 ? 23.395  36.312  -62.747  1.00 48.50  ? 681  TRP   C CD2 1 
ATOM   9900  N  NE1 . TRP   C  1 380 ? 23.165  38.502  -62.325  1.00 49.44  ? 681  TRP   C NE1 1 
ATOM   9901  C  CE2 . TRP   C  1 380 ? 23.949  37.409  -62.057  1.00 54.43  ? 681  TRP   C CE2 1 
ATOM   9902  C  CE3 . TRP   C  1 380 ? 24.018  35.067  -62.638  1.00 45.77  ? 681  TRP   C CE3 1 
ATOM   9903  C  CZ2 . TRP   C  1 380 ? 25.097  37.296  -61.271  1.00 52.81  ? 681  TRP   C CZ2 1 
ATOM   9904  C  CZ3 . TRP   C  1 380 ? 25.165  34.959  -61.859  1.00 41.57  ? 681  TRP   C CZ3 1 
ATOM   9905  C  CH2 . TRP   C  1 380 ? 25.687  36.062  -61.181  1.00 41.78  ? 681  TRP   C CH2 1 
ATOM   9906  N  N   . VAL   C  1 381 ? 22.603  33.604  -65.907  1.00 36.28  ? 682  VAL   C N   1 
ATOM   9907  C  CA  . VAL   C  1 381 ? 23.614  32.551  -65.905  1.00 33.22  ? 682  VAL   C CA  1 
ATOM   9908  C  C   . VAL   C  1 381 ? 24.549  32.685  -67.096  1.00 47.84  ? 682  VAL   C C   1 
ATOM   9909  O  O   . VAL   C  1 381 ? 25.751  32.403  -66.988  1.00 53.14  ? 682  VAL   C O   1 
ATOM   9910  C  CB  . VAL   C  1 381 ? 22.930  31.173  -65.897  1.00 34.73  ? 682  VAL   C CB  1 
ATOM   9911  C  CG1 . VAL   C  1 381 ? 23.940  30.096  -66.210  1.00 29.13  ? 682  VAL   C CG1 1 
ATOM   9912  C  CG2 . VAL   C  1 381 ? 22.196  30.928  -64.557  1.00 29.67  ? 682  VAL   C CG2 1 
ATOM   9913  N  N   . TRP   C  1 382 ? 24.005  33.090  -68.260  1.00 39.12  ? 683  TRP   C N   1 
ATOM   9914  C  CA  . TRP   C  1 382 ? 24.751  33.221  -69.506  1.00 31.64  ? 683  TRP   C CA  1 
ATOM   9915  C  C   . TRP   C  1 382 ? 25.256  34.638  -69.764  1.00 37.10  ? 683  TRP   C C   1 
ATOM   9916  O  O   . TRP   C  1 382 ? 26.296  34.807  -70.413  1.00 41.08  ? 683  TRP   C O   1 
ATOM   9917  C  CB  . TRP   C  1 382 ? 23.883  32.787  -70.691  1.00 39.84  ? 683  TRP   C CB  1 
ATOM   9918  C  CG  . TRP   C  1 382 ? 23.720  31.309  -70.817  1.00 47.26  ? 683  TRP   C CG  1 
ATOM   9919  C  CD1 . TRP   C  1 382 ? 23.111  30.479  -69.931  1.00 48.52  ? 683  TRP   C CD1 1 
ATOM   9920  C  CD2 . TRP   C  1 382 ? 24.176  30.476  -71.902  1.00 56.06  ? 683  TRP   C CD2 1 
ATOM   9921  N  NE1 . TRP   C  1 382 ? 23.162  29.178  -70.387  1.00 58.19  ? 683  TRP   C NE1 1 
ATOM   9922  C  CE2 . TRP   C  1 382 ? 23.811  29.151  -71.595  1.00 57.41  ? 683  TRP   C CE2 1 
ATOM   9923  C  CE3 . TRP   C  1 382 ? 24.855  30.724  -73.096  1.00 52.44  ? 683  TRP   C CE3 1 
ATOM   9924  C  CZ2 . TRP   C  1 382 ? 24.106  28.077  -72.439  1.00 50.03  ? 683  TRP   C CZ2 1 
ATOM   9925  C  CZ3 . TRP   C  1 382 ? 25.144  29.654  -73.933  1.00 49.87  ? 683  TRP   C CZ3 1 
ATOM   9926  C  CH2 . TRP   C  1 382 ? 24.771  28.350  -73.597  1.00 51.78  ? 683  TRP   C CH2 1 
ATOM   9927  N  N   . ILE   C  1 383 ? 24.540  35.662  -69.295  1.00 30.13  ? 684  ILE   C N   1 
ATOM   9928  C  CA  . ILE   C  1 383 ? 24.985  37.032  -69.526  1.00 29.44  ? 684  ILE   C CA  1 
ATOM   9929  C  C   . ILE   C  1 383 ? 26.265  37.340  -68.749  1.00 46.97  ? 684  ILE   C C   1 
ATOM   9930  O  O   . ILE   C  1 383 ? 27.148  38.053  -69.243  1.00 47.87  ? 684  ILE   C O   1 
ATOM   9931  C  CB  . ILE   C  1 383 ? 23.866  38.014  -69.164  1.00 28.57  ? 684  ILE   C CB  1 
ATOM   9932  C  CG1 . ILE   C  1 383 ? 22.679  37.802  -70.075  1.00 34.52  ? 684  ILE   C CG1 1 
ATOM   9933  C  CG2 . ILE   C  1 383 ? 24.348  39.440  -69.297  1.00 37.85  ? 684  ILE   C CG2 1 
ATOM   9934  C  CD1 . ILE   C  1 383 ? 23.011  37.998  -71.503  1.00 40.40  ? 684  ILE   C CD1 1 
ATOM   9935  N  N   . VAL   C  1 384 ? 26.379  36.832  -67.524  1.00 47.64  ? 685  VAL   C N   1 
ATOM   9936  C  CA  . VAL   C  1 384 ? 27.524  37.172  -66.661  1.00 41.36  ? 685  VAL   C CA  1 
ATOM   9937  C  C   . VAL   C  1 384 ? 28.782  36.490  -67.196  1.00 37.28  ? 685  VAL   C C   1 
ATOM   9938  O  O   . VAL   C  1 384 ? 28.776  35.259  -67.384  1.00 38.71  ? 685  VAL   C O   1 
ATOM   9939  C  CB  . VAL   C  1 384 ? 27.246  36.748  -65.214  1.00 29.62  ? 685  VAL   C CB  1 
ATOM   9940  C  CG1 . VAL   C  1 384 ? 28.533  36.667  -64.443  1.00 30.28  ? 685  VAL   C CG1 1 
ATOM   9941  C  CG2 . VAL   C  1 384 ? 26.318  37.752  -64.544  1.00 46.10  ? 685  VAL   C CG2 1 
ATOM   9942  N  N   . PRO   C  1 385 ? 29.871  37.224  -67.446  1.00 34.25  ? 686  PRO   C N   1 
ATOM   9943  C  CA  . PRO   C  1 385 ? 31.037  36.611  -68.071  1.00 39.61  ? 686  PRO   C CA  1 
ATOM   9944  C  C   . PRO   C  1 385 ? 31.666  35.557  -67.178  1.00 48.81  ? 686  PRO   C C   1 
ATOM   9945  O  O   . PRO   C  1 385 ? 31.537  35.609  -65.943  1.00 56.68  ? 686  PRO   C O   1 
ATOM   9946  C  CB  . PRO   C  1 385 ? 31.990  37.801  -68.276  1.00 38.80  ? 686  PRO   C CB  1 
ATOM   9947  C  CG  . PRO   C  1 385 ? 31.121  38.978  -68.345  1.00 37.46  ? 686  PRO   C CG  1 
ATOM   9948  C  CD  . PRO   C  1 385 ? 29.924  38.698  -67.473  1.00 37.86  ? 686  PRO   C CD  1 
ATOM   9949  N  N   . PRO   C  1 386 ? 32.381  34.587  -67.758  1.00 53.69  ? 687  PRO   C N   1 
ATOM   9950  C  CA  . PRO   C  1 386 ? 32.958  33.491  -66.966  1.00 42.86  ? 687  PRO   C CA  1 
ATOM   9951  C  C   . PRO   C  1 386 ? 34.246  33.836  -66.241  1.00 47.68  ? 687  PRO   C C   1 
ATOM   9952  O  O   . PRO   C  1 386 ? 34.857  32.938  -65.650  1.00 60.14  ? 687  PRO   C O   1 
ATOM   9953  C  CB  . PRO   C  1 386 ? 33.222  32.400  -68.019  1.00 35.42  ? 687  PRO   C CB  1 
ATOM   9954  C  CG  . PRO   C  1 386 ? 32.780  32.952  -69.325  1.00 40.63  ? 687  PRO   C CG  1 
ATOM   9955  C  CD  . PRO   C  1 386 ? 32.658  34.428  -69.195  1.00 43.63  ? 687  PRO   C CD  1 
ATOM   9956  N  N   . MET   C  1 387 ? 34.707  35.081  -66.304  1.00 42.45  ? 688  MET   C N   1 
ATOM   9957  C  CA  . MET   C  1 387 ? 35.740  35.556  -65.401  1.00 48.70  ? 688  MET   C CA  1 
ATOM   9958  C  C   . MET   C  1 387 ? 35.356  36.936  -64.886  1.00 55.75  ? 688  MET   C C   1 
ATOM   9959  O  O   . MET   C  1 387 ? 34.742  37.734  -65.605  1.00 51.02  ? 688  MET   C O   1 
ATOM   9960  C  CB  . MET   C  1 387 ? 37.101  35.612  -66.071  1.00 45.75  ? 688  MET   C CB  1 
ATOM   9961  C  CG  . MET   C  1 387 ? 37.348  36.885  -66.837  1.00 50.92  ? 688  MET   C CG  1 
ATOM   9962  S  SD  . MET   C  1 387 ? 38.944  36.857  -67.641  1.00 58.39  ? 688  MET   C SD  1 
ATOM   9963  C  CE  . MET   C  1 387 ? 39.823  38.074  -66.670  1.00 63.16  ? 688  MET   C CE  1 
ATOM   9964  N  N   . SER   C  1 388 ? 35.704  37.197  -63.624  1.00 47.41  ? 689  SER   C N   1 
ATOM   9965  C  CA  . SER   C  1 388 ? 35.589  38.522  -63.013  1.00 38.71  ? 689  SER   C CA  1 
ATOM   9966  C  C   . SER   C  1 388 ? 34.143  38.992  -62.935  1.00 37.74  ? 689  SER   C C   1 
ATOM   9967  O  O   . SER   C  1 388 ? 33.873  40.194  -62.993  1.00 41.85  ? 689  SER   C O   1 
ATOM   9968  C  CB  . SER   C  1 388 ? 36.445  39.557  -63.752  1.00 41.87  ? 689  SER   C CB  1 
ATOM   9969  O  OG  . SER   C  1 388 ? 37.658  38.977  -64.202  1.00 43.68  ? 689  SER   C OG  1 
ATOM   9970  N  N   . GLY   C  1 389 ? 33.214  38.053  -62.786  1.00 33.33  ? 690  GLY   C N   1 
ATOM   9971  C  CA  . GLY   C  1 389 ? 31.806  38.378  -62.660  1.00 38.39  ? 690  GLY   C CA  1 
ATOM   9972  C  C   . GLY   C  1 389 ? 31.451  39.674  -61.952  1.00 46.46  ? 690  GLY   C C   1 
ATOM   9973  O  O   . GLY   C  1 389 ? 30.928  40.600  -62.586  1.00 47.05  ? 690  GLY   C O   1 
ATOM   9974  N  N   . SER   C  1 390 ? 31.764  39.772  -60.651  1.00 40.59  ? 691  SER   C N   1 
ATOM   9975  C  CA  . SER   C  1 390 ? 31.225  40.863  -59.853  1.00 47.59  ? 691  SER   C CA  1 
ATOM   9976  C  C   . SER   C  1 390 ? 31.820  42.229  -60.210  1.00 42.27  ? 691  SER   C C   1 
ATOM   9977  O  O   . SER   C  1 390 ? 31.202  43.249  -59.883  1.00 43.31  ? 691  SER   C O   1 
ATOM   9978  C  CB  . SER   C  1 390 ? 31.385  40.560  -58.351  1.00 52.47  ? 691  SER   C CB  1 
ATOM   9979  O  OG  . SER   C  1 390 ? 32.659  40.919  -57.847  1.00 60.43  ? 691  SER   C OG  1 
ATOM   9980  N  N   . ILE   C  1 391 ? 32.962  42.298  -60.897  1.00 38.66  ? 692  ILE   C N   1 
ATOM   9981  C  CA  . ILE   C  1 391 ? 33.462  43.623  -61.270  1.00 51.74  ? 692  ILE   C CA  1 
ATOM   9982  C  C   . ILE   C  1 391 ? 32.898  44.058  -62.623  1.00 52.80  ? 692  ILE   C C   1 
ATOM   9983  O  O   . ILE   C  1 391 ? 33.333  45.074  -63.171  1.00 61.57  ? 692  ILE   C O   1 
ATOM   9984  C  CB  . ILE   C  1 391 ? 35.009  43.720  -61.269  1.00 46.20  ? 692  ILE   C CB  1 
ATOM   9985  C  CG1 . ILE   C  1 391 ? 35.646  42.589  -62.072  1.00 46.73  ? 692  ILE   C CG1 1 
ATOM   9986  C  CG2 . ILE   C  1 391 ? 35.544  43.794  -59.841  1.00 45.06  ? 692  ILE   C CG2 1 
ATOM   9987  C  CD1 . ILE   C  1 391 ? 36.937  42.982  -62.742  1.00 44.82  ? 692  ILE   C CD1 1 
ATOM   9988  N  N   . THR   C  1 392 ? 31.919  43.314  -63.175  1.00 39.52  ? 693  THR   C N   1 
ATOM   9989  C  CA  . THR   C  1 392 ? 31.150  43.798  -64.322  1.00 48.54  ? 693  THR   C CA  1 
ATOM   9990  C  C   . THR   C  1 392 ? 29.717  44.118  -63.904  1.00 49.39  ? 693  THR   C C   1 
ATOM   9991  O  O   . THR   C  1 392 ? 29.185  43.521  -62.962  1.00 40.73  ? 693  THR   C O   1 
ATOM   9992  C  CB  . THR   C  1 392 ? 31.112  42.784  -65.484  1.00 50.94  ? 693  THR   C CB  1 
ATOM   9993  O  OG1 . THR   C  1 392 ? 30.188  41.734  -65.177  1.00 47.48  ? 693  THR   C OG1 1 
ATOM   9994  C  CG2 . THR   C  1 392 ? 32.502  42.200  -65.786  1.00 49.65  ? 693  THR   C CG2 1 
ATOM   9995  N  N   . PRO   C  1 393 ? 29.047  45.046  -64.597  1.00 42.53  ? 694  PRO   C N   1 
ATOM   9996  C  CA  . PRO   C  1 393 ? 27.768  45.554  -64.077  1.00 45.48  ? 694  PRO   C CA  1 
ATOM   9997  C  C   . PRO   C  1 393 ? 26.609  44.586  -64.199  1.00 55.03  ? 694  PRO   C C   1 
ATOM   9998  O  O   . PRO   C  1 393 ? 25.590  44.782  -63.526  1.00 60.40  ? 694  PRO   C O   1 
ATOM   9999  C  CB  . PRO   C  1 393 ? 27.515  46.801  -64.930  1.00 34.68  ? 694  PRO   C CB  1 
ATOM   10000 C  CG  . PRO   C  1 393 ? 28.210  46.480  -66.227  1.00 44.88  ? 694  PRO   C CG  1 
ATOM   10001 C  CD  . PRO   C  1 393 ? 29.435  45.695  -65.862  1.00 46.01  ? 694  PRO   C CD  1 
ATOM   10002 N  N   . VAL   C  1 394 ? 26.700  43.563  -65.043  1.00 52.08  ? 695  VAL   C N   1 
ATOM   10003 C  CA  . VAL   C  1 394 ? 25.550  42.677  -65.158  1.00 41.91  ? 695  VAL   C CA  1 
ATOM   10004 C  C   . VAL   C  1 394 ? 25.470  41.744  -63.963  1.00 36.74  ? 695  VAL   C C   1 
ATOM   10005 O  O   . VAL   C  1 394 ? 24.381  41.234  -63.660  1.00 38.14  ? 695  VAL   C O   1 
ATOM   10006 C  CB  . VAL   C  1 394 ? 25.566  41.881  -66.476  1.00 35.53  ? 695  VAL   C CB  1 
ATOM   10007 C  CG1 . VAL   C  1 394 ? 25.110  42.762  -67.667  1.00 32.32  ? 695  VAL   C CG1 1 
ATOM   10008 C  CG2 . VAL   C  1 394 ? 26.937  41.343  -66.732  1.00 34.37  ? 695  VAL   C CG2 1 
ATOM   10009 N  N   . PHE   C  1 395 ? 26.589  41.528  -63.257  1.00 35.50  ? 696  PHE   C N   1 
ATOM   10010 C  CA  . PHE   C  1 395 ? 26.550  40.690  -62.055  1.00 44.61  ? 696  PHE   C CA  1 
ATOM   10011 C  C   . PHE   C  1 395 ? 25.551  41.222  -61.034  1.00 44.98  ? 696  PHE   C C   1 
ATOM   10012 O  O   . PHE   C  1 395 ? 24.801  40.442  -60.434  1.00 38.05  ? 696  PHE   C O   1 
ATOM   10013 C  CB  . PHE   C  1 395 ? 27.936  40.584  -61.425  1.00 44.41  ? 696  PHE   C CB  1 
ATOM   10014 C  CG  . PHE   C  1 395 ? 27.976  39.761  -60.152  1.00 44.27  ? 696  PHE   C CG  1 
ATOM   10015 C  CD1 . PHE   C  1 395 ? 28.442  38.457  -60.177  1.00 42.31  ? 696  PHE   C CD1 1 
ATOM   10016 C  CD2 . PHE   C  1 395 ? 27.593  40.305  -58.924  1.00 43.14  ? 696  PHE   C CD2 1 
ATOM   10017 C  CE1 . PHE   C  1 395 ? 28.501  37.712  -59.023  1.00 49.22  ? 696  PHE   C CE1 1 
ATOM   10018 C  CE2 . PHE   C  1 395 ? 27.634  39.551  -57.766  1.00 46.93  ? 696  PHE   C CE2 1 
ATOM   10019 C  CZ  . PHE   C  1 395 ? 28.099  38.258  -57.811  1.00 44.45  ? 696  PHE   C CZ  1 
ATOM   10020 N  N   . HIS   C  1 396 ? 25.530  42.545  -60.825  1.00 39.30  ? 697  HIS   C N   1 
ATOM   10021 C  CA  . HIS   C  1 396 ? 24.664  43.205  -59.857  1.00 43.88  ? 697  HIS   C CA  1 
ATOM   10022 C  C   . HIS   C  1 396 ? 23.315  43.606  -60.441  1.00 47.97  ? 697  HIS   C C   1 
ATOM   10023 O  O   . HIS   C  1 396 ? 22.666  44.513  -59.907  1.00 54.24  ? 697  HIS   C O   1 
ATOM   10024 C  CB  . HIS   C  1 396 ? 25.374  44.437  -59.287  1.00 44.85  ? 697  HIS   C CB  1 
ATOM   10025 C  CG  . HIS   C  1 396 ? 26.790  44.167  -58.894  1.00 48.86  ? 697  HIS   C CG  1 
ATOM   10026 N  ND1 . HIS   C  1 396 ? 27.162  43.894  -57.596  1.00 46.91  ? 697  HIS   C ND1 1 
ATOM   10027 C  CD2 . HIS   C  1 396 ? 27.919  44.077  -59.638  1.00 48.14  ? 697  HIS   C CD2 1 
ATOM   10028 C  CE1 . HIS   C  1 396 ? 28.463  43.665  -57.553  1.00 51.28  ? 697  HIS   C CE1 1 
ATOM   10029 N  NE2 . HIS   C  1 396 ? 28.944  43.760  -58.780  1.00 49.79  ? 697  HIS   C NE2 1 
ATOM   10030 N  N   . GLN   C  1 397 ? 22.877  42.972  -61.524  1.00 54.10  ? 698  GLN   C N   1 
ATOM   10031 C  CA  . GLN   C  1 397 ? 21.651  43.368  -62.205  1.00 49.43  ? 698  GLN   C CA  1 
ATOM   10032 C  C   . GLN   C  1 397 ? 20.665  42.203  -62.212  1.00 46.85  ? 698  GLN   C C   1 
ATOM   10033 O  O   . GLN   C  1 397 ? 20.963  41.129  -62.745  1.00 50.35  ? 698  GLN   C O   1 
ATOM   10034 C  CB  . GLN   C  1 397 ? 21.955  43.852  -63.622  1.00 44.59  ? 698  GLN   C CB  1 
ATOM   10035 C  CG  . GLN   C  1 397 ? 20.716  44.138  -64.460  1.00 40.71  ? 698  GLN   C CG  1 
ATOM   10036 C  CD  . GLN   C  1 397 ? 20.011  45.423  -64.064  1.00 45.18  ? 698  GLN   C CD  1 
ATOM   10037 O  OE1 . GLN   C  1 397 ? 20.578  46.518  -64.174  1.00 38.33  ? 698  GLN   C OE1 1 
ATOM   10038 N  NE2 . GLN   C  1 397 ? 18.755  45.300  -63.611  1.00 47.68  ? 698  GLN   C NE2 1 
ATOM   10039 N  N   . GLU   C  1 398 ? 19.499  42.416  -61.605  1.00 43.97  ? 699  GLU   C N   1 
ATOM   10040 C  CA  . GLU   C  1 398 ? 18.440  41.419  -61.627  1.00 44.39  ? 699  GLU   C CA  1 
ATOM   10041 C  C   . GLU   C  1 398 ? 17.865  41.320  -63.025  1.00 50.22  ? 699  GLU   C C   1 
ATOM   10042 O  O   . GLU   C  1 398 ? 17.656  42.335  -63.696  1.00 53.98  ? 699  GLU   C O   1 
ATOM   10043 C  CB  . GLU   C  1 398 ? 17.337  41.787  -60.631  1.00 47.02  ? 699  GLU   C CB  1 
ATOM   10044 C  CG  . GLU   C  1 398 ? 17.806  41.755  -59.177  1.00 53.25  ? 699  GLU   C CG  1 
ATOM   10045 C  CD  . GLU   C  1 398 ? 16.709  42.085  -58.166  1.00 57.96  ? 699  GLU   C CD  1 
ATOM   10046 O  OE1 . GLU   C  1 398 ? 16.920  41.789  -56.964  1.00 50.84  ? 699  GLU   C OE1 1 
ATOM   10047 O  OE2 . GLU   C  1 398 ? 15.649  42.635  -58.561  1.00 60.92  ? 699  GLU   C OE2 1 
ATOM   10048 N  N   . MET   C  1 399 ? 17.603  40.093  -63.460  1.00 47.90  ? 700  MET   C N   1 
ATOM   10049 C  CA  . MET   C  1 399 ? 17.077  39.843  -64.790  1.00 41.74  ? 700  MET   C CA  1 
ATOM   10050 C  C   . MET   C  1 399 ? 15.883  38.904  -64.703  1.00 56.91  ? 700  MET   C C   1 
ATOM   10051 O  O   . MET   C  1 399 ? 15.873  37.947  -63.917  1.00 70.32  ? 700  MET   C O   1 
ATOM   10052 C  CB  . MET   C  1 399 ? 18.148  39.249  -65.708  1.00 37.55  ? 700  MET   C CB  1 
ATOM   10053 C  CG  . MET   C  1 399 ? 19.282  40.223  -66.071  1.00 44.43  ? 700  MET   C CG  1 
ATOM   10054 S  SD  . MET   C  1 399 ? 20.750  39.360  -66.689  1.00 42.31  ? 700  MET   C SD  1 
ATOM   10055 C  CE  . MET   C  1 399 ? 22.020  40.632  -66.544  1.00 29.89  ? 700  MET   C CE  1 
ATOM   10056 N  N   . LEU   C  1 400 ? 14.874  39.204  -65.505  1.00 44.79  ? 701  LEU   C N   1 
ATOM   10057 C  CA  . LEU   C  1 400 ? 13.726  38.341  -65.696  1.00 39.88  ? 701  LEU   C CA  1 
ATOM   10058 C  C   . LEU   C  1 400 ? 13.932  37.532  -66.963  1.00 47.17  ? 701  LEU   C C   1 
ATOM   10059 O  O   . LEU   C  1 400 ? 14.349  38.073  -67.991  1.00 52.29  ? 701  LEU   C O   1 
ATOM   10060 C  CB  . LEU   C  1 400 ? 12.452  39.162  -65.813  1.00 41.54  ? 701  LEU   C CB  1 
ATOM   10061 C  CG  . LEU   C  1 400 ? 11.897  39.715  -64.529  1.00 57.51  ? 701  LEU   C CG  1 
ATOM   10062 C  CD1 . LEU   C  1 400 ? 10.800  40.676  -64.873  1.00 60.19  ? 701  LEU   C CD1 1 
ATOM   10063 C  CD2 . LEU   C  1 400 ? 11.366  38.550  -63.736  1.00 65.88  ? 701  LEU   C CD2 1 
ATOM   10064 N  N   . ASN   C  1 401 ? 13.646  36.237  -66.894  1.00 48.02  ? 702  ASN   C N   1 
ATOM   10065 C  CA  . ASN   C  1 401 ? 13.846  35.349  -68.031  1.00 50.13  ? 702  ASN   C CA  1 
ATOM   10066 C  C   . ASN   C  1 401 ? 12.508  34.776  -68.467  1.00 58.88  ? 702  ASN   C C   1 
ATOM   10067 O  O   . ASN   C  1 401 ? 11.802  34.158  -67.657  1.00 52.76  ? 702  ASN   C O   1 
ATOM   10068 C  CB  . ASN   C  1 401 ? 14.816  34.223  -67.696  1.00 56.31  ? 702  ASN   C CB  1 
ATOM   10069 C  CG  . ASN   C  1 401 ? 15.400  33.605  -68.931  1.00 50.72  ? 702  ASN   C CG  1 
ATOM   10070 O  OD1 . ASN   C  1 401 ? 15.359  34.202  -69.983  1.00 44.79  ? 702  ASN   C OD1 1 
ATOM   10071 N  ND2 . ASN   C  1 401 ? 15.945  32.409  -68.810  1.00 61.10  ? 702  ASN   C ND2 1 
ATOM   10072 N  N   . TYR   C  1 402 ? 12.172  34.981  -69.746  1.00 56.74  ? 703  TYR   C N   1 
ATOM   10073 C  CA  . TYR   C  1 402 ? 10.951  34.481  -70.362  1.00 42.09  ? 703  TYR   C CA  1 
ATOM   10074 C  C   . TYR   C  1 402 ? 11.216  34.320  -71.854  1.00 46.16  ? 703  TYR   C C   1 
ATOM   10075 O  O   . TYR   C  1 402 ? 12.187  34.862  -72.383  1.00 47.53  ? 703  TYR   C O   1 
ATOM   10076 C  CB  . TYR   C  1 402 ? 9.756   35.407  -70.087  1.00 39.78  ? 703  TYR   C CB  1 
ATOM   10077 C  CG  . TYR   C  1 402 ? 10.027  36.899  -70.243  1.00 47.86  ? 703  TYR   C CG  1 
ATOM   10078 C  CD1 . TYR   C  1 402 ? 9.721   37.572  -71.424  1.00 52.28  ? 703  TYR   C CD1 1 
ATOM   10079 C  CD2 . TYR   C  1 402 ? 10.572  37.636  -69.206  1.00 53.94  ? 703  TYR   C CD2 1 
ATOM   10080 C  CE1 . TYR   C  1 402 ? 9.960   38.934  -71.561  1.00 51.39  ? 703  TYR   C CE1 1 
ATOM   10081 C  CE2 . TYR   C  1 402 ? 10.817  38.995  -69.335  1.00 55.40  ? 703  TYR   C CE2 1 
ATOM   10082 C  CZ  . TYR   C  1 402 ? 10.506  39.638  -70.508  1.00 54.26  ? 703  TYR   C CZ  1 
ATOM   10083 O  OH  . TYR   C  1 402 ? 10.754  40.987  -70.617  1.00 51.93  ? 703  TYR   C OH  1 
ATOM   10084 N  N   . ARG   C  1 403 ? 10.343  33.552  -72.521  1.00 56.86  ? 704  ARG   C N   1 
ATOM   10085 C  CA  . ARG   C  1 403 ? 10.523  33.079  -73.894  1.00 46.27  ? 704  ARG   C CA  1 
ATOM   10086 C  C   . ARG   C  1 403 ? 9.549   33.783  -74.835  1.00 60.19  ? 704  ARG   C C   1 
ATOM   10087 O  O   . ARG   C  1 403 ? 8.329   33.604  -74.728  1.00 59.64  ? 704  ARG   C O   1 
ATOM   10088 C  CB  . ARG   C  1 403 ? 10.314  31.563  -73.991  1.00 49.26  ? 704  ARG   C CB  1 
ATOM   10089 C  CG  . ARG   C  1 403 ? 11.397  30.672  -73.378  1.00 50.00  ? 704  ARG   C CG  1 
ATOM   10090 C  CD  . ARG   C  1 403 ? 12.406  30.101  -74.411  1.00 69.07  ? 704  ARG   C CD  1 
ATOM   10091 N  NE  . ARG   C  1 403 ? 12.019  28.920  -75.218  1.00 71.27  ? 704  ARG   C NE  1 
ATOM   10092 C  CZ  . ARG   C  1 403 ? 11.343  27.843  -74.800  1.00 57.36  ? 704  ARG   C CZ  1 
ATOM   10093 N  NH1 . ARG   C  1 403 ? 10.854  27.754  -73.572  1.00 48.26  ? 704  ARG   C NH1 1 
ATOM   10094 N  NH2 . ARG   C  1 403 ? 11.118  26.847  -75.638  1.00 53.96  ? 704  ARG   C NH2 1 
ATOM   10095 N  N   . LEU   C  1 404 ? 10.097  34.537  -75.789  1.00 62.67  ? 705  LEU   C N   1 
ATOM   10096 C  CA  . LEU   C  1 404 ? 9.336   35.266  -76.796  1.00 53.04  ? 705  LEU   C CA  1 
ATOM   10097 C  C   . LEU   C  1 404 ? 9.627   34.700  -78.180  1.00 49.16  ? 705  LEU   C C   1 
ATOM   10098 O  O   . LEU   C  1 404 ? 10.765  34.328  -78.477  1.00 45.19  ? 705  LEU   C O   1 
ATOM   10099 C  CB  . LEU   C  1 404 ? 9.700   36.759  -76.789  1.00 45.80  ? 705  LEU   C CB  1 
ATOM   10100 C  CG  . LEU   C  1 404 ? 9.486   37.570  -75.517  1.00 39.97  ? 705  LEU   C CG  1 
ATOM   10101 C  CD1 . LEU   C  1 404 ? 9.764   39.024  -75.799  1.00 40.40  ? 705  LEU   C CD1 1 
ATOM   10102 C  CD2 . LEU   C  1 404 ? 8.081   37.386  -74.992  1.00 35.30  ? 705  LEU   C CD2 1 
ATOM   10103 N  N   . THR   C  1 405 ? 8.592   34.648  -79.043  1.00 48.57  ? 706  THR   C N   1 
ATOM   10104 C  CA  A THR   C  1 405 ? 8.823   34.263  -80.426  0.55 42.88  ? 706  THR   C CA  1 
ATOM   10105 C  CA  B THR   C  1 405 ? 8.860   34.275  -80.428  0.45 43.04  ? 706  THR   C CA  1 
ATOM   10106 C  C   . THR   C  1 405 ? 8.759   35.493  -81.333  1.00 45.12  ? 706  THR   C C   1 
ATOM   10107 O  O   . THR   C  1 405 ? 8.047   36.456  -81.022  1.00 43.26  ? 706  THR   C O   1 
ATOM   10108 C  CB  A THR   C  1 405 ? 7.790   33.219  -80.869  0.55 41.92  ? 706  THR   C CB  1 
ATOM   10109 C  CB  B THR   C  1 405 ? 7.913   33.193  -80.962  0.45 41.52  ? 706  THR   C CB  1 
ATOM   10110 O  OG1 A THR   C  1 405 ? 8.354   32.370  -81.874  0.55 41.61  ? 706  THR   C OG1 1 
ATOM   10111 O  OG1 B THR   C  1 405 ? 6.552   33.574  -80.708  0.45 42.53  ? 706  THR   C OG1 1 
ATOM   10112 C  CG2 A THR   C  1 405 ? 6.534   33.877  -81.396  0.55 41.96  ? 706  THR   C CG2 1 
ATOM   10113 C  CG2 B THR   C  1 405 ? 8.233   31.858  -80.322  0.45 37.49  ? 706  THR   C CG2 1 
ATOM   10114 N  N   . PRO   C  1 406 ? 9.501   35.510  -82.465  1.00 45.54  ? 707  PRO   C N   1 
ATOM   10115 C  CA  . PRO   C  1 406 ? 10.447  34.533  -83.046  1.00 48.01  ? 707  PRO   C CA  1 
ATOM   10116 C  C   . PRO   C  1 406 ? 11.661  34.257  -82.181  1.00 50.69  ? 707  PRO   C C   1 
ATOM   10117 O  O   . PRO   C  1 406 ? 12.117  35.159  -81.473  1.00 52.49  ? 707  PRO   C O   1 
ATOM   10118 C  CB  . PRO   C  1 406 ? 10.886  35.198  -84.363  1.00 42.83  ? 707  PRO   C CB  1 
ATOM   10119 C  CG  . PRO   C  1 406 ? 9.754   36.114  -84.690  1.00 49.89  ? 707  PRO   C CG  1 
ATOM   10120 C  CD  . PRO   C  1 406 ? 9.286   36.651  -83.373  1.00 39.80  ? 707  PRO   C CD  1 
ATOM   10121 N  N   . SER   C  1 407 ? 12.178  33.030  -82.259  1.00 44.45  ? 708  SER   C N   1 
ATOM   10122 C  CA  . SER   C  1 407 ? 13.261  32.589  -81.401  1.00 45.60  ? 708  SER   C CA  1 
ATOM   10123 C  C   . SER   C  1 407 ? 14.225  31.701  -82.166  1.00 41.37  ? 708  SER   C C   1 
ATOM   10124 O  O   . SER   C  1 407 ? 13.889  31.122  -83.204  1.00 56.33  ? 708  SER   C O   1 
ATOM   10125 C  CB  . SER   C  1 407 ? 12.726  31.819  -80.192  1.00 58.73  ? 708  SER   C CB  1 
ATOM   10126 O  OG  . SER   C  1 407 ? 11.954  30.710  -80.624  1.00 67.74  ? 708  SER   C OG  1 
ATOM   10127 N  N   . PHE   C  1 408 ? 15.445  31.625  -81.638  1.00 40.32  ? 709  PHE   C N   1 
ATOM   10128 C  CA  . PHE   C  1 408 ? 16.377  30.550  -81.951  1.00 31.85  ? 709  PHE   C CA  1 
ATOM   10129 C  C   . PHE   C  1 408 ? 16.188  29.443  -80.929  1.00 40.06  ? 709  PHE   C C   1 
ATOM   10130 O  O   . PHE   C  1 408 ? 15.883  29.703  -79.762  1.00 47.45  ? 709  PHE   C O   1 
ATOM   10131 C  CB  . PHE   C  1 408 ? 17.829  31.035  -81.924  1.00 26.53  ? 709  PHE   C CB  1 
ATOM   10132 C  CG  . PHE   C  1 408 ? 18.124  32.070  -82.946  1.00 32.55  ? 709  PHE   C CG  1 
ATOM   10133 C  CD1 . PHE   C  1 408 ? 18.184  33.408  -82.604  1.00 44.97  ? 709  PHE   C CD1 1 
ATOM   10134 C  CD2 . PHE   C  1 408 ? 18.279  31.718  -84.276  1.00 37.61  ? 709  PHE   C CD2 1 
ATOM   10135 C  CE1 . PHE   C  1 408 ? 18.440  34.376  -83.574  1.00 35.51  ? 709  PHE   C CE1 1 
ATOM   10136 C  CE2 . PHE   C  1 408 ? 18.539  32.665  -85.224  1.00 26.15  ? 709  PHE   C CE2 1 
ATOM   10137 C  CZ  . PHE   C  1 408 ? 18.609  33.994  -84.886  1.00 31.78  ? 709  PHE   C CZ  1 
ATOM   10138 N  N   . GLU   C  1 409 ? 16.360  28.211  -81.368  1.00 29.81  ? 710  GLU   C N   1 
ATOM   10139 C  CA  . GLU   C  1 409 ? 16.149  27.063  -80.509  1.00 32.39  ? 710  GLU   C CA  1 
ATOM   10140 C  C   . GLU   C  1 409 ? 17.280  26.087  -80.746  1.00 36.08  ? 710  GLU   C C   1 
ATOM   10141 O  O   . GLU   C  1 409 ? 17.972  26.146  -81.758  1.00 56.61  ? 710  GLU   C O   1 
ATOM   10142 C  CB  . GLU   C  1 409 ? 14.803  26.367  -80.791  1.00 31.81  ? 710  GLU   C CB  1 
ATOM   10143 C  CG  . GLU   C  1 409 ? 13.549  27.274  -80.731  1.00 39.63  ? 710  GLU   C CG  1 
ATOM   10144 C  CD  . GLU   C  1 409 ? 13.207  27.786  -79.307  1.00 59.58  ? 710  GLU   C CD  1 
ATOM   10145 O  OE1 . GLU   C  1 409 ? 13.783  27.287  -78.310  1.00 60.88  ? 710  GLU   C OE1 1 
ATOM   10146 O  OE2 . GLU   C  1 409 ? 12.333  28.683  -79.185  1.00 62.97  ? 710  GLU   C OE2 1 
ATOM   10147 N  N   . TYR   C  1 410 ? 17.475  25.191  -79.806  1.00 37.70  ? 711  TYR   C N   1 
ATOM   10148 C  CA  . TYR   C  1 410 ? 18.367  24.093  -80.093  1.00 39.79  ? 711  TYR   C CA  1 
ATOM   10149 C  C   . TYR   C  1 410 ? 17.615  23.025  -80.858  1.00 49.06  ? 711  TYR   C C   1 
ATOM   10150 O  O   . TYR   C  1 410 ? 16.385  23.056  -80.989  1.00 54.42  ? 711  TYR   C O   1 
ATOM   10151 C  CB  . TYR   C  1 410 ? 18.937  23.501  -78.808  1.00 53.34  ? 711  TYR   C CB  1 
ATOM   10152 C  CG  . TYR   C  1 410 ? 19.752  24.484  -78.037  1.00 53.68  ? 711  TYR   C CG  1 
ATOM   10153 C  CD1 . TYR   C  1 410 ? 19.232  25.116  -76.928  1.00 59.74  ? 711  TYR   C CD1 1 
ATOM   10154 C  CD2 . TYR   C  1 410 ? 21.038  24.795  -78.433  1.00 56.23  ? 711  TYR   C CD2 1 
ATOM   10155 C  CE1 . TYR   C  1 410 ? 19.972  26.033  -76.230  1.00 59.27  ? 711  TYR   C CE1 1 
ATOM   10156 C  CE2 . TYR   C  1 410 ? 21.793  25.715  -77.734  1.00 58.38  ? 711  TYR   C CE2 1 
ATOM   10157 C  CZ  . TYR   C  1 410 ? 21.252  26.329  -76.637  1.00 59.91  ? 711  TYR   C CZ  1 
ATOM   10158 O  OH  . TYR   C  1 410 ? 21.998  27.231  -75.932  1.00 68.75  ? 711  TYR   C OH  1 
ATOM   10159 N  N   . GLN   C  1 411 ? 18.376  22.064  -81.357  1.00 51.27  ? 712  GLN   C N   1 
ATOM   10160 C  CA  . GLN   C  1 411 ? 17.838  20.939  -82.099  1.00 50.34  ? 712  GLN   C CA  1 
ATOM   10161 C  C   . GLN   C  1 411 ? 18.838  19.811  -82.002  1.00 45.61  ? 712  GLN   C C   1 
ATOM   10162 O  O   . GLN   C  1 411 ? 20.026  20.056  -81.759  1.00 53.18  ? 712  GLN   C O   1 
ATOM   10163 C  CB  . GLN   C  1 411 ? 17.561  21.312  -83.569  1.00 42.47  ? 712  GLN   C CB  1 
ATOM   10164 C  CG  . GLN   C  1 411 ? 18.780  21.643  -84.399  1.00 40.41  ? 712  GLN   C CG  1 
ATOM   10165 C  CD  . GLN   C  1 411 ? 18.385  22.181  -85.774  1.00 49.80  ? 712  GLN   C CD  1 
ATOM   10166 O  OE1 . GLN   C  1 411 ? 17.527  21.611  -86.463  1.00 45.07  ? 712  GLN   C OE1 1 
ATOM   10167 N  NE2 . GLN   C  1 411 ? 18.987  23.303  -86.160  1.00 42.56  ? 712  GLN   C NE2 1 
ATOM   10168 N  N   . PRO   C  1 412 ? 18.394  18.573  -82.158  1.00 39.95  ? 713  PRO   C N   1 
ATOM   10169 C  CA  . PRO   C  1 412 ? 19.312  17.442  -82.036  1.00 48.74  ? 713  PRO   C CA  1 
ATOM   10170 C  C   . PRO   C  1 412 ? 20.457  17.553  -83.030  1.00 59.66  ? 713  PRO   C C   1 
ATOM   10171 O  O   . PRO   C  1 412 ? 20.345  18.217  -84.060  1.00 71.25  ? 713  PRO   C O   1 
ATOM   10172 C  CB  . PRO   C  1 412 ? 18.417  16.237  -82.340  1.00 51.94  ? 713  PRO   C CB  1 
ATOM   10173 C  CG  . PRO   C  1 412 ? 17.017  16.711  -82.005  1.00 42.35  ? 713  PRO   C CG  1 
ATOM   10174 C  CD  . PRO   C  1 412 ? 16.994  18.153  -82.355  1.00 41.68  ? 713  PRO   C CD  1 
ATOM   10175 N  N   . ASP   C  1 413 ? 21.586  16.944  -82.681  1.00 61.11  ? 714  ASP   C N   1 
ATOM   10176 C  CA  . ASP   C  1 413 ? 22.661  16.774  -83.644  1.00 62.68  ? 714  ASP   C CA  1 
ATOM   10177 C  C   . ASP   C  1 413 ? 22.166  15.842  -84.742  1.00 68.46  ? 714  ASP   C C   1 
ATOM   10178 O  O   . ASP   C  1 413 ? 21.614  14.776  -84.432  1.00 70.33  ? 714  ASP   C O   1 
ATOM   10179 C  CB  . ASP   C  1 413 ? 23.906  16.179  -82.988  1.00 71.78  ? 714  ASP   C CB  1 
ATOM   10180 C  CG  . ASP   C  1 413 ? 24.415  17.003  -81.816  1.00 76.06  ? 714  ASP   C CG  1 
ATOM   10181 O  OD1 . ASP   C  1 413 ? 24.546  18.238  -81.976  1.00 77.38  ? 714  ASP   C OD1 1 
ATOM   10182 O  OD2 . ASP   C  1 413 ? 24.692  16.407  -80.743  1.00 72.96  ? 714  ASP   C OD2 1 
ATOM   10183 N  N   . PRO   C  1 414 ? 22.337  16.196  -86.022  1.00 66.64  ? 715  PRO   C N   1 
ATOM   10184 C  CA  . PRO   C  1 414 ? 21.682  15.409  -87.087  1.00 56.99  ? 715  PRO   C CA  1 
ATOM   10185 C  C   . PRO   C  1 414 ? 22.066  13.938  -87.097  1.00 66.43  ? 715  PRO   C C   1 
ATOM   10186 O  O   . PRO   C  1 414 ? 21.196  13.082  -87.302  1.00 79.23  ? 715  PRO   C O   1 
ATOM   10187 C  CB  . PRO   C  1 414 ? 22.118  16.124  -88.377  1.00 49.11  ? 715  PRO   C CB  1 
ATOM   10188 C  CG  . PRO   C  1 414 ? 23.266  16.992  -87.998  1.00 55.75  ? 715  PRO   C CG  1 
ATOM   10189 C  CD  . PRO   C  1 414 ? 23.078  17.353  -86.552  1.00 62.21  ? 715  PRO   C CD  1 
ATOM   10190 N  N   . TRP   C  1 415 ? 23.333  13.608  -86.849  1.00 66.17  ? 716  TRP   C N   1 
ATOM   10191 C  CA  . TRP   C  1 415 ? 23.765  12.218  -86.946  1.00 66.02  ? 716  TRP   C CA  1 
ATOM   10192 C  C   . TRP   C  1 415 ? 23.084  11.304  -85.930  1.00 71.73  ? 716  TRP   C C   1 
ATOM   10193 O  O   . TRP   C  1 415 ? 23.064  10.086  -86.139  1.00 75.08  ? 716  TRP   C O   1 
ATOM   10194 C  CB  . TRP   C  1 415 ? 25.279  12.132  -86.790  1.00 69.62  ? 716  TRP   C CB  1 
ATOM   10195 C  CG  . TRP   C  1 415 ? 25.772  12.671  -85.493  1.00 74.75  ? 716  TRP   C CG  1 
ATOM   10196 C  CD1 . TRP   C  1 415 ? 25.853  12.003  -84.307  1.00 80.91  ? 716  TRP   C CD1 1 
ATOM   10197 C  CD2 . TRP   C  1 415 ? 26.256  13.997  -85.242  1.00 70.12  ? 716  TRP   C CD2 1 
ATOM   10198 N  NE1 . TRP   C  1 415 ? 26.367  12.827  -83.333  1.00 80.82  ? 716  TRP   C NE1 1 
ATOM   10199 C  CE2 . TRP   C  1 415 ? 26.622  14.057  -83.884  1.00 73.20  ? 716  TRP   C CE2 1 
ATOM   10200 C  CE3 . TRP   C  1 415 ? 26.419  15.133  -86.031  1.00 67.09  ? 716  TRP   C CE3 1 
ATOM   10201 C  CZ2 . TRP   C  1 415 ? 27.136  15.209  -83.304  1.00 67.39  ? 716  TRP   C CZ2 1 
ATOM   10202 C  CZ3 . TRP   C  1 415 ? 26.926  16.274  -85.451  1.00 65.07  ? 716  TRP   C CZ3 1 
ATOM   10203 C  CH2 . TRP   C  1 415 ? 27.278  16.304  -84.105  1.00 67.06  ? 716  TRP   C CH2 1 
ATOM   10204 N  N   . ASN   C  1 416 ? 22.534  11.845  -84.836  1.00 74.59  ? 717  ASN   C N   1 
ATOM   10205 C  CA  . ASN   C  1 416 ? 21.684  11.025  -83.974  1.00 76.67  ? 717  ASN   C CA  1 
ATOM   10206 C  C   . ASN   C  1 416 ? 20.411  10.576  -84.682  1.00 80.01  ? 717  ASN   C C   1 
ATOM   10207 O  O   . ASN   C  1 416 ? 19.803  9.581   -84.266  1.00 74.07  ? 717  ASN   C O   1 
ATOM   10208 C  CB  . ASN   C  1 416 ? 21.269  11.775  -82.701  1.00 71.32  ? 717  ASN   C CB  1 
ATOM   10209 C  CG  . ASN   C  1 416 ? 22.441  12.325  -81.920  1.00 68.94  ? 717  ASN   C CG  1 
ATOM   10210 O  OD1 . ASN   C  1 416 ? 23.549  11.786  -81.964  1.00 71.74  ? 717  ASN   C OD1 1 
ATOM   10211 N  ND2 . ASN   C  1 416 ? 22.198  13.412  -81.188  1.00 64.37  ? 717  ASN   C ND2 1 
ATOM   10212 N  N   . THR   C  1 417 ? 19.998  11.283  -85.744  1.00 84.60  ? 718  THR   C N   1 
ATOM   10213 C  CA  . THR   C  1 417 ? 18.645  11.174  -86.270  1.00 83.06  ? 718  THR   C CA  1 
ATOM   10214 C  C   . THR   C  1 417 ? 18.545  10.967  -87.780  1.00 86.92  ? 718  THR   C C   1 
ATOM   10215 O  O   . THR   C  1 417 ? 17.428  10.805  -88.283  1.00 92.71  ? 718  THR   C O   1 
ATOM   10216 C  CB  . THR   C  1 417 ? 17.849  12.431  -85.897  1.00 70.01  ? 718  THR   C CB  1 
ATOM   10217 O  OG1 . THR   C  1 417 ? 18.572  13.584  -86.337  1.00 70.12  ? 718  THR   C OG1 1 
ATOM   10218 C  CG2 . THR   C  1 417 ? 17.671  12.523  -84.398  1.00 64.02  ? 718  THR   C CG2 1 
ATOM   10219 N  N   . HIS   C  1 418 ? 19.658  10.945  -88.512  1.00 87.71  ? 719  HIS   C N   1 
ATOM   10220 C  CA  . HIS   C  1 418 ? 19.630  10.958  -89.972  1.00 91.53  ? 719  HIS   C CA  1 
ATOM   10221 C  C   . HIS   C  1 418 ? 19.609  9.545   -90.541  1.00 97.09  ? 719  HIS   C C   1 
ATOM   10222 O  O   . HIS   C  1 418 ? 20.484  8.732   -90.232  1.00 89.78  ? 719  HIS   C O   1 
ATOM   10223 C  CB  . HIS   C  1 418 ? 20.841  11.712  -90.517  1.00 87.09  ? 719  HIS   C CB  1 
ATOM   10224 C  CG  . HIS   C  1 418 ? 21.077  11.502  -91.978  1.00 84.79  ? 719  HIS   C CG  1 
ATOM   10225 N  ND1 . HIS   C  1 418 ? 20.308  12.105  -92.949  1.00 86.43  ? 719  HIS   C ND1 1 
ATOM   10226 C  CD2 . HIS   C  1 418 ? 21.999  10.758  -92.634  1.00 86.63  ? 719  HIS   C CD2 1 
ATOM   10227 C  CE1 . HIS   C  1 418 ? 20.748  11.744  -94.142  1.00 87.45  ? 719  HIS   C CE1 1 
ATOM   10228 N  NE2 . HIS   C  1 418 ? 21.771  10.924  -93.979  1.00 87.06  ? 719  HIS   C NE2 1 
ATOM   10229 N  N   . VAL   C  1 419 ? 18.626  9.268   -91.396  1.00 114.47 ? 720  VAL   C N   1 
ATOM   10230 C  CA  . VAL   C  1 419 ? 18.500  7.965   -92.046  1.00 124.22 ? 720  VAL   C CA  1 
ATOM   10231 C  C   . VAL   C  1 419 ? 19.415  7.956   -93.266  1.00 127.94 ? 720  VAL   C C   1 
ATOM   10232 O  O   . VAL   C  1 419 ? 19.110  8.585   -94.281  1.00 135.48 ? 720  VAL   C O   1 
ATOM   10233 C  CB  . VAL   C  1 419 ? 17.048  7.671   -92.442  1.00 128.47 ? 720  VAL   C CB  1 
ATOM   10234 C  CG1 . VAL   C  1 419 ? 16.937  6.269   -93.028  1.00 131.15 ? 720  VAL   C CG1 1 
ATOM   10235 C  CG2 . VAL   C  1 419 ? 16.129  7.821   -91.239  1.00 128.69 ? 720  VAL   C CG2 1 
ATOM   10236 N  N   . TRP   C  1 420 ? 20.534  7.233   -93.176  1.00 115.20 ? 721  TRP   C N   1 
ATOM   10237 C  CA  . TRP   C  1 420 ? 21.571  7.313   -94.202  1.00 107.56 ? 721  TRP   C CA  1 
ATOM   10238 C  C   . TRP   C  1 420 ? 21.149  6.637   -95.504  1.00 105.50 ? 721  TRP   C C   1 
ATOM   10239 O  O   . TRP   C  1 420 ? 20.337  5.706   -95.516  1.00 109.55 ? 721  TRP   C O   1 
ATOM   10240 C  CB  . TRP   C  1 420 ? 22.868  6.682   -93.702  1.00 104.78 ? 721  TRP   C CB  1 
ATOM   10241 C  CG  . TRP   C  1 420 ? 23.726  7.630   -92.933  1.00 102.27 ? 721  TRP   C CG  1 
ATOM   10242 C  CD1 . TRP   C  1 420 ? 23.662  7.895   -91.595  1.00 98.31  ? 721  TRP   C CD1 1 
ATOM   10243 C  CD2 . TRP   C  1 420 ? 24.781  8.449   -93.456  1.00 96.56  ? 721  TRP   C CD2 1 
ATOM   10244 N  NE1 . TRP   C  1 420 ? 24.612  8.828   -91.251  1.00 91.17  ? 721  TRP   C NE1 1 
ATOM   10245 C  CE2 . TRP   C  1 420 ? 25.314  9.182   -92.374  1.00 89.88  ? 721  TRP   C CE2 1 
ATOM   10246 C  CE3 . TRP   C  1 420 ? 25.326  8.633   -94.732  1.00 91.33  ? 721  TRP   C CE3 1 
ATOM   10247 C  CZ2 . TRP   C  1 420 ? 26.369  10.085  -92.529  1.00 82.46  ? 721  TRP   C CZ2 1 
ATOM   10248 C  CZ3 . TRP   C  1 420 ? 26.375  9.530   -94.884  1.00 84.05  ? 721  TRP   C CZ3 1 
ATOM   10249 C  CH2 . TRP   C  1 420 ? 26.884  10.245  -93.788  1.00 81.94  ? 721  TRP   C CH2 1 
ATOM   10250 N  N   . LYS   C  1 421 ? 21.727  7.112   -96.611  1.00 93.90  ? 722  LYS   C N   1 
ATOM   10251 C  CA  . LYS   C  1 421 ? 21.425  6.560   -97.936  1.00 93.33  ? 722  LYS   C CA  1 
ATOM   10252 C  C   . LYS   C  1 421 ? 22.642  5.866   -98.562  1.00 94.92  ? 722  LYS   C C   1 
ATOM   10253 O  O   . LYS   C  1 421 ? 22.547  4.761   -99.101  1.00 94.32  ? 722  LYS   C O   1 
ATOM   10254 C  CB  . LYS   C  1 421 ? 20.921  7.658   -98.881  1.00 88.65  ? 722  LYS   C CB  1 
ATOM   10255 C  CG  . LYS   C  1 421 ? 19.927  8.637   -98.263  1.00 81.47  ? 722  LYS   C CG  1 
ATOM   10256 C  CD  . LYS   C  1 421 ? 18.667  8.759   -99.105  1.00 80.00  ? 722  LYS   C CD  1 
ATOM   10257 C  CE  . LYS   C  1 421 ? 18.092  10.177  -99.057  1.00 79.77  ? 722  LYS   C CE  1 
ATOM   10258 N  NZ  . LYS   C  1 421 ? 16.900  10.312  -98.150  1.00 79.49  ? 722  LYS   C NZ  1 
ATOM   10259 N  N   . ARG   D  1 3   ? 7.623   10.903  -60.376  1.00 96.07  ? 304  ARG   D N   1 
ATOM   10260 C  CA  . ARG   D  1 3   ? 8.555   11.252  -61.447  1.00 107.21 ? 304  ARG   D CA  1 
ATOM   10261 C  C   . ARG   D  1 3   ? 9.854   11.834  -60.887  1.00 108.48 ? 304  ARG   D C   1 
ATOM   10262 O  O   . ARG   D  1 3   ? 9.956   12.159  -59.702  1.00 113.32 ? 304  ARG   D O   1 
ATOM   10263 C  CB  . ARG   D  1 3   ? 7.917   12.236  -62.450  1.00 111.83 ? 304  ARG   D CB  1 
ATOM   10264 C  CG  . ARG   D  1 3   ? 7.822   13.704  -62.000  1.00 103.16 ? 304  ARG   D CG  1 
ATOM   10265 C  CD  . ARG   D  1 3   ? 6.995   13.844  -60.722  1.00 101.22 ? 304  ARG   D CD  1 
ATOM   10266 N  NE  . ARG   D  1 3   ? 6.352   15.145  -60.577  1.00 100.63 ? 304  ARG   D NE  1 
ATOM   10267 C  CZ  . ARG   D  1 3   ? 7.003   16.294  -60.425  1.00 103.28 ? 304  ARG   D CZ  1 
ATOM   10268 N  NH1 . ARG   D  1 3   ? 8.332   16.323  -60.417  1.00 106.09 ? 304  ARG   D NH1 1 
ATOM   10269 N  NH2 . ARG   D  1 3   ? 6.320   17.422  -60.290  1.00 100.77 ? 304  ARG   D NH2 1 
ATOM   10270 N  N   . PHE   D  1 4   ? 10.846  11.959  -61.756  1.00 99.66  ? 305  PHE   D N   1 
ATOM   10271 C  CA  . PHE   D  1 4   ? 12.206  12.295  -61.381  1.00 87.48  ? 305  PHE   D CA  1 
ATOM   10272 C  C   . PHE   D  1 4   ? 12.634  13.544  -62.145  1.00 80.32  ? 305  PHE   D C   1 
ATOM   10273 O  O   . PHE   D  1 4   ? 11.860  14.120  -62.912  1.00 83.01  ? 305  PHE   D O   1 
ATOM   10274 C  CB  . PHE   D  1 4   ? 13.140  11.112  -61.656  1.00 90.70  ? 305  PHE   D CB  1 
ATOM   10275 C  CG  . PHE   D  1 4   ? 12.741  9.833   -60.943  1.00 105.09 ? 305  PHE   D CG  1 
ATOM   10276 C  CD1 . PHE   D  1 4   ? 11.639  9.090   -61.365  1.00 114.57 ? 305  PHE   D CD1 1 
ATOM   10277 C  CD2 . PHE   D  1 4   ? 13.481  9.359   -59.868  1.00 104.96 ? 305  PHE   D CD2 1 
ATOM   10278 C  CE1 . PHE   D  1 4   ? 11.271  7.915   -60.712  1.00 113.81 ? 305  PHE   D CE1 1 
ATOM   10279 C  CE2 . PHE   D  1 4   ? 13.124  8.178   -59.212  1.00 104.93 ? 305  PHE   D CE2 1 
ATOM   10280 C  CZ  . PHE   D  1 4   ? 12.019  7.457   -59.634  1.00 108.01 ? 305  PHE   D CZ  1 
ATOM   10281 N  N   . LEU   D  1 5   ? 13.879  13.962  -61.925  1.00 68.01  ? 306  LEU   D N   1 
ATOM   10282 C  CA  . LEU   D  1 5   ? 14.435  15.128  -62.604  1.00 55.91  ? 306  LEU   D CA  1 
ATOM   10283 C  C   . LEU   D  1 5   ? 15.946  15.012  -62.586  1.00 58.26  ? 306  LEU   D C   1 
ATOM   10284 O  O   . LEU   D  1 5   ? 16.528  14.796  -61.522  1.00 68.52  ? 306  LEU   D O   1 
ATOM   10285 C  CB  . LEU   D  1 5   ? 14.004  16.424  -61.928  1.00 51.10  ? 306  LEU   D CB  1 
ATOM   10286 C  CG  . LEU   D  1 5   ? 12.992  17.285  -62.674  1.00 59.32  ? 306  LEU   D CG  1 
ATOM   10287 C  CD1 . LEU   D  1 5   ? 12.545  18.442  -61.804  1.00 57.21  ? 306  LEU   D CD1 1 
ATOM   10288 C  CD2 . LEU   D  1 5   ? 13.601  17.793  -63.975  1.00 71.07  ? 306  LEU   D CD2 1 
ATOM   10289 N  N   . LYS   D  1 6   ? 16.580  15.158  -63.745  1.00 52.97  ? 307  LYS   D N   1 
ATOM   10290 C  CA  . LYS   D  1 6   ? 18.010  14.920  -63.848  1.00 44.89  ? 307  LYS   D CA  1 
ATOM   10291 C  C   . LYS   D  1 6   ? 18.757  16.229  -64.017  1.00 50.16  ? 307  LYS   D C   1 
ATOM   10292 O  O   . LYS   D  1 6   ? 18.238  17.199  -64.582  1.00 58.48  ? 307  LYS   D O   1 
ATOM   10293 C  CB  . LYS   D  1 6   ? 18.343  13.967  -64.999  1.00 48.04  ? 307  LYS   D CB  1 
ATOM   10294 C  CG  . LYS   D  1 6   ? 17.814  12.550  -64.764  1.00 53.29  ? 307  LYS   D CG  1 
ATOM   10295 C  CD  . LYS   D  1 6   ? 18.593  11.517  -65.550  1.00 64.40  ? 307  LYS   D CD  1 
ATOM   10296 C  CE  . LYS   D  1 6   ? 18.124  10.105  -65.214  1.00 75.33  ? 307  LYS   D CE  1 
ATOM   10297 N  NZ  . LYS   D  1 6   ? 19.180  9.071   -65.478  1.00 81.50  ? 307  LYS   D NZ  1 
ATOM   10298 N  N   . VAL   D  1 7   ? 19.970  16.249  -63.471  1.00 43.75  ? 308  VAL   D N   1 
ATOM   10299 C  CA  . VAL   D  1 7   ? 20.912  17.339  -63.658  1.00 46.74  ? 308  VAL   D CA  1 
ATOM   10300 C  C   . VAL   D  1 7   ? 22.180  16.719  -64.213  1.00 46.67  ? 308  VAL   D C   1 
ATOM   10301 O  O   . VAL   D  1 7   ? 22.412  15.514  -64.100  1.00 54.11  ? 308  VAL   D O   1 
ATOM   10302 C  CB  . VAL   D  1 7   ? 21.203  18.132  -62.366  1.00 45.69  ? 308  VAL   D CB  1 
ATOM   10303 C  CG1 . VAL   D  1 7   ? 19.929  18.735  -61.826  1.00 42.51  ? 308  VAL   D CG1 1 
ATOM   10304 C  CG2 . VAL   D  1 7   ? 21.854  17.240  -61.350  1.00 51.20  ? 308  VAL   D CG2 1 
ATOM   10305 N  N   . LYS   D  1 8   ? 23.002  17.560  -64.821  1.00 44.13  ? 309  LYS   D N   1 
ATOM   10306 C  CA  . LYS   D  1 8   ? 24.103  17.099  -65.646  1.00 51.29  ? 309  LYS   D CA  1 
ATOM   10307 C  C   . LYS   D  1 8   ? 25.283  18.020  -65.429  1.00 52.47  ? 309  LYS   D C   1 
ATOM   10308 O  O   . LYS   D  1 8   ? 25.116  19.241  -65.369  1.00 55.11  ? 309  LYS   D O   1 
ATOM   10309 C  CB  . LYS   D  1 8   ? 23.720  17.087  -67.142  1.00 46.71  ? 309  LYS   D CB  1 
ATOM   10310 C  CG  . LYS   D  1 8   ? 24.738  16.402  -68.047  1.00 55.08  ? 309  LYS   D CG  1 
ATOM   10311 C  CD  . LYS   D  1 8   ? 24.572  16.785  -69.529  1.00 56.24  ? 309  LYS   D CD  1 
ATOM   10312 C  CE  . LYS   D  1 8   ? 25.661  16.168  -70.377  1.00 59.14  ? 309  LYS   D CE  1 
ATOM   10313 N  NZ  . LYS   D  1 8   ? 25.390  16.324  -71.832  1.00 65.97  ? 309  LYS   D NZ  1 
ATOM   10314 N  N   . ASN   D  1 9   ? 26.468  17.431  -65.302  1.00 53.43  ? 310  ASN   D N   1 
ATOM   10315 C  CA  . ASN   D  1 9   ? 27.708  18.191  -65.304  1.00 53.21  ? 310  ASN   D CA  1 
ATOM   10316 C  C   . ASN   D  1 9   ? 28.227  18.209  -66.731  1.00 48.04  ? 310  ASN   D C   1 
ATOM   10317 O  O   . ASN   D  1 9   ? 28.533  17.157  -67.296  1.00 44.31  ? 310  ASN   D O   1 
ATOM   10318 C  CB  . ASN   D  1 9   ? 28.741  17.587  -64.353  1.00 56.73  ? 310  ASN   D CB  1 
ATOM   10319 C  CG  . ASN   D  1 9   ? 29.863  18.552  -64.028  1.00 56.35  ? 310  ASN   D CG  1 
ATOM   10320 O  OD1 . ASN   D  1 9   ? 30.825  18.683  -64.785  1.00 56.97  ? 310  ASN   D OD1 1 
ATOM   10321 N  ND2 . ASN   D  1 9   ? 29.743  19.235  -62.896  1.00 65.69  ? 310  ASN   D ND2 1 
ATOM   10322 N  N   . TRP   D  1 10  ? 28.291  19.396  -67.325  1.00 59.82  ? 311  TRP   D N   1 
ATOM   10323 C  CA  . TRP   D  1 10  ? 28.707  19.501  -68.716  1.00 54.61  ? 311  TRP   D CA  1 
ATOM   10324 C  C   . TRP   D  1 10  ? 30.217  19.413  -68.883  1.00 58.40  ? 311  TRP   D C   1 
ATOM   10325 O  O   . TRP   D  1 10  ? 30.691  19.274  -70.015  1.00 66.88  ? 311  TRP   D O   1 
ATOM   10326 C  CB  . TRP   D  1 10  ? 28.165  20.796  -69.321  1.00 41.65  ? 311  TRP   D CB  1 
ATOM   10327 C  CG  . TRP   D  1 10  ? 26.696  20.741  -69.538  1.00 47.16  ? 311  TRP   D CG  1 
ATOM   10328 C  CD1 . TRP   D  1 10  ? 25.719  21.138  -68.673  1.00 47.74  ? 311  TRP   D CD1 1 
ATOM   10329 C  CD2 . TRP   D  1 10  ? 26.022  20.235  -70.695  1.00 46.79  ? 311  TRP   D CD2 1 
ATOM   10330 N  NE1 . TRP   D  1 10  ? 24.477  20.919  -69.226  1.00 50.57  ? 311  TRP   D NE1 1 
ATOM   10331 C  CE2 . TRP   D  1 10  ? 24.638  20.366  -70.468  1.00 47.39  ? 311  TRP   D CE2 1 
ATOM   10332 C  CE3 . TRP   D  1 10  ? 26.456  19.680  -71.900  1.00 47.06  ? 311  TRP   D CE3 1 
ATOM   10333 C  CZ2 . TRP   D  1 10  ? 23.690  19.968  -71.401  1.00 58.42  ? 311  TRP   D CZ2 1 
ATOM   10334 C  CZ3 . TRP   D  1 10  ? 25.505  19.292  -72.837  1.00 52.00  ? 311  TRP   D CZ3 1 
ATOM   10335 C  CH2 . TRP   D  1 10  ? 24.142  19.441  -72.582  1.00 54.56  ? 311  TRP   D CH2 1 
ATOM   10336 N  N   . GLU   D  1 11  ? 30.970  19.485  -67.787  1.00 55.52  ? 312  GLU   D N   1 
ATOM   10337 C  CA  . GLU   D  1 11  ? 32.407  19.229  -67.805  1.00 61.08  ? 312  GLU   D CA  1 
ATOM   10338 C  C   . GLU   D  1 11  ? 32.696  17.729  -67.743  1.00 63.50  ? 312  GLU   D C   1 
ATOM   10339 O  O   . GLU   D  1 11  ? 33.530  17.224  -68.504  1.00 67.97  ? 312  GLU   D O   1 
ATOM   10340 C  CB  . GLU   D  1 11  ? 33.070  19.962  -66.625  1.00 58.05  ? 312  GLU   D CB  1 
ATOM   10341 C  CG  . GLU   D  1 11  ? 34.576  20.089  -66.678  1.00 60.00  ? 312  GLU   D CG  1 
ATOM   10342 C  CD  . GLU   D  1 11  ? 35.195  20.394  -65.311  1.00 69.00  ? 312  GLU   D CD  1 
ATOM   10343 O  OE1 . GLU   D  1 11  ? 34.523  21.041  -64.476  1.00 67.07  ? 312  GLU   D OE1 1 
ATOM   10344 O  OE2 . GLU   D  1 11  ? 36.354  19.976  -65.071  1.00 66.02  ? 312  GLU   D OE2 1 
ATOM   10345 N  N   . THR   D  1 12  ? 31.990  17.001  -66.867  1.00 55.84  ? 313  THR   D N   1 
ATOM   10346 C  CA  . THR   D  1 12  ? 32.273  15.606  -66.565  1.00 48.94  ? 313  THR   D CA  1 
ATOM   10347 C  C   . THR   D  1 12  ? 31.255  14.621  -67.123  1.00 56.99  ? 313  THR   D C   1 
ATOM   10348 O  O   . THR   D  1 12  ? 31.537  13.419  -67.136  1.00 63.39  ? 313  THR   D O   1 
ATOM   10349 C  CB  . THR   D  1 12  ? 32.351  15.399  -65.044  1.00 56.23  ? 313  THR   D CB  1 
ATOM   10350 O  OG1 . THR   D  1 12  ? 31.032  15.425  -64.486  1.00 52.73  ? 313  THR   D OG1 1 
ATOM   10351 C  CG2 . THR   D  1 12  ? 33.194  16.487  -64.398  1.00 61.28  ? 313  THR   D CG2 1 
ATOM   10352 N  N   . GLU   D  1 13  ? 30.088  15.086  -67.575  1.00 57.04  ? 314  GLU   D N   1 
ATOM   10353 C  CA  . GLU   D  1 13  ? 28.960  14.279  -68.061  1.00 63.96  ? 314  GLU   D CA  1 
ATOM   10354 C  C   . GLU   D  1 13  ? 28.319  13.416  -66.971  1.00 66.67  ? 314  GLU   D C   1 
ATOM   10355 O  O   . GLU   D  1 13  ? 27.430  12.601  -67.278  1.00 64.40  ? 314  GLU   D O   1 
ATOM   10356 C  CB  . GLU   D  1 13  ? 29.338  13.395  -69.263  1.00 67.87  ? 314  GLU   D CB  1 
ATOM   10357 C  CG  . GLU   D  1 13  ? 30.449  13.938  -70.148  1.00 67.08  ? 314  GLU   D CG  1 
ATOM   10358 C  CD  . GLU   D  1 13  ? 30.040  14.113  -71.582  1.00 82.96  ? 314  GLU   D CD  1 
ATOM   10359 O  OE1 . GLU   D  1 13  ? 28.888  14.543  -71.829  1.00 87.78  ? 314  GLU   D OE1 1 
ATOM   10360 O  OE2 . GLU   D  1 13  ? 30.881  13.826  -72.464  1.00 90.27  ? 314  GLU   D OE2 1 
ATOM   10361 N  N   . VAL   D  1 14  ? 28.725  13.585  -65.706  1.00 65.04  ? 315  VAL   D N   1 
ATOM   10362 C  CA  . VAL   D  1 14  ? 28.048  12.931  -64.591  1.00 57.90  ? 315  VAL   D CA  1 
ATOM   10363 C  C   . VAL   D  1 14  ? 26.598  13.390  -64.526  1.00 60.39  ? 315  VAL   D C   1 
ATOM   10364 O  O   . VAL   D  1 14  ? 26.300  14.586  -64.660  1.00 61.58  ? 315  VAL   D O   1 
ATOM   10365 C  CB  . VAL   D  1 14  ? 28.781  13.250  -63.277  1.00 62.21  ? 315  VAL   D CB  1 
ATOM   10366 C  CG1 . VAL   D  1 14  ? 27.992  12.748  -62.073  1.00 51.39  ? 315  VAL   D CG1 1 
ATOM   10367 C  CG2 . VAL   D  1 14  ? 30.176  12.662  -63.293  1.00 68.01  ? 315  VAL   D CG2 1 
ATOM   10368 N  N   . VAL   D  1 15  ? 25.681  12.447  -64.296  1.00 55.73  ? 316  VAL   D N   1 
ATOM   10369 C  CA  . VAL   D  1 15  ? 24.259  12.767  -64.232  1.00 51.60  ? 316  VAL   D CA  1 
ATOM   10370 C  C   . VAL   D  1 15  ? 23.662  12.239  -62.935  1.00 48.04  ? 316  VAL   D C   1 
ATOM   10371 O  O   . VAL   D  1 15  ? 23.908  11.095  -62.543  1.00 54.90  ? 316  VAL   D O   1 
ATOM   10372 C  CB  . VAL   D  1 15  ? 23.498  12.216  -65.453  1.00 51.89  ? 316  VAL   D CB  1 
ATOM   10373 C  CG1 . VAL   D  1 15  ? 22.030  12.658  -65.417  1.00 45.22  ? 316  VAL   D CG1 1 
ATOM   10374 C  CG2 . VAL   D  1 15  ? 24.184  12.686  -66.731  1.00 48.39  ? 316  VAL   D CG2 1 
ATOM   10375 N  N   . LEU   D  1 16  ? 22.863  13.083  -62.278  1.00 51.29  ? 317  LEU   D N   1 
ATOM   10376 C  CA  . LEU   D  1 16  ? 22.279  12.823  -60.968  1.00 52.01  ? 317  LEU   D CA  1 
ATOM   10377 C  C   . LEU   D  1 16  ? 20.774  13.008  -61.052  1.00 57.97  ? 317  LEU   D C   1 
ATOM   10378 O  O   . LEU   D  1 16  ? 20.284  13.864  -61.794  1.00 57.62  ? 317  LEU   D O   1 
ATOM   10379 C  CB  . LEU   D  1 16  ? 22.834  13.771  -59.892  1.00 41.66  ? 317  LEU   D CB  1 
ATOM   10380 C  CG  . LEU   D  1 16  ? 24.347  13.924  -59.840  1.00 44.96  ? 317  LEU   D CG  1 
ATOM   10381 C  CD1 . LEU   D  1 16  ? 24.718  14.965  -58.811  1.00 39.45  ? 317  LEU   D CD1 1 
ATOM   10382 C  CD2 . LEU   D  1 16  ? 24.984  12.580  -59.501  1.00 53.69  ? 317  LEU   D CD2 1 
ATOM   10383 N  N   . THR   D  1 17  ? 20.047  12.227  -60.253  1.00 62.44  ? 318  THR   D N   1 
ATOM   10384 C  CA  . THR   D  1 17  ? 18.590  12.139  -60.323  1.00 63.18  ? 318  THR   D CA  1 
ATOM   10385 C  C   . THR   D  1 17  ? 17.962  12.697  -59.046  1.00 63.88  ? 318  THR   D C   1 
ATOM   10386 O  O   . THR   D  1 17  ? 18.025  12.076  -57.979  1.00 68.83  ? 318  THR   D O   1 
ATOM   10387 C  CB  . THR   D  1 17  ? 18.154  10.697  -60.547  1.00 59.03  ? 318  THR   D CB  1 
ATOM   10388 O  OG1 . THR   D  1 17  ? 18.641  10.250  -61.814  1.00 51.54  ? 318  THR   D OG1 1 
ATOM   10389 C  CG2 . THR   D  1 17  ? 16.639  10.590  -60.507  1.00 60.01  ? 318  THR   D CG2 1 
ATOM   10390 N  N   . ASP   D  1 18  ? 17.318  13.842  -59.172  1.00 58.27  ? 319  ASP   D N   1 
ATOM   10391 C  CA  . ASP   D  1 18  ? 16.803  14.577  -58.030  1.00 56.35  ? 319  ASP   D CA  1 
ATOM   10392 C  C   . ASP   D  1 18  ? 15.371  14.140  -57.765  1.00 57.52  ? 319  ASP   D C   1 
ATOM   10393 O  O   . ASP   D  1 18  ? 14.457  14.521  -58.501  1.00 68.18  ? 319  ASP   D O   1 
ATOM   10394 C  CB  . ASP   D  1 18  ? 16.886  16.072  -58.316  1.00 59.41  ? 319  ASP   D CB  1 
ATOM   10395 C  CG  . ASP   D  1 18  ? 16.482  16.912  -57.142  1.00 62.36  ? 319  ASP   D CG  1 
ATOM   10396 O  OD1 . ASP   D  1 18  ? 15.328  16.765  -56.685  1.00 64.15  ? 319  ASP   D OD1 1 
ATOM   10397 O  OD2 . ASP   D  1 18  ? 17.323  17.719  -56.680  1.00 61.60  ? 319  ASP   D OD2 1 
ATOM   10398 N  N   . THR   D  1 19  ? 15.173  13.349  -56.711  1.00 50.92  ? 320  THR   D N   1 
ATOM   10399 C  CA  . THR   D  1 19  ? 13.830  13.071  -56.214  1.00 52.30  ? 320  THR   D CA  1 
ATOM   10400 C  C   . THR   D  1 19  ? 13.431  13.933  -55.015  1.00 55.90  ? 320  THR   D C   1 
ATOM   10401 O  O   . THR   D  1 19  ? 12.232  14.056  -54.741  1.00 58.76  ? 320  THR   D O   1 
ATOM   10402 C  CB  . THR   D  1 19  ? 13.706  11.602  -55.817  1.00 50.05  ? 320  THR   D CB  1 
ATOM   10403 O  OG1 . THR   D  1 19  ? 14.374  11.409  -54.565  1.00 49.51  ? 320  THR   D OG1 1 
ATOM   10404 C  CG2 . THR   D  1 19  ? 14.360  10.728  -56.852  1.00 44.88  ? 320  THR   D CG2 1 
ATOM   10405 N  N   . LEU   D  1 20  ? 14.394  14.540  -54.311  1.00 47.55  ? 321  LEU   D N   1 
ATOM   10406 C  CA  . LEU   D  1 20  ? 14.094  15.305  -53.098  1.00 55.88  ? 321  LEU   D CA  1 
ATOM   10407 C  C   . LEU   D  1 20  ? 13.212  16.518  -53.369  1.00 56.25  ? 321  LEU   D C   1 
ATOM   10408 O  O   . LEU   D  1 20  ? 12.513  16.975  -52.458  1.00 55.25  ? 321  LEU   D O   1 
ATOM   10409 C  CB  . LEU   D  1 20  ? 15.397  15.762  -52.423  1.00 46.86  ? 321  LEU   D CB  1 
ATOM   10410 C  CG  . LEU   D  1 20  ? 15.298  16.506  -51.088  1.00 54.89  ? 321  LEU   D CG  1 
ATOM   10411 C  CD1 . LEU   D  1 20  ? 14.848  15.556  -49.996  1.00 53.00  ? 321  LEU   D CD1 1 
ATOM   10412 C  CD2 . LEU   D  1 20  ? 16.620  17.182  -50.705  1.00 51.39  ? 321  LEU   D CD2 1 
ATOM   10413 N  N   . HIS   D  1 21  ? 13.234  17.055  -54.596  1.00 53.42  ? 322  HIS   D N   1 
ATOM   10414 C  CA  . HIS   D  1 21  ? 12.461  18.255  -54.897  1.00 49.11  ? 322  HIS   D CA  1 
ATOM   10415 C  C   . HIS   D  1 21  ? 10.972  18.016  -54.746  1.00 42.43  ? 322  HIS   D C   1 
ATOM   10416 O  O   . HIS   D  1 21  ? 10.222  18.981  -54.574  1.00 43.93  ? 322  HIS   D O   1 
ATOM   10417 C  CB  . HIS   D  1 21  ? 12.758  18.750  -56.314  1.00 58.67  ? 322  HIS   D CB  1 
ATOM   10418 C  CG  . HIS   D  1 21  ? 12.160  17.887  -57.380  1.00 58.92  ? 322  HIS   D CG  1 
ATOM   10419 N  ND1 . HIS   D  1 21  ? 12.779  16.748  -57.851  1.00 58.73  ? 322  HIS   D ND1 1 
ATOM   10420 C  CD2 . HIS   D  1 21  ? 10.981  17.975  -58.037  1.00 57.53  ? 322  HIS   D CD2 1 
ATOM   10421 C  CE1 . HIS   D  1 21  ? 12.003  16.170  -58.751  1.00 59.41  ? 322  HIS   D CE1 1 
ATOM   10422 N  NE2 . HIS   D  1 21  ? 10.909  16.896  -58.886  1.00 62.28  ? 322  HIS   D NE2 1 
ATOM   10423 N  N   . LEU   D  1 22  ? 10.534  16.755  -54.791  1.00 46.94  ? 323  LEU   D N   1 
ATOM   10424 C  CA  . LEU   D  1 22  ? 9.123   16.437  -54.587  1.00 50.70  ? 323  LEU   D CA  1 
ATOM   10425 C  C   . LEU   D  1 22  ? 8.608   16.956  -53.255  1.00 61.41  ? 323  LEU   D C   1 
ATOM   10426 O  O   . LEU   D  1 22  ? 7.413   17.242  -53.122  1.00 65.76  ? 323  LEU   D O   1 
ATOM   10427 C  CB  . LEU   D  1 22  ? 8.913   14.924  -54.648  1.00 48.91  ? 323  LEU   D CB  1 
ATOM   10428 C  CG  . LEU   D  1 22  ? 9.400   14.189  -55.897  1.00 52.55  ? 323  LEU   D CG  1 
ATOM   10429 C  CD1 . LEU   D  1 22  ? 9.413   12.679  -55.660  1.00 53.11  ? 323  LEU   D CD1 1 
ATOM   10430 C  CD2 . LEU   D  1 22  ? 8.551   14.554  -57.116  1.00 46.81  ? 323  LEU   D CD2 1 
ATOM   10431 N  N   . LYS   D  1 23  ? 9.489   17.087  -52.264  1.00 61.50  ? 324  LYS   D N   1 
ATOM   10432 C  CA  . LYS   D  1 23  ? 9.104   17.358  -50.891  1.00 51.20  ? 324  LYS   D CA  1 
ATOM   10433 C  C   . LYS   D  1 23  ? 9.153   18.831  -50.513  1.00 60.03  ? 324  LYS   D C   1 
ATOM   10434 O  O   . LYS   D  1 23  ? 8.859   19.162  -49.362  1.00 70.99  ? 324  LYS   D O   1 
ATOM   10435 C  CB  . LYS   D  1 23  ? 9.981   16.541  -49.945  1.00 52.82  ? 324  LYS   D CB  1 
ATOM   10436 C  CG  . LYS   D  1 23  ? 9.480   15.105  -49.783  1.00 69.77  ? 324  LYS   D CG  1 
ATOM   10437 C  CD  . LYS   D  1 23  ? 10.258  14.326  -48.746  1.00 79.61  ? 324  LYS   D CD  1 
ATOM   10438 C  CE  . LYS   D  1 23  ? 11.690  14.086  -49.204  1.00 83.11  ? 324  LYS   D CE  1 
ATOM   10439 N  NZ  . LYS   D  1 23  ? 11.773  13.363  -50.509  1.00 85.23  ? 324  LYS   D NZ  1 
ATOM   10440 N  N   . SER   D  1 24  ? 9.523   19.721  -51.429  1.00 59.09  ? 325  SER   D N   1 
ATOM   10441 C  CA  . SER   D  1 24  ? 9.487   21.149  -51.137  1.00 64.53  ? 325  SER   D CA  1 
ATOM   10442 C  C   . SER   D  1 24  ? 8.062   21.652  -51.279  1.00 67.21  ? 325  SER   D C   1 
ATOM   10443 O  O   . SER   D  1 24  ? 7.316   21.166  -52.126  1.00 71.62  ? 325  SER   D O   1 
ATOM   10444 C  CB  . SER   D  1 24  ? 10.408  21.927  -52.077  1.00 66.73  ? 325  SER   D CB  1 
ATOM   10445 O  OG  . SER   D  1 24  ? 9.953   21.857  -53.417  1.00 69.89  ? 325  SER   D OG  1 
ATOM   10446 N  N   . THR   D  1 25  ? 7.672   22.606  -50.431  1.00 71.00  ? 326  THR   D N   1 
ATOM   10447 C  CA  . THR   D  1 25  ? 6.353   23.234  -50.548  1.00 84.99  ? 326  THR   D CA  1 
ATOM   10448 C  C   . THR   D  1 25  ? 6.441   24.711  -50.201  1.00 80.33  ? 326  THR   D C   1 
ATOM   10449 O  O   . THR   D  1 25  ? 5.606   25.250  -49.471  1.00 84.33  ? 326  THR   D O   1 
ATOM   10450 C  CB  . THR   D  1 25  ? 5.294   22.544  -49.675  1.00 92.22  ? 326  THR   D CB  1 
ATOM   10451 O  OG1 . THR   D  1 25  ? 5.634   21.164  -49.481  1.00 97.80  ? 326  THR   D OG1 1 
ATOM   10452 C  CG2 . THR   D  1 25  ? 3.913   22.617  -50.345  1.00 85.20  ? 326  THR   D CG2 1 
ATOM   10453 N  N   . LEU   D  1 26  ? 7.461   25.381  -50.716  1.00 76.51  ? 327  LEU   D N   1 
ATOM   10454 C  CA  . LEU   D  1 26  ? 7.591   26.822  -50.586  1.00 82.25  ? 327  LEU   D CA  1 
ATOM   10455 C  C   . LEU   D  1 26  ? 7.956   27.406  -51.946  1.00 85.49  ? 327  LEU   D C   1 
ATOM   10456 O  O   . LEU   D  1 26  ? 8.644   26.769  -52.750  1.00 90.73  ? 327  LEU   D O   1 
ATOM   10457 C  CB  . LEU   D  1 26  ? 8.646   27.196  -49.529  1.00 86.08  ? 327  LEU   D CB  1 
ATOM   10458 C  CG  . LEU   D  1 26  ? 8.415   26.671  -48.107  1.00 84.26  ? 327  LEU   D CG  1 
ATOM   10459 C  CD1 . LEU   D  1 26  ? 9.571   27.038  -47.194  1.00 79.50  ? 327  LEU   D CD1 1 
ATOM   10460 C  CD2 . LEU   D  1 26  ? 7.110   27.213  -47.548  1.00 86.40  ? 327  LEU   D CD2 1 
ATOM   10461 N  N   . GLU   D  1 27  ? 7.487   28.625  -52.194  1.00 76.08  ? 328  GLU   D N   1 
ATOM   10462 C  CA  . GLU   D  1 27  ? 7.683   29.263  -53.488  1.00 68.15  ? 328  GLU   D CA  1 
ATOM   10463 C  C   . GLU   D  1 27  ? 9.150   29.600  -53.731  1.00 72.18  ? 328  GLU   D C   1 
ATOM   10464 O  O   . GLU   D  1 27  ? 9.873   29.995  -52.813  1.00 77.18  ? 328  GLU   D O   1 
ATOM   10465 C  CB  . GLU   D  1 27  ? 6.850   30.538  -53.576  1.00 66.15  ? 328  GLU   D CB  1 
ATOM   10466 C  CG  . GLU   D  1 27  ? 5.371   30.334  -53.847  1.00 70.50  ? 328  GLU   D CG  1 
ATOM   10467 C  CD  . GLU   D  1 27  ? 4.633   31.655  -53.992  1.00 84.78  ? 328  GLU   D CD  1 
ATOM   10468 O  OE1 . GLU   D  1 27  ? 3.387   31.656  -53.873  1.00 89.25  ? 328  GLU   D OE1 1 
ATOM   10469 O  OE2 . GLU   D  1 27  ? 5.302   32.694  -54.217  1.00 89.37  ? 328  GLU   D OE2 1 
ATOM   10470 N  N   . THR   D  1 28  ? 9.582   29.447  -54.988  1.00 67.40  ? 329  THR   D N   1 
ATOM   10471 C  CA  . THR   D  1 28  ? 10.871  29.947  -55.451  1.00 58.13  ? 329  THR   D CA  1 
ATOM   10472 C  C   . THR   D  1 28  ? 10.782  31.347  -56.025  1.00 51.15  ? 329  THR   D C   1 
ATOM   10473 O  O   . THR   D  1 28  ? 11.819  31.983  -56.227  1.00 54.09  ? 329  THR   D O   1 
ATOM   10474 C  CB  . THR   D  1 28  ? 11.441  29.048  -56.552  1.00 69.89  ? 329  THR   D CB  1 
ATOM   10475 O  OG1 . THR   D  1 28  ? 10.475  28.923  -57.614  1.00 70.30  ? 329  THR   D OG1 1 
ATOM   10476 C  CG2 . THR   D  1 28  ? 11.825  27.668  -56.004  1.00 75.33  ? 329  THR   D CG2 1 
ATOM   10477 N  N   . GLY   D  1 29  ? 9.573   31.822  -56.328  1.00 54.59  ? 330  GLY   D N   1 
ATOM   10478 C  CA  . GLY   D  1 29  ? 9.356   33.058  -57.034  1.00 57.26  ? 330  GLY   D CA  1 
ATOM   10479 C  C   . GLY   D  1 29  ? 9.112   32.865  -58.517  1.00 61.40  ? 330  GLY   D C   1 
ATOM   10480 O  O   . GLY   D  1 29  ? 8.319   33.609  -59.115  1.00 64.64  ? 330  GLY   D O   1 
ATOM   10481 N  N   . CYS   D  1 30  ? 9.765   31.876  -59.119  1.00 54.57  ? 331  CYS   D N   1 
ATOM   10482 C  CA  . CYS   D  1 30  ? 9.577   31.600  -60.537  1.00 45.68  ? 331  CYS   D CA  1 
ATOM   10483 C  C   . CYS   D  1 30  ? 8.156   31.136  -60.807  1.00 47.62  ? 331  CYS   D C   1 
ATOM   10484 O  O   . CYS   D  1 30  ? 7.588   30.348  -60.048  1.00 57.63  ? 331  CYS   D O   1 
ATOM   10485 C  CB  . CYS   D  1 30  ? 10.563  30.526  -61.013  1.00 42.83  ? 331  CYS   D CB  1 
ATOM   10486 S  SG  . CYS   D  1 30  ? 12.325  30.993  -61.057  1.00 49.12  ? 331  CYS   D SG  1 
ATOM   10487 N  N   . THR   D  1 31  ? 7.585   31.607  -61.907  1.00 54.34  ? 332  THR   D N   1 
ATOM   10488 C  CA  . THR   D  1 31  ? 6.325   31.069  -62.386  1.00 53.19  ? 332  THR   D CA  1 
ATOM   10489 C  C   . THR   D  1 31  ? 6.611   30.036  -63.464  1.00 48.74  ? 332  THR   D C   1 
ATOM   10490 O  O   . THR   D  1 31  ? 7.762   29.748  -63.798  1.00 50.45  ? 332  THR   D O   1 
ATOM   10491 C  CB  . THR   D  1 31  ? 5.410   32.171  -62.920  1.00 64.41  ? 332  THR   D CB  1 
ATOM   10492 O  OG1 . THR   D  1 31  ? 5.767   32.469  -64.278  1.00 73.21  ? 332  THR   D OG1 1 
ATOM   10493 C  CG2 . THR   D  1 31  ? 5.519   33.442  -62.050  1.00 59.15  ? 332  THR   D CG2 1 
ATOM   10494 N  N   . GLU   D  1 32  ? 5.544   29.463  -64.011  1.00 46.61  ? 333  GLU   D N   1 
ATOM   10495 C  CA  . GLU   D  1 32  ? 5.698   28.451  -65.048  1.00 57.27  ? 333  GLU   D CA  1 
ATOM   10496 C  C   . GLU   D  1 32  ? 6.275   29.037  -66.331  1.00 55.88  ? 333  GLU   D C   1 
ATOM   10497 O  O   . GLU   D  1 32  ? 6.920   28.315  -67.108  1.00 52.45  ? 333  GLU   D O   1 
ATOM   10498 C  CB  . GLU   D  1 32  ? 4.344   27.801  -65.327  1.00 69.25  ? 333  GLU   D CB  1 
ATOM   10499 C  CG  . GLU   D  1 32  ? 4.409   26.302  -65.474  1.00 79.15  ? 333  GLU   D CG  1 
ATOM   10500 C  CD  . GLU   D  1 32  ? 3.157   25.606  -64.972  1.00 85.45  ? 333  GLU   D CD  1 
ATOM   10501 O  OE1 . GLU   D  1 32  ? 2.040   26.139  -65.190  1.00 83.37  ? 333  GLU   D OE1 1 
ATOM   10502 O  OE2 . GLU   D  1 32  ? 3.303   24.524  -64.352  1.00 85.76  ? 333  GLU   D OE2 1 
ATOM   10503 N  N   . TYR   D  1 33  ? 6.053   30.340  -66.558  1.00 47.39  ? 334  TYR   D N   1 
ATOM   10504 C  CA  . TYR   D  1 33  ? 6.418   31.026  -67.788  1.00 38.62  ? 334  TYR   D CA  1 
ATOM   10505 C  C   . TYR   D  1 33  ? 7.335   32.218  -67.571  1.00 46.09  ? 334  TYR   D C   1 
ATOM   10506 O  O   . TYR   D  1 33  ? 7.577   32.961  -68.524  1.00 43.12  ? 334  TYR   D O   1 
ATOM   10507 C  CB  . TYR   D  1 33  ? 5.162   31.528  -68.523  1.00 52.37  ? 334  TYR   D CB  1 
ATOM   10508 C  CG  . TYR   D  1 33  ? 4.263   30.454  -69.126  1.00 60.30  ? 334  TYR   D CG  1 
ATOM   10509 C  CD1 . TYR   D  1 33  ? 4.368   30.101  -70.468  1.00 65.11  ? 334  TYR   D CD1 1 
ATOM   10510 C  CD2 . TYR   D  1 33  ? 3.306   29.810  -68.356  1.00 66.14  ? 334  TYR   D CD2 1 
ATOM   10511 C  CE1 . TYR   D  1 33  ? 3.547   29.124  -71.022  1.00 67.72  ? 334  TYR   D CE1 1 
ATOM   10512 C  CE2 . TYR   D  1 33  ? 2.486   28.837  -68.898  1.00 69.05  ? 334  TYR   D CE2 1 
ATOM   10513 C  CZ  . TYR   D  1 33  ? 2.605   28.497  -70.230  1.00 67.06  ? 334  TYR   D CZ  1 
ATOM   10514 O  OH  . TYR   D  1 33  ? 1.786   27.517  -70.758  1.00 69.00  ? 334  TYR   D OH  1 
ATOM   10515 N  N   . ILE   D  1 34  ? 7.791   32.467  -66.346  1.00 51.92  ? 335  ILE   D N   1 
ATOM   10516 C  CA  . ILE   D  1 34  ? 8.797   33.487  -66.057  1.00 50.06  ? 335  ILE   D CA  1 
ATOM   10517 C  C   . ILE   D  1 34  ? 9.776   32.869  -65.079  1.00 43.92  ? 335  ILE   D C   1 
ATOM   10518 O  O   . ILE   D  1 34  ? 9.366   32.124  -64.185  1.00 51.39  ? 335  ILE   D O   1 
ATOM   10519 C  CB  . ILE   D  1 34  ? 8.188   34.785  -65.473  1.00 51.70  ? 335  ILE   D CB  1 
ATOM   10520 C  CG1 . ILE   D  1 34  ? 7.541   35.641  -66.563  1.00 71.40  ? 335  ILE   D CG1 1 
ATOM   10521 C  CG2 . ILE   D  1 34  ? 9.259   35.621  -64.772  1.00 49.74  ? 335  ILE   D CG2 1 
ATOM   10522 C  CD1 . ILE   D  1 34  ? 6.071   35.338  -66.868  1.00 83.37  ? 335  ILE   D CD1 1 
ATOM   10523 N  N   . CYS   D  1 35  ? 11.070  33.147  -65.257  1.00 40.80  ? 336  CYS   D N   1 
ATOM   10524 C  CA  . CYS   D  1 35  ? 12.086  32.713  -64.305  1.00 40.47  ? 336  CYS   D CA  1 
ATOM   10525 C  C   . CYS   D  1 35  ? 12.659  33.919  -63.573  1.00 53.19  ? 336  CYS   D C   1 
ATOM   10526 O  O   . CYS   D  1 35  ? 12.977  34.939  -64.193  1.00 50.52  ? 336  CYS   D O   1 
ATOM   10527 C  CB  . CYS   D  1 35  ? 13.234  31.940  -64.973  1.00 46.81  ? 336  CYS   D CB  1 
ATOM   10528 S  SG  . CYS   D  1 35  ? 14.636  31.500  -63.817  1.00 47.20  ? 336  CYS   D SG  1 
ATOM   10529 N  N   . MET   D  1 36  ? 12.796  33.790  -62.246  1.00 60.80  ? 337  MET   D N   1 
ATOM   10530 C  CA  . MET   D  1 36  ? 13.272  34.873  -61.387  1.00 59.28  ? 337  MET   D CA  1 
ATOM   10531 C  C   . MET   D  1 36  ? 14.514  34.460  -60.610  1.00 49.52  ? 337  MET   D C   1 
ATOM   10532 O  O   . MET   D  1 36  ? 14.790  35.000  -59.537  1.00 56.32  ? 337  MET   D O   1 
ATOM   10533 C  CB  . MET   D  1 36  ? 12.156  35.338  -60.445  1.00 54.36  ? 337  MET   D CB  1 
ATOM   10534 C  CG  . MET   D  1 36  ? 10.857  35.612  -61.193  1.00 59.15  ? 337  MET   D CG  1 
ATOM   10535 S  SD  . MET   D  1 36  ? 9.634   36.648  -60.385  1.00 68.57  ? 337  MET   D SD  1 
ATOM   10536 C  CE  . MET   D  1 36  ? 10.571  38.147  -60.125  1.00 73.21  ? 337  MET   D CE  1 
ATOM   10537 N  N   . GLY   D  1 37  ? 15.275  33.513  -61.152  1.00 45.87  ? 338  GLY   D N   1 
ATOM   10538 C  CA  . GLY   D  1 37  ? 16.431  32.937  -60.489  1.00 48.18  ? 338  GLY   D CA  1 
ATOM   10539 C  C   . GLY   D  1 37  ? 17.548  33.907  -60.180  1.00 44.79  ? 338  GLY   D C   1 
ATOM   10540 O  O   . GLY   D  1 37  ? 18.482  33.524  -59.468  1.00 53.43  ? 338  GLY   D O   1 
ATOM   10541 N  N   . SER   D  1 38  ? 17.500  35.132  -60.704  1.00 44.65  ? 339  SER   D N   1 
ATOM   10542 C  CA  . SER   D  1 38  ? 18.501  36.150  -60.390  1.00 43.64  ? 339  SER   D CA  1 
ATOM   10543 C  C   . SER   D  1 38  ? 17.935  37.301  -59.571  1.00 39.20  ? 339  SER   D C   1 
ATOM   10544 O  O   . SER   D  1 38  ? 18.669  38.254  -59.273  1.00 46.38  ? 339  SER   D O   1 
ATOM   10545 C  CB  . SER   D  1 38  ? 19.140  36.705  -61.672  1.00 49.43  ? 339  SER   D CB  1 
ATOM   10546 O  OG  . SER   D  1 38  ? 18.224  37.468  -62.460  1.00 50.86  ? 339  SER   D OG  1 
ATOM   10547 N  N   . ILE   D  1 39  ? 16.645  37.256  -59.228  1.00 42.40  ? 340  ILE   D N   1 
ATOM   10548 C  CA  . ILE   D  1 39  ? 16.063  38.242  -58.320  1.00 45.74  ? 340  ILE   D CA  1 
ATOM   10549 C  C   . ILE   D  1 39  ? 16.541  37.943  -56.902  1.00 44.93  ? 340  ILE   D C   1 
ATOM   10550 O  O   . ILE   D  1 39  ? 16.433  36.801  -56.424  1.00 47.10  ? 340  ILE   D O   1 
ATOM   10551 C  CB  . ILE   D  1 39  ? 14.529  38.212  -58.411  1.00 39.85  ? 340  ILE   D CB  1 
ATOM   10552 C  CG1 . ILE   D  1 39  ? 14.076  38.231  -59.875  1.00 45.61  ? 340  ILE   D CG1 1 
ATOM   10553 C  CG2 . ILE   D  1 39  ? 13.911  39.352  -57.620  1.00 48.97  ? 340  ILE   D CG2 1 
ATOM   10554 C  CD1 . ILE   D  1 39  ? 14.638  39.365  -60.672  1.00 40.21  ? 340  ILE   D CD1 1 
ATOM   10555 N  N   . MET   D  1 40  ? 17.079  38.963  -56.223  1.00 39.82  ? 341  MET   D N   1 
ATOM   10556 C  CA  . MET   D  1 40  ? 17.684  38.734  -54.908  1.00 52.98  ? 341  MET   D CA  1 
ATOM   10557 C  C   . MET   D  1 40  ? 16.650  38.328  -53.859  1.00 55.85  ? 341  MET   D C   1 
ATOM   10558 O  O   . MET   D  1 40  ? 16.856  37.349  -53.131  1.00 56.63  ? 341  MET   D O   1 
ATOM   10559 C  CB  . MET   D  1 40  ? 18.453  39.965  -54.445  1.00 62.90  ? 341  MET   D CB  1 
ATOM   10560 C  CG  . MET   D  1 40  ? 19.297  39.676  -53.212  1.00 82.72  ? 341  MET   D CG  1 
ATOM   10561 S  SD  . MET   D  1 40  ? 20.707  40.786  -53.039  1.00 94.33  ? 341  MET   D SD  1 
ATOM   10562 C  CE  . MET   D  1 40  ? 21.725  40.209  -54.380  1.00 82.99  ? 341  MET   D CE  1 
ATOM   10563 N  N   . HIS   D  1 41  ? 15.557  39.083  -53.734  1.00 59.76  ? 342  HIS   D N   1 
ATOM   10564 C  CA  . HIS   D  1 41  ? 14.426  38.695  -52.879  1.00 67.54  ? 342  HIS   D CA  1 
ATOM   10565 C  C   . HIS   D  1 41  ? 13.169  38.581  -53.738  1.00 76.93  ? 342  HIS   D C   1 
ATOM   10566 O  O   . HIS   D  1 41  ? 12.666  39.612  -54.226  1.00 82.14  ? 342  HIS   D O   1 
ATOM   10567 C  CB  . HIS   D  1 41  ? 14.171  39.698  -51.743  1.00 71.60  ? 342  HIS   D CB  1 
ATOM   10568 C  CG  . HIS   D  1 41  ? 15.396  40.124  -50.983  1.00 72.70  ? 342  HIS   D CG  1 
ATOM   10569 N  ND1 . HIS   D  1 41  ? 16.131  39.260  -50.196  1.00 72.48  ? 342  HIS   D ND1 1 
ATOM   10570 C  CD2 . HIS   D  1 41  ? 15.992  41.336  -50.863  1.00 71.26  ? 342  HIS   D CD2 1 
ATOM   10571 C  CE1 . HIS   D  1 41  ? 17.142  39.915  -49.651  1.00 69.77  ? 342  HIS   D CE1 1 
ATOM   10572 N  NE2 . HIS   D  1 41  ? 17.080  41.176  -50.038  1.00 68.79  ? 342  HIS   D NE2 1 
ATOM   10573 N  N   . PRO   D  1 42  ? 12.615  37.386  -53.971  1.00 78.47  ? 343  PRO   D N   1 
ATOM   10574 C  CA  . PRO   D  1 42  ? 11.317  37.315  -54.657  1.00 81.76  ? 343  PRO   D CA  1 
ATOM   10575 C  C   . PRO   D  1 42  ? 10.191  37.022  -53.677  1.00 92.02  ? 343  PRO   D C   1 
ATOM   10576 O  O   . PRO   D  1 42  ? 10.395  36.313  -52.684  1.00 101.54 ? 343  PRO   D O   1 
ATOM   10577 C  CB  . PRO   D  1 42  ? 11.508  36.174  -55.669  1.00 77.20  ? 343  PRO   D CB  1 
ATOM   10578 C  CG  . PRO   D  1 42  ? 12.813  35.472  -55.259  1.00 79.54  ? 343  PRO   D CG  1 
ATOM   10579 C  CD  . PRO   D  1 42  ? 13.249  36.064  -53.923  1.00 75.31  ? 343  PRO   D CD  1 
ATOM   10580 N  N   . SER   D  1 43  ? 9.004   37.568  -53.930  1.00 91.93  ? 344  SER   D N   1 
ATOM   10581 C  CA  . SER   D  1 43  ? 7.884   37.383  -53.008  1.00 92.23  ? 344  SER   D CA  1 
ATOM   10582 C  C   . SER   D  1 43  ? 6.899   36.349  -53.536  1.00 92.45  ? 344  SER   D C   1 
ATOM   10583 O  O   . SER   D  1 43  ? 5.851   36.125  -52.932  1.00 96.14  ? 344  SER   D O   1 
ATOM   10584 C  CB  . SER   D  1 43  ? 7.156   38.707  -52.753  1.00 85.74  ? 344  SER   D CB  1 
ATOM   10585 O  OG  . SER   D  1 43  ? 6.310   39.049  -53.840  1.00 74.63  ? 344  SER   D OG  1 
ATOM   10586 N  N   . PRO   D  1 49  ? 4.437   42.321  -37.715  1.00 109.57 ? 350  PRO   D N   1 
ATOM   10587 C  CA  . PRO   D  1 49  ? 3.945   42.026  -36.363  1.00 115.06 ? 350  PRO   D CA  1 
ATOM   10588 C  C   . PRO   D  1 49  ? 2.742   41.075  -36.346  1.00 121.31 ? 350  PRO   D C   1 
ATOM   10589 O  O   . PRO   D  1 49  ? 2.700   40.141  -35.543  1.00 116.56 ? 350  PRO   D O   1 
ATOM   10590 C  CB  . PRO   D  1 49  ? 3.569   43.410  -35.832  1.00 112.36 ? 350  PRO   D CB  1 
ATOM   10591 C  CG  . PRO   D  1 49  ? 4.591   44.302  -36.458  1.00 110.14 ? 350  PRO   D CG  1 
ATOM   10592 C  CD  . PRO   D  1 49  ? 4.844   43.731  -37.851  1.00 108.73 ? 350  PRO   D CD  1 
ATOM   10593 N  N   . GLU   D  1 50  ? 1.769   41.312  -37.225  1.00 132.18 ? 351  GLU   D N   1 
ATOM   10594 C  CA  . GLU   D  1 50  ? 0.691   40.350  -37.431  1.00 135.55 ? 351  GLU   D CA  1 
ATOM   10595 C  C   . GLU   D  1 50  ? 1.131   39.163  -38.291  1.00 132.89 ? 351  GLU   D C   1 
ATOM   10596 O  O   . GLU   D  1 50  ? 0.308   38.286  -38.571  1.00 124.91 ? 351  GLU   D O   1 
ATOM   10597 C  CB  . GLU   D  1 50  ? -0.531  41.040  -38.056  1.00 137.86 ? 351  GLU   D CB  1 
ATOM   10598 C  CG  . GLU   D  1 50  ? -1.673  41.395  -37.057  1.00 136.66 ? 351  GLU   D CG  1 
ATOM   10599 C  CD  . GLU   D  1 50  ? -1.343  42.552  -36.104  1.00 128.31 ? 351  GLU   D CD  1 
ATOM   10600 O  OE1 . GLU   D  1 50  ? -0.527  42.355  -35.170  1.00 126.63 ? 351  GLU   D OE1 1 
ATOM   10601 O  OE2 . GLU   D  1 50  ? -1.906  43.656  -36.295  1.00 120.54 ? 351  GLU   D OE2 1 
ATOM   10602 N  N   . ASP   D  1 51  ? 2.403   39.118  -38.706  1.00 140.38 ? 352  ASP   D N   1 
ATOM   10603 C  CA  . ASP   D  1 51  ? 2.971   37.957  -39.387  1.00 137.38 ? 352  ASP   D CA  1 
ATOM   10604 C  C   . ASP   D  1 51  ? 3.284   36.863  -38.361  1.00 129.63 ? 352  ASP   D C   1 
ATOM   10605 O  O   . ASP   D  1 51  ? 4.438   36.484  -38.161  1.00 134.73 ? 352  ASP   D O   1 
ATOM   10606 C  CB  . ASP   D  1 51  ? 4.237   38.320  -40.175  1.00 137.18 ? 352  ASP   D CB  1 
ATOM   10607 C  CG  . ASP   D  1 51  ? 4.270   39.787  -40.631  1.00 135.13 ? 352  ASP   D CG  1 
ATOM   10608 O  OD1 . ASP   D  1 51  ? 4.954   40.598  -39.962  1.00 130.37 ? 352  ASP   D OD1 1 
ATOM   10609 O  OD2 . ASP   D  1 51  ? 3.600   40.137  -41.638  1.00 135.29 ? 352  ASP   D OD2 1 
ATOM   10610 N  N   . VAL   D  1 52  ? 2.240   36.387  -37.678  1.00 101.33 ? 353  VAL   D N   1 
ATOM   10611 C  CA  . VAL   D  1 52  ? 2.346   35.274  -36.735  1.00 79.67  ? 353  VAL   D CA  1 
ATOM   10612 C  C   . VAL   D  1 52  ? 1.288   34.245  -37.078  1.00 63.97  ? 353  VAL   D C   1 
ATOM   10613 O  O   . VAL   D  1 52  ? 0.096   34.569  -37.131  1.00 57.19  ? 353  VAL   D O   1 
ATOM   10614 C  CB  . VAL   D  1 52  ? 2.189   35.717  -35.265  1.00 77.64  ? 353  VAL   D CB  1 
ATOM   10615 C  CG1 . VAL   D  1 52  ? 3.497   36.261  -34.735  1.00 71.48  ? 353  VAL   D CG1 1 
ATOM   10616 C  CG2 . VAL   D  1 52  ? 1.055   36.750  -35.131  1.00 83.47  ? 353  VAL   D CG2 1 
ATOM   10617 N  N   . ALA   D  1 53  ? 1.724   33.009  -37.284  1.00 57.29  ? 354  ALA   D N   1 
ATOM   10618 C  CA  . ALA   D  1 53  ? 0.826   31.945  -37.695  1.00 72.87  ? 354  ALA   D CA  1 
ATOM   10619 C  C   . ALA   D  1 53  ? -0.315  31.769  -36.697  1.00 73.13  ? 354  ALA   D C   1 
ATOM   10620 O  O   . ALA   D  1 53  ? -0.156  31.970  -35.492  1.00 79.72  ? 354  ALA   D O   1 
ATOM   10621 C  CB  . ALA   D  1 53  ? 1.602   30.637  -37.846  1.00 77.87  ? 354  ALA   D CB  1 
ATOM   10622 N  N   . THR   D  1 54  ? -1.484  31.412  -37.221  1.00 71.94  ? 355  THR   D N   1 
ATOM   10623 C  CA  . THR   D  1 54  ? -2.626  31.042  -36.406  1.00 78.25  ? 355  THR   D CA  1 
ATOM   10624 C  C   . THR   D  1 54  ? -2.456  29.622  -35.872  1.00 85.38  ? 355  THR   D C   1 
ATOM   10625 O  O   . THR   D  1 54  ? -1.550  28.883  -36.271  1.00 88.06  ? 355  THR   D O   1 
ATOM   10626 C  CB  . THR   D  1 54  ? -3.913  31.136  -37.219  1.00 81.27  ? 355  THR   D CB  1 
ATOM   10627 O  OG1 . THR   D  1 54  ? -3.878  30.172  -38.280  1.00 85.48  ? 355  THR   D OG1 1 
ATOM   10628 C  CG2 . THR   D  1 54  ? -4.057  32.520  -37.822  1.00 83.65  ? 355  THR   D CG2 1 
ATOM   10629 N  N   . LYS   D  1 55  ? -3.345  29.240  -34.950  1.00 89.73  ? 356  LYS   D N   1 
ATOM   10630 C  CA  . LYS   D  1 55  ? -3.362  27.860  -34.475  1.00 82.86  ? 356  LYS   D CA  1 
ATOM   10631 C  C   . LYS   D  1 55  ? -3.464  26.890  -35.645  1.00 82.27  ? 356  LYS   D C   1 
ATOM   10632 O  O   . LYS   D  1 55  ? -2.717  25.911  -35.727  1.00 80.20  ? 356  LYS   D O   1 
ATOM   10633 C  CB  . LYS   D  1 55  ? -4.525  27.641  -33.503  1.00 74.31  ? 356  LYS   D CB  1 
ATOM   10634 C  CG  . LYS   D  1 55  ? -4.268  28.091  -32.090  1.00 65.62  ? 356  LYS   D CG  1 
ATOM   10635 C  CD  . LYS   D  1 55  ? -5.450  27.777  -31.198  1.00 60.75  ? 356  LYS   D CD  1 
ATOM   10636 C  CE  . LYS   D  1 55  ? -5.140  28.177  -29.761  1.00 71.39  ? 356  LYS   D CE  1 
ATOM   10637 N  NZ  . LYS   D  1 55  ? -6.225  27.857  -28.775  1.00 71.50  ? 356  LYS   D NZ  1 
ATOM   10638 N  N   . ASP   D  1 56  ? -4.378  27.169  -36.577  1.00 86.93  ? 357  ASP   D N   1 
ATOM   10639 C  CA  . ASP   D  1 56  ? -4.645  26.230  -37.663  1.00 90.69  ? 357  ASP   D CA  1 
ATOM   10640 C  C   . ASP   D  1 56  ? -3.533  26.229  -38.700  1.00 82.01  ? 357  ASP   D C   1 
ATOM   10641 O  O   . ASP   D  1 56  ? -3.314  25.211  -39.362  1.00 88.57  ? 357  ASP   D O   1 
ATOM   10642 C  CB  . ASP   D  1 56  ? -5.984  26.552  -38.326  1.00 93.85  ? 357  ASP   D CB  1 
ATOM   10643 C  CG  . ASP   D  1 56  ? -7.152  26.408  -37.373  1.00 92.88  ? 357  ASP   D CG  1 
ATOM   10644 O  OD1 . ASP   D  1 56  ? -7.023  25.664  -36.372  1.00 83.76  ? 357  ASP   D OD1 1 
ATOM   10645 O  OD2 . ASP   D  1 56  ? -8.200  27.036  -37.633  1.00 97.27  ? 357  ASP   D OD2 1 
ATOM   10646 N  N   . GLN   D  1 57  ? -2.832  27.349  -38.873  1.00 68.81  ? 358  GLN   D N   1 
ATOM   10647 C  CA  . GLN   D  1 57  ? -1.664  27.322  -39.740  1.00 59.53  ? 358  GLN   D CA  1 
ATOM   10648 C  C   . GLN   D  1 57  ? -0.532  26.522  -39.114  1.00 63.82  ? 358  GLN   D C   1 
ATOM   10649 O  O   . GLN   D  1 57  ? 0.264   25.921  -39.840  1.00 57.21  ? 358  GLN   D O   1 
ATOM   10650 C  CB  . GLN   D  1 57  ? -1.195  28.742  -40.053  1.00 65.51  ? 358  GLN   D CB  1 
ATOM   10651 C  CG  . GLN   D  1 57  ? -2.178  29.576  -40.871  1.00 77.78  ? 358  GLN   D CG  1 
ATOM   10652 C  CD  . GLN   D  1 57  ? -1.686  31.002  -41.114  1.00 85.42  ? 358  GLN   D CD  1 
ATOM   10653 O  OE1 . GLN   D  1 57  ? -1.331  31.732  -40.180  1.00 84.16  ? 358  GLN   D OE1 1 
ATOM   10654 N  NE2 . GLN   D  1 57  ? -1.656  31.399  -42.378  1.00 88.62  ? 358  GLN   D NE2 1 
ATOM   10655 N  N   . LEU   D  1 58  ? -0.458  26.480  -37.772  1.00 69.38  ? 359  LEU   D N   1 
ATOM   10656 C  CA  . LEU   D  1 58  ? 0.699   25.895  -37.091  1.00 59.94  ? 359  LEU   D CA  1 
ATOM   10657 C  C   . LEU   D  1 58  ? 0.660   24.369  -37.104  1.00 64.00  ? 359  LEU   D C   1 
ATOM   10658 O  O   . LEU   D  1 58  ? 1.681   23.722  -37.369  1.00 58.18  ? 359  LEU   D O   1 
ATOM   10659 C  CB  . LEU   D  1 58  ? 0.805   26.414  -35.648  1.00 46.70  ? 359  LEU   D CB  1 
ATOM   10660 C  CG  . LEU   D  1 58  ? 2.207   26.323  -35.050  1.00 43.20  ? 359  LEU   D CG  1 
ATOM   10661 C  CD1 . LEU   D  1 58  ? 3.192   26.954  -35.979  1.00 50.35  ? 359  LEU   D CD1 1 
ATOM   10662 C  CD2 . LEU   D  1 58  ? 2.332   26.965  -33.669  1.00 53.18  ? 359  LEU   D CD2 1 
ATOM   10663 N  N   . PHE   D  1 59  ? -0.502  23.774  -36.809  1.00 72.30  ? 360  PHE   D N   1 
ATOM   10664 C  CA  . PHE   D  1 59  ? -0.619  22.319  -36.719  1.00 78.90  ? 360  PHE   D CA  1 
ATOM   10665 C  C   . PHE   D  1 59  ? 0.091   21.623  -37.879  1.00 72.13  ? 360  PHE   D C   1 
ATOM   10666 O  O   . PHE   D  1 59  ? 1.068   20.900  -37.639  1.00 76.27  ? 360  PHE   D O   1 
ATOM   10667 C  CB  . PHE   D  1 59  ? -2.087  21.881  -36.667  1.00 91.06  ? 360  PHE   D CB  1 
ATOM   10668 C  CG  . PHE   D  1 59  ? -2.818  22.300  -35.418  1.00 96.95  ? 360  PHE   D CG  1 
ATOM   10669 C  CD1 . PHE   D  1 59  ? -2.283  22.077  -34.159  1.00 91.98  ? 360  PHE   D CD1 1 
ATOM   10670 C  CD2 . PHE   D  1 59  ? -4.064  22.906  -35.512  1.00 103.39 ? 360  PHE   D CD2 1 
ATOM   10671 C  CE1 . PHE   D  1 59  ? -2.981  22.458  -33.020  1.00 91.28  ? 360  PHE   D CE1 1 
ATOM   10672 C  CE2 . PHE   D  1 59  ? -4.759  23.288  -34.380  1.00 100.76 ? 360  PHE   D CE2 1 
ATOM   10673 C  CZ  . PHE   D  1 59  ? -4.217  23.066  -33.135  1.00 94.14  ? 360  PHE   D CZ  1 
ATOM   10674 N  N   . PRO   D  1 60  ? -0.311  21.840  -39.142  1.00 64.76  ? 361  PRO   D N   1 
ATOM   10675 C  CA  . PRO   D  1 60  ? 0.286   21.039  -40.220  1.00 59.82  ? 361  PRO   D CA  1 
ATOM   10676 C  C   . PRO   D  1 60  ? 1.762   21.315  -40.415  1.00 61.54  ? 361  PRO   D C   1 
ATOM   10677 O  O   . PRO   D  1 60  ? 2.495   20.421  -40.857  1.00 69.29  ? 361  PRO   D O   1 
ATOM   10678 C  CB  . PRO   D  1 60  ? -0.534  21.444  -41.449  1.00 57.39  ? 361  PRO   D CB  1 
ATOM   10679 C  CG  . PRO   D  1 60  ? -0.898  22.837  -41.186  1.00 55.79  ? 361  PRO   D CG  1 
ATOM   10680 C  CD  . PRO   D  1 60  ? -1.113  22.946  -39.697  1.00 61.00  ? 361  PRO   D CD  1 
ATOM   10681 N  N   . LEU   D  1 61  ? 2.225   22.523  -40.094  1.00 55.31  ? 362  LEU   D N   1 
ATOM   10682 C  CA  . LEU   D  1 61  ? 3.655   22.795  -40.162  1.00 57.26  ? 362  LEU   D CA  1 
ATOM   10683 C  C   . LEU   D  1 61  ? 4.411   21.961  -39.139  1.00 58.56  ? 362  LEU   D C   1 
ATOM   10684 O  O   . LEU   D  1 61  ? 5.376   21.265  -39.478  1.00 55.78  ? 362  LEU   D O   1 
ATOM   10685 C  CB  . LEU   D  1 61  ? 3.922   24.284  -39.943  1.00 54.83  ? 362  LEU   D CB  1 
ATOM   10686 C  CG  . LEU   D  1 61  ? 3.396   25.262  -40.997  1.00 53.53  ? 362  LEU   D CG  1 
ATOM   10687 C  CD1 . LEU   D  1 61  ? 3.783   26.680  -40.619  1.00 59.62  ? 362  LEU   D CD1 1 
ATOM   10688 C  CD2 . LEU   D  1 61  ? 3.925   24.922  -42.387  1.00 48.28  ? 362  LEU   D CD2 1 
ATOM   10689 N  N   . ALA   D  1 62  ? 3.979   22.012  -37.879  1.00 62.06  ? 363  ALA   D N   1 
ATOM   10690 C  CA  . ALA   D  1 62  ? 4.672   21.251  -36.852  1.00 51.58  ? 363  ALA   D CA  1 
ATOM   10691 C  C   . ALA   D  1 62  ? 4.556   19.753  -37.113  1.00 53.87  ? 363  ALA   D C   1 
ATOM   10692 O  O   . ALA   D  1 62  ? 5.529   19.011  -36.929  1.00 54.21  ? 363  ALA   D O   1 
ATOM   10693 C  CB  . ALA   D  1 62  ? 4.133   21.621  -35.473  1.00 45.67  ? 363  ALA   D CB  1 
ATOM   10694 N  N   . LYS   D  1 63  ? 3.388   19.289  -37.570  1.00 52.95  ? 364  LYS   D N   1 
ATOM   10695 C  CA  . LYS   D  1 63  ? 3.270   17.874  -37.915  1.00 56.24  ? 364  LYS   D CA  1 
ATOM   10696 C  C   . LYS   D  1 63  ? 4.315   17.472  -38.945  1.00 63.20  ? 364  LYS   D C   1 
ATOM   10697 O  O   . LYS   D  1 63  ? 4.918   16.395  -38.842  1.00 67.40  ? 364  LYS   D O   1 
ATOM   10698 C  CB  . LYS   D  1 63  ? 1.875   17.546  -38.442  1.00 44.85  ? 364  LYS   D CB  1 
ATOM   10699 C  CG  . LYS   D  1 63  ? 1.577   16.037  -38.430  1.00 47.72  ? 364  LYS   D CG  1 
ATOM   10700 C  CD  . LYS   D  1 63  ? 1.211   15.501  -39.812  1.00 61.46  ? 364  LYS   D CD  1 
ATOM   10701 C  CE  . LYS   D  1 63  ? 0.760   14.042  -39.768  1.00 64.86  ? 364  LYS   D CE  1 
ATOM   10702 N  NZ  . LYS   D  1 63  ? 1.807   13.104  -39.258  1.00 68.07  ? 364  LYS   D NZ  1 
ATOM   10703 N  N   . GLU   D  1 64  ? 4.554   18.323  -39.941  1.00 62.54  ? 365  GLU   D N   1 
ATOM   10704 C  CA  . GLU   D  1 64  ? 5.535   17.962  -40.958  1.00 66.83  ? 365  GLU   D CA  1 
ATOM   10705 C  C   . GLU   D  1 64  ? 6.926   17.862  -40.350  1.00 56.13  ? 365  GLU   D C   1 
ATOM   10706 O  O   . GLU   D  1 64  ? 7.672   16.914  -40.632  1.00 46.83  ? 365  GLU   D O   1 
ATOM   10707 C  CB  . GLU   D  1 64  ? 5.509   18.973  -42.111  1.00 73.96  ? 365  GLU   D CB  1 
ATOM   10708 C  CG  . GLU   D  1 64  ? 5.307   18.346  -43.503  1.00 83.44  ? 365  GLU   D CG  1 
ATOM   10709 C  CD  . GLU   D  1 64  ? 6.587   17.727  -44.089  1.00 92.81  ? 365  GLU   D CD  1 
ATOM   10710 O  OE1 . GLU   D  1 64  ? 7.282   16.974  -43.361  1.00 99.28  ? 365  GLU   D OE1 1 
ATOM   10711 O  OE2 . GLU   D  1 64  ? 6.900   17.998  -45.281  1.00 85.91  ? 365  GLU   D OE2 1 
ATOM   10712 N  N   . PHE   D  1 65  ? 7.276   18.818  -39.487  1.00 52.70  ? 366  PHE   D N   1 
ATOM   10713 C  CA  . PHE   D  1 65  ? 8.613   18.832  -38.910  1.00 52.99  ? 366  PHE   D CA  1 
ATOM   10714 C  C   . PHE   D  1 65  ? 8.838   17.635  -37.993  1.00 50.87  ? 366  PHE   D C   1 
ATOM   10715 O  O   . PHE   D  1 65  ? 9.841   16.926  -38.130  1.00 62.68  ? 366  PHE   D O   1 
ATOM   10716 C  CB  . PHE   D  1 65  ? 8.868   20.137  -38.153  1.00 50.15  ? 366  PHE   D CB  1 
ATOM   10717 C  CG  . PHE   D  1 65  ? 10.139  20.118  -37.364  1.00 47.50  ? 366  PHE   D CG  1 
ATOM   10718 C  CD1 . PHE   D  1 65  ? 11.364  20.141  -38.002  1.00 49.14  ? 366  PHE   D CD1 1 
ATOM   10719 C  CD2 . PHE   D  1 65  ? 10.112  20.031  -35.985  1.00 49.91  ? 366  PHE   D CD2 1 
ATOM   10720 C  CE1 . PHE   D  1 65  ? 12.549  20.092  -37.278  1.00 47.71  ? 366  PHE   D CE1 1 
ATOM   10721 C  CE2 . PHE   D  1 65  ? 11.280  19.990  -35.265  1.00 50.90  ? 366  PHE   D CE2 1 
ATOM   10722 C  CZ  . PHE   D  1 65  ? 12.504  20.021  -35.914  1.00 49.19  ? 366  PHE   D CZ  1 
ATOM   10723 N  N   . ILE   D  1 66  ? 7.928   17.395  -37.044  1.00 47.01  ? 367  ILE   D N   1 
ATOM   10724 C  CA  . ILE   D  1 66  ? 8.123   16.273  -36.127  1.00 47.27  ? 367  ILE   D CA  1 
ATOM   10725 C  C   . ILE   D  1 66  ? 8.244   14.976  -36.914  1.00 53.32  ? 367  ILE   D C   1 
ATOM   10726 O  O   . ILE   D  1 66  ? 9.116   14.137  -36.638  1.00 44.54  ? 367  ILE   D O   1 
ATOM   10727 C  CB  . ILE   D  1 66  ? 6.986   16.209  -35.089  1.00 45.50  ? 367  ILE   D CB  1 
ATOM   10728 C  CG1 . ILE   D  1 66  ? 6.884   17.520  -34.314  1.00 34.89  ? 367  ILE   D CG1 1 
ATOM   10729 C  CG2 . ILE   D  1 66  ? 7.228   15.081  -34.098  1.00 48.52  ? 367  ILE   D CG2 1 
ATOM   10730 C  CD1 . ILE   D  1 66  ? 8.132   17.859  -33.550  1.00 40.54  ? 367  ILE   D CD1 1 
ATOM   10731 N  N   . ASP   D  1 67  ? 7.414   14.826  -37.950  1.00 60.50  ? 368  ASP   D N   1 
ATOM   10732 C  CA  . ASP   D  1 67  ? 7.471   13.637  -38.794  1.00 58.87  ? 368  ASP   D CA  1 
ATOM   10733 C  C   . ASP   D  1 67  ? 8.845   13.474  -39.427  1.00 57.23  ? 368  ASP   D C   1 
ATOM   10734 O  O   . ASP   D  1 67  ? 9.440   12.393  -39.367  1.00 56.51  ? 368  ASP   D O   1 
ATOM   10735 C  CB  . ASP   D  1 67  ? 6.394   13.708  -39.870  1.00 53.84  ? 368  ASP   D CB  1 
ATOM   10736 C  CG  . ASP   D  1 67  ? 5.011   13.463  -39.321  1.00 56.63  ? 368  ASP   D CG  1 
ATOM   10737 O  OD1 . ASP   D  1 67  ? 4.877   12.958  -38.185  1.00 61.31  ? 368  ASP   D OD1 1 
ATOM   10738 O  OD2 . ASP   D  1 67  ? 4.042   13.766  -40.038  1.00 65.40  ? 368  ASP   D OD2 1 
ATOM   10739 N  N   . GLN   D  1 68  ? 9.370   14.535  -40.043  1.00 48.50  ? 369  GLN   D N   1 
ATOM   10740 C  CA  . GLN   D  1 68  ? 10.669  14.364  -40.671  1.00 52.25  ? 369  GLN   D CA  1 
ATOM   10741 C  C   . GLN   D  1 68  ? 11.766  14.234  -39.625  1.00 55.63  ? 369  GLN   D C   1 
ATOM   10742 O  O   . GLN   D  1 68  ? 12.778  13.562  -39.870  1.00 51.44  ? 369  GLN   D O   1 
ATOM   10743 C  CB  . GLN   D  1 68  ? 10.962  15.479  -41.676  1.00 59.45  ? 369  GLN   D CB  1 
ATOM   10744 C  CG  . GLN   D  1 68  ? 10.807  16.891  -41.197  1.00 69.85  ? 369  GLN   D CG  1 
ATOM   10745 C  CD  . GLN   D  1 68  ? 11.718  17.859  -41.959  1.00 74.68  ? 369  GLN   D CD  1 
ATOM   10746 O  OE1 . GLN   D  1 68  ? 12.921  17.601  -42.130  1.00 73.69  ? 369  GLN   D OE1 1 
ATOM   10747 N  NE2 . GLN   D  1 68  ? 11.152  18.981  -42.405  1.00 68.29  ? 369  GLN   D NE2 1 
ATOM   10748 N  N   . TYR   D  1 69  ? 11.571  14.812  -38.436  1.00 57.91  ? 370  TYR   D N   1 
ATOM   10749 C  CA  . TYR   D  1 69  ? 12.535  14.567  -37.368  1.00 55.84  ? 370  TYR   D CA  1 
ATOM   10750 C  C   . TYR   D  1 69  ? 12.536  13.102  -36.974  1.00 50.50  ? 370  TYR   D C   1 
ATOM   10751 O  O   . TYR   D  1 69  ? 13.592  12.461  -36.915  1.00 50.72  ? 370  TYR   D O   1 
ATOM   10752 C  CB  . TYR   D  1 69  ? 12.261  15.415  -36.132  1.00 51.69  ? 370  TYR   D CB  1 
ATOM   10753 C  CG  . TYR   D  1 69  ? 13.190  14.975  -35.029  1.00 55.01  ? 370  TYR   D CG  1 
ATOM   10754 C  CD1 . TYR   D  1 69  ? 14.557  15.188  -35.141  1.00 59.33  ? 370  TYR   D CD1 1 
ATOM   10755 C  CD2 . TYR   D  1 69  ? 12.720  14.302  -33.911  1.00 51.93  ? 370  TYR   D CD2 1 
ATOM   10756 C  CE1 . TYR   D  1 69  ? 15.431  14.765  -34.154  1.00 57.27  ? 370  TYR   D CE1 1 
ATOM   10757 C  CE2 . TYR   D  1 69  ? 13.590  13.879  -32.911  1.00 50.78  ? 370  TYR   D CE2 1 
ATOM   10758 C  CZ  . TYR   D  1 69  ? 14.944  14.111  -33.039  1.00 52.85  ? 370  TYR   D CZ  1 
ATOM   10759 O  OH  . TYR   D  1 69  ? 15.826  13.687  -32.062  1.00 52.02  ? 370  TYR   D OH  1 
ATOM   10760 N  N   . TYR   D  1 70  ? 11.361  12.550  -36.698  1.00 42.99  ? 371  TYR   D N   1 
ATOM   10761 C  CA  . TYR   D  1 70  ? 11.364  11.170  -36.252  1.00 52.26  ? 371  TYR   D CA  1 
ATOM   10762 C  C   . TYR   D  1 70  ? 11.802  10.234  -37.363  1.00 50.98  ? 371  TYR   D C   1 
ATOM   10763 O  O   . TYR   D  1 70  ? 12.425  9.203   -37.091  1.00 60.02  ? 371  TYR   D O   1 
ATOM   10764 C  CB  . TYR   D  1 70  ? 9.998   10.801  -35.678  1.00 53.45  ? 371  TYR   D CB  1 
ATOM   10765 C  CG  . TYR   D  1 70  ? 9.957   11.173  -34.224  1.00 46.41  ? 371  TYR   D CG  1 
ATOM   10766 C  CD1 . TYR   D  1 70  ? 9.684   12.472  -33.838  1.00 45.98  ? 371  TYR   D CD1 1 
ATOM   10767 C  CD2 . TYR   D  1 70  ? 10.289  10.257  -33.244  1.00 35.21  ? 371  TYR   D CD2 1 
ATOM   10768 C  CE1 . TYR   D  1 70  ? 9.682   12.840  -32.522  1.00 49.57  ? 371  TYR   D CE1 1 
ATOM   10769 C  CE2 . TYR   D  1 70  ? 10.288  10.618  -31.917  1.00 49.49  ? 371  TYR   D CE2 1 
ATOM   10770 C  CZ  . TYR   D  1 70  ? 9.981   11.909  -31.562  1.00 53.88  ? 371  TYR   D CZ  1 
ATOM   10771 O  OH  . TYR   D  1 70  ? 9.967   12.282  -30.238  1.00 61.93  ? 371  TYR   D OH  1 
ATOM   10772 N  N   . SER   D  1 71  ? 11.550  10.596  -38.614  1.00 57.11  ? 372  SER   D N   1 
ATOM   10773 C  CA  . SER   D  1 71  ? 12.040  9.766   -39.704  1.00 60.77  ? 372  SER   D CA  1 
ATOM   10774 C  C   . SER   D  1 71  ? 13.566  9.764   -39.731  1.00 57.44  ? 372  SER   D C   1 
ATOM   10775 O  O   . SER   D  1 71  ? 14.197  8.703   -39.824  1.00 62.37  ? 372  SER   D O   1 
ATOM   10776 C  CB  . SER   D  1 71  ? 11.454  10.246  -41.026  1.00 50.41  ? 372  SER   D CB  1 
ATOM   10777 O  OG  . SER   D  1 71  ? 12.375  10.022  -42.073  1.00 74.69  ? 372  SER   D OG  1 
ATOM   10778 N  N   . SER   D  1 72  ? 14.172  10.945  -39.588  1.00 48.93  ? 373  SER   D N   1 
ATOM   10779 C  CA  . SER   D  1 72  ? 15.626  11.064  -39.646  1.00 44.95  ? 373  SER   D CA  1 
ATOM   10780 C  C   . SER   D  1 72  ? 16.326  10.126  -38.671  1.00 53.61  ? 373  SER   D C   1 
ATOM   10781 O  O   . SER   D  1 72  ? 17.408  9.615   -38.968  1.00 53.61  ? 373  SER   D O   1 
ATOM   10782 C  CB  . SER   D  1 72  ? 16.032  12.494  -39.337  1.00 55.59  ? 373  SER   D CB  1 
ATOM   10783 O  OG  . SER   D  1 72  ? 15.814  12.734  -37.955  1.00 69.43  ? 373  SER   D OG  1 
ATOM   10784 N  N   . ILE   D  1 73  ? 15.738  9.904   -37.493  1.00 60.23  ? 374  ILE   D N   1 
ATOM   10785 C  CA  . ILE   D  1 73  ? 16.347  9.060   -36.462  1.00 58.18  ? 374  ILE   D CA  1 
ATOM   10786 C  C   . ILE   D  1 73  ? 15.745  7.651   -36.441  1.00 54.01  ? 374  ILE   D C   1 
ATOM   10787 O  O   . ILE   D  1 73  ? 15.848  6.959   -35.427  1.00 56.62  ? 374  ILE   D O   1 
ATOM   10788 C  CB  . ILE   D  1 73  ? 16.259  9.711   -35.071  1.00 55.15  ? 374  ILE   D CB  1 
ATOM   10789 C  CG1 . ILE   D  1 73  ? 14.813  9.675   -34.538  1.00 50.64  ? 374  ILE   D CG1 1 
ATOM   10790 C  CG2 . ILE   D  1 73  ? 16.841  11.132  -35.115  1.00 50.20  ? 374  ILE   D CG2 1 
ATOM   10791 C  CD1 . ILE   D  1 73  ? 14.585  10.441  -33.229  1.00 51.63  ? 374  ILE   D CD1 1 
ATOM   10792 N  N   . LYS   D  1 74  ? 15.122  7.210   -37.541  1.00 56.42  ? 375  LYS   D N   1 
ATOM   10793 C  CA  . LYS   D  1 74  ? 14.633  5.832   -37.653  1.00 68.12  ? 375  LYS   D CA  1 
ATOM   10794 C  C   . LYS   D  1 74  ? 13.652  5.487   -36.534  1.00 75.60  ? 375  LYS   D C   1 
ATOM   10795 O  O   . LYS   D  1 74  ? 13.737  4.421   -35.924  1.00 80.24  ? 375  LYS   D O   1 
ATOM   10796 C  CB  . LYS   D  1 74  ? 15.795  4.835   -37.655  1.00 75.42  ? 375  LYS   D CB  1 
ATOM   10797 C  CG  . LYS   D  1 74  ? 16.264  4.382   -39.011  1.00 81.64  ? 375  LYS   D CG  1 
ATOM   10798 C  CD  . LYS   D  1 74  ? 15.812  2.946   -39.276  1.00 86.17  ? 375  LYS   D CD  1 
ATOM   10799 C  CE  . LYS   D  1 74  ? 16.543  2.370   -40.473  1.00 86.53  ? 375  LYS   D CE  1 
ATOM   10800 N  NZ  . LYS   D  1 74  ? 16.951  3.440   -41.436  1.00 86.71  ? 375  LYS   D NZ  1 
ATOM   10801 N  N   . ARG   D  1 75  ? 12.730  6.408   -36.236  1.00 76.06  ? 376  ARG   D N   1 
ATOM   10802 C  CA  . ARG   D  1 75  ? 11.721  6.202   -35.202  1.00 75.40  ? 376  ARG   D CA  1 
ATOM   10803 C  C   . ARG   D  1 75  ? 10.334  6.604   -35.687  1.00 79.62  ? 376  ARG   D C   1 
ATOM   10804 O  O   . ARG   D  1 75  ? 9.465   6.940   -34.875  1.00 81.82  ? 376  ARG   D O   1 
ATOM   10805 C  CB  . ARG   D  1 75  ? 12.063  6.975   -33.934  1.00 73.11  ? 376  ARG   D CB  1 
ATOM   10806 C  CG  . ARG   D  1 75  ? 13.285  6.466   -33.199  1.00 71.13  ? 376  ARG   D CG  1 
ATOM   10807 C  CD  . ARG   D  1 75  ? 13.056  5.084   -32.645  1.00 67.85  ? 376  ARG   D CD  1 
ATOM   10808 N  NE  . ARG   D  1 75  ? 14.136  4.693   -31.748  1.00 76.05  ? 376  ARG   D NE  1 
ATOM   10809 C  CZ  . ARG   D  1 75  ? 15.278  4.136   -32.140  1.00 85.26  ? 376  ARG   D CZ  1 
ATOM   10810 N  NH1 . ARG   D  1 75  ? 16.198  3.818   -31.238  1.00 79.99  ? 376  ARG   D NH1 1 
ATOM   10811 N  NH2 . ARG   D  1 75  ? 15.502  3.900   -33.429  1.00 92.15  ? 376  ARG   D NH2 1 
ATOM   10812 N  N   . PHE   D  1 76  ? 10.111  6.579   -37.004  1.00 73.18  ? 377  PHE   D N   1 
ATOM   10813 C  CA  . PHE   D  1 76  ? 8.856   7.069   -37.558  1.00 65.87  ? 377  PHE   D CA  1 
ATOM   10814 C  C   . PHE   D  1 76  ? 7.716   6.131   -37.181  1.00 69.14  ? 377  PHE   D C   1 
ATOM   10815 O  O   . PHE   D  1 76  ? 7.822   4.911   -37.332  1.00 83.52  ? 377  PHE   D O   1 
ATOM   10816 C  CB  . PHE   D  1 76  ? 8.955   7.210   -39.083  1.00 74.36  ? 377  PHE   D CB  1 
ATOM   10817 C  CG  . PHE   D  1 76  ? 7.696   7.739   -39.718  1.00 72.32  ? 377  PHE   D CG  1 
ATOM   10818 C  CD1 . PHE   D  1 76  ? 7.422   9.098   -39.710  1.00 63.36  ? 377  PHE   D CD1 1 
ATOM   10819 C  CD2 . PHE   D  1 76  ? 6.769   6.877   -40.285  1.00 69.87  ? 377  PHE   D CD2 1 
ATOM   10820 C  CE1 . PHE   D  1 76  ? 6.260   9.582   -40.245  1.00 55.87  ? 377  PHE   D CE1 1 
ATOM   10821 C  CE2 . PHE   D  1 76  ? 5.603   7.362   -40.836  1.00 69.31  ? 377  PHE   D CE2 1 
ATOM   10822 C  CZ  . PHE   D  1 76  ? 5.349   8.716   -40.815  1.00 64.89  ? 377  PHE   D CZ  1 
ATOM   10823 N  N   . GLY   D  1 77  ? 6.618   6.700   -36.693  1.00 59.83  ? 378  GLY   D N   1 
ATOM   10824 C  CA  . GLY   D  1 77  ? 5.496   5.881   -36.286  1.00 51.18  ? 378  GLY   D CA  1 
ATOM   10825 C  C   . GLY   D  1 77  ? 5.690   5.157   -34.979  1.00 67.27  ? 378  GLY   D C   1 
ATOM   10826 O  O   . GLY   D  1 77  ? 4.875   4.297   -34.632  1.00 75.97  ? 378  GLY   D O   1 
ATOM   10827 N  N   . SER   D  1 78  ? 6.751   5.475   -34.244  1.00 69.26  ? 379  SER   D N   1 
ATOM   10828 C  CA  . SER   D  1 78  ? 7.034   4.834   -32.974  1.00 75.19  ? 379  SER   D CA  1 
ATOM   10829 C  C   . SER   D  1 78  ? 6.146   5.404   -31.869  1.00 80.10  ? 379  SER   D C   1 
ATOM   10830 O  O   . SER   D  1 78  ? 5.419   6.388   -32.052  1.00 76.67  ? 379  SER   D O   1 
ATOM   10831 C  CB  . SER   D  1 78  ? 8.500   5.019   -32.601  1.00 73.01  ? 379  SER   D CB  1 
ATOM   10832 O  OG  . SER   D  1 78  ? 8.715   6.327   -32.096  1.00 68.51  ? 379  SER   D OG  1 
ATOM   10833 N  N   . LYS   D  1 79  ? 6.216   4.768   -30.696  1.00 81.42  ? 380  LYS   D N   1 
ATOM   10834 C  CA  . LYS   D  1 79  ? 5.521   5.299   -29.529  1.00 81.28  ? 380  LYS   D CA  1 
ATOM   10835 C  C   . LYS   D  1 79  ? 5.985   6.720   -29.221  1.00 71.26  ? 380  LYS   D C   1 
ATOM   10836 O  O   . LYS   D  1 79  ? 5.167   7.619   -28.997  1.00 73.35  ? 380  LYS   D O   1 
ATOM   10837 C  CB  . LYS   D  1 79  ? 5.745   4.387   -28.321  1.00 93.13  ? 380  LYS   D CB  1 
ATOM   10838 C  CG  . LYS   D  1 79  ? 5.147   2.982   -28.417  1.00 100.07 ? 380  LYS   D CG  1 
ATOM   10839 C  CD  . LYS   D  1 79  ? 5.593   2.144   -27.209  1.00 101.51 ? 380  LYS   D CD  1 
ATOM   10840 C  CE  . LYS   D  1 79  ? 5.120   0.697   -27.279  1.00 98.44  ? 380  LYS   D CE  1 
ATOM   10841 N  NZ  . LYS   D  1 79  ? 3.759   0.535   -26.717  1.00 97.01  ? 380  LYS   D NZ  1 
ATOM   10842 N  N   . ALA   D  1 80  ? 7.303   6.945   -29.226  1.00 55.76  ? 381  ALA   D N   1 
ATOM   10843 C  CA  . ALA   D  1 80  ? 7.829   8.272   -28.919  1.00 56.97  ? 381  ALA   D CA  1 
ATOM   10844 C  C   . ALA   D  1 80  ? 7.389   9.297   -29.953  1.00 64.11  ? 381  ALA   D C   1 
ATOM   10845 O  O   . ALA   D  1 80  ? 7.146   10.466  -29.620  1.00 60.50  ? 381  ALA   D O   1 
ATOM   10846 C  CB  . ALA   D  1 80  ? 9.353   8.229   -28.839  1.00 55.11  ? 381  ALA   D CB  1 
ATOM   10847 N  N   . HIS   D  1 81  ? 7.302   8.881   -31.217  1.00 62.35  ? 382  HIS   D N   1 
ATOM   10848 C  CA  . HIS   D  1 81  ? 6.817   9.783   -32.255  1.00 63.54  ? 382  HIS   D CA  1 
ATOM   10849 C  C   . HIS   D  1 81  ? 5.344   10.101  -32.037  1.00 59.67  ? 382  HIS   D C   1 
ATOM   10850 O  O   . HIS   D  1 81  ? 4.953   11.273  -31.973  1.00 55.57  ? 382  HIS   D O   1 
ATOM   10851 C  CB  . HIS   D  1 81  ? 7.057   9.158   -33.639  1.00 63.16  ? 382  HIS   D CB  1 
ATOM   10852 C  CG  . HIS   D  1 81  ? 6.510   9.955   -34.786  1.00 58.33  ? 382  HIS   D CG  1 
ATOM   10853 N  ND1 . HIS   D  1 81  ? 6.388   9.436   -36.059  1.00 61.55  ? 382  HIS   D ND1 1 
ATOM   10854 C  CD2 . HIS   D  1 81  ? 6.068   11.231  -34.859  1.00 58.28  ? 382  HIS   D CD2 1 
ATOM   10855 C  CE1 . HIS   D  1 81  ? 5.886   10.355  -36.863  1.00 58.54  ? 382  HIS   D CE1 1 
ATOM   10856 N  NE2 . HIS   D  1 81  ? 5.684   11.456  -36.160  1.00 61.33  ? 382  HIS   D NE2 1 
ATOM   10857 N  N   . MET   D  1 82  ? 4.518   9.062   -31.893  1.00 64.86  ? 383  MET   D N   1 
ATOM   10858 C  CA  . MET   D  1 82  ? 3.082   9.269   -31.751  1.00 64.43  ? 383  MET   D CA  1 
ATOM   10859 C  C   . MET   D  1 82  ? 2.770   10.159  -30.555  1.00 71.04  ? 383  MET   D C   1 
ATOM   10860 O  O   . MET   D  1 82  ? 1.880   11.016  -30.627  1.00 73.84  ? 383  MET   D O   1 
ATOM   10861 C  CB  . MET   D  1 82  ? 2.374   7.917   -31.642  1.00 64.78  ? 383  MET   D CB  1 
ATOM   10862 C  CG  . MET   D  1 82  ? 1.483   7.589   -32.853  1.00 82.11  ? 383  MET   D CG  1 
ATOM   10863 S  SD  . MET   D  1 82  ? 1.979   8.425   -34.393  1.00 93.80  ? 383  MET   D SD  1 
ATOM   10864 C  CE  . MET   D  1 82  ? 0.416   9.074   -34.989  1.00 91.98  ? 383  MET   D CE  1 
ATOM   10865 N  N   . GLU   D  1 83  ? 3.526   10.003  -29.463  1.00 71.02  ? 384  GLU   D N   1 
ATOM   10866 C  CA  . GLU   D  1 83  ? 3.276   10.799  -28.265  1.00 67.99  ? 384  GLU   D CA  1 
ATOM   10867 C  C   . GLU   D  1 83  ? 3.770   12.228  -28.428  1.00 61.74  ? 384  GLU   D C   1 
ATOM   10868 O  O   . GLU   D  1 83  ? 3.135   13.165  -27.929  1.00 62.35  ? 384  GLU   D O   1 
ATOM   10869 C  CB  . GLU   D  1 83  ? 3.928   10.147  -27.043  1.00 74.56  ? 384  GLU   D CB  1 
ATOM   10870 C  CG  . GLU   D  1 83  ? 3.139   8.960   -26.498  1.00 80.73  ? 384  GLU   D CG  1 
ATOM   10871 C  CD  . GLU   D  1 83  ? 3.833   8.241   -25.358  1.00 72.54  ? 384  GLU   D CD  1 
ATOM   10872 O  OE1 . GLU   D  1 83  ? 4.964   8.651   -24.989  1.00 64.20  ? 384  GLU   D OE1 1 
ATOM   10873 O  OE2 . GLU   D  1 83  ? 3.230   7.266   -24.845  1.00 66.89  ? 384  GLU   D OE2 1 
ATOM   10874 N  N   . ARG   D  1 84  ? 4.900   12.417  -29.117  1.00 55.20  ? 385  ARG   D N   1 
ATOM   10875 C  CA  . ARG   D  1 84  ? 5.433   13.765  -29.285  1.00 53.10  ? 385  ARG   D CA  1 
ATOM   10876 C  C   . ARG   D  1 84  ? 4.467   14.633  -30.078  1.00 64.62  ? 385  ARG   D C   1 
ATOM   10877 O  O   . ARG   D  1 84  ? 4.227   15.793  -29.716  1.00 62.82  ? 385  ARG   D O   1 
ATOM   10878 C  CB  . ARG   D  1 84  ? 6.799   13.710  -29.959  1.00 40.55  ? 385  ARG   D CB  1 
ATOM   10879 C  CG  . ARG   D  1 84  ? 7.351   15.058  -30.376  1.00 46.96  ? 385  ARG   D CG  1 
ATOM   10880 C  CD  . ARG   D  1 84  ? 7.639   15.947  -29.187  1.00 52.82  ? 385  ARG   D CD  1 
ATOM   10881 N  NE  . ARG   D  1 84  ? 8.179   17.235  -29.609  1.00 54.87  ? 385  ARG   D NE  1 
ATOM   10882 C  CZ  . ARG   D  1 84  ? 8.113   18.346  -28.881  1.00 55.74  ? 385  ARG   D CZ  1 
ATOM   10883 N  NH1 . ARG   D  1 84  ? 7.534   18.327  -27.694  1.00 68.44  ? 385  ARG   D NH1 1 
ATOM   10884 N  NH2 . ARG   D  1 84  ? 8.623   19.480  -29.333  1.00 51.93  ? 385  ARG   D NH2 1 
ATOM   10885 N  N   . LEU   D  1 85  ? 3.892   14.074  -31.155  1.00 70.88  ? 386  LEU   D N   1 
ATOM   10886 C  CA  . LEU   D  1 85  ? 2.869   14.774  -31.932  1.00 67.60  ? 386  LEU   D CA  1 
ATOM   10887 C  C   . LEU   D  1 85  ? 1.703   15.187  -31.050  1.00 70.20  ? 386  LEU   D C   1 
ATOM   10888 O  O   . LEU   D  1 85  ? 1.303   16.358  -31.037  1.00 66.41  ? 386  LEU   D O   1 
ATOM   10889 C  CB  . LEU   D  1 85  ? 2.365   13.886  -33.070  1.00 63.20  ? 386  LEU   D CB  1 
ATOM   10890 C  CG  . LEU   D  1 85  ? 3.132   13.832  -34.385  1.00 57.71  ? 386  LEU   D CG  1 
ATOM   10891 C  CD1 . LEU   D  1 85  ? 2.752   12.576  -35.120  1.00 62.65  ? 386  LEU   D CD1 1 
ATOM   10892 C  CD2 . LEU   D  1 85  ? 2.789   15.050  -35.194  1.00 50.19  ? 386  LEU   D CD2 1 
ATOM   10893 N  N   . GLU   D  1 86  ? 1.130   14.219  -30.326  1.00 70.81  ? 387  GLU   D N   1 
ATOM   10894 C  CA  . GLU   D  1 86  ? 0.082   14.498  -29.351  1.00 72.68  ? 387  GLU   D CA  1 
ATOM   10895 C  C   . GLU   D  1 86  ? 0.454   15.673  -28.457  1.00 68.29  ? 387  GLU   D C   1 
ATOM   10896 O  O   . GLU   D  1 86  ? -0.374  16.554  -28.195  1.00 71.04  ? 387  GLU   D O   1 
ATOM   10897 C  CB  . GLU   D  1 86  ? -0.168  13.248  -28.510  1.00 81.71  ? 387  GLU   D CB  1 
ATOM   10898 C  CG  . GLU   D  1 86  ? -0.878  13.505  -27.201  1.00 92.47  ? 387  GLU   D CG  1 
ATOM   10899 C  CD  . GLU   D  1 86  ? -2.375  13.342  -27.312  1.00 109.08 ? 387  GLU   D CD  1 
ATOM   10900 O  OE1 . GLU   D  1 86  ? -2.841  12.865  -28.371  1.00 118.25 ? 387  GLU   D OE1 1 
ATOM   10901 O  OE2 . GLU   D  1 86  ? -3.085  13.688  -26.341  1.00 113.90 ? 387  GLU   D OE2 1 
ATOM   10902 N  N   . GLU   D  1 87  ? 1.709   15.712  -28.005  1.00 56.99  ? 388  GLU   D N   1 
ATOM   10903 C  CA  . GLU   D  1 87  ? 2.161   16.779  -27.119  1.00 59.33  ? 388  GLU   D CA  1 
ATOM   10904 C  C   . GLU   D  1 87  ? 2.147   18.137  -27.824  1.00 62.43  ? 388  GLU   D C   1 
ATOM   10905 O  O   . GLU   D  1 87  ? 1.717   19.136  -27.234  1.00 69.27  ? 388  GLU   D O   1 
ATOM   10906 C  CB  . GLU   D  1 87  ? 3.560   16.439  -26.592  1.00 55.81  ? 388  GLU   D CB  1 
ATOM   10907 C  CG  . GLU   D  1 87  ? 3.967   17.084  -25.276  1.00 46.42  ? 388  GLU   D CG  1 
ATOM   10908 C  CD  . GLU   D  1 87  ? 5.446   16.852  -24.938  1.00 56.49  ? 388  GLU   D CD  1 
ATOM   10909 O  OE1 . GLU   D  1 87  ? 6.200   16.362  -25.811  1.00 55.25  ? 388  GLU   D OE1 1 
ATOM   10910 O  OE2 . GLU   D  1 87  ? 5.862   17.163  -23.795  1.00 60.45  ? 388  GLU   D OE2 1 
ATOM   10911 N  N   . VAL   D  1 88  ? 2.605   18.198  -29.084  1.00 52.58  ? 389  VAL   D N   1 
ATOM   10912 C  CA  . VAL   D  1 88  ? 2.654   19.478  -29.791  1.00 52.51  ? 389  VAL   D CA  1 
ATOM   10913 C  C   . VAL   D  1 88  ? 1.251   20.013  -30.016  1.00 60.57  ? 389  VAL   D C   1 
ATOM   10914 O  O   . VAL   D  1 88  ? 1.016   21.222  -29.932  1.00 67.03  ? 389  VAL   D O   1 
ATOM   10915 C  CB  . VAL   D  1 88  ? 3.421   19.360  -31.125  1.00 50.73  ? 389  VAL   D CB  1 
ATOM   10916 C  CG1 . VAL   D  1 88  ? 3.371   20.682  -31.888  1.00 50.11  ? 389  VAL   D CG1 1 
ATOM   10917 C  CG2 . VAL   D  1 88  ? 4.879   18.967  -30.901  1.00 47.90  ? 389  VAL   D CG2 1 
ATOM   10918 N  N   . ASN   D  1 89  ? 0.297   19.126  -30.303  1.00 69.42  ? 390  ASN   D N   1 
ATOM   10919 C  CA  . ASN   D  1 89  ? -1.088  19.551  -30.485  1.00 76.91  ? 390  ASN   D CA  1 
ATOM   10920 C  C   . ASN   D  1 89  ? -1.646  20.176  -29.214  1.00 75.36  ? 390  ASN   D C   1 
ATOM   10921 O  O   . ASN   D  1 89  ? -2.204  21.278  -29.250  1.00 80.59  ? 390  ASN   D O   1 
ATOM   10922 C  CB  . ASN   D  1 89  ? -1.944  18.366  -30.919  1.00 89.95  ? 390  ASN   D CB  1 
ATOM   10923 C  CG  . ASN   D  1 89  ? -2.089  18.273  -32.422  1.00 95.13  ? 390  ASN   D CG  1 
ATOM   10924 O  OD1 . ASN   D  1 89  ? -3.091  17.753  -32.930  1.00 101.15 ? 390  ASN   D OD1 1 
ATOM   10925 N  ND2 . ASN   D  1 89  ? -1.084  18.777  -33.148  1.00 89.27  ? 390  ASN   D ND2 1 
ATOM   10926 N  N   . LYS   D  1 90  ? -1.519  19.470  -28.084  1.00 72.12  ? 391  LYS   D N   1 
ATOM   10927 C  CA  . LYS   D  1 90  ? -1.859  20.023  -26.775  1.00 70.68  ? 391  LYS   D CA  1 
ATOM   10928 C  C   . LYS   D  1 90  ? -1.360  21.450  -26.637  1.00 60.77  ? 391  LYS   D C   1 
ATOM   10929 O  O   . LYS   D  1 90  ? -2.106  22.357  -26.253  1.00 65.24  ? 391  LYS   D O   1 
ATOM   10930 C  CB  . LYS   D  1 90  ? -1.240  19.165  -25.664  1.00 78.58  ? 391  LYS   D CB  1 
ATOM   10931 C  CG  . LYS   D  1 90  ? -2.019  17.938  -25.221  1.00 82.94  ? 391  LYS   D CG  1 
ATOM   10932 C  CD  . LYS   D  1 90  ? -1.145  17.098  -24.286  1.00 88.87  ? 391  LYS   D CD  1 
ATOM   10933 C  CE  . LYS   D  1 90  ? -1.972  16.209  -23.358  1.00 98.23  ? 391  LYS   D CE  1 
ATOM   10934 N  NZ  . LYS   D  1 90  ? -2.893  15.282  -24.085  1.00 101.09 ? 391  LYS   D NZ  1 
ATOM   10935 N  N   . GLU   D  1 91  ? -0.083  21.651  -26.956  1.00 48.19  ? 392  GLU   D N   1 
ATOM   10936 C  CA  . GLU   D  1 91  ? 0.573   22.922  -26.684  1.00 48.63  ? 392  GLU   D CA  1 
ATOM   10937 C  C   . GLU   D  1 91  ? 0.094   24.014  -27.637  1.00 64.48  ? 392  GLU   D C   1 
ATOM   10938 O  O   . GLU   D  1 91  ? -0.046  25.175  -27.236  1.00 76.30  ? 392  GLU   D O   1 
ATOM   10939 C  CB  . GLU   D  1 91  ? 2.084   22.727  -26.775  1.00 43.56  ? 392  GLU   D CB  1 
ATOM   10940 C  CG  . GLU   D  1 91  ? 2.949   23.728  -26.024  1.00 40.59  ? 392  GLU   D CG  1 
ATOM   10941 C  CD  . GLU   D  1 91  ? 4.371   23.209  -25.872  1.00 56.07  ? 392  GLU   D CD  1 
ATOM   10942 O  OE1 . GLU   D  1 91  ? 5.305   24.019  -25.684  1.00 64.72  ? 392  GLU   D OE1 1 
ATOM   10943 O  OE2 . GLU   D  1 91  ? 4.559   21.977  -25.952  1.00 59.81  ? 392  GLU   D OE2 1 
ATOM   10944 N  N   . ILE   D  1 92  ? -0.161  23.672  -28.903  1.00 61.68  ? 393  ILE   D N   1 
ATOM   10945 C  CA  . ILE   D  1 92  ? -0.677  24.679  -29.824  1.00 61.71  ? 393  ILE   D CA  1 
ATOM   10946 C  C   . ILE   D  1 92  ? -2.132  25.000  -29.500  1.00 81.70  ? 393  ILE   D C   1 
ATOM   10947 O  O   . ILE   D  1 92  ? -2.590  26.127  -29.727  1.00 89.66  ? 393  ILE   D O   1 
ATOM   10948 C  CB  . ILE   D  1 92  ? -0.509  24.221  -31.281  1.00 54.60  ? 393  ILE   D CB  1 
ATOM   10949 C  CG1 . ILE   D  1 92  ? 0.947   23.842  -31.558  1.00 54.48  ? 393  ILE   D CG1 1 
ATOM   10950 C  CG2 . ILE   D  1 92  ? -0.935  25.321  -32.224  1.00 55.11  ? 393  ILE   D CG2 1 
ATOM   10951 C  CD1 . ILE   D  1 92  ? 1.220   23.398  -32.986  1.00 46.09  ? 393  ILE   D CD1 1 
ATOM   10952 N  N   . ASP   D  1 93  ? -2.879  24.027  -28.964  1.00 89.99  ? 394  ASP   D N   1 
ATOM   10953 C  CA  . ASP   D  1 93  ? -4.239  24.289  -28.491  1.00 85.07  ? 394  ASP   D CA  1 
ATOM   10954 C  C   . ASP   D  1 93  ? -4.234  25.183  -27.258  1.00 70.01  ? 394  ASP   D C   1 
ATOM   10955 O  O   . ASP   D  1 93  ? -4.973  26.172  -27.191  1.00 70.14  ? 394  ASP   D O   1 
ATOM   10956 C  CB  . ASP   D  1 93  ? -4.950  22.978  -28.169  1.00 92.38  ? 394  ASP   D CB  1 
ATOM   10957 C  CG  . ASP   D  1 93  ? -5.897  22.542  -29.255  1.00 96.86  ? 394  ASP   D CG  1 
ATOM   10958 O  OD1 . ASP   D  1 93  ? -5.731  22.997  -30.409  1.00 99.64  ? 394  ASP   D OD1 1 
ATOM   10959 O  OD2 . ASP   D  1 93  ? -6.807  21.744  -28.942  1.00 92.71  ? 394  ASP   D OD2 1 
ATOM   10960 N  N   . THR   D  1 94  ? -3.410  24.850  -26.267  1.00 60.96  ? 395  THR   D N   1 
ATOM   10961 C  CA  . THR   D  1 94  ? -3.421  25.601  -25.022  1.00 69.38  ? 395  THR   D CA  1 
ATOM   10962 C  C   . THR   D  1 94  ? -2.646  26.906  -25.104  1.00 78.41  ? 395  THR   D C   1 
ATOM   10963 O  O   . THR   D  1 94  ? -2.940  27.825  -24.335  1.00 90.82  ? 395  THR   D O   1 
ATOM   10964 C  CB  . THR   D  1 94  ? -2.854  24.756  -23.879  1.00 65.88  ? 395  THR   D CB  1 
ATOM   10965 O  OG1 . THR   D  1 94  ? -1.478  24.463  -24.135  1.00 66.41  ? 395  THR   D OG1 1 
ATOM   10966 C  CG2 . THR   D  1 94  ? -3.626  23.459  -23.755  1.00 65.45  ? 395  THR   D CG2 1 
ATOM   10967 N  N   . THR   D  1 95  ? -1.664  27.017  -26.002  1.00 73.69  ? 396  THR   D N   1 
ATOM   10968 C  CA  . THR   D  1 95  ? -0.794  28.187  -26.018  1.00 64.05  ? 396  THR   D CA  1 
ATOM   10969 C  C   . THR   D  1 95  ? -0.704  28.891  -27.362  1.00 70.12  ? 396  THR   D C   1 
ATOM   10970 O  O   . THR   D  1 95  ? -0.080  29.957  -27.428  1.00 78.40  ? 396  THR   D O   1 
ATOM   10971 C  CB  . THR   D  1 95  ? 0.636   27.813  -25.578  1.00 64.63  ? 396  THR   D CB  1 
ATOM   10972 O  OG1 . THR   D  1 95  ? 1.268   27.021  -26.594  1.00 71.24  ? 396  THR   D OG1 1 
ATOM   10973 C  CG2 . THR   D  1 95  ? 0.639   27.034  -24.248  1.00 55.10  ? 396  THR   D CG2 1 
ATOM   10974 N  N   . SER   D  1 96  ? -1.282  28.335  -28.426  1.00 58.06  ? 397  SER   D N   1 
ATOM   10975 C  CA  . SER   D  1 96  ? -1.180  28.891  -29.772  1.00 61.14  ? 397  SER   D CA  1 
ATOM   10976 C  C   . SER   D  1 96  ? 0.258   28.944  -30.275  1.00 56.39  ? 397  SER   D C   1 
ATOM   10977 O  O   . SER   D  1 96  ? 0.573   29.755  -31.147  1.00 57.04  ? 397  SER   D O   1 
ATOM   10978 C  CB  . SER   D  1 96  ? -1.813  30.282  -29.837  1.00 70.81  ? 397  SER   D CB  1 
ATOM   10979 O  OG  . SER   D  1 96  ? -2.916  30.353  -28.950  1.00 81.60  ? 397  SER   D OG  1 
ATOM   10980 N  N   . THR   D  1 97  ? 1.127   28.096  -29.723  1.00 52.30  ? 398  THR   D N   1 
ATOM   10981 C  CA  . THR   D  1 97  ? 2.535   27.951  -30.098  1.00 51.16  ? 398  THR   D CA  1 
ATOM   10982 C  C   . THR   D  1 97  ? 3.029   26.675  -29.434  1.00 53.03  ? 398  THR   D C   1 
ATOM   10983 O  O   . THR   D  1 97  ? 2.279   26.011  -28.711  1.00 60.92  ? 398  THR   D O   1 
ATOM   10984 C  CB  . THR   D  1 97  ? 3.387   29.139  -29.659  1.00 54.41  ? 398  THR   D CB  1 
ATOM   10985 O  OG1 . THR   D  1 97  ? 4.753   28.880  -29.986  1.00 56.32  ? 398  THR   D OG1 1 
ATOM   10986 C  CG2 . THR   D  1 97  ? 3.273   29.331  -28.159  1.00 57.19  ? 398  THR   D CG2 1 
ATOM   10987 N  N   . TYR   D  1 98  ? 4.294   26.327  -29.680  1.00 44.28  ? 399  TYR   D N   1 
ATOM   10988 C  CA  . TYR   D  1 98  ? 4.875   25.179  -28.995  1.00 42.22  ? 399  TYR   D CA  1 
ATOM   10989 C  C   . TYR   D  1 98  ? 6.377   25.379  -28.828  1.00 47.11  ? 399  TYR   D C   1 
ATOM   10990 O  O   . TYR   D  1 98  ? 6.941   26.392  -29.247  1.00 57.78  ? 399  TYR   D O   1 
ATOM   10991 C  CB  . TYR   D  1 98  ? 4.530   23.876  -29.717  1.00 40.10  ? 399  TYR   D CB  1 
ATOM   10992 C  CG  . TYR   D  1 98  ? 5.264   23.605  -31.007  1.00 46.51  ? 399  TYR   D CG  1 
ATOM   10993 C  CD1 . TYR   D  1 98  ? 6.274   22.662  -31.057  1.00 48.10  ? 399  TYR   D CD1 1 
ATOM   10994 C  CD2 . TYR   D  1 98  ? 4.922   24.254  -32.182  1.00 48.66  ? 399  TYR   D CD2 1 
ATOM   10995 C  CE1 . TYR   D  1 98  ? 6.940   22.389  -32.229  1.00 47.87  ? 399  TYR   D CE1 1 
ATOM   10996 C  CE2 . TYR   D  1 98  ? 5.584   23.982  -33.361  1.00 50.06  ? 399  TYR   D CE2 1 
ATOM   10997 C  CZ  . TYR   D  1 98  ? 6.598   23.049  -33.372  1.00 47.72  ? 399  TYR   D CZ  1 
ATOM   10998 O  OH  . TYR   D  1 98  ? 7.282   22.748  -34.525  1.00 51.29  ? 399  TYR   D OH  1 
ATOM   10999 N  N   . GLN   D  1 99  ? 7.021   24.401  -28.189  1.00 37.05  ? 400  GLN   D N   1 
ATOM   11000 C  CA  . GLN   D  1 99  ? 8.421   24.500  -27.792  1.00 41.60  ? 400  GLN   D CA  1 
ATOM   11001 C  C   . GLN   D  1 99  ? 9.197   23.294  -28.299  1.00 47.51  ? 400  GLN   D C   1 
ATOM   11002 O  O   . GLN   D  1 99  ? 8.805   22.151  -28.037  1.00 48.29  ? 400  GLN   D O   1 
ATOM   11003 C  CB  . GLN   D  1 99  ? 8.545   24.576  -26.262  1.00 50.27  ? 400  GLN   D CB  1 
ATOM   11004 C  CG  . GLN   D  1 99  ? 8.041   25.852  -25.665  1.00 44.89  ? 400  GLN   D CG  1 
ATOM   11005 C  CD  . GLN   D  1 99  ? 8.926   27.016  -26.023  1.00 52.84  ? 400  GLN   D CD  1 
ATOM   11006 O  OE1 . GLN   D  1 99  ? 10.131  26.988  -25.774  1.00 65.55  ? 400  GLN   D OE1 1 
ATOM   11007 N  NE2 . GLN   D  1 99  ? 8.340   28.049  -26.614  1.00 50.43  ? 400  GLN   D NE2 1 
ATOM   11008 N  N   . LEU   D  1 100 ? 10.311  23.542  -28.989  1.00 44.40  ? 401  LEU   D N   1 
ATOM   11009 C  CA  . LEU   D  1 100 ? 11.121  22.450  -29.520  1.00 40.74  ? 401  LEU   D CA  1 
ATOM   11010 C  C   . LEU   D  1 100 ? 11.950  21.813  -28.410  1.00 47.75  ? 401  LEU   D C   1 
ATOM   11011 O  O   . LEU   D  1 100 ? 12.594  22.520  -27.628  1.00 50.95  ? 401  LEU   D O   1 
ATOM   11012 C  CB  . LEU   D  1 100 ? 12.055  22.958  -30.618  1.00 33.86  ? 401  LEU   D CB  1 
ATOM   11013 C  CG  . LEU   D  1 100 ? 11.456  23.444  -31.956  1.00 33.85  ? 401  LEU   D CG  1 
ATOM   11014 C  CD1 . LEU   D  1 100 ? 12.561  23.845  -32.869  1.00 24.80  ? 401  LEU   D CD1 1 
ATOM   11015 C  CD2 . LEU   D  1 100 ? 10.610  22.376  -32.615  1.00 36.77  ? 401  LEU   D CD2 1 
ATOM   11016 N  N   . LYS   D  1 101 ? 11.959  20.483  -28.354  1.00 41.71  ? 402  LYS   D N   1 
ATOM   11017 C  CA  . LYS   D  1 101 ? 12.966  19.797  -27.558  1.00 27.13  ? 402  LYS   D CA  1 
ATOM   11018 C  C   . LYS   D  1 101 ? 14.361  20.218  -28.019  1.00 39.04  ? 402  LYS   D C   1 
ATOM   11019 O  O   . LYS   D  1 101 ? 14.542  20.781  -29.100  1.00 67.28  ? 402  LYS   D O   1 
ATOM   11020 C  CB  . LYS   D  1 101 ? 12.823  18.284  -27.685  1.00 36.11  ? 402  LYS   D CB  1 
ATOM   11021 C  CG  . LYS   D  1 101 ? 11.441  17.732  -27.344  1.00 48.05  ? 402  LYS   D CG  1 
ATOM   11022 C  CD  . LYS   D  1 101 ? 11.108  17.866  -25.849  1.00 59.27  ? 402  LYS   D CD  1 
ATOM   11023 C  CE  . LYS   D  1 101 ? 10.251  16.704  -25.342  1.00 60.27  ? 402  LYS   D CE  1 
ATOM   11024 N  NZ  . LYS   D  1 101 ? 9.200   17.174  -24.399  1.00 67.56  ? 402  LYS   D NZ  1 
ATOM   11025 N  N   . ASP   D  1 102 ? 15.360  19.940  -27.187  1.00 48.37  ? 403  ASP   D N   1 
ATOM   11026 C  CA  . ASP   D  1 102 ? 16.730  20.275  -27.556  1.00 42.46  ? 403  ASP   D CA  1 
ATOM   11027 C  C   . ASP   D  1 102 ? 17.184  19.466  -28.760  1.00 44.65  ? 403  ASP   D C   1 
ATOM   11028 O  O   . ASP   D  1 102 ? 17.902  19.977  -29.624  1.00 52.47  ? 403  ASP   D O   1 
ATOM   11029 C  CB  . ASP   D  1 102 ? 17.669  20.021  -26.376  1.00 51.60  ? 403  ASP   D CB  1 
ATOM   11030 C  CG  . ASP   D  1 102 ? 17.391  20.920  -25.195  1.00 66.22  ? 403  ASP   D CG  1 
ATOM   11031 O  OD1 . ASP   D  1 102 ? 16.417  21.712  -25.249  1.00 66.58  ? 403  ASP   D OD1 1 
ATOM   11032 O  OD2 . ASP   D  1 102 ? 18.162  20.830  -24.211  1.00 72.59  ? 403  ASP   D OD2 1 
ATOM   11033 N  N   . THR   D  1 103 ? 16.801  18.189  -28.818  1.00 38.62  ? 404  THR   D N   1 
ATOM   11034 C  CA  . THR   D  1 103 ? 17.141  17.387  -29.982  1.00 34.54  ? 404  THR   D CA  1 
ATOM   11035 C  C   . THR   D  1 103 ? 16.579  18.020  -31.246  1.00 46.74  ? 404  THR   D C   1 
ATOM   11036 O  O   . THR   D  1 103 ? 17.295  18.233  -32.227  1.00 38.81  ? 404  THR   D O   1 
ATOM   11037 C  CB  . THR   D  1 103 ? 16.612  15.959  -29.823  1.00 42.09  ? 404  THR   D CB  1 
ATOM   11038 O  OG1 . THR   D  1 103 ? 15.378  15.950  -29.072  1.00 45.67  ? 404  THR   D OG1 1 
ATOM   11039 C  CG2 . THR   D  1 103 ? 17.658  15.057  -29.173  1.00 34.21  ? 404  THR   D CG2 1 
ATOM   11040 N  N   . GLU   D  1 104 ? 15.297  18.373  -31.210  1.00 55.99  ? 405  GLU   D N   1 
ATOM   11041 C  CA  . GLU   D  1 104 ? 14.647  18.986  -32.358  1.00 45.98  ? 405  GLU   D CA  1 
ATOM   11042 C  C   . GLU   D  1 104 ? 15.352  20.276  -32.758  1.00 42.12  ? 405  GLU   D C   1 
ATOM   11043 O  O   . GLU   D  1 104 ? 15.618  20.497  -33.942  1.00 42.08  ? 405  GLU   D O   1 
ATOM   11044 C  CB  . GLU   D  1 104 ? 13.158  19.209  -32.034  1.00 40.92  ? 405  GLU   D CB  1 
ATOM   11045 C  CG  . GLU   D  1 104 ? 12.448  17.902  -31.582  1.00 29.93  ? 405  GLU   D CG  1 
ATOM   11046 C  CD  . GLU   D  1 104 ? 11.056  18.092  -30.977  1.00 40.46  ? 405  GLU   D CD  1 
ATOM   11047 O  OE1 . GLU   D  1 104 ? 10.341  17.068  -30.816  1.00 37.52  ? 405  GLU   D OE1 1 
ATOM   11048 O  OE2 . GLU   D  1 104 ? 10.678  19.240  -30.647  1.00 47.15  ? 405  GLU   D OE2 1 
ATOM   11049 N  N   . LEU   D  1 105 ? 15.727  21.109  -31.786  1.00 49.21  ? 406  LEU   D N   1 
ATOM   11050 C  CA  . LEU   D  1 105 ? 16.320  22.396  -32.138  1.00 44.52  ? 406  LEU   D CA  1 
ATOM   11051 C  C   . LEU   D  1 105 ? 17.671  22.222  -32.815  1.00 50.79  ? 406  LEU   D C   1 
ATOM   11052 O  O   . LEU   D  1 105 ? 17.997  22.958  -33.746  1.00 48.91  ? 406  LEU   D O   1 
ATOM   11053 C  CB  . LEU   D  1 105 ? 16.458  23.280  -30.903  1.00 35.64  ? 406  LEU   D CB  1 
ATOM   11054 C  CG  . LEU   D  1 105 ? 17.022  24.693  -31.125  1.00 38.31  ? 406  LEU   D CG  1 
ATOM   11055 C  CD1 . LEU   D  1 105 ? 15.969  25.661  -31.666  1.00 28.94  ? 406  LEU   D CD1 1 
ATOM   11056 C  CD2 . LEU   D  1 105 ? 17.566  25.221  -29.827  1.00 42.98  ? 406  LEU   D CD2 1 
ATOM   11057 N  N   . ILE   D  1 106 ? 18.476  21.257  -32.368  1.00 53.37  ? 407  ILE   D N   1 
ATOM   11058 C  CA  . ILE   D  1 106 ? 19.770  21.034  -33.011  1.00 39.63  ? 407  ILE   D CA  1 
ATOM   11059 C  C   . ILE   D  1 106 ? 19.584  20.480  -34.421  1.00 49.62  ? 407  ILE   D C   1 
ATOM   11060 O  O   . ILE   D  1 106 ? 20.314  20.854  -35.354  1.00 39.84  ? 407  ILE   D O   1 
ATOM   11061 C  CB  . ILE   D  1 106 ? 20.625  20.095  -32.155  1.00 35.02  ? 407  ILE   D CB  1 
ATOM   11062 C  CG1 . ILE   D  1 106 ? 21.044  20.784  -30.860  1.00 34.56  ? 407  ILE   D CG1 1 
ATOM   11063 C  CG2 . ILE   D  1 106 ? 21.835  19.623  -32.919  1.00 23.31  ? 407  ILE   D CG2 1 
ATOM   11064 C  CD1 . ILE   D  1 106 ? 21.450  19.796  -29.807  1.00 36.20  ? 407  ILE   D CD1 1 
ATOM   11065 N  N   . TYR   D  1 107 ? 18.624  19.560  -34.588  1.00 48.69  ? 408  TYR   D N   1 
ATOM   11066 C  CA  . TYR   D  1 107 ? 18.323  18.991  -35.897  1.00 43.92  ? 408  TYR   D CA  1 
ATOM   11067 C  C   . TYR   D  1 107 ? 17.827  20.064  -36.857  1.00 45.21  ? 408  TYR   D C   1 
ATOM   11068 O  O   . TYR   D  1 107 ? 18.243  20.123  -38.020  1.00 55.98  ? 408  TYR   D O   1 
ATOM   11069 C  CB  . TYR   D  1 107 ? 17.276  17.884  -35.755  1.00 36.18  ? 408  TYR   D CB  1 
ATOM   11070 C  CG  . TYR   D  1 107 ? 16.676  17.447  -37.082  1.00 36.85  ? 408  TYR   D CG  1 
ATOM   11071 C  CD1 . TYR   D  1 107 ? 17.182  16.355  -37.769  1.00 39.58  ? 408  TYR   D CD1 1 
ATOM   11072 C  CD2 . TYR   D  1 107 ? 15.595  18.123  -37.643  1.00 38.59  ? 408  TYR   D CD2 1 
ATOM   11073 C  CE1 . TYR   D  1 107 ? 16.638  15.948  -38.990  1.00 39.94  ? 408  TYR   D CE1 1 
ATOM   11074 C  CE2 . TYR   D  1 107 ? 15.054  17.736  -38.863  1.00 50.46  ? 408  TYR   D CE2 1 
ATOM   11075 C  CZ  . TYR   D  1 107 ? 15.575  16.643  -39.533  1.00 48.15  ? 408  TYR   D CZ  1 
ATOM   11076 O  OH  . TYR   D  1 107 ? 15.013  16.240  -40.729  1.00 52.41  ? 408  TYR   D OH  1 
ATOM   11077 N  N   . GLY   D  1 108 ? 16.900  20.899  -36.392  1.00 42.56  ? 409  GLY   D N   1 
ATOM   11078 C  CA  . GLY   D  1 108 ? 16.343  21.921  -37.254  1.00 42.58  ? 409  GLY   D CA  1 
ATOM   11079 C  C   . GLY   D  1 108 ? 17.380  22.921  -37.709  1.00 41.53  ? 409  GLY   D C   1 
ATOM   11080 O  O   . GLY   D  1 108 ? 17.360  23.363  -38.853  1.00 60.34  ? 409  GLY   D O   1 
ATOM   11081 N  N   . ALA   D  1 109 ? 18.305  23.289  -36.823  1.00 38.43  ? 410  ALA   D N   1 
ATOM   11082 C  CA  . ALA   D  1 109 ? 19.302  24.285  -37.190  1.00 39.84  ? 410  ALA   D CA  1 
ATOM   11083 C  C   . ALA   D  1 109 ? 20.358  23.711  -38.121  1.00 40.19  ? 410  ALA   D C   1 
ATOM   11084 O  O   . ALA   D  1 109 ? 20.911  24.431  -38.956  1.00 37.54  ? 410  ALA   D O   1 
ATOM   11085 C  CB  . ALA   D  1 109 ? 19.964  24.849  -35.932  1.00 37.13  ? 410  ALA   D CB  1 
ATOM   11086 N  N   . LYS   D  1 110 ? 20.658  22.428  -37.985  1.00 37.83  ? 411  LYS   D N   1 
ATOM   11087 C  CA  . LYS   D  1 110 ? 21.584  21.792  -38.904  1.00 35.41  ? 411  LYS   D CA  1 
ATOM   11088 C  C   . LYS   D  1 110 ? 20.960  21.636  -40.291  1.00 48.39  ? 411  LYS   D C   1 
ATOM   11089 O  O   . LYS   D  1 110 ? 21.640  21.797  -41.317  1.00 39.70  ? 411  LYS   D O   1 
ATOM   11090 C  CB  . LYS   D  1 110 ? 22.000  20.437  -38.338  1.00 22.11  ? 411  LYS   D CB  1 
ATOM   11091 C  CG  . LYS   D  1 110 ? 23.025  20.494  -37.241  1.00 33.64  ? 411  LYS   D CG  1 
ATOM   11092 C  CD  . LYS   D  1 110 ? 23.451  19.100  -36.914  1.00 33.58  ? 411  LYS   D CD  1 
ATOM   11093 C  CE  . LYS   D  1 110 ? 24.277  19.060  -35.647  1.00 42.80  ? 411  LYS   D CE  1 
ATOM   11094 N  NZ  . LYS   D  1 110 ? 24.530  17.628  -35.291  1.00 44.90  ? 411  LYS   D NZ  1 
ATOM   11095 N  N   . HIS   D  1 111 ? 19.664  21.340  -40.347  1.00 44.77  ? 412  HIS   D N   1 
ATOM   11096 C  CA  . HIS   D  1 111 ? 19.056  21.137  -41.650  1.00 48.74  ? 412  HIS   D CA  1 
ATOM   11097 C  C   . HIS   D  1 111 ? 18.755  22.452  -42.360  1.00 48.14  ? 412  HIS   D C   1 
ATOM   11098 O  O   . HIS   D  1 111 ? 18.847  22.515  -43.590  1.00 52.66  ? 412  HIS   D O   1 
ATOM   11099 C  CB  . HIS   D  1 111 ? 17.827  20.248  -41.500  1.00 42.06  ? 412  HIS   D CB  1 
ATOM   11100 C  CG  . HIS   D  1 111 ? 18.185  18.801  -41.401  1.00 41.24  ? 412  HIS   D CG  1 
ATOM   11101 N  ND1 . HIS   D  1 111 ? 18.928  18.295  -40.359  1.00 40.16  ? 412  HIS   D ND1 1 
ATOM   11102 C  CD2 . HIS   D  1 111 ? 17.955  17.760  -42.239  1.00 41.23  ? 412  HIS   D CD2 1 
ATOM   11103 C  CE1 . HIS   D  1 111 ? 19.130  17.001  -40.552  1.00 45.31  ? 412  HIS   D CE1 1 
ATOM   11104 N  NE2 . HIS   D  1 111 ? 18.546  16.649  -41.684  1.00 43.23  ? 412  HIS   D NE2 1 
ATOM   11105 N  N   . ALA   D  1 112 ? 18.463  23.523  -41.629  1.00 37.91  ? 413  ALA   D N   1 
ATOM   11106 C  CA  . ALA   D  1 112 ? 18.335  24.803  -42.306  1.00 42.20  ? 413  ALA   D CA  1 
ATOM   11107 C  C   . ALA   D  1 112 ? 19.635  25.192  -42.994  1.00 44.60  ? 413  ALA   D C   1 
ATOM   11108 O  O   . ALA   D  1 112 ? 19.610  25.803  -44.064  1.00 44.03  ? 413  ALA   D O   1 
ATOM   11109 C  CB  . ALA   D  1 112 ? 17.908  25.890  -41.329  1.00 38.47  ? 413  ALA   D CB  1 
ATOM   11110 N  N   . TRP   D  1 113 ? 20.779  24.847  -42.408  1.00 41.98  ? 414  TRP   D N   1 
ATOM   11111 C  CA  . TRP   D  1 113 ? 22.033  25.066  -43.118  1.00 43.17  ? 414  TRP   D CA  1 
ATOM   11112 C  C   . TRP   D  1 113 ? 22.137  24.132  -44.320  1.00 44.93  ? 414  TRP   D C   1 
ATOM   11113 O  O   . TRP   D  1 113 ? 22.540  24.552  -45.409  1.00 59.37  ? 414  TRP   D O   1 
ATOM   11114 C  CB  . TRP   D  1 113 ? 23.213  24.865  -42.165  1.00 33.75  ? 414  TRP   D CB  1 
ATOM   11115 C  CG  . TRP   D  1 113 ? 24.563  25.159  -42.756  1.00 44.74  ? 414  TRP   D CG  1 
ATOM   11116 C  CD1 . TRP   D  1 113 ? 24.830  25.802  -43.946  1.00 32.16  ? 414  TRP   D CD1 1 
ATOM   11117 C  CD2 . TRP   D  1 113 ? 25.844  24.820  -42.186  1.00 54.46  ? 414  TRP   D CD2 1 
ATOM   11118 N  NE1 . TRP   D  1 113 ? 26.194  25.873  -44.140  1.00 44.02  ? 414  TRP   D NE1 1 
ATOM   11119 C  CE2 . TRP   D  1 113 ? 26.836  25.278  -43.082  1.00 55.80  ? 414  TRP   D CE2 1 
ATOM   11120 C  CE3 . TRP   D  1 113 ? 26.248  24.179  -41.005  1.00 49.50  ? 414  TRP   D CE3 1 
ATOM   11121 C  CZ2 . TRP   D  1 113 ? 28.208  25.109  -42.834  1.00 58.58  ? 414  TRP   D CZ2 1 
ATOM   11122 C  CZ3 . TRP   D  1 113 ? 27.620  24.014  -40.764  1.00 35.36  ? 414  TRP   D CZ3 1 
ATOM   11123 C  CH2 . TRP   D  1 113 ? 28.573  24.482  -41.667  1.00 47.86  ? 414  TRP   D CH2 1 
ATOM   11124 N  N   . ARG   D  1 114 ? 21.756  22.869  -44.139  1.00 39.20  ? 415  ARG   D N   1 
ATOM   11125 C  CA  . ARG   D  1 114 ? 21.841  21.883  -45.207  1.00 30.25  ? 415  ARG   D CA  1 
ATOM   11126 C  C   . ARG   D  1 114 ? 20.968  22.288  -46.383  1.00 42.80  ? 415  ARG   D C   1 
ATOM   11127 O  O   . ARG   D  1 114 ? 21.304  22.004  -47.537  1.00 46.64  ? 415  ARG   D O   1 
ATOM   11128 C  CB  . ARG   D  1 114 ? 21.408  20.517  -44.652  1.00 31.34  ? 415  ARG   D CB  1 
ATOM   11129 C  CG  . ARG   D  1 114 ? 21.550  19.284  -45.581  1.00 37.92  ? 415  ARG   D CG  1 
ATOM   11130 C  CD  . ARG   D  1 114 ? 20.938  18.032  -44.893  1.00 31.73  ? 415  ARG   D CD  1 
ATOM   11131 N  NE  . ARG   D  1 114 ? 21.326  16.775  -45.533  1.00 33.64  ? 415  ARG   D NE  1 
ATOM   11132 C  CZ  . ARG   D  1 114 ? 20.978  15.569  -45.089  1.00 38.70  ? 415  ARG   D CZ  1 
ATOM   11133 N  NH1 . ARG   D  1 114 ? 21.369  14.474  -45.730  1.00 41.95  ? 415  ARG   D NH1 1 
ATOM   11134 N  NH2 . ARG   D  1 114 ? 20.250  15.452  -43.993  1.00 53.89  ? 415  ARG   D NH2 1 
ATOM   11135 N  N   . ASN   D  1 115 ? 19.852  22.955  -46.102  1.00 34.82  ? 416  ASN   D N   1 
ATOM   11136 C  CA  . ASN   D  1 115 ? 18.884  23.357  -47.100  1.00 30.79  ? 416  ASN   D CA  1 
ATOM   11137 C  C   . ASN   D  1 115 ? 19.169  24.727  -47.681  1.00 42.99  ? 416  ASN   D C   1 
ATOM   11138 O  O   . ASN   D  1 115 ? 18.502  25.106  -48.652  1.00 44.06  ? 416  ASN   D O   1 
ATOM   11139 C  CB  . ASN   D  1 115 ? 17.486  23.369  -46.494  1.00 25.98  ? 416  ASN   D CB  1 
ATOM   11140 C  CG  . ASN   D  1 115 ? 17.045  22.004  -46.017  1.00 29.25  ? 416  ASN   D CG  1 
ATOM   11141 O  OD1 . ASN   D  1 115 ? 17.562  20.982  -46.463  1.00 41.27  ? 416  ASN   D OD1 1 
ATOM   11142 N  ND2 . ASN   D  1 115 ? 16.072  21.979  -45.110  1.00 30.63  ? 416  ASN   D ND2 1 
ATOM   11143 N  N   . ALA   D  1 116 ? 20.124  25.481  -47.109  1.00 35.72  ? 417  ALA   D N   1 
ATOM   11144 C  CA  . ALA   D  1 116 ? 20.504  26.783  -47.664  1.00 42.43  ? 417  ALA   D CA  1 
ATOM   11145 C  C   . ALA   D  1 116 ? 21.066  26.650  -49.081  1.00 40.91  ? 417  ALA   D C   1 
ATOM   11146 O  O   . ALA   D  1 116 ? 22.240  26.311  -49.270  1.00 38.88  ? 417  ALA   D O   1 
ATOM   11147 C  CB  . ALA   D  1 116 ? 21.527  27.486  -46.778  1.00 26.65  ? 417  ALA   D CB  1 
ATOM   11148 N  N   . SER   D  1 117 ? 20.253  26.959  -50.088  1.00 37.14  ? 418  SER   D N   1 
ATOM   11149 C  CA  A SER   D  1 117 ? 20.668  26.687  -51.457  0.69 38.39  ? 418  SER   D CA  1 
ATOM   11150 C  CA  B SER   D  1 117 ? 20.662  26.694  -51.464  0.31 38.43  ? 418  SER   D CA  1 
ATOM   11151 C  C   . SER   D  1 117 ? 21.798  27.609  -51.901  1.00 42.06  ? 418  SER   D C   1 
ATOM   11152 O  O   . SER   D  1 117 ? 22.663  27.189  -52.672  1.00 49.29  ? 418  SER   D O   1 
ATOM   11153 C  CB  A SER   D  1 117 ? 19.463  26.787  -52.398  0.69 37.92  ? 418  SER   D CB  1 
ATOM   11154 C  CB  B SER   D  1 117 ? 19.465  26.834  -52.400  0.31 37.34  ? 418  SER   D CB  1 
ATOM   11155 O  OG  A SER   D  1 117 ? 18.762  28.015  -52.241  0.69 34.21  ? 418  SER   D OG  1 
ATOM   11156 O  OG  B SER   D  1 117 ? 18.466  25.880  -52.087  0.31 34.04  ? 418  SER   D OG  1 
ATOM   11157 N  N   . ARG   D  1 118 ? 21.833  28.843  -51.403  1.00 38.64  ? 419  ARG   D N   1 
ATOM   11158 C  CA  . ARG   D  1 118 ? 22.872  29.795  -51.781  1.00 35.21  ? 419  ARG   D CA  1 
ATOM   11159 C  C   . ARG   D  1 118 ? 24.220  29.551  -51.120  1.00 33.47  ? 419  ARG   D C   1 
ATOM   11160 O  O   . ARG   D  1 118 ? 25.144  30.337  -51.365  1.00 39.46  ? 419  ARG   D O   1 
ATOM   11161 C  CB  . ARG   D  1 118 ? 22.433  31.222  -51.441  1.00 37.98  ? 419  ARG   D CB  1 
ATOM   11162 C  CG  . ARG   D  1 118 ? 21.115  31.607  -52.091  1.00 45.30  ? 419  ARG   D CG  1 
ATOM   11163 C  CD  . ARG   D  1 118 ? 20.762  33.075  -51.928  1.00 42.25  ? 419  ARG   D CD  1 
ATOM   11164 N  NE  . ARG   D  1 118 ? 19.821  33.441  -52.978  1.00 50.80  ? 419  ARG   D NE  1 
ATOM   11165 C  CZ  . ARG   D  1 118 ? 19.149  34.587  -53.057  1.00 50.27  ? 419  ARG   D CZ  1 
ATOM   11166 N  NH1 . ARG   D  1 118 ? 19.299  35.530  -52.138  1.00 42.61  ? 419  ARG   D NH1 1 
ATOM   11167 N  NH2 . ARG   D  1 118 ? 18.316  34.784  -54.079  1.00 44.49  ? 419  ARG   D NH2 1 
ATOM   11168 N  N   . CYS   D  1 119 ? 24.372  28.529  -50.277  1.00 32.23  ? 420  CYS   D N   1 
ATOM   11169 C  CA  . CYS   D  1 119 ? 25.581  28.375  -49.478  1.00 34.31  ? 420  CYS   D CA  1 
ATOM   11170 C  C   . CYS   D  1 119 ? 26.415  27.230  -50.022  1.00 34.11  ? 420  CYS   D C   1 
ATOM   11171 O  O   . CYS   D  1 119 ? 25.945  26.082  -50.086  1.00 29.77  ? 420  CYS   D O   1 
ATOM   11172 C  CB  . CYS   D  1 119 ? 25.272  28.142  -48.000  1.00 44.06  ? 420  CYS   D CB  1 
ATOM   11173 S  SG  . CYS   D  1 119 ? 26.760  27.743  -47.000  1.00 46.25  ? 420  CYS   D SG  1 
ATOM   11174 N  N   . VAL   D  1 120 ? 27.669  27.554  -50.360  1.00 29.40  ? 421  VAL   D N   1 
ATOM   11175 C  CA  . VAL   D  1 120 ? 28.632  26.613  -50.915  1.00 35.22  ? 421  VAL   D CA  1 
ATOM   11176 C  C   . VAL   D  1 120 ? 29.415  25.859  -49.850  1.00 36.17  ? 421  VAL   D C   1 
ATOM   11177 O  O   . VAL   D  1 120 ? 30.230  24.993  -50.192  1.00 40.39  ? 421  VAL   D O   1 
ATOM   11178 C  CB  . VAL   D  1 120 ? 29.582  27.403  -51.843  1.00 46.11  ? 421  VAL   D CB  1 
ATOM   11179 C  CG1 . VAL   D  1 120 ? 30.544  28.202  -51.020  1.00 33.20  ? 421  VAL   D CG1 1 
ATOM   11180 C  CG2 . VAL   D  1 120 ? 30.314  26.500  -52.833  1.00 48.03  ? 421  VAL   D CG2 1 
ATOM   11181 N  N   . GLY   D  1 121 ? 29.200  26.150  -48.568  1.00 39.66  ? 422  GLY   D N   1 
ATOM   11182 C  CA  . GLY   D  1 121 ? 29.971  25.534  -47.512  1.00 32.01  ? 422  GLY   D CA  1 
ATOM   11183 C  C   . GLY   D  1 121 ? 29.322  24.343  -46.849  1.00 41.30  ? 422  GLY   D C   1 
ATOM   11184 O  O   . GLY   D  1 121 ? 29.845  23.848  -45.843  1.00 44.76  ? 422  GLY   D O   1 
ATOM   11185 N  N   . ARG   D  1 122 ? 28.214  23.846  -47.386  1.00 38.74  ? 423  ARG   D N   1 
ATOM   11186 C  CA  . ARG   D  1 122 ? 27.393  22.853  -46.700  1.00 31.05  ? 423  ARG   D CA  1 
ATOM   11187 C  C   . ARG   D  1 122 ? 28.034  21.476  -46.574  1.00 38.59  ? 423  ARG   D C   1 
ATOM   11188 O  O   . ARG   D  1 122 ? 27.404  20.590  -45.983  1.00 42.22  ? 423  ARG   D O   1 
ATOM   11189 C  CB  . ARG   D  1 122 ? 26.059  22.707  -47.420  1.00 35.28  ? 423  ARG   D CB  1 
ATOM   11190 C  CG  . ARG   D  1 122 ? 25.253  23.984  -47.471  1.00 38.08  ? 423  ARG   D CG  1 
ATOM   11191 C  CD  . ARG   D  1 122 ? 23.974  23.714  -48.217  1.00 47.16  ? 423  ARG   D CD  1 
ATOM   11192 N  NE  . ARG   D  1 122 ? 24.015  24.117  -49.622  1.00 42.94  ? 423  ARG   D NE  1 
ATOM   11193 C  CZ  . ARG   D  1 122 ? 23.100  23.730  -50.500  1.00 46.80  ? 423  ARG   D CZ  1 
ATOM   11194 N  NH1 . ARG   D  1 122 ? 22.123  22.924  -50.097  1.00 33.12  ? 423  ARG   D NH1 1 
ATOM   11195 N  NH2 . ARG   D  1 122 ? 23.165  24.135  -51.769  1.00 53.58  ? 423  ARG   D NH2 1 
ATOM   11196 N  N   . ILE   D  1 123 ? 29.242  21.242  -47.088  1.00 36.87  ? 424  ILE   D N   1 
ATOM   11197 C  CA  . ILE   D  1 123 ? 29.786  19.911  -46.869  1.00 40.43  ? 424  ILE   D CA  1 
ATOM   11198 C  C   . ILE   D  1 123 ? 29.999  19.696  -45.380  1.00 45.10  ? 424  ILE   D C   1 
ATOM   11199 O  O   . ILE   D  1 123 ? 29.917  18.563  -44.895  1.00 49.26  ? 424  ILE   D O   1 
ATOM   11200 C  CB  . ILE   D  1 123 ? 31.079  19.671  -47.675  1.00 35.69  ? 424  ILE   D CB  1 
ATOM   11201 C  CG1 . ILE   D  1 123 ? 31.504  18.204  -47.506  1.00 37.32  ? 424  ILE   D CG1 1 
ATOM   11202 C  CG2 . ILE   D  1 123 ? 32.175  20.615  -47.218  1.00 42.97  ? 424  ILE   D CG2 1 
ATOM   11203 C  CD1 . ILE   D  1 123 ? 32.569  17.718  -48.420  1.00 30.15  ? 424  ILE   D CD1 1 
ATOM   11204 N  N   . GLN   D  1 124 ? 30.214  20.781  -44.632  1.00 49.61  ? 425  GLN   D N   1 
ATOM   11205 C  CA  . GLN   D  1 124 ? 30.428  20.798  -43.184  1.00 51.29  ? 425  GLN   D CA  1 
ATOM   11206 C  C   . GLN   D  1 124 ? 29.139  20.738  -42.376  1.00 53.23  ? 425  GLN   D C   1 
ATOM   11207 O  O   . GLN   D  1 124 ? 29.213  20.755  -41.143  1.00 64.80  ? 425  GLN   D O   1 
ATOM   11208 C  CB  . GLN   D  1 124 ? 31.166  22.084  -42.770  1.00 49.54  ? 425  GLN   D CB  1 
ATOM   11209 C  CG  . GLN   D  1 124 ? 32.579  22.246  -43.270  1.00 53.88  ? 425  GLN   D CG  1 
ATOM   11210 C  CD  . GLN   D  1 124 ? 33.553  21.405  -42.492  1.00 61.33  ? 425  GLN   D CD  1 
ATOM   11211 O  OE1 . GLN   D  1 124 ? 33.161  20.609  -41.648  1.00 69.61  ? 425  GLN   D OE1 1 
ATOM   11212 N  NE2 . GLN   D  1 124 ? 34.833  21.576  -42.770  1.00 71.30  ? 425  GLN   D NE2 1 
ATOM   11213 N  N   . TRP   D  1 125 ? 27.976  20.673  -43.032  1.00 50.70  ? 426  TRP   D N   1 
ATOM   11214 C  CA  . TRP   D  1 125 ? 26.715  21.076  -42.409  1.00 47.63  ? 426  TRP   D CA  1 
ATOM   11215 C  C   . TRP   D  1 125 ? 26.431  20.356  -41.094  1.00 55.80  ? 426  TRP   D C   1 
ATOM   11216 O  O   . TRP   D  1 125 ? 25.825  20.932  -40.186  1.00 50.65  ? 426  TRP   D O   1 
ATOM   11217 C  CB  . TRP   D  1 125 ? 25.560  20.846  -43.378  1.00 40.33  ? 426  TRP   D CB  1 
ATOM   11218 C  CG  . TRP   D  1 125 ? 25.140  19.420  -43.522  1.00 44.85  ? 426  TRP   D CG  1 
ATOM   11219 C  CD1 . TRP   D  1 125 ? 25.588  18.522  -44.446  1.00 50.57  ? 426  TRP   D CD1 1 
ATOM   11220 C  CD2 . TRP   D  1 125 ? 24.172  18.728  -42.726  1.00 46.40  ? 426  TRP   D CD2 1 
ATOM   11221 N  NE1 . TRP   D  1 125 ? 24.968  17.305  -44.269  1.00 44.61  ? 426  TRP   D NE1 1 
ATOM   11222 C  CE2 . TRP   D  1 125 ? 24.092  17.404  -43.220  1.00 43.40  ? 426  TRP   D CE2 1 
ATOM   11223 C  CE3 . TRP   D  1 125 ? 23.368  19.096  -41.640  1.00 41.33  ? 426  TRP   D CE3 1 
ATOM   11224 C  CZ2 . TRP   D  1 125 ? 23.236  16.446  -42.664  1.00 41.54  ? 426  TRP   D CZ2 1 
ATOM   11225 C  CZ3 . TRP   D  1 125 ? 22.525  18.145  -41.088  1.00 40.29  ? 426  TRP   D CZ3 1 
ATOM   11226 C  CH2 . TRP   D  1 125 ? 22.466  16.836  -41.598  1.00 40.46  ? 426  TRP   D CH2 1 
ATOM   11227 N  N   . SER   D  1 126 ? 26.832  19.092  -40.974  1.00 46.39  ? 427  SER   D N   1 
ATOM   11228 C  CA  . SER   D  1 126 ? 26.472  18.344  -39.782  1.00 45.23  ? 427  SER   D CA  1 
ATOM   11229 C  C   . SER   D  1 126 ? 27.401  18.616  -38.609  1.00 52.62  ? 427  SER   D C   1 
ATOM   11230 O  O   . SER   D  1 126 ? 27.096  18.190  -37.494  1.00 55.81  ? 427  SER   D O   1 
ATOM   11231 C  CB  . SER   D  1 126 ? 26.459  16.852  -40.078  1.00 48.03  ? 427  SER   D CB  1 
ATOM   11232 O  OG  . SER   D  1 126 ? 27.763  16.412  -40.412  1.00 62.53  ? 427  SER   D OG  1 
ATOM   11233 N  N   . LYS   D  1 127 ? 28.529  19.281  -38.843  1.00 51.06  ? 428  LYS   D N   1 
ATOM   11234 C  CA  . LYS   D  1 127 ? 29.419  19.739  -37.781  1.00 39.62  ? 428  LYS   D CA  1 
ATOM   11235 C  C   . LYS   D  1 127 ? 29.071  21.180  -37.420  1.00 48.87  ? 428  LYS   D C   1 
ATOM   11236 O  O   . LYS   D  1 127 ? 29.840  22.109  -37.652  1.00 62.80  ? 428  LYS   D O   1 
ATOM   11237 C  CB  . LYS   D  1 127 ? 30.877  19.635  -38.217  1.00 42.20  ? 428  LYS   D CB  1 
ATOM   11238 C  CG  . LYS   D  1 127 ? 31.541  18.285  -38.027  1.00 51.42  ? 428  LYS   D CG  1 
ATOM   11239 C  CD  . LYS   D  1 127 ? 33.081  18.460  -37.912  1.00 69.41  ? 428  LYS   D CD  1 
ATOM   11240 C  CE  . LYS   D  1 127 ? 33.707  17.719  -36.695  1.00 72.03  ? 428  LYS   D CE  1 
ATOM   11241 N  NZ  . LYS   D  1 127 ? 33.323  18.232  -35.324  1.00 55.55  ? 428  LYS   D NZ  1 
ATOM   11242 N  N   . LEU   D  1 128 ? 27.870  21.365  -36.892  1.00 42.79  ? 429  LEU   D N   1 
ATOM   11243 C  CA  . LEU   D  1 128 ? 27.432  22.664  -36.406  1.00 37.41  ? 429  LEU   D CA  1 
ATOM   11244 C  C   . LEU   D  1 128 ? 27.285  22.589  -34.891  1.00 44.39  ? 429  LEU   D C   1 
ATOM   11245 O  O   . LEU   D  1 128 ? 26.823  21.576  -34.358  1.00 47.13  ? 429  LEU   D O   1 
ATOM   11246 C  CB  . LEU   D  1 128 ? 26.111  23.071  -37.042  1.00 21.36  ? 429  LEU   D CB  1 
ATOM   11247 C  CG  . LEU   D  1 128 ? 25.622  24.463  -36.647  1.00 28.88  ? 429  LEU   D CG  1 
ATOM   11248 C  CD1 . LEU   D  1 128 ? 26.543  25.557  -37.164  1.00 24.26  ? 429  LEU   D CD1 1 
ATOM   11249 C  CD2 . LEU   D  1 128 ? 24.214  24.704  -37.087  1.00 20.60  ? 429  LEU   D CD2 1 
ATOM   11250 N  N   . GLN   D  1 129 ? 27.684  23.651  -34.199  1.00 33.44  ? 430  GLN   D N   1 
ATOM   11251 C  CA  . GLN   D  1 129 ? 27.624  23.700  -32.747  1.00 34.85  ? 430  GLN   D CA  1 
ATOM   11252 C  C   . GLN   D  1 129 ? 26.479  24.622  -32.357  1.00 39.36  ? 430  GLN   D C   1 
ATOM   11253 O  O   . GLN   D  1 129 ? 26.575  25.841  -32.543  1.00 37.70  ? 430  GLN   D O   1 
ATOM   11254 C  CB  . GLN   D  1 129 ? 28.944  24.180  -32.157  1.00 34.63  ? 430  GLN   D CB  1 
ATOM   11255 C  CG  . GLN   D  1 129 ? 28.943  24.174  -30.619  1.00 43.75  ? 430  GLN   D CG  1 
ATOM   11256 C  CD  . GLN   D  1 129 ? 28.657  22.789  -30.028  1.00 49.67  ? 430  GLN   D CD  1 
ATOM   11257 O  OE1 . GLN   D  1 129 ? 29.342  21.812  -30.338  1.00 52.07  ? 430  GLN   D OE1 1 
ATOM   11258 N  NE2 . GLN   D  1 129 ? 27.638  22.707  -29.182  1.00 50.91  ? 430  GLN   D NE2 1 
ATOM   11259 N  N   . VAL   D  1 130 ? 25.390  24.046  -31.831  1.00 41.58  ? 431  VAL   D N   1 
ATOM   11260 C  CA  . VAL   D  1 130 ? 24.178  24.816  -31.560  1.00 37.26  ? 431  VAL   D CA  1 
ATOM   11261 C  C   . VAL   D  1 130 ? 24.189  25.265  -30.105  1.00 45.15  ? 431  VAL   D C   1 
ATOM   11262 O  O   . VAL   D  1 130 ? 24.439  24.464  -29.199  1.00 51.42  ? 431  VAL   D O   1 
ATOM   11263 C  CB  . VAL   D  1 130 ? 22.919  24.003  -31.880  1.00 38.18  ? 431  VAL   D CB  1 
ATOM   11264 C  CG1 . VAL   D  1 130 ? 21.696  24.881  -31.680  1.00 33.12  ? 431  VAL   D CG1 1 
ATOM   11265 C  CG2 . VAL   D  1 130 ? 22.977  23.505  -33.321  1.00 46.28  ? 431  VAL   D CG2 1 
ATOM   11266 N  N   . PHE   D  1 131 ? 23.944  26.554  -29.888  1.00 38.55  ? 432  PHE   D N   1 
ATOM   11267 C  CA  . PHE   D  1 131 ? 23.935  27.176  -28.571  1.00 32.78  ? 432  PHE   D CA  1 
ATOM   11268 C  C   . PHE   D  1 131 ? 22.501  27.603  -28.268  1.00 38.87  ? 432  PHE   D C   1 
ATOM   11269 O  O   . PHE   D  1 131 ? 22.044  28.648  -28.752  1.00 40.95  ? 432  PHE   D O   1 
ATOM   11270 C  CB  . PHE   D  1 131 ? 24.894  28.372  -28.534  1.00 42.10  ? 432  PHE   D CB  1 
ATOM   11271 C  CG  . PHE   D  1 131 ? 26.352  27.990  -28.544  1.00 38.03  ? 432  PHE   D CG  1 
ATOM   11272 C  CD1 . PHE   D  1 131 ? 26.894  27.256  -27.505  1.00 39.10  ? 432  PHE   D CD1 1 
ATOM   11273 C  CD2 . PHE   D  1 131 ? 27.186  28.381  -29.567  1.00 31.09  ? 432  PHE   D CD2 1 
ATOM   11274 C  CE1 . PHE   D  1 131 ? 28.229  26.906  -27.499  1.00 34.12  ? 432  PHE   D CE1 1 
ATOM   11275 C  CE2 . PHE   D  1 131 ? 28.535  28.016  -29.573  1.00 29.48  ? 432  PHE   D CE2 1 
ATOM   11276 C  CZ  . PHE   D  1 131 ? 29.047  27.285  -28.529  1.00 32.57  ? 432  PHE   D CZ  1 
ATOM   11277 N  N   . ASP   D  1 132 ? 21.808  26.814  -27.439  1.00 38.41  ? 433  ASP   D N   1 
ATOM   11278 C  CA  . ASP   D  1 132 ? 20.430  27.105  -27.043  1.00 34.89  ? 433  ASP   D CA  1 
ATOM   11279 C  C   . ASP   D  1 132 ? 20.400  28.329  -26.140  1.00 35.90  ? 433  ASP   D C   1 
ATOM   11280 O  O   . ASP   D  1 132 ? 20.811  28.266  -24.979  1.00 50.68  ? 433  ASP   D O   1 
ATOM   11281 C  CB  . ASP   D  1 132 ? 19.823  25.905  -26.332  1.00 32.02  ? 433  ASP   D CB  1 
ATOM   11282 C  CG  . ASP   D  1 132 ? 18.330  26.015  -26.175  1.00 38.38  ? 433  ASP   D CG  1 
ATOM   11283 O  OD1 . ASP   D  1 132 ? 17.706  24.957  -25.914  1.00 42.56  ? 433  ASP   D OD1 1 
ATOM   11284 O  OD2 . ASP   D  1 132 ? 17.778  27.138  -26.315  1.00 34.67  ? 433  ASP   D OD2 1 
ATOM   11285 N  N   . ALA   D  1 133 ? 19.911  29.444  -26.660  1.00 29.05  ? 434  ALA   D N   1 
ATOM   11286 C  CA  . ALA   D  1 133 ? 19.800  30.668  -25.884  1.00 35.13  ? 434  ALA   D CA  1 
ATOM   11287 C  C   . ALA   D  1 133 ? 18.343  31.074  -25.705  1.00 39.25  ? 434  ALA   D C   1 
ATOM   11288 O  O   . ALA   D  1 133 ? 18.025  32.259  -25.538  1.00 28.80  ? 434  ALA   D O   1 
ATOM   11289 C  CB  . ALA   D  1 133 ? 20.591  31.798  -26.536  1.00 48.76  ? 434  ALA   D CB  1 
ATOM   11290 N  N   . ARG   D  1 134 ? 17.448  30.090  -25.724  1.00 33.70  ? 435  ARG   D N   1 
ATOM   11291 C  CA  . ARG   D  1 134 ? 16.032  30.386  -25.621  1.00 31.62  ? 435  ARG   D CA  1 
ATOM   11292 C  C   . ARG   D  1 134 ? 15.613  30.862  -24.240  1.00 41.77  ? 435  ARG   D C   1 
ATOM   11293 O  O   . ARG   D  1 134 ? 14.462  31.276  -24.092  1.00 45.53  ? 435  ARG   D O   1 
ATOM   11294 C  CB  . ARG   D  1 134 ? 15.248  29.155  -26.056  1.00 29.90  ? 435  ARG   D CB  1 
ATOM   11295 C  CG  . ARG   D  1 134 ? 15.337  28.974  -27.591  1.00 34.92  ? 435  ARG   D CG  1 
ATOM   11296 C  CD  . ARG   D  1 134 ? 14.714  27.687  -28.068  1.00 37.90  ? 435  ARG   D CD  1 
ATOM   11297 N  NE  . ARG   D  1 134 ? 15.293  26.545  -27.375  1.00 41.20  ? 435  ARG   D NE  1 
ATOM   11298 C  CZ  . ARG   D  1 134 ? 14.699  25.366  -27.314  1.00 40.03  ? 435  ARG   D CZ  1 
ATOM   11299 N  NH1 . ARG   D  1 134 ? 13.520  25.212  -27.897  1.00 47.57  ? 435  ARG   D NH1 1 
ATOM   11300 N  NH2 . ARG   D  1 134 ? 15.265  24.357  -26.669  1.00 37.47  ? 435  ARG   D NH2 1 
ATOM   11301 N  N   . ASP   D  1 135 ? 16.514  30.855  -23.241  1.00 48.28  ? 436  ASP   D N   1 
ATOM   11302 C  CA  . ASP   D  1 135 ? 16.190  31.362  -21.906  1.00 48.14  ? 436  ASP   D CA  1 
ATOM   11303 C  C   . ASP   D  1 135 ? 16.598  32.811  -21.705  1.00 46.03  ? 436  ASP   D C   1 
ATOM   11304 O  O   . ASP   D  1 135 ? 16.366  33.349  -20.622  1.00 45.79  ? 436  ASP   D O   1 
ATOM   11305 C  CB  . ASP   D  1 135 ? 16.819  30.490  -20.797  1.00 37.92  ? 436  ASP   D CB  1 
ATOM   11306 C  CG  . ASP   D  1 135 ? 18.336  30.452  -20.837  1.00 43.68  ? 436  ASP   D CG  1 
ATOM   11307 O  OD1 . ASP   D  1 135 ? 18.941  29.950  -19.870  1.00 49.92  ? 436  ASP   D OD1 1 
ATOM   11308 O  OD2 . ASP   D  1 135 ? 18.939  30.904  -21.821  1.00 53.03  ? 436  ASP   D OD2 1 
ATOM   11309 N  N   . CYS   D  1 136 ? 17.140  33.460  -22.735  1.00 47.98  ? 437  CYS   D N   1 
ATOM   11310 C  CA  . CYS   D  1 136 ? 17.566  34.849  -22.630  1.00 39.03  ? 437  CYS   D CA  1 
ATOM   11311 C  C   . CYS   D  1 136 ? 16.353  35.759  -22.510  1.00 52.03  ? 437  CYS   D C   1 
ATOM   11312 O  O   . CYS   D  1 136 ? 15.302  35.494  -23.106  1.00 59.41  ? 437  CYS   D O   1 
ATOM   11313 C  CB  . CYS   D  1 136 ? 18.406  35.217  -23.853  1.00 25.36  ? 437  CYS   D CB  1 
ATOM   11314 S  SG  . CYS   D  1 136 ? 19.372  36.743  -23.754  1.00 35.75  ? 437  CYS   D SG  1 
ATOM   11315 N  N   . THR   D  1 137 ? 16.474  36.813  -21.694  1.00 46.40  ? 438  THR   D N   1 
ATOM   11316 C  CA  . THR   D  1 137 ? 15.358  37.730  -21.494  1.00 37.56  ? 438  THR   D CA  1 
ATOM   11317 C  C   . THR   D  1 137 ? 15.706  39.197  -21.700  1.00 34.64  ? 438  THR   D C   1 
ATOM   11318 O  O   . THR   D  1 137 ? 14.781  40.020  -21.760  1.00 34.66  ? 438  THR   D O   1 
ATOM   11319 C  CB  . THR   D  1 137 ? 14.742  37.558  -20.088  1.00 45.56  ? 438  THR   D CB  1 
ATOM   11320 O  OG1 . THR   D  1 137 ? 15.580  38.149  -19.077  1.00 31.28  ? 438  THR   D OG1 1 
ATOM   11321 C  CG2 . THR   D  1 137 ? 14.516  36.076  -19.764  1.00 39.90  ? 438  THR   D CG2 1 
ATOM   11322 N  N   . THR   D  1 138 ? 16.989  39.551  -21.825  1.00 35.98  ? 439  THR   D N   1 
ATOM   11323 C  CA  . THR   D  1 138 ? 17.431  40.944  -21.871  1.00 37.75  ? 439  THR   D CA  1 
ATOM   11324 C  C   . THR   D  1 138 ? 18.600  41.100  -22.837  1.00 40.74  ? 439  THR   D C   1 
ATOM   11325 O  O   . THR   D  1 138 ? 19.376  40.163  -23.082  1.00 31.64  ? 439  THR   D O   1 
ATOM   11326 C  CB  . THR   D  1 138 ? 17.918  41.468  -20.502  1.00 43.27  ? 439  THR   D CB  1 
ATOM   11327 O  OG1 . THR   D  1 138 ? 19.130  40.784  -20.141  1.00 46.19  ? 439  THR   D OG1 1 
ATOM   11328 C  CG2 . THR   D  1 138 ? 16.875  41.288  -19.423  1.00 31.96  ? 439  THR   D CG2 1 
ATOM   11329 N  N   . ALA   D  1 139 ? 18.750  42.334  -23.335  1.00 40.21  ? 440  ALA   D N   1 
ATOM   11330 C  CA  . ALA   D  1 139 ? 19.853  42.646  -24.237  1.00 41.99  ? 440  ALA   D CA  1 
ATOM   11331 C  C   . ALA   D  1 139 ? 21.190  42.238  -23.637  1.00 49.75  ? 440  ALA   D C   1 
ATOM   11332 O  O   . ALA   D  1 139 ? 22.035  41.654  -24.332  1.00 52.42  ? 440  ALA   D O   1 
ATOM   11333 C  CB  . ALA   D  1 139 ? 19.853  44.136  -24.573  1.00 43.33  ? 440  ALA   D CB  1 
ATOM   11334 N  N   . HIS   D  1 140 ? 21.392  42.528  -22.344  1.00 44.21  ? 441  HIS   D N   1 
ATOM   11335 C  CA  . HIS   D  1 140 ? 22.625  42.136  -21.669  1.00 34.28  ? 441  HIS   D CA  1 
ATOM   11336 C  C   . HIS   D  1 140 ? 22.835  40.642  -21.767  1.00 35.12  ? 441  HIS   D C   1 
ATOM   11337 O  O   . HIS   D  1 140 ? 23.954  40.181  -22.036  1.00 39.57  ? 441  HIS   D O   1 
ATOM   11338 C  CB  . HIS   D  1 140 ? 22.598  42.560  -20.190  1.00 36.76  ? 441  HIS   D CB  1 
ATOM   11339 C  CG  . HIS   D  1 140 ? 22.993  43.984  -19.965  1.00 29.81  ? 441  HIS   D CG  1 
ATOM   11340 N  ND1 . HIS   D  1 140 ? 22.086  45.023  -20.019  1.00 38.15  ? 441  HIS   D ND1 1 
ATOM   11341 C  CD2 . HIS   D  1 140 ? 24.203  44.549  -19.733  1.00 32.27  ? 441  HIS   D CD2 1 
ATOM   11342 C  CE1 . HIS   D  1 140 ? 22.719  46.166  -19.801  1.00 41.83  ? 441  HIS   D CE1 1 
ATOM   11343 N  NE2 . HIS   D  1 140 ? 24.004  45.907  -19.623  1.00 32.76  ? 441  HIS   D NE2 1 
ATOM   11344 N  N   . GLY   D  1 141 ? 21.766  39.867  -21.544  1.00 38.94  ? 442  GLY   D N   1 
ATOM   11345 C  CA  . GLY   D  1 141 ? 21.862  38.430  -21.716  1.00 42.34  ? 442  GLY   D CA  1 
ATOM   11346 C  C   . GLY   D  1 141 ? 22.321  38.051  -23.109  1.00 47.04  ? 442  GLY   D C   1 
ATOM   11347 O  O   . GLY   D  1 141 ? 23.187  37.180  -23.270  1.00 41.25  ? 442  GLY   D O   1 
ATOM   11348 N  N   . MET   D  1 142 ? 21.762  38.719  -24.133  1.00 46.58  ? 443  MET   D N   1 
ATOM   11349 C  CA  . MET   D  1 142 ? 22.148  38.462  -25.522  1.00 36.76  ? 443  MET   D CA  1 
ATOM   11350 C  C   . MET   D  1 142 ? 23.625  38.764  -25.760  1.00 37.72  ? 443  MET   D C   1 
ATOM   11351 O  O   . MET   D  1 142 ? 24.333  37.970  -26.396  1.00 31.03  ? 443  MET   D O   1 
ATOM   11352 C  CB  . MET   D  1 142 ? 21.279  39.286  -26.476  1.00 39.56  ? 443  MET   D CB  1 
ATOM   11353 C  CG  . MET   D  1 142 ? 19.869  38.744  -26.720  1.00 28.04  ? 443  MET   D CG  1 
ATOM   11354 S  SD  . MET   D  1 142 ? 18.777  39.985  -27.471  1.00 45.31  ? 443  MET   D SD  1 
ATOM   11355 C  CE  . MET   D  1 142 ? 19.308  39.972  -29.219  1.00 23.10  ? 443  MET   D CE  1 
ATOM   11356 N  N   . PHE   D  1 143 ? 24.106  39.919  -25.270  1.00 36.31  ? 444  PHE   D N   1 
ATOM   11357 C  CA  . PHE   D  1 143 ? 25.530  40.245  -25.372  1.00 33.12  ? 444  PHE   D CA  1 
ATOM   11358 C  C   . PHE   D  1 143 ? 26.396  39.144  -24.772  1.00 42.43  ? 444  PHE   D C   1 
ATOM   11359 O  O   . PHE   D  1 143 ? 27.403  38.729  -25.356  1.00 52.64  ? 444  PHE   D O   1 
ATOM   11360 C  CB  . PHE   D  1 143 ? 25.809  41.587  -24.690  1.00 39.97  ? 444  PHE   D CB  1 
ATOM   11361 C  CG  . PHE   D  1 143 ? 27.261  41.930  -24.605  1.00 46.52  ? 444  PHE   D CG  1 
ATOM   11362 C  CD1 . PHE   D  1 143 ? 27.925  41.895  -23.386  1.00 53.85  ? 444  PHE   D CD1 1 
ATOM   11363 C  CD2 . PHE   D  1 143 ? 27.971  42.271  -25.732  1.00 39.06  ? 444  PHE   D CD2 1 
ATOM   11364 C  CE1 . PHE   D  1 143 ? 29.270  42.204  -23.299  1.00 49.91  ? 444  PHE   D CE1 1 
ATOM   11365 C  CE2 . PHE   D  1 143 ? 29.313  42.582  -25.654  1.00 43.50  ? 444  PHE   D CE2 1 
ATOM   11366 C  CZ  . PHE   D  1 143 ? 29.965  42.549  -24.426  1.00 53.85  ? 444  PHE   D CZ  1 
ATOM   11367 N  N   . ASN   D  1 144 ? 26.004  38.647  -23.603  1.00 41.19  ? 445  ASN   D N   1 
ATOM   11368 C  CA  . ASN   D  1 144 ? 26.727  37.551  -22.980  1.00 35.78  ? 445  ASN   D CA  1 
ATOM   11369 C  C   . ASN   D  1 144 ? 26.729  36.324  -23.890  1.00 36.54  ? 445  ASN   D C   1 
ATOM   11370 O  O   . ASN   D  1 144 ? 27.787  35.781  -24.225  1.00 39.60  ? 445  ASN   D O   1 
ATOM   11371 C  CB  . ASN   D  1 144 ? 26.089  37.266  -21.611  1.00 46.25  ? 445  ASN   D CB  1 
ATOM   11372 C  CG  . ASN   D  1 144 ? 26.827  36.212  -20.801  1.00 47.10  ? 445  ASN   D CG  1 
ATOM   11373 O  OD1 . ASN   D  1 144 ? 28.035  36.270  -20.633  1.00 41.45  ? 445  ASN   D OD1 1 
ATOM   11374 N  ND2 . ASN   D  1 144 ? 26.078  35.249  -20.270  1.00 51.11  ? 445  ASN   D ND2 1 
ATOM   11375 N  N   . TYR   D  1 145 ? 25.541  35.883  -24.317  1.00 37.55  ? 446  TYR   D N   1 
ATOM   11376 C  CA  . TYR   D  1 145 ? 25.440  34.744  -25.232  1.00 45.20  ? 446  TYR   D CA  1 
ATOM   11377 C  C   . TYR   D  1 145 ? 26.252  34.940  -26.519  1.00 43.62  ? 446  TYR   D C   1 
ATOM   11378 O  O   . TYR   D  1 145 ? 26.841  33.985  -27.052  1.00 31.68  ? 446  TYR   D O   1 
ATOM   11379 C  CB  . TYR   D  1 145 ? 23.975  34.495  -25.591  1.00 45.48  ? 446  TYR   D CB  1 
ATOM   11380 C  CG  . TYR   D  1 145 ? 23.292  33.457  -24.737  1.00 39.63  ? 446  TYR   D CG  1 
ATOM   11381 C  CD1 . TYR   D  1 145 ? 22.235  33.794  -23.904  1.00 27.37  ? 446  TYR   D CD1 1 
ATOM   11382 C  CD2 . TYR   D  1 145 ? 23.716  32.133  -24.759  1.00 34.08  ? 446  TYR   D CD2 1 
ATOM   11383 C  CE1 . TYR   D  1 145 ? 21.607  32.830  -23.127  1.00 23.36  ? 446  TYR   D CE1 1 
ATOM   11384 C  CE2 . TYR   D  1 145 ? 23.105  31.177  -23.991  1.00 35.05  ? 446  TYR   D CE2 1 
ATOM   11385 C  CZ  . TYR   D  1 145 ? 22.056  31.525  -23.177  1.00 31.91  ? 446  TYR   D CZ  1 
ATOM   11386 O  OH  . TYR   D  1 145 ? 21.445  30.549  -22.428  1.00 42.34  ? 446  TYR   D OH  1 
ATOM   11387 N  N   . ILE   D  1 146 ? 26.272  36.159  -27.052  1.00 37.46  ? 447  ILE   D N   1 
ATOM   11388 C  CA  . ILE   D  1 146 ? 26.940  36.354  -28.332  1.00 45.81  ? 447  ILE   D CA  1 
ATOM   11389 C  C   . ILE   D  1 146 ? 28.455  36.375  -28.151  1.00 42.74  ? 447  ILE   D C   1 
ATOM   11390 O  O   . ILE   D  1 146 ? 29.194  35.871  -29.006  1.00 37.60  ? 447  ILE   D O   1 
ATOM   11391 C  CB  . ILE   D  1 146 ? 26.405  37.626  -29.033  1.00 40.29  ? 447  ILE   D CB  1 
ATOM   11392 C  CG1 . ILE   D  1 146 ? 25.042  37.349  -29.672  1.00 33.36  ? 447  ILE   D CG1 1 
ATOM   11393 C  CG2 . ILE   D  1 146 ? 27.371  38.123  -30.082  1.00 28.50  ? 447  ILE   D CG2 1 
ATOM   11394 C  CD1 . ILE   D  1 146 ? 24.342  38.595  -30.184  1.00 36.85  ? 447  ILE   D CD1 1 
ATOM   11395 N  N   . CYS   D  1 147 ? 28.938  36.935  -27.032  1.00 47.96  ? 448  CYS   D N   1 
ATOM   11396 C  CA  . CYS   D  1 147 ? 30.375  36.959  -26.758  1.00 39.89  ? 448  CYS   D CA  1 
ATOM   11397 C  C   . CYS   D  1 147 ? 30.949  35.556  -26.617  1.00 46.11  ? 448  CYS   D C   1 
ATOM   11398 O  O   . CYS   D  1 147 ? 32.105  35.306  -26.995  1.00 45.58  ? 448  CYS   D O   1 
ATOM   11399 C  CB  . CYS   D  1 147 ? 30.658  37.736  -25.476  1.00 35.49  ? 448  CYS   D CB  1 
ATOM   11400 S  SG  . CYS   D  1 147 ? 30.831  39.512  -25.637  1.00 45.52  ? 448  CYS   D SG  1 
ATOM   11401 N  N   . ASN   D  1 148 ? 30.176  34.632  -26.058  1.00 47.59  ? 449  ASN   D N   1 
ATOM   11402 C  CA  . ASN   D  1 148 ? 30.687  33.279  -25.928  1.00 40.77  ? 449  ASN   D CA  1 
ATOM   11403 C  C   . ASN   D  1 148 ? 30.630  32.563  -27.262  1.00 36.81  ? 449  ASN   D C   1 
ATOM   11404 O  O   . ASN   D  1 148 ? 31.493  31.726  -27.556  1.00 36.93  ? 449  ASN   D O   1 
ATOM   11405 C  CB  . ASN   D  1 148 ? 29.906  32.526  -24.844  1.00 46.03  ? 449  ASN   D CB  1 
ATOM   11406 C  CG  . ASN   D  1 148 ? 30.031  33.172  -23.461  1.00 44.87  ? 449  ASN   D CG  1 
ATOM   11407 O  OD1 . ASN   D  1 148 ? 31.041  33.821  -23.143  1.00 43.45  ? 449  ASN   D OD1 1 
ATOM   11408 N  ND2 . ASN   D  1 148 ? 29.007  32.989  -22.635  1.00 39.42  ? 449  ASN   D ND2 1 
ATOM   11409 N  N   . HIS   D  1 149 ? 29.640  32.906  -28.088  1.00 42.71  ? 450  HIS   D N   1 
ATOM   11410 C  CA  . HIS   D  1 149 ? 29.628  32.452  -29.474  1.00 32.20  ? 450  HIS   D CA  1 
ATOM   11411 C  C   . HIS   D  1 149 ? 30.913  32.862  -30.176  1.00 37.97  ? 450  HIS   D C   1 
ATOM   11412 O  O   . HIS   D  1 149 ? 31.665  32.014  -30.673  1.00 43.50  ? 450  HIS   D O   1 
ATOM   11413 C  CB  . HIS   D  1 149 ? 28.399  33.018  -30.187  1.00 35.76  ? 450  HIS   D CB  1 
ATOM   11414 C  CG  . HIS   D  1 149 ? 28.230  32.541  -31.598  1.00 43.80  ? 450  HIS   D CG  1 
ATOM   11415 N  ND1 . HIS   D  1 149 ? 27.004  32.194  -32.117  1.00 41.68  ? 450  HIS   D ND1 1 
ATOM   11416 C  CD2 . HIS   D  1 149 ? 29.125  32.362  -32.600  1.00 47.25  ? 450  HIS   D CD2 1 
ATOM   11417 C  CE1 . HIS   D  1 149 ? 27.152  31.812  -33.374  1.00 46.63  ? 450  HIS   D CE1 1 
ATOM   11418 N  NE2 . HIS   D  1 149 ? 28.431  31.901  -33.690  1.00 40.35  ? 450  HIS   D NE2 1 
ATOM   11419 N  N   . VAL   D  1 150 ? 31.193  34.169  -30.196  1.00 32.31  ? 451  VAL   D N   1 
ATOM   11420 C  CA  . VAL   D  1 150 ? 32.380  34.684  -30.873  1.00 26.96  ? 451  VAL   D CA  1 
ATOM   11421 C  C   . VAL   D  1 150 ? 33.631  33.961  -30.395  1.00 40.94  ? 451  VAL   D C   1 
ATOM   11422 O  O   . VAL   D  1 150 ? 34.426  33.458  -31.199  1.00 53.45  ? 451  VAL   D O   1 
ATOM   11423 C  CB  . VAL   D  1 150 ? 32.490  36.198  -30.646  1.00 31.10  ? 451  VAL   D CB  1 
ATOM   11424 C  CG1 . VAL   D  1 150 ? 33.867  36.700  -31.072  1.00 25.14  ? 451  VAL   D CG1 1 
ATOM   11425 C  CG2 . VAL   D  1 150 ? 31.360  36.896  -31.364  1.00 25.90  ? 451  VAL   D CG2 1 
ATOM   11426 N  N   . LYS   D  1 151 ? 33.797  33.864  -29.071  1.00 47.82  ? 452  LYS   D N   1 
ATOM   11427 C  CA  . LYS   D  1 151 ? 35.014  33.295  -28.499  1.00 45.14  ? 452  LYS   D CA  1 
ATOM   11428 C  C   . LYS   D  1 151 ? 35.165  31.827  -28.867  1.00 37.35  ? 452  LYS   D C   1 
ATOM   11429 O  O   . LYS   D  1 151 ? 36.272  31.373  -29.173  1.00 42.68  ? 452  LYS   D O   1 
ATOM   11430 C  CB  . LYS   D  1 151 ? 35.007  33.476  -26.973  1.00 46.47  ? 452  LYS   D CB  1 
ATOM   11431 C  CG  . LYS   D  1 151 ? 36.240  32.931  -26.232  1.00 42.51  ? 452  LYS   D CG  1 
ATOM   11432 C  CD  . LYS   D  1 151 ? 36.339  33.606  -24.870  1.00 37.72  ? 452  LYS   D CD  1 
ATOM   11433 C  CE  . LYS   D  1 151 ? 37.692  33.426  -24.214  1.00 47.14  ? 452  LYS   D CE  1 
ATOM   11434 N  NZ  . LYS   D  1 151 ? 37.879  34.383  -23.079  1.00 49.15  ? 452  LYS   D NZ  1 
ATOM   11435 N  N   . TYR   D  1 152 ? 34.069  31.065  -28.826  1.00 36.90  ? 453  TYR   D N   1 
ATOM   11436 C  CA  . TYR   D  1 152 ? 34.127  29.649  -29.192  1.00 41.46  ? 453  TYR   D CA  1 
ATOM   11437 C  C   . TYR   D  1 152 ? 34.388  29.482  -30.687  1.00 50.69  ? 453  TYR   D C   1 
ATOM   11438 O  O   . TYR   D  1 152 ? 35.228  28.665  -31.099  1.00 48.10  ? 453  TYR   D O   1 
ATOM   11439 C  CB  . TYR   D  1 152 ? 32.819  28.948  -28.795  1.00 42.33  ? 453  TYR   D CB  1 
ATOM   11440 C  CG  . TYR   D  1 152 ? 32.657  27.564  -29.407  1.00 46.42  ? 453  TYR   D CG  1 
ATOM   11441 C  CD1 . TYR   D  1 152 ? 33.156  26.444  -28.762  1.00 49.63  ? 453  TYR   D CD1 1 
ATOM   11442 C  CD2 . TYR   D  1 152 ? 32.024  27.384  -30.633  1.00 46.57  ? 453  TYR   D CD2 1 
ATOM   11443 C  CE1 . TYR   D  1 152 ? 33.031  25.187  -29.316  1.00 51.50  ? 453  TYR   D CE1 1 
ATOM   11444 C  CE2 . TYR   D  1 152 ? 31.902  26.122  -31.196  1.00 47.63  ? 453  TYR   D CE2 1 
ATOM   11445 C  CZ  . TYR   D  1 152 ? 32.410  25.030  -30.528  1.00 48.25  ? 453  TYR   D CZ  1 
ATOM   11446 O  OH  . TYR   D  1 152 ? 32.306  23.766  -31.064  1.00 60.84  ? 453  TYR   D OH  1 
ATOM   11447 N  N   . ALA   D  1 153 ? 33.662  30.251  -31.512  1.00 48.74  ? 454  ALA   D N   1 
ATOM   11448 C  CA  . ALA   D  1 153 ? 33.799  30.154  -32.963  1.00 36.47  ? 454  ALA   D CA  1 
ATOM   11449 C  C   . ALA   D  1 153 ? 35.205  30.528  -33.399  1.00 39.84  ? 454  ALA   D C   1 
ATOM   11450 O  O   . ALA   D  1 153 ? 35.826  29.813  -34.186  1.00 43.54  ? 454  ALA   D O   1 
ATOM   11451 C  CB  . ALA   D  1 153 ? 32.762  31.046  -33.654  1.00 24.85  ? 454  ALA   D CB  1 
ATOM   11452 N  N   . THR   D  1 154 ? 35.738  31.631  -32.861  1.00 44.90  ? 455  THR   D N   1 
ATOM   11453 C  CA  . THR   D  1 154 ? 37.046  32.116  -33.292  1.00 40.88  ? 455  THR   D CA  1 
ATOM   11454 C  C   . THR   D  1 154 ? 38.165  31.138  -32.922  1.00 56.98  ? 455  THR   D C   1 
ATOM   11455 O  O   . THR   D  1 154 ? 39.090  30.926  -33.722  1.00 67.89  ? 455  THR   D O   1 
ATOM   11456 C  CB  . THR   D  1 154 ? 37.302  33.510  -32.706  1.00 32.57  ? 455  THR   D CB  1 
ATOM   11457 O  OG1 . THR   D  1 154 ? 36.300  34.436  -33.174  1.00 33.04  ? 455  THR   D OG1 1 
ATOM   11458 C  CG2 . THR   D  1 154 ? 38.664  34.018  -33.123  1.00 24.46  ? 455  THR   D CG2 1 
ATOM   11459 N  N   . ASN   D  1 155 ? 38.095  30.529  -31.721  1.00 53.43  ? 456  ASN   D N   1 
ATOM   11460 C  CA  . ASN   D  1 155 ? 38.992  29.436  -31.277  1.00 31.86  ? 456  ASN   D CA  1 
ATOM   11461 C  C   . ASN   D  1 155 ? 40.450  29.729  -31.617  1.00 38.56  ? 456  ASN   D C   1 
ATOM   11462 O  O   . ASN   D  1 155 ? 41.205  28.843  -32.024  1.00 44.69  ? 456  ASN   D O   1 
ATOM   11463 C  CB  . ASN   D  1 155 ? 38.544  28.089  -31.869  1.00 31.57  ? 456  ASN   D CB  1 
ATOM   11464 C  CG  . ASN   D  1 155 ? 39.273  26.903  -31.290  1.00 41.39  ? 456  ASN   D CG  1 
ATOM   11465 O  OD1 . ASN   D  1 155 ? 39.622  26.891  -30.121  1.00 57.01  ? 456  ASN   D OD1 1 
ATOM   11466 N  ND2 . ASN   D  1 155 ? 39.490  25.881  -32.107  1.00 40.28  ? 456  ASN   D ND2 1 
ATOM   11467 N  N   . LYS   D  1 156 ? 40.847  31.000  -31.463  1.00 43.89  ? 457  LYS   D N   1 
ATOM   11468 C  CA  . LYS   D  1 156 ? 42.241  31.430  -31.633  1.00 47.74  ? 457  LYS   D CA  1 
ATOM   11469 C  C   . LYS   D  1 156 ? 42.753  31.176  -33.051  1.00 47.66  ? 457  LYS   D C   1 
ATOM   11470 O  O   . LYS   D  1 156 ? 43.911  30.807  -33.263  1.00 39.87  ? 457  LYS   D O   1 
ATOM   11471 C  CB  . LYS   D  1 156 ? 43.160  30.770  -30.595  1.00 57.95  ? 457  LYS   D CB  1 
ATOM   11472 C  CG  . LYS   D  1 156 ? 43.039  31.364  -29.207  1.00 65.00  ? 457  LYS   D CG  1 
ATOM   11473 C  CD  . LYS   D  1 156 ? 44.266  31.057  -28.364  1.00 79.47  ? 457  LYS   D CD  1 
ATOM   11474 C  CE  . LYS   D  1 156 ? 44.374  29.563  -28.036  1.00 85.94  ? 457  LYS   D CE  1 
ATOM   11475 N  NZ  . LYS   D  1 156 ? 44.243  29.244  -26.564  1.00 76.66  ? 457  LYS   D NZ  1 
ATOM   11476 N  N   . GLY   D  1 157 ? 41.895  31.413  -34.036  1.00 52.07  ? 458  GLY   D N   1 
ATOM   11477 C  CA  . GLY   D  1 157 ? 42.251  31.257  -35.416  1.00 45.91  ? 458  GLY   D CA  1 
ATOM   11478 C  C   . GLY   D  1 157 ? 41.728  29.989  -36.048  1.00 53.73  ? 458  GLY   D C   1 
ATOM   11479 O  O   . GLY   D  1 157 ? 41.618  29.918  -37.285  1.00 53.22  ? 458  GLY   D O   1 
ATOM   11480 N  N   . ASN   D  1 158 ? 41.391  28.989  -35.241  1.00 35.69  ? 459  ASN   D N   1 
ATOM   11481 C  CA  . ASN   D  1 158 ? 40.947  27.713  -35.786  1.00 46.93  ? 459  ASN   D CA  1 
ATOM   11482 C  C   . ASN   D  1 158 ? 39.420  27.669  -35.763  1.00 56.22  ? 459  ASN   D C   1 
ATOM   11483 O  O   . ASN   D  1 158 ? 38.812  27.018  -34.922  1.00 52.86  ? 459  ASN   D O   1 
ATOM   11484 C  CB  . ASN   D  1 158 ? 41.569  26.577  -35.002  1.00 31.75  ? 459  ASN   D CB  1 
ATOM   11485 C  CG  . ASN   D  1 158 ? 41.253  25.244  -35.587  1.00 45.10  ? 459  ASN   D CG  1 
ATOM   11486 O  OD1 . ASN   D  1 158 ? 40.560  25.144  -36.600  1.00 59.85  ? 459  ASN   D OD1 1 
ATOM   11487 N  ND2 . ASN   D  1 158 ? 41.774  24.197  -34.971  1.00 40.98  ? 459  ASN   D ND2 1 
ATOM   11488 N  N   . LEU   D  1 159 ? 38.801  28.326  -36.752  1.00 59.99  ? 460  LEU   D N   1 
ATOM   11489 C  CA  . LEU   D  1 159 ? 37.377  28.634  -36.670  1.00 44.47  ? 460  LEU   D CA  1 
ATOM   11490 C  C   . LEU   D  1 159 ? 36.507  27.387  -36.723  1.00 43.74  ? 460  LEU   D C   1 
ATOM   11491 O  O   . LEU   D  1 159 ? 36.821  26.403  -37.400  1.00 46.80  ? 460  LEU   D O   1 
ATOM   11492 C  CB  . LEU   D  1 159 ? 36.961  29.566  -37.788  1.00 41.08  ? 460  LEU   D CB  1 
ATOM   11493 C  CG  . LEU   D  1 159 ? 37.930  30.714  -38.033  1.00 52.94  ? 460  LEU   D CG  1 
ATOM   11494 C  CD1 . LEU   D  1 159 ? 37.377  31.567  -39.140  1.00 68.21  ? 460  LEU   D CD1 1 
ATOM   11495 C  CD2 . LEU   D  1 159 ? 38.084  31.546  -36.816  1.00 43.10  ? 460  LEU   D CD2 1 
ATOM   11496 N  N   . ARG   D  1 160 ? 35.399  27.449  -35.983  1.00 37.76  ? 461  ARG   D N   1 
ATOM   11497 C  CA  . ARG   D  1 160 ? 34.407  26.389  -35.881  1.00 45.40  ? 461  ARG   D CA  1 
ATOM   11498 C  C   . ARG   D  1 160 ? 33.019  26.947  -36.170  1.00 53.65  ? 461  ARG   D C   1 
ATOM   11499 O  O   . ARG   D  1 160 ? 32.678  28.056  -35.745  1.00 54.01  ? 461  ARG   D O   1 
ATOM   11500 C  CB  . ARG   D  1 160 ? 34.397  25.765  -34.488  1.00 49.49  ? 461  ARG   D CB  1 
ATOM   11501 C  CG  . ARG   D  1 160 ? 35.757  25.395  -33.950  1.00 46.25  ? 461  ARG   D CG  1 
ATOM   11502 C  CD  . ARG   D  1 160 ? 35.643  24.708  -32.596  1.00 45.93  ? 461  ARG   D CD  1 
ATOM   11503 N  NE  . ARG   D  1 160 ? 35.881  25.611  -31.478  1.00 39.03  ? 461  ARG   D NE  1 
ATOM   11504 C  CZ  . ARG   D  1 160 ? 36.168  25.183  -30.263  1.00 48.90  ? 461  ARG   D CZ  1 
ATOM   11505 N  NH1 . ARG   D  1 160 ? 36.239  23.879  -30.048  1.00 53.91  ? 461  ARG   D NH1 1 
ATOM   11506 N  NH2 . ARG   D  1 160 ? 36.357  26.038  -29.267  1.00 43.30  ? 461  ARG   D NH2 1 
ATOM   11507 N  N   . SER   D  1 161 ? 32.212  26.158  -36.873  1.00 49.40  ? 462  SER   D N   1 
ATOM   11508 C  CA  . SER   D  1 161 ? 30.843  26.558  -37.175  1.00 47.85  ? 462  SER   D CA  1 
ATOM   11509 C  C   . SER   D  1 161 ? 30.017  26.587  -35.899  1.00 35.97  ? 462  SER   D C   1 
ATOM   11510 O  O   . SER   D  1 161 ? 30.114  25.689  -35.060  1.00 31.56  ? 462  SER   D O   1 
ATOM   11511 C  CB  . SER   D  1 161 ? 30.201  25.591  -38.176  1.00 51.57  ? 462  SER   D CB  1 
ATOM   11512 O  OG  . SER   D  1 161 ? 31.155  25.002  -39.057  1.00 57.87  ? 462  SER   D OG  1 
ATOM   11513 N  N   . ALA   D  1 162 ? 29.169  27.602  -35.773  1.00 25.42  ? 463  ALA   D N   1 
ATOM   11514 C  CA  . ALA   D  1 162 ? 28.310  27.671  -34.610  1.00 27.36  ? 463  ALA   D CA  1 
ATOM   11515 C  C   . ALA   D  1 162 ? 27.188  28.665  -34.856  1.00 31.23  ? 463  ALA   D C   1 
ATOM   11516 O  O   . ALA   D  1 162 ? 27.371  29.668  -35.545  1.00 37.42  ? 463  ALA   D O   1 
ATOM   11517 C  CB  . ALA   D  1 162 ? 29.109  28.079  -33.359  1.00 31.04  ? 463  ALA   D CB  1 
ATOM   11518 N  N   . ILE   D  1 163 ? 26.046  28.389  -34.226  1.00 44.25  ? 464  ILE   D N   1 
ATOM   11519 C  CA  . ILE   D  1 163 ? 24.849  29.217  -34.243  1.00 32.60  ? 464  ILE   D CA  1 
ATOM   11520 C  C   . ILE   D  1 163 ? 24.374  29.365  -32.808  1.00 33.33  ? 464  ILE   D C   1 
ATOM   11521 O  O   . ILE   D  1 163 ? 24.500  28.438  -31.999  1.00 32.49  ? 464  ILE   D O   1 
ATOM   11522 C  CB  . ILE   D  1 163 ? 23.745  28.582  -35.097  1.00 29.22  ? 464  ILE   D CB  1 
ATOM   11523 C  CG1 . ILE   D  1 163 ? 22.508  29.469  -35.160  1.00 25.43  ? 464  ILE   D CG1 1 
ATOM   11524 C  CG2 . ILE   D  1 163 ? 23.374  27.231  -34.554  1.00 20.07  ? 464  ILE   D CG2 1 
ATOM   11525 C  CD1 . ILE   D  1 163 ? 21.465  28.950  -36.159  1.00 31.10  ? 464  ILE   D CD1 1 
ATOM   11526 N  N   . THR   D  1 164 ? 23.805  30.528  -32.497  1.00 33.25  ? 465  THR   D N   1 
ATOM   11527 C  CA  . THR   D  1 164 ? 23.168  30.760  -31.206  1.00 44.02  ? 465  THR   D CA  1 
ATOM   11528 C  C   . THR   D  1 164 ? 21.739  31.239  -31.426  1.00 38.48  ? 465  THR   D C   1 
ATOM   11529 O  O   . THR   D  1 164 ? 21.519  32.275  -32.060  1.00 35.94  ? 465  THR   D O   1 
ATOM   11530 C  CB  . THR   D  1 164 ? 23.950  31.770  -30.365  1.00 40.88  ? 465  THR   D CB  1 
ATOM   11531 O  OG1 . THR   D  1 164 ? 25.261  31.250  -30.094  1.00 40.96  ? 465  THR   D OG1 1 
ATOM   11532 C  CG2 . THR   D  1 164 ? 23.252  31.973  -29.063  1.00 31.17  ? 465  THR   D CG2 1 
ATOM   11533 N  N   . ILE   D  1 165 ? 20.783  30.516  -30.842  1.00 41.74  ? 466  ILE   D N   1 
ATOM   11534 C  CA  . ILE   D  1 165 ? 19.360  30.629  -31.143  1.00 39.84  ? 466  ILE   D CA  1 
ATOM   11535 C  C   . ILE   D  1 165 ? 18.647  31.241  -29.939  1.00 46.40  ? 466  ILE   D C   1 
ATOM   11536 O  O   . ILE   D  1 165 ? 18.621  30.646  -28.854  1.00 46.13  ? 466  ILE   D O   1 
ATOM   11537 C  CB  . ILE   D  1 165 ? 18.779  29.250  -31.488  1.00 38.47  ? 466  ILE   D CB  1 
ATOM   11538 C  CG1 . ILE   D  1 165 ? 19.531  28.641  -32.668  1.00 36.05  ? 466  ILE   D CG1 1 
ATOM   11539 C  CG2 . ILE   D  1 165 ? 17.308  29.333  -31.767  1.00 40.63  ? 466  ILE   D CG2 1 
ATOM   11540 C  CD1 . ILE   D  1 165 ? 19.037  27.244  -33.022  1.00 35.96  ? 466  ILE   D CD1 1 
ATOM   11541 N  N   . PHE   D  1 166 ? 18.054  32.414  -30.140  1.00 48.55  ? 467  PHE   D N   1 
ATOM   11542 C  CA  . PHE   D  1 166 ? 17.401  33.201  -29.099  1.00 39.11  ? 467  PHE   D CA  1 
ATOM   11543 C  C   . PHE   D  1 166 ? 15.896  32.936  -29.105  1.00 37.01  ? 467  PHE   D C   1 
ATOM   11544 O  O   . PHE   D  1 166 ? 15.421  32.185  -29.954  1.00 43.08  ? 467  PHE   D O   1 
ATOM   11545 C  CB  . PHE   D  1 166 ? 17.719  34.674  -29.324  1.00 40.99  ? 467  PHE   D CB  1 
ATOM   11546 C  CG  . PHE   D  1 166 ? 19.139  35.027  -29.026  1.00 47.71  ? 467  PHE   D CG  1 
ATOM   11547 C  CD1 . PHE   D  1 166 ? 19.537  35.327  -27.740  1.00 41.21  ? 467  PHE   D CD1 1 
ATOM   11548 C  CD2 . PHE   D  1 166 ? 20.082  35.076  -30.032  1.00 52.74  ? 467  PHE   D CD2 1 
ATOM   11549 C  CE1 . PHE   D  1 166 ? 20.853  35.661  -27.464  1.00 41.83  ? 467  PHE   D CE1 1 
ATOM   11550 C  CE2 . PHE   D  1 166 ? 21.402  35.413  -29.756  1.00 50.59  ? 467  PHE   D CE2 1 
ATOM   11551 C  CZ  . PHE   D  1 166 ? 21.783  35.708  -28.472  1.00 43.06  ? 467  PHE   D CZ  1 
ATOM   11552 N  N   . PRO   D  1 167 ? 15.112  33.490  -28.178  1.00 48.35  ? 468  PRO   D N   1 
ATOM   11553 C  CA  . PRO   D  1 167 ? 13.697  33.096  -28.104  1.00 50.20  ? 468  PRO   D CA  1 
ATOM   11554 C  C   . PRO   D  1 167 ? 12.936  33.312  -29.407  1.00 45.73  ? 468  PRO   D C   1 
ATOM   11555 O  O   . PRO   D  1 167 ? 13.068  34.342  -30.072  1.00 44.36  ? 468  PRO   D O   1 
ATOM   11556 C  CB  . PRO   D  1 167 ? 13.143  33.979  -26.979  1.00 48.66  ? 468  PRO   D CB  1 
ATOM   11557 C  CG  . PRO   D  1 167 ? 14.265  34.195  -26.101  1.00 34.66  ? 468  PRO   D CG  1 
ATOM   11558 C  CD  . PRO   D  1 167 ? 15.482  34.292  -26.994  1.00 45.19  ? 468  PRO   D CD  1 
ATOM   11559 N  N   . GLN   D  1 168 ? 12.100  32.332  -29.751  1.00 41.72  ? 469  GLN   D N   1 
ATOM   11560 C  CA  . GLN   D  1 168 ? 11.354  32.406  -30.997  1.00 34.64  ? 469  GLN   D CA  1 
ATOM   11561 C  C   . GLN   D  1 168 ? 10.341  33.544  -30.950  1.00 40.28  ? 469  GLN   D C   1 
ATOM   11562 O  O   . GLN   D  1 168 ? 10.053  34.123  -29.910  1.00 45.80  ? 469  GLN   D O   1 
ATOM   11563 C  CB  . GLN   D  1 168 ? 10.609  31.110  -31.243  1.00 33.85  ? 469  GLN   D CB  1 
ATOM   11564 C  CG  . GLN   D  1 168 ? 9.457   30.938  -30.274  1.00 35.82  ? 469  GLN   D CG  1 
ATOM   11565 C  CD  . GLN   D  1 168 ? 9.272   29.501  -29.876  1.00 40.23  ? 469  GLN   D CD  1 
ATOM   11566 O  OE1 . GLN   D  1 168 ? 10.238  28.770  -29.676  1.00 61.77  ? 469  GLN   D OE1 1 
ATOM   11567 N  NE2 . GLN   D  1 168 ? 8.029   29.082  -29.761  1.00 36.52  ? 469  GLN   D NE2 1 
ATOM   11568 N  N   . ARG   D  1 169 ? 9.784   33.846  -32.108  1.00 53.12  ? 470  ARG   D N   1 
ATOM   11569 C  CA  . ARG   D  1 169 ? 8.770   34.880  -32.191  1.00 45.10  ? 470  ARG   D CA  1 
ATOM   11570 C  C   . ARG   D  1 169 ? 7.533   34.404  -31.456  1.00 38.96  ? 470  ARG   D C   1 
ATOM   11571 O  O   . ARG   D  1 169 ? 7.277   33.202  -31.369  1.00 45.54  ? 470  ARG   D O   1 
ATOM   11572 C  CB  . ARG   D  1 169 ? 8.465   35.190  -33.656  1.00 43.25  ? 470  ARG   D CB  1 
ATOM   11573 C  CG  . ARG   D  1 169 ? 7.574   36.395  -33.889  1.00 56.22  ? 470  ARG   D CG  1 
ATOM   11574 C  CD  . ARG   D  1 169 ? 7.444   36.706  -35.363  1.00 55.54  ? 470  ARG   D CD  1 
ATOM   11575 N  NE  . ARG   D  1 169 ? 8.536   37.546  -35.823  1.00 52.86  ? 470  ARG   D NE  1 
ATOM   11576 C  CZ  . ARG   D  1 169 ? 8.936   37.598  -37.083  1.00 75.43  ? 470  ARG   D CZ  1 
ATOM   11577 N  NH1 . ARG   D  1 169 ? 8.330   36.837  -37.987  1.00 85.40  ? 470  ARG   D NH1 1 
ATOM   11578 N  NH2 . ARG   D  1 169 ? 9.947   38.388  -37.439  1.00 80.09  ? 470  ARG   D NH2 1 
ATOM   11579 N  N   . THR   D  1 170 ? 6.786   35.349  -30.870  1.00 40.40  ? 471  THR   D N   1 
ATOM   11580 C  CA  . THR   D  1 170 ? 5.543   34.999  -30.181  1.00 43.64  ? 471  THR   D CA  1 
ATOM   11581 C  C   . THR   D  1 170 ? 4.357   35.711  -30.809  1.00 52.72  ? 471  THR   D C   1 
ATOM   11582 O  O   . THR   D  1 170 ? 3.478   35.050  -31.366  1.00 59.93  ? 471  THR   D O   1 
ATOM   11583 C  CB  . THR   D  1 170 ? 5.589   35.295  -28.658  1.00 48.24  ? 471  THR   D CB  1 
ATOM   11584 O  OG1 . THR   D  1 170 ? 5.656   36.703  -28.396  1.00 53.03  ? 471  THR   D OG1 1 
ATOM   11585 C  CG2 . THR   D  1 170 ? 6.762   34.598  -27.970  1.00 41.10  ? 471  THR   D CG2 1 
ATOM   11586 N  N   . ASP   D  1 171 ? 4.313   37.044  -30.746  1.00 49.60  ? 472  ASP   D N   1 
ATOM   11587 C  CA  . ASP   D  1 171 ? 3.240   37.810  -31.365  1.00 50.60  ? 472  ASP   D CA  1 
ATOM   11588 C  C   . ASP   D  1 171 ? 3.776   38.955  -32.213  1.00 56.50  ? 472  ASP   D C   1 
ATOM   11589 O  O   . ASP   D  1 171 ? 3.054   39.927  -32.453  1.00 66.03  ? 472  ASP   D O   1 
ATOM   11590 C  CB  . ASP   D  1 171 ? 2.286   38.352  -30.305  1.00 58.19  ? 472  ASP   D CB  1 
ATOM   11591 C  CG  . ASP   D  1 171 ? 2.995   39.164  -29.241  1.00 64.65  ? 472  ASP   D CG  1 
ATOM   11592 O  OD1 . ASP   D  1 171 ? 4.150   38.836  -28.914  1.00 69.07  ? 472  ASP   D OD1 1 
ATOM   11593 O  OD2 . ASP   D  1 171 ? 2.389   40.126  -28.723  1.00 68.47  ? 472  ASP   D OD2 1 
ATOM   11594 N  N   . GLY   D  1 172 ? 5.028   38.868  -32.657  1.00 50.25  ? 473  GLY   D N   1 
ATOM   11595 C  CA  . GLY   D  1 172 ? 5.634   39.912  -33.455  1.00 51.67  ? 473  GLY   D CA  1 
ATOM   11596 C  C   . GLY   D  1 172 ? 5.989   41.166  -32.677  1.00 62.25  ? 473  GLY   D C   1 
ATOM   11597 O  O   . GLY   D  1 172 ? 6.850   41.946  -33.098  1.00 64.83  ? 473  GLY   D O   1 
ATOM   11598 N  N   . LYS   D  1 173 ? 5.343   41.372  -31.531  1.00 60.49  ? 474  LYS   D N   1 
ATOM   11599 C  CA  . LYS   D  1 173 ? 5.596   42.558  -30.729  1.00 59.12  ? 474  LYS   D CA  1 
ATOM   11600 C  C   . LYS   D  1 173 ? 6.736   42.381  -29.732  1.00 56.87  ? 474  LYS   D C   1 
ATOM   11601 O  O   . LYS   D  1 173 ? 7.165   43.366  -29.130  1.00 55.92  ? 474  LYS   D O   1 
ATOM   11602 C  CB  . LYS   D  1 173 ? 4.330   42.970  -29.976  1.00 63.35  ? 474  LYS   D CB  1 
ATOM   11603 C  CG  . LYS   D  1 173 ? 3.030   42.841  -30.762  1.00 74.59  ? 474  LYS   D CG  1 
ATOM   11604 C  CD  . LYS   D  1 173 ? 3.039   43.657  -32.056  1.00 85.48  ? 474  LYS   D CD  1 
ATOM   11605 C  CE  . LYS   D  1 173 ? 3.270   45.134  -31.779  1.00 95.77  ? 474  LYS   D CE  1 
ATOM   11606 N  NZ  . LYS   D  1 173 ? 2.217   45.712  -30.891  1.00 101.93 ? 474  LYS   D NZ  1 
ATOM   11607 N  N   . HIS   D  1 174 ? 7.243   41.167  -29.545  1.00 61.65  ? 475  HIS   D N   1 
ATOM   11608 C  CA  . HIS   D  1 174 ? 8.277   40.875  -28.558  1.00 54.90  ? 475  HIS   D CA  1 
ATOM   11609 C  C   . HIS   D  1 174 ? 9.398   40.091  -29.194  1.00 51.99  ? 475  HIS   D C   1 
ATOM   11610 O  O   . HIS   D  1 174 ? 9.839   39.071  -28.665  1.00 49.00  ? 475  HIS   D O   1 
ATOM   11611 C  CB  . HIS   D  1 174 ? 7.710   40.101  -27.373  1.00 58.53  ? 475  HIS   D CB  1 
ATOM   11612 C  CG  . HIS   D  1 174 ? 6.569   40.785  -26.700  1.00 63.12  ? 475  HIS   D CG  1 
ATOM   11613 N  ND1 . HIS   D  1 174 ? 5.334   40.920  -27.293  1.00 64.45  ? 475  HIS   D ND1 1 
ATOM   11614 C  CD2 . HIS   D  1 174 ? 6.483   41.401  -25.498  1.00 66.07  ? 475  HIS   D CD2 1 
ATOM   11615 C  CE1 . HIS   D  1 174 ? 4.532   41.585  -26.482  1.00 68.46  ? 475  HIS   D CE1 1 
ATOM   11616 N  NE2 . HIS   D  1 174 ? 5.203   41.887  -25.385  1.00 70.64  ? 475  HIS   D NE2 1 
ATOM   11617 N  N   . ASP   D  1 175 ? 9.844   40.546  -30.362  1.00 53.65  ? 476  ASP   D N   1 
ATOM   11618 C  CA  . ASP   D  1 175 ? 10.885  39.853  -31.109  1.00 48.20  ? 476  ASP   D CA  1 
ATOM   11619 C  C   . ASP   D  1 175 ? 12.236  40.150  -30.487  1.00 47.66  ? 476  ASP   D C   1 
ATOM   11620 O  O   . ASP   D  1 175 ? 12.492  41.278  -30.052  1.00 47.98  ? 476  ASP   D O   1 
ATOM   11621 C  CB  . ASP   D  1 175 ? 10.908  40.298  -32.578  1.00 58.69  ? 476  ASP   D CB  1 
ATOM   11622 C  CG  . ASP   D  1 175 ? 9.674   39.863  -33.360  1.00 70.60  ? 476  ASP   D CG  1 
ATOM   11623 O  OD1 . ASP   D  1 175 ? 8.810   39.158  -32.795  1.00 81.70  ? 476  ASP   D OD1 1 
ATOM   11624 O  OD2 . ASP   D  1 175 ? 9.573   40.234  -34.551  1.00 69.31  ? 476  ASP   D OD2 1 
ATOM   11625 N  N   . PHE   D  1 176 ? 13.091  39.130  -30.426  1.00 37.33  ? 477  PHE   D N   1 
ATOM   11626 C  CA  . PHE   D  1 176 ? 14.514  39.329  -30.222  1.00 32.29  ? 477  PHE   D CA  1 
ATOM   11627 C  C   . PHE   D  1 176 ? 15.162  39.569  -31.583  1.00 51.58  ? 477  PHE   D C   1 
ATOM   11628 O  O   . PHE   D  1 176 ? 14.812  38.923  -32.577  1.00 46.62  ? 477  PHE   D O   1 
ATOM   11629 C  CB  . PHE   D  1 176 ? 15.148  38.110  -29.551  1.00 38.00  ? 477  PHE   D CB  1 
ATOM   11630 C  CG  . PHE   D  1 176 ? 14.730  37.902  -28.127  1.00 53.06  ? 477  PHE   D CG  1 
ATOM   11631 C  CD1 . PHE   D  1 176 ? 13.415  37.625  -27.805  1.00 61.29  ? 477  PHE   D CD1 1 
ATOM   11632 C  CD2 . PHE   D  1 176 ? 15.666  37.942  -27.106  1.00 52.72  ? 477  PHE   D CD2 1 
ATOM   11633 C  CE1 . PHE   D  1 176 ? 13.040  37.421  -26.498  1.00 64.18  ? 477  PHE   D CE1 1 
ATOM   11634 C  CE2 . PHE   D  1 176 ? 15.302  37.742  -25.797  1.00 49.04  ? 477  PHE   D CE2 1 
ATOM   11635 C  CZ  . PHE   D  1 176 ? 13.983  37.485  -25.491  1.00 58.02  ? 477  PHE   D CZ  1 
ATOM   11636 N  N   . ARG   D  1 177 ? 16.126  40.481  -31.619  1.00 50.65  ? 478  ARG   D N   1 
ATOM   11637 C  CA  . ARG   D  1 177 ? 16.738  40.868  -32.877  1.00 32.90  ? 478  ARG   D CA  1 
ATOM   11638 C  C   . ARG   D  1 177 ? 18.180  41.303  -32.659  1.00 41.29  ? 478  ARG   D C   1 
ATOM   11639 O  O   . ARG   D  1 177 ? 18.442  42.154  -31.804  1.00 44.32  ? 478  ARG   D O   1 
ATOM   11640 C  CB  . ARG   D  1 177 ? 15.959  42.020  -33.511  1.00 44.61  ? 478  ARG   D CB  1 
ATOM   11641 C  CG  . ARG   D  1 177 ? 14.669  41.611  -34.182  1.00 49.41  ? 478  ARG   D CG  1 
ATOM   11642 C  CD  . ARG   D  1 177 ? 14.882  40.472  -35.175  1.00 44.59  ? 478  ARG   D CD  1 
ATOM   11643 N  NE  . ARG   D  1 177 ? 15.533  40.871  -36.418  1.00 53.51  ? 478  ARG   D NE  1 
ATOM   11644 C  CZ  . ARG   D  1 177 ? 14.897  41.403  -37.460  1.00 54.60  ? 478  ARG   D CZ  1 
ATOM   11645 N  NH1 . ARG   D  1 177 ? 13.595  41.644  -37.414  1.00 58.59  ? 478  ARG   D NH1 1 
ATOM   11646 N  NH2 . ARG   D  1 177 ? 15.569  41.704  -38.550  1.00 51.44  ? 478  ARG   D NH2 1 
ATOM   11647 N  N   . VAL   D  1 178 ? 19.101  40.775  -33.462  1.00 39.55  ? 479  VAL   D N   1 
ATOM   11648 C  CA  . VAL   D  1 178 ? 20.401  41.410  -33.628  1.00 33.87  ? 479  VAL   D CA  1 
ATOM   11649 C  C   . VAL   D  1 178 ? 20.247  42.419  -34.756  1.00 39.68  ? 479  VAL   D C   1 
ATOM   11650 O  O   . VAL   D  1 178 ? 20.063  42.040  -35.914  1.00 54.84  ? 479  VAL   D O   1 
ATOM   11651 C  CB  . VAL   D  1 178 ? 21.512  40.399  -33.929  1.00 39.01  ? 479  VAL   D CB  1 
ATOM   11652 C  CG1 . VAL   D  1 178 ? 22.874  41.081  -33.809  1.00 41.49  ? 479  VAL   D CG1 1 
ATOM   11653 C  CG2 . VAL   D  1 178 ? 21.439  39.200  -32.976  1.00 40.16  ? 479  VAL   D CG2 1 
ATOM   11654 N  N   . TRP   D  1 179 ? 20.294  43.709  -34.420  1.00 40.54  ? 480  TRP   D N   1 
ATOM   11655 C  CA  . TRP   D  1 179 ? 20.159  44.732  -35.453  1.00 38.89  ? 480  TRP   D CA  1 
ATOM   11656 C  C   . TRP   D  1 179 ? 21.358  44.756  -36.396  1.00 43.74  ? 480  TRP   D C   1 
ATOM   11657 O  O   . TRP   D  1 179 ? 21.226  45.189  -37.540  1.00 61.21  ? 480  TRP   D O   1 
ATOM   11658 C  CB  . TRP   D  1 179 ? 19.949  46.110  -34.823  1.00 34.14  ? 480  TRP   D CB  1 
ATOM   11659 C  CG  . TRP   D  1 179 ? 18.588  46.300  -34.274  1.00 30.53  ? 480  TRP   D CG  1 
ATOM   11660 C  CD1 . TRP   D  1 179 ? 17.797  45.350  -33.678  1.00 28.58  ? 480  TRP   D CD1 1 
ATOM   11661 C  CD2 . TRP   D  1 179 ? 17.815  47.511  -34.298  1.00 30.01  ? 480  TRP   D CD2 1 
ATOM   11662 N  NE1 . TRP   D  1 179 ? 16.582  45.913  -33.312  1.00 33.64  ? 480  TRP   D NE1 1 
ATOM   11663 C  CE2 . TRP   D  1 179 ? 16.573  47.233  -33.691  1.00 32.54  ? 480  TRP   D CE2 1 
ATOM   11664 C  CE3 . TRP   D  1 179 ? 18.051  48.795  -34.780  1.00 33.30  ? 480  TRP   D CE3 1 
ATOM   11665 C  CZ2 . TRP   D  1 179 ? 15.577  48.194  -33.567  1.00 43.45  ? 480  TRP   D CZ2 1 
ATOM   11666 C  CZ3 . TRP   D  1 179 ? 17.057  49.749  -34.653  1.00 37.53  ? 480  TRP   D CZ3 1 
ATOM   11667 C  CH2 . TRP   D  1 179 ? 15.839  49.444  -34.052  1.00 40.75  ? 480  TRP   D CH2 1 
ATOM   11668 N  N   . ASN   D  1 180 ? 22.527  44.317  -35.939  1.00 46.38  ? 481  ASN   D N   1 
ATOM   11669 C  CA  . ASN   D  1 180 ? 23.671  44.166  -36.831  1.00 44.04  ? 481  ASN   D CA  1 
ATOM   11670 C  C   . ASN   D  1 180 ? 23.366  43.139  -37.902  1.00 48.78  ? 481  ASN   D C   1 
ATOM   11671 O  O   . ASN   D  1 180 ? 22.800  42.084  -37.603  1.00 50.57  ? 481  ASN   D O   1 
ATOM   11672 C  CB  . ASN   D  1 180 ? 24.900  43.695  -36.064  1.00 36.93  ? 481  ASN   D CB  1 
ATOM   11673 C  CG  . ASN   D  1 180 ? 25.187  44.543  -34.867  1.00 42.26  ? 481  ASN   D CG  1 
ATOM   11674 O  OD1 . ASN   D  1 180 ? 24.519  44.441  -33.839  1.00 49.70  ? 481  ASN   D OD1 1 
ATOM   11675 N  ND2 . ASN   D  1 180 ? 26.183  45.399  -34.990  1.00 38.78  ? 481  ASN   D ND2 1 
ATOM   11676 N  N   . SER   D  1 181 ? 23.787  43.432  -39.149  1.00 44.55  ? 482  SER   D N   1 
ATOM   11677 C  CA  . SER   D  1 181 ? 23.680  42.446  -40.224  1.00 43.27  ? 482  SER   D CA  1 
ATOM   11678 C  C   . SER   D  1 181 ? 24.698  41.329  -40.034  1.00 44.65  ? 482  SER   D C   1 
ATOM   11679 O  O   . SER   D  1 181 ? 24.411  40.167  -40.332  1.00 50.03  ? 482  SER   D O   1 
ATOM   11680 C  CB  . SER   D  1 181 ? 23.838  43.104  -41.599  1.00 48.52  ? 482  SER   D CB  1 
ATOM   11681 O  OG  . SER   D  1 181 ? 25.077  43.789  -41.738  1.00 52.18  ? 482  SER   D OG  1 
ATOM   11682 N  N   . GLN   D  1 182 ? 25.876  41.651  -39.508  1.00 47.15  ? 483  GLN   D N   1 
ATOM   11683 C  CA  . GLN   D  1 182 ? 26.821  40.648  -39.030  1.00 49.34  ? 483  GLN   D CA  1 
ATOM   11684 C  C   . GLN   D  1 182 ? 27.327  41.053  -37.653  1.00 44.92  ? 483  GLN   D C   1 
ATOM   11685 O  O   . GLN   D  1 182 ? 27.174  42.203  -37.238  1.00 54.06  ? 483  GLN   D O   1 
ATOM   11686 C  CB  . GLN   D  1 182 ? 28.000  40.479  -39.990  1.00 47.91  ? 483  GLN   D CB  1 
ATOM   11687 C  CG  . GLN   D  1 182 ? 27.616  40.103  -41.404  1.00 49.97  ? 483  GLN   D CG  1 
ATOM   11688 C  CD  . GLN   D  1 182 ? 28.779  40.266  -42.362  1.00 52.13  ? 483  GLN   D CD  1 
ATOM   11689 O  OE1 . GLN   D  1 182 ? 29.911  39.845  -42.072  1.00 42.50  ? 483  GLN   D OE1 1 
ATOM   11690 N  NE2 . GLN   D  1 182 ? 28.520  40.908  -43.492  1.00 50.91  ? 483  GLN   D NE2 1 
ATOM   11691 N  N   . LEU   D  1 183 ? 27.968  40.113  -36.942  1.00 47.44  ? 484  LEU   D N   1 
ATOM   11692 C  CA  . LEU   D  1 183 ? 28.419  40.429  -35.578  1.00 47.65  ? 484  LEU   D CA  1 
ATOM   11693 C  C   . LEU   D  1 183 ? 29.679  41.301  -35.593  1.00 46.84  ? 484  LEU   D C   1 
ATOM   11694 O  O   . LEU   D  1 183 ? 29.742  42.331  -34.913  1.00 44.79  ? 484  LEU   D O   1 
ATOM   11695 C  CB  . LEU   D  1 183 ? 28.640  39.146  -34.763  1.00 32.51  ? 484  LEU   D CB  1 
ATOM   11696 C  CG  . LEU   D  1 183 ? 27.504  38.110  -34.610  1.00 33.21  ? 484  LEU   D CG  1 
ATOM   11697 C  CD1 . LEU   D  1 183 ? 27.960  36.856  -33.841  1.00 22.29  ? 484  LEU   D CD1 1 
ATOM   11698 C  CD2 . LEU   D  1 183 ? 26.300  38.676  -33.941  1.00 24.27  ? 484  LEU   D CD2 1 
ATOM   11699 N  N   . ILE   D  1 184 ? 30.682  40.933  -36.379  1.00 48.67  ? 485  ILE   D N   1 
ATOM   11700 C  CA  . ILE   D  1 184 ? 31.847  41.782  -36.605  1.00 44.29  ? 485  ILE   D CA  1 
ATOM   11701 C  C   . ILE   D  1 184 ? 31.727  42.397  -37.991  1.00 46.78  ? 485  ILE   D C   1 
ATOM   11702 O  O   . ILE   D  1 184 ? 31.530  41.676  -38.970  1.00 42.47  ? 485  ILE   D O   1 
ATOM   11703 C  CB  . ILE   D  1 184 ? 33.150  40.987  -36.472  1.00 35.85  ? 485  ILE   D CB  1 
ATOM   11704 C  CG1 . ILE   D  1 184 ? 33.134  40.204  -35.156  1.00 49.52  ? 485  ILE   D CG1 1 
ATOM   11705 C  CG2 . ILE   D  1 184 ? 34.310  41.929  -36.543  1.00 37.01  ? 485  ILE   D CG2 1 
ATOM   11706 C  CD1 . ILE   D  1 184 ? 34.078  39.019  -35.143  1.00 59.10  ? 485  ILE   D CD1 1 
ATOM   11707 N  N   . ARG   D  1 185 ? 31.865  43.722  -38.063  1.00 41.68  ? 486  ARG   D N   1 
ATOM   11708 C  CA  . ARG   D  1 185 ? 31.703  44.553  -39.248  1.00 49.78  ? 486  ARG   D CA  1 
ATOM   11709 C  C   . ARG   D  1 185 ? 32.271  45.933  -38.943  1.00 50.38  ? 486  ARG   D C   1 
ATOM   11710 O  O   . ARG   D  1 185 ? 32.186  46.407  -37.807  1.00 40.50  ? 486  ARG   D O   1 
ATOM   11711 C  CB  . ARG   D  1 185 ? 30.239  44.711  -39.656  1.00 56.87  ? 486  ARG   D CB  1 
ATOM   11712 C  CG  . ARG   D  1 185 ? 29.691  43.604  -40.476  1.00 58.20  ? 486  ARG   D CG  1 
ATOM   11713 C  CD  . ARG   D  1 185 ? 28.666  44.141  -41.404  1.00 61.71  ? 486  ARG   D CD  1 
ATOM   11714 N  NE  . ARG   D  1 185 ? 29.254  44.435  -42.694  1.00 75.29  ? 486  ARG   D NE  1 
ATOM   11715 C  CZ  . ARG   D  1 185 ? 28.539  44.569  -43.802  1.00 75.22  ? 486  ARG   D CZ  1 
ATOM   11716 N  NH1 . ARG   D  1 185 ? 27.219  44.447  -43.756  1.00 72.36  ? 486  ARG   D NH1 1 
ATOM   11717 N  NH2 . ARG   D  1 185 ? 29.141  44.841  -44.946  1.00 73.33  ? 486  ARG   D NH2 1 
ATOM   11718 N  N   . TYR   D  1 186 ? 32.821  46.587  -39.970  1.00 44.08  ? 487  TYR   D N   1 
ATOM   11719 C  CA  . TYR   D  1 186 ? 33.423  47.898  -39.774  1.00 35.32  ? 487  TYR   D CA  1 
ATOM   11720 C  C   . TYR   D  1 186 ? 32.447  49.039  -40.071  1.00 44.31  ? 487  TYR   D C   1 
ATOM   11721 O  O   . TYR   D  1 186 ? 31.508  48.914  -40.861  1.00 54.17  ? 487  TYR   D O   1 
ATOM   11722 C  CB  . TYR   D  1 186 ? 34.681  48.046  -40.619  1.00 28.07  ? 487  TYR   D CB  1 
ATOM   11723 C  CG  . TYR   D  1 186 ? 35.755  47.017  -40.331  1.00 35.56  ? 487  TYR   D CG  1 
ATOM   11724 C  CD1 . TYR   D  1 186 ? 36.155  46.122  -41.304  1.00 45.00  ? 487  TYR   D CD1 1 
ATOM   11725 C  CD2 . TYR   D  1 186 ? 36.378  46.954  -39.098  1.00 49.42  ? 487  TYR   D CD2 1 
ATOM   11726 C  CE1 . TYR   D  1 186 ? 37.139  45.190  -41.065  1.00 49.02  ? 487  TYR   D CE1 1 
ATOM   11727 C  CE2 . TYR   D  1 186 ? 37.376  46.014  -38.842  1.00 51.88  ? 487  TYR   D CE2 1 
ATOM   11728 C  CZ  . TYR   D  1 186 ? 37.749  45.131  -39.832  1.00 48.80  ? 487  TYR   D CZ  1 
ATOM   11729 O  OH  . TYR   D  1 186 ? 38.734  44.182  -39.586  1.00 36.71  ? 487  TYR   D OH  1 
ATOM   11730 N  N   . ALA   D  1 187 ? 32.683  50.165  -39.418  1.00 47.94  ? 488  ALA   D N   1 
ATOM   11731 C  CA  . ALA   D  1 187 ? 31.774  51.287  -39.512  1.00 51.47  ? 488  ALA   D CA  1 
ATOM   11732 C  C   . ALA   D  1 187 ? 31.980  52.019  -40.823  1.00 57.08  ? 488  ALA   D C   1 
ATOM   11733 O  O   . ALA   D  1 187 ? 32.999  51.865  -41.497  1.00 58.45  ? 488  ALA   D O   1 
ATOM   11734 C  CB  . ALA   D  1 187 ? 31.976  52.253  -38.348  1.00 51.71  ? 488  ALA   D CB  1 
ATOM   11735 N  N   . GLY   D  1 188 ? 30.994  52.836  -41.172  1.00 60.25  ? 489  GLY   D N   1 
ATOM   11736 C  CA  . GLY   D  1 188 ? 31.068  53.650  -42.362  1.00 60.56  ? 489  GLY   D CA  1 
ATOM   11737 C  C   . GLY   D  1 188 ? 30.675  55.074  -42.049  1.00 65.23  ? 489  GLY   D C   1 
ATOM   11738 O  O   . GLY   D  1 188 ? 29.640  55.319  -41.424  1.00 69.47  ? 489  GLY   D O   1 
ATOM   11739 N  N   . TYR   D  1 189 ? 31.498  56.028  -42.466  1.00 60.87  ? 490  TYR   D N   1 
ATOM   11740 C  CA  . TYR   D  1 189 ? 31.240  57.431  -42.189  1.00 56.72  ? 490  TYR   D CA  1 
ATOM   11741 C  C   . TYR   D  1 189 ? 31.320  58.191  -43.499  1.00 62.97  ? 490  TYR   D C   1 
ATOM   11742 O  O   . TYR   D  1 189 ? 32.402  58.302  -44.084  1.00 62.56  ? 490  TYR   D O   1 
ATOM   11743 C  CB  . TYR   D  1 189 ? 32.242  57.997  -41.195  1.00 50.42  ? 490  TYR   D CB  1 
ATOM   11744 C  CG  . TYR   D  1 189 ? 32.565  57.123  -40.016  1.00 55.31  ? 490  TYR   D CG  1 
ATOM   11745 C  CD1 . TYR   D  1 189 ? 33.627  56.227  -40.058  1.00 57.10  ? 490  TYR   D CD1 1 
ATOM   11746 C  CD2 . TYR   D  1 189 ? 31.838  57.223  -38.837  1.00 56.17  ? 490  TYR   D CD2 1 
ATOM   11747 C  CE1 . TYR   D  1 189 ? 33.939  55.443  -38.957  1.00 61.32  ? 490  TYR   D CE1 1 
ATOM   11748 C  CE2 . TYR   D  1 189 ? 32.141  56.442  -37.739  1.00 59.00  ? 490  TYR   D CE2 1 
ATOM   11749 C  CZ  . TYR   D  1 189 ? 33.191  55.558  -37.803  1.00 61.00  ? 490  TYR   D CZ  1 
ATOM   11750 O  OH  . TYR   D  1 189 ? 33.495  54.789  -36.704  1.00 63.56  ? 490  TYR   D OH  1 
ATOM   11751 N  N   . LYS   D  1 190 ? 30.189  58.727  -43.946  1.00 59.54  ? 491  LYS   D N   1 
ATOM   11752 C  CA  . LYS   D  1 190 ? 30.198  59.628  -45.088  1.00 59.51  ? 491  LYS   D CA  1 
ATOM   11753 C  C   . LYS   D  1 190 ? 30.674  61.007  -44.635  1.00 66.92  ? 491  LYS   D C   1 
ATOM   11754 O  O   . LYS   D  1 190 ? 30.328  61.469  -43.544  1.00 72.85  ? 491  LYS   D O   1 
ATOM   11755 C  CB  . LYS   D  1 190 ? 28.803  59.693  -45.726  1.00 63.86  ? 491  LYS   D CB  1 
ATOM   11756 C  CG  . LYS   D  1 190 ? 28.789  59.715  -47.276  1.00 74.57  ? 491  LYS   D CG  1 
ATOM   11757 C  CD  . LYS   D  1 190 ? 27.409  59.307  -47.846  1.00 81.16  ? 491  LYS   D CD  1 
ATOM   11758 C  CE  . LYS   D  1 190 ? 27.066  60.056  -49.156  1.00 79.79  ? 491  LYS   D CE  1 
ATOM   11759 N  NZ  . LYS   D  1 190 ? 25.604  60.007  -49.495  1.00 73.25  ? 491  LYS   D NZ  1 
ATOM   11760 N  N   . GLN   D  1 191 ? 31.493  61.647  -45.465  1.00 65.72  ? 492  GLN   D N   1 
ATOM   11761 C  CA  . GLN   D  1 191 ? 32.114  62.937  -45.197  1.00 66.27  ? 492  GLN   D CA  1 
ATOM   11762 C  C   . GLN   D  1 191 ? 31.317  64.061  -45.854  1.00 61.11  ? 492  GLN   D C   1 
ATOM   11763 O  O   . GLN   D  1 191 ? 30.457  63.819  -46.703  1.00 71.72  ? 492  GLN   D O   1 
ATOM   11764 C  CB  . GLN   D  1 191 ? 33.559  62.925  -45.706  1.00 66.78  ? 492  GLN   D CB  1 
ATOM   11765 C  CG  . GLN   D  1 191 ? 34.306  61.639  -45.394  1.00 70.78  ? 492  GLN   D CG  1 
ATOM   11766 C  CD  . GLN   D  1 191 ? 35.147  61.727  -44.141  1.00 78.29  ? 492  GLN   D CD  1 
ATOM   11767 O  OE1 . GLN   D  1 191 ? 34.659  61.503  -43.025  1.00 80.00  ? 492  GLN   D OE1 1 
ATOM   11768 N  NE2 . GLN   D  1 191 ? 36.430  62.041  -44.317  1.00 77.26  ? 492  GLN   D NE2 1 
ATOM   11769 N  N   . PRO   D  1 192 ? 31.564  65.317  -45.475  1.00 50.60  ? 493  PRO   D N   1 
ATOM   11770 C  CA  . PRO   D  1 192 ? 30.823  66.417  -46.117  1.00 61.41  ? 493  PRO   D CA  1 
ATOM   11771 C  C   . PRO   D  1 192 ? 31.110  66.548  -47.601  1.00 73.22  ? 493  PRO   D C   1 
ATOM   11772 O  O   . PRO   D  1 192 ? 30.264  67.054  -48.353  1.00 75.39  ? 493  PRO   D O   1 
ATOM   11773 C  CB  . PRO   D  1 192 ? 31.310  67.654  -45.350  1.00 58.33  ? 493  PRO   D CB  1 
ATOM   11774 C  CG  . PRO   D  1 192 ? 32.671  67.249  -44.832  1.00 56.97  ? 493  PRO   D CG  1 
ATOM   11775 C  CD  . PRO   D  1 192 ? 32.465  65.822  -44.422  1.00 50.06  ? 493  PRO   D CD  1 
ATOM   11776 N  N   . ASP   D  1 193 ? 32.294  66.129  -48.036  1.00 71.12  ? 494  ASP   D N   1 
ATOM   11777 C  CA  . ASP   D  1 193 ? 32.712  66.227  -49.423  1.00 60.98  ? 494  ASP   D CA  1 
ATOM   11778 C  C   . ASP   D  1 193 ? 32.265  65.029  -50.235  1.00 61.11  ? 494  ASP   D C   1 
ATOM   11779 O  O   . ASP   D  1 193 ? 32.753  64.834  -51.354  1.00 74.89  ? 494  ASP   D O   1 
ATOM   11780 C  CB  . ASP   D  1 193 ? 34.235  66.384  -49.504  1.00 63.51  ? 494  ASP   D CB  1 
ATOM   11781 C  CG  . ASP   D  1 193 ? 34.986  65.182  -48.942  1.00 75.21  ? 494  ASP   D CG  1 
ATOM   11782 O  OD1 . ASP   D  1 193 ? 35.652  64.472  -49.731  1.00 75.13  ? 494  ASP   D OD1 1 
ATOM   11783 O  OD2 . ASP   D  1 193 ? 34.908  64.951  -47.711  1.00 85.95  ? 494  ASP   D OD2 1 
ATOM   11784 N  N   . GLY   D  1 194 ? 31.356  64.222  -49.693  1.00 57.12  ? 495  GLY   D N   1 
ATOM   11785 C  CA  . GLY   D  1 194 ? 30.841  63.064  -50.380  1.00 58.52  ? 495  GLY   D CA  1 
ATOM   11786 C  C   . GLY   D  1 194 ? 31.691  61.822  -50.288  1.00 61.57  ? 495  GLY   D C   1 
ATOM   11787 O  O   . GLY   D  1 194 ? 31.175  60.721  -50.530  1.00 65.74  ? 495  GLY   D O   1 
ATOM   11788 N  N   . SER   D  1 195 ? 32.977  61.951  -49.965  1.00 61.49  ? 496  SER   D N   1 
ATOM   11789 C  CA  . SER   D  1 195 ? 33.818  60.776  -49.782  1.00 60.13  ? 496  SER   D CA  1 
ATOM   11790 C  C   . SER   D  1 195 ? 33.272  59.922  -48.647  1.00 64.75  ? 496  SER   D C   1 
ATOM   11791 O  O   . SER   D  1 195 ? 32.414  60.349  -47.872  1.00 62.04  ? 496  SER   D O   1 
ATOM   11792 C  CB  . SER   D  1 195 ? 35.263  61.179  -49.497  1.00 61.93  ? 496  SER   D CB  1 
ATOM   11793 O  OG  . SER   D  1 195 ? 35.328  62.223  -48.547  1.00 64.41  ? 496  SER   D OG  1 
ATOM   11794 N  N   . THR   D  1 196 ? 33.766  58.688  -48.562  1.00 71.07  ? 497  THR   D N   1 
ATOM   11795 C  CA  . THR   D  1 196 ? 33.286  57.744  -47.561  1.00 70.37  ? 497  THR   D CA  1 
ATOM   11796 C  C   . THR   D  1 196 ? 34.454  57.069  -46.851  1.00 71.16  ? 497  THR   D C   1 
ATOM   11797 O  O   . THR   D  1 196 ? 35.330  56.481  -47.493  1.00 71.59  ? 497  THR   D O   1 
ATOM   11798 C  CB  . THR   D  1 196 ? 32.363  56.694  -48.181  1.00 73.68  ? 497  THR   D CB  1 
ATOM   11799 O  OG1 . THR   D  1 196 ? 31.180  57.330  -48.686  1.00 77.84  ? 497  THR   D OG1 1 
ATOM   11800 C  CG2 . THR   D  1 196 ? 31.973  55.659  -47.130  1.00 76.72  ? 497  THR   D CG2 1 
ATOM   11801 N  N   . LEU   D  1 197 ? 34.451  57.148  -45.522  1.00 72.51  ? 498  LEU   D N   1 
ATOM   11802 C  CA  . LEU   D  1 197 ? 35.472  56.548  -44.678  1.00 57.71  ? 498  LEU   D CA  1 
ATOM   11803 C  C   . LEU   D  1 197 ? 34.946  55.241  -44.123  1.00 51.92  ? 498  LEU   D C   1 
ATOM   11804 O  O   . LEU   D  1 197 ? 33.781  55.158  -43.731  1.00 55.16  ? 498  LEU   D O   1 
ATOM   11805 C  CB  . LEU   D  1 197 ? 35.849  57.483  -43.532  1.00 54.89  ? 498  LEU   D CB  1 
ATOM   11806 C  CG  . LEU   D  1 197 ? 37.012  56.987  -42.684  1.00 63.10  ? 498  LEU   D CG  1 
ATOM   11807 C  CD1 . LEU   D  1 197 ? 38.178  56.649  -43.587  1.00 53.81  ? 498  LEU   D CD1 1 
ATOM   11808 C  CD2 . LEU   D  1 197 ? 37.397  58.021  -41.612  1.00 69.22  ? 498  LEU   D CD2 1 
ATOM   11809 N  N   . GLY   D  1 198 ? 35.801  54.222  -44.111  1.00 52.67  ? 499  GLY   D N   1 
ATOM   11810 C  CA  . GLY   D  1 198 ? 35.335  52.895  -43.732  1.00 56.77  ? 499  GLY   D CA  1 
ATOM   11811 C  C   . GLY   D  1 198 ? 34.572  52.181  -44.842  1.00 51.24  ? 499  GLY   D C   1 
ATOM   11812 O  O   . GLY   D  1 198 ? 34.855  52.340  -46.033  1.00 63.79  ? 499  GLY   D O   1 
ATOM   11813 N  N   . ASP   D  1 199 ? 33.577  51.405  -44.440  1.00 49.73  ? 500  ASP   D N   1 
ATOM   11814 C  CA  . ASP   D  1 199 ? 32.864  50.459  -45.286  1.00 44.88  ? 500  ASP   D CA  1 
ATOM   11815 C  C   . ASP   D  1 199 ? 31.541  51.073  -45.715  1.00 54.77  ? 500  ASP   D C   1 
ATOM   11816 O  O   . ASP   D  1 199 ? 30.620  51.177  -44.892  1.00 59.50  ? 500  ASP   D O   1 
ATOM   11817 C  CB  . ASP   D  1 199 ? 32.628  49.161  -44.515  1.00 53.49  ? 500  ASP   D CB  1 
ATOM   11818 C  CG  . ASP   D  1 199 ? 31.974  48.073  -45.340  1.00 63.31  ? 500  ASP   D CG  1 
ATOM   11819 O  OD1 . ASP   D  1 199 ? 30.953  48.338  -46.004  1.00 69.30  ? 500  ASP   D OD1 1 
ATOM   11820 O  OD2 . ASP   D  1 199 ? 32.480  46.932  -45.295  1.00 65.65  ? 500  ASP   D OD2 1 
ATOM   11821 N  N   . PRO   D  1 200 ? 31.394  51.483  -46.972  1.00 55.54  ? 501  PRO   D N   1 
ATOM   11822 C  CA  . PRO   D  1 200 ? 30.198  52.249  -47.372  1.00 50.82  ? 501  PRO   D CA  1 
ATOM   11823 C  C   . PRO   D  1 200 ? 28.892  51.498  -47.219  1.00 53.33  ? 501  PRO   D C   1 
ATOM   11824 O  O   . PRO   D  1 200 ? 27.827  52.135  -47.239  1.00 41.72  ? 501  PRO   D O   1 
ATOM   11825 C  CB  . PRO   D  1 200 ? 30.484  52.576  -48.837  1.00 40.21  ? 501  PRO   D CB  1 
ATOM   11826 C  CG  . PRO   D  1 200 ? 31.980  52.592  -48.904  1.00 41.85  ? 501  PRO   D CG  1 
ATOM   11827 C  CD  . PRO   D  1 200 ? 32.463  51.537  -47.978  1.00 41.99  ? 501  PRO   D CD  1 
ATOM   11828 N  N   . ALA   D  1 201 ? 28.938  50.171  -47.061  1.00 57.79  ? 502  ALA   D N   1 
ATOM   11829 C  CA  . ALA   D  1 201 ? 27.717  49.400  -46.843  1.00 56.06  ? 502  ALA   D CA  1 
ATOM   11830 C  C   . ALA   D  1 201 ? 27.081  49.727  -45.502  1.00 58.74  ? 502  ALA   D C   1 
ATOM   11831 O  O   . ALA   D  1 201 ? 25.854  49.786  -45.383  1.00 67.82  ? 502  ALA   D O   1 
ATOM   11832 C  CB  . ALA   D  1 201 ? 28.020  47.905  -46.914  1.00 53.83  ? 502  ALA   D CB  1 
ATOM   11833 N  N   . ASN   D  1 202 ? 27.895  49.931  -44.483  1.00 59.06  ? 503  ASN   D N   1 
ATOM   11834 C  CA  . ASN   D  1 202 ? 27.404  50.006  -43.120  1.00 56.92  ? 503  ASN   D CA  1 
ATOM   11835 C  C   . ASN   D  1 202 ? 27.068  51.429  -42.696  1.00 55.14  ? 503  ASN   D C   1 
ATOM   11836 O  O   . ASN   D  1 202 ? 26.745  51.659  -41.530  1.00 58.23  ? 503  ASN   D O   1 
ATOM   11837 C  CB  . ASN   D  1 202 ? 28.438  49.365  -42.196  1.00 51.39  ? 503  ASN   D CB  1 
ATOM   11838 C  CG  . ASN   D  1 202 ? 28.777  47.939  -42.624  1.00 58.78  ? 503  ASN   D CG  1 
ATOM   11839 O  OD1 . ASN   D  1 202 ? 27.879  47.165  -42.952  1.00 58.70  ? 503  ASN   D OD1 1 
ATOM   11840 N  ND2 . ASN   D  1 202 ? 30.068  47.590  -42.631  1.00 59.96  ? 503  ASN   D ND2 1 
ATOM   11841 N  N   . VAL   D  1 203 ? 27.084  52.376  -43.632  1.00 55.80  ? 504  VAL   D N   1 
ATOM   11842 C  CA  . VAL   D  1 203 ? 26.926  53.783  -43.278  1.00 55.60  ? 504  VAL   D CA  1 
ATOM   11843 C  C   . VAL   D  1 203 ? 25.582  54.032  -42.602  1.00 61.75  ? 504  VAL   D C   1 
ATOM   11844 O  O   . VAL   D  1 203 ? 25.486  54.813  -41.646  1.00 63.08  ? 504  VAL   D O   1 
ATOM   11845 C  CB  . VAL   D  1 203 ? 27.116  54.650  -44.533  1.00 53.08  ? 504  VAL   D CB  1 
ATOM   11846 C  CG1 . VAL   D  1 203 ? 26.799  56.106  -44.246  1.00 54.85  ? 504  VAL   D CG1 1 
ATOM   11847 C  CG2 . VAL   D  1 203 ? 28.545  54.489  -45.045  1.00 57.89  ? 504  VAL   D CG2 1 
ATOM   11848 N  N   . GLN   D  1 204 ? 24.523  53.367  -43.070  1.00 64.54  ? 505  GLN   D N   1 
ATOM   11849 C  CA  . GLN   D  1 204 ? 23.218  53.586  -42.454  1.00 62.91  ? 505  GLN   D CA  1 
ATOM   11850 C  C   . GLN   D  1 204 ? 23.202  53.073  -41.018  1.00 55.68  ? 505  GLN   D C   1 
ATOM   11851 O  O   . GLN   D  1 204 ? 22.694  53.754  -40.115  1.00 45.79  ? 505  GLN   D O   1 
ATOM   11852 C  CB  . GLN   D  1 204 ? 22.114  52.920  -43.279  1.00 68.61  ? 505  GLN   D CB  1 
ATOM   11853 C  CG  . GLN   D  1 204 ? 20.801  53.718  -43.286  1.00 79.80  ? 505  GLN   D CG  1 
ATOM   11854 C  CD  . GLN   D  1 204 ? 19.560  52.859  -43.032  1.00 82.16  ? 505  GLN   D CD  1 
ATOM   11855 O  OE1 . GLN   D  1 204 ? 19.213  51.986  -43.832  1.00 79.57  ? 505  GLN   D OE1 1 
ATOM   11856 N  NE2 . GLN   D  1 204 ? 18.882  53.115  -41.913  1.00 80.02  ? 505  GLN   D NE2 1 
ATOM   11857 N  N   . PHE   D  1 205 ? 23.763  51.877  -40.792  1.00 47.33  ? 506  PHE   D N   1 
ATOM   11858 C  CA  . PHE   D  1 205 ? 23.822  51.316  -39.444  1.00 44.88  ? 506  PHE   D CA  1 
ATOM   11859 C  C   . PHE   D  1 205 ? 24.750  52.129  -38.545  1.00 51.97  ? 506  PHE   D C   1 
ATOM   11860 O  O   . PHE   D  1 205 ? 24.422  52.393  -37.381  1.00 53.35  ? 506  PHE   D O   1 
ATOM   11861 C  CB  . PHE   D  1 205 ? 24.277  49.858  -39.498  1.00 37.08  ? 506  PHE   D CB  1 
ATOM   11862 C  CG  . PHE   D  1 205 ? 24.137  49.140  -38.193  1.00 50.69  ? 506  PHE   D CG  1 
ATOM   11863 C  CD1 . PHE   D  1 205 ? 22.930  48.558  -37.838  1.00 58.01  ? 506  PHE   D CD1 1 
ATOM   11864 C  CD2 . PHE   D  1 205 ? 25.204  49.042  -37.312  1.00 50.43  ? 506  PHE   D CD2 1 
ATOM   11865 C  CE1 . PHE   D  1 205 ? 22.788  47.883  -36.616  1.00 52.31  ? 506  PHE   D CE1 1 
ATOM   11866 C  CE2 . PHE   D  1 205 ? 25.068  48.361  -36.098  1.00 49.53  ? 506  PHE   D CE2 1 
ATOM   11867 C  CZ  . PHE   D  1 205 ? 23.862  47.787  -35.751  1.00 47.22  ? 506  PHE   D CZ  1 
ATOM   11868 N  N   . THR   D  1 206 ? 25.911  52.537  -39.067  1.00 49.48  ? 507  THR   D N   1 
ATOM   11869 C  CA  . THR   D  1 206 ? 26.784  53.442  -38.326  1.00 46.94  ? 507  THR   D CA  1 
ATOM   11870 C  C   . THR   D  1 206 ? 26.037  54.695  -37.881  1.00 61.75  ? 507  THR   D C   1 
ATOM   11871 O  O   . THR   D  1 206 ? 26.229  55.186  -36.761  1.00 71.33  ? 507  THR   D O   1 
ATOM   11872 C  CB  . THR   D  1 206 ? 27.994  53.814  -39.180  1.00 40.02  ? 507  THR   D CB  1 
ATOM   11873 O  OG1 . THR   D  1 206 ? 28.732  52.631  -39.515  1.00 37.21  ? 507  THR   D OG1 1 
ATOM   11874 C  CG2 . THR   D  1 206 ? 28.891  54.749  -38.432  1.00 32.98  ? 507  THR   D CG2 1 
ATOM   11875 N  N   . GLU   D  1 207 ? 25.165  55.223  -38.738  1.00 70.90  ? 508  GLU   D N   1 
ATOM   11876 C  CA  . GLU   D  1 207 ? 24.350  56.357  -38.320  1.00 75.42  ? 508  GLU   D CA  1 
ATOM   11877 C  C   . GLU   D  1 207 ? 23.442  55.977  -37.152  1.00 64.08  ? 508  GLU   D C   1 
ATOM   11878 O  O   . GLU   D  1 207 ? 23.271  56.763  -36.211  1.00 62.31  ? 508  GLU   D O   1 
ATOM   11879 C  CB  . GLU   D  1 207 ? 23.544  56.892  -39.510  1.00 82.27  ? 508  GLU   D CB  1 
ATOM   11880 C  CG  . GLU   D  1 207 ? 24.372  57.715  -40.496  1.00 90.59  ? 508  GLU   D CG  1 
ATOM   11881 C  CD  . GLU   D  1 207 ? 23.606  58.083  -41.766  1.00 102.44 ? 508  GLU   D CD  1 
ATOM   11882 O  OE1 . GLU   D  1 207 ? 22.677  57.336  -42.156  1.00 106.06 ? 508  GLU   D OE1 1 
ATOM   11883 O  OE2 . GLU   D  1 207 ? 23.942  59.123  -42.378  1.00 100.50 ? 508  GLU   D OE2 1 
ATOM   11884 N  N   . ILE   D  1 208 ? 22.871  54.767  -37.176  1.00 54.56  ? 509  ILE   D N   1 
ATOM   11885 C  CA  . ILE   D  1 208 ? 21.949  54.387  -36.108  1.00 49.91  ? 509  ILE   D CA  1 
ATOM   11886 C  C   . ILE   D  1 208 ? 22.689  54.319  -34.786  1.00 49.66  ? 509  ILE   D C   1 
ATOM   11887 O  O   . ILE   D  1 208 ? 22.298  54.973  -33.815  1.00 59.94  ? 509  ILE   D O   1 
ATOM   11888 C  CB  . ILE   D  1 208 ? 21.236  53.059  -36.420  1.00 46.07  ? 509  ILE   D CB  1 
ATOM   11889 C  CG1 . ILE   D  1 208 ? 20.655  53.070  -37.832  1.00 53.89  ? 509  ILE   D CG1 1 
ATOM   11890 C  CG2 . ILE   D  1 208 ? 20.102  52.855  -35.455  1.00 44.53  ? 509  ILE   D CG2 1 
ATOM   11891 C  CD1 . ILE   D  1 208 ? 19.517  52.068  -38.045  1.00 49.36  ? 509  ILE   D CD1 1 
ATOM   11892 N  N   . CYS   D  1 209 ? 23.792  53.556  -34.745  1.00 48.75  ? 510  CYS   D N   1 
ATOM   11893 C  CA  . CYS   D  1 209 ? 24.625  53.450  -33.545  1.00 54.35  ? 510  CYS   D CA  1 
ATOM   11894 C  C   . CYS   D  1 209 ? 24.943  54.821  -32.971  1.00 62.04  ? 510  CYS   D C   1 
ATOM   11895 O  O   . CYS   D  1 209 ? 24.639  55.115  -31.810  1.00 64.10  ? 510  CYS   D O   1 
ATOM   11896 C  CB  . CYS   D  1 209 ? 25.935  52.728  -33.859  1.00 48.35  ? 510  CYS   D CB  1 
ATOM   11897 S  SG  . CYS   D  1 209 ? 25.762  51.102  -34.561  1.00 48.86  ? 510  CYS   D SG  1 
ATOM   11898 N  N   . ILE   D  1 210 ? 25.575  55.668  -33.783  1.00 58.99  ? 511  ILE   D N   1 
ATOM   11899 C  CA  . ILE   D  1 210 ? 25.961  56.998  -33.333  1.00 59.91  ? 511  ILE   D CA  1 
ATOM   11900 C  C   . ILE   D  1 210 ? 24.771  57.715  -32.717  1.00 62.31  ? 511  ILE   D C   1 
ATOM   11901 O  O   . ILE   D  1 210 ? 24.885  58.358  -31.669  1.00 67.58  ? 511  ILE   D O   1 
ATOM   11902 C  CB  . ILE   D  1 210 ? 26.562  57.785  -34.507  1.00 57.37  ? 511  ILE   D CB  1 
ATOM   11903 C  CG1 . ILE   D  1 210 ? 27.915  57.191  -34.882  1.00 51.66  ? 511  ILE   D CG1 1 
ATOM   11904 C  CG2 . ILE   D  1 210 ? 26.675  59.233  -34.148  1.00 51.57  ? 511  ILE   D CG2 1 
ATOM   11905 C  CD1 . ILE   D  1 210 ? 28.498  57.816  -36.114  1.00 49.66  ? 511  ILE   D CD1 1 
ATOM   11906 N  N   . GLN   D  1 211 ? 23.597  57.569  -33.330  1.00 67.02  ? 512  GLN   D N   1 
ATOM   11907 C  CA  . GLN   D  1 211 ? 22.389  58.175  -32.780  1.00 69.82  ? 512  GLN   D CA  1 
ATOM   11908 C  C   . GLN   D  1 211 ? 22.060  57.622  -31.404  1.00 62.25  ? 512  GLN   D C   1 
ATOM   11909 O  O   . GLN   D  1 211 ? 21.561  58.352  -30.540  1.00 54.85  ? 512  GLN   D O   1 
ATOM   11910 C  CB  . GLN   D  1 211 ? 21.217  57.941  -33.729  1.00 74.28  ? 512  GLN   D CB  1 
ATOM   11911 C  CG  . GLN   D  1 211 ? 19.915  58.475  -33.225  1.00 79.05  ? 512  GLN   D CG  1 
ATOM   11912 C  CD  . GLN   D  1 211 ? 19.220  59.265  -34.283  1.00 95.41  ? 512  GLN   D CD  1 
ATOM   11913 O  OE1 . GLN   D  1 211 ? 18.838  60.413  -34.061  1.00 103.52 ? 512  GLN   D OE1 1 
ATOM   11914 N  NE2 . GLN   D  1 211 ? 19.068  58.667  -35.463  1.00 98.17  ? 512  GLN   D NE2 1 
ATOM   11915 N  N   . GLN   D  1 212 ? 22.331  56.343  -31.185  1.00 57.68  ? 513  GLN   D N   1 
ATOM   11916 C  CA  . GLN   D  1 212 ? 22.024  55.677  -29.935  1.00 58.24  ? 513  GLN   D CA  1 
ATOM   11917 C  C   . GLN   D  1 212 ? 23.129  55.821  -28.902  1.00 59.68  ? 513  GLN   D C   1 
ATOM   11918 O  O   . GLN   D  1 212 ? 23.117  55.095  -27.905  1.00 67.72  ? 513  GLN   D O   1 
ATOM   11919 C  CB  . GLN   D  1 212 ? 21.748  54.193  -30.183  1.00 66.21  ? 513  GLN   D CB  1 
ATOM   11920 C  CG  . GLN   D  1 212 ? 20.758  53.896  -31.294  1.00 69.04  ? 513  GLN   D CG  1 
ATOM   11921 C  CD  . GLN   D  1 212 ? 19.395  54.494  -31.037  1.00 79.59  ? 513  GLN   D CD  1 
ATOM   11922 O  OE1 . GLN   D  1 212 ? 19.063  54.851  -29.905  1.00 83.48  ? 513  GLN   D OE1 1 
ATOM   11923 N  NE2 . GLN   D  1 212 ? 18.592  54.607  -32.092  1.00 84.79  ? 513  GLN   D NE2 1 
ATOM   11924 N  N   . GLY   D  1 213 ? 24.093  56.714  -29.121  1.00 54.42  ? 514  GLY   D N   1 
ATOM   11925 C  CA  . GLY   D  1 213 ? 25.088  57.040  -28.118  1.00 56.90  ? 514  GLY   D CA  1 
ATOM   11926 C  C   . GLY   D  1 213 ? 26.475  56.506  -28.381  1.00 61.02  ? 514  GLY   D C   1 
ATOM   11927 O  O   . GLY   D  1 213 ? 27.384  56.790  -27.593  1.00 64.16  ? 514  GLY   D O   1 
ATOM   11928 N  N   . TRP   D  1 214 ? 26.676  55.745  -29.451  1.00 57.09  ? 515  TRP   D N   1 
ATOM   11929 C  CA  . TRP   D  1 214 ? 28.007  55.245  -29.755  1.00 52.27  ? 515  TRP   D CA  1 
ATOM   11930 C  C   . TRP   D  1 214 ? 28.957  56.398  -30.036  1.00 61.91  ? 515  TRP   D C   1 
ATOM   11931 O  O   . TRP   D  1 214 ? 28.616  57.355  -30.736  1.00 60.33  ? 515  TRP   D O   1 
ATOM   11932 C  CB  . TRP   D  1 214 ? 27.954  54.304  -30.954  1.00 63.72  ? 515  TRP   D CB  1 
ATOM   11933 C  CG  . TRP   D  1 214 ? 29.238  53.568  -31.181  1.00 67.95  ? 515  TRP   D CG  1 
ATOM   11934 C  CD1 . TRP   D  1 214 ? 29.932  52.836  -30.264  1.00 64.40  ? 515  TRP   D CD1 1 
ATOM   11935 C  CD2 . TRP   D  1 214 ? 29.978  53.481  -32.407  1.00 61.76  ? 515  TRP   D CD2 1 
ATOM   11936 N  NE1 . TRP   D  1 214 ? 31.062  52.306  -30.839  1.00 65.09  ? 515  TRP   D NE1 1 
ATOM   11937 C  CE2 . TRP   D  1 214 ? 31.113  52.686  -32.153  1.00 60.94  ? 515  TRP   D CE2 1 
ATOM   11938 C  CE3 . TRP   D  1 214 ? 29.793  54.002  -33.684  1.00 57.33  ? 515  TRP   D CE3 1 
ATOM   11939 C  CZ2 . TRP   D  1 214 ? 32.059  52.405  -33.130  1.00 52.53  ? 515  TRP   D CZ2 1 
ATOM   11940 C  CZ3 . TRP   D  1 214 ? 30.727  53.716  -34.649  1.00 61.66  ? 515  TRP   D CZ3 1 
ATOM   11941 C  CH2 . TRP   D  1 214 ? 31.847  52.926  -34.368  1.00 56.82  ? 515  TRP   D CH2 1 
ATOM   11942 N  N   . LYS   D  1 215 ? 30.153  56.307  -29.467  1.00 71.40  ? 516  LYS   D N   1 
ATOM   11943 C  CA  . LYS   D  1 215 ? 31.185  57.313  -29.654  1.00 70.27  ? 516  LYS   D CA  1 
ATOM   11944 C  C   . LYS   D  1 215 ? 32.179  56.771  -30.659  1.00 65.57  ? 516  LYS   D C   1 
ATOM   11945 O  O   . LYS   D  1 215 ? 32.971  55.881  -30.320  1.00 70.70  ? 516  LYS   D O   1 
ATOM   11946 C  CB  . LYS   D  1 215 ? 31.871  57.625  -28.325  1.00 77.47  ? 516  LYS   D CB  1 
ATOM   11947 C  CG  . LYS   D  1 215 ? 30.918  58.168  -27.262  1.00 85.02  ? 516  LYS   D CG  1 
ATOM   11948 C  CD  . LYS   D  1 215 ? 30.924  59.689  -27.247  1.00 84.25  ? 516  LYS   D CD  1 
ATOM   11949 C  CE  . LYS   D  1 215 ? 29.642  60.234  -26.669  1.00 81.46  ? 516  LYS   D CE  1 
ATOM   11950 N  NZ  . LYS   D  1 215 ? 28.501  59.976  -27.584  1.00 74.09  ? 516  LYS   D NZ  1 
ATOM   11951 N  N   . PRO   D  1 216 ? 32.173  57.243  -31.899  1.00 70.30  ? 517  PRO   D N   1 
ATOM   11952 C  CA  . PRO   D  1 216 ? 32.905  56.552  -32.964  1.00 62.22  ? 517  PRO   D CA  1 
ATOM   11953 C  C   . PRO   D  1 216 ? 34.343  57.030  -33.061  1.00 61.85  ? 517  PRO   D C   1 
ATOM   11954 O  O   . PRO   D  1 216 ? 34.609  58.240  -33.025  1.00 68.92  ? 517  PRO   D O   1 
ATOM   11955 C  CB  . PRO   D  1 216 ? 32.108  56.921  -34.221  1.00 63.41  ? 517  PRO   D CB  1 
ATOM   11956 C  CG  . PRO   D  1 216 ? 31.562  58.270  -33.919  1.00 64.62  ? 517  PRO   D CG  1 
ATOM   11957 C  CD  . PRO   D  1 216 ? 31.298  58.304  -32.428  1.00 70.39  ? 517  PRO   D CD  1 
ATOM   11958 N  N   . PRO   D  1 217 ? 35.304  56.108  -33.194  1.00 55.87  ? 518  PRO   D N   1 
ATOM   11959 C  CA  . PRO   D  1 217 ? 36.692  56.520  -33.479  1.00 54.92  ? 518  PRO   D CA  1 
ATOM   11960 C  C   . PRO   D  1 217 ? 36.844  57.290  -34.776  1.00 61.02  ? 518  PRO   D C   1 
ATOM   11961 O  O   . PRO   D  1 217 ? 37.824  58.026  -34.929  1.00 64.75  ? 518  PRO   D O   1 
ATOM   11962 C  CB  . PRO   D  1 217 ? 37.452  55.188  -33.553  1.00 49.58  ? 518  PRO   D CB  1 
ATOM   11963 C  CG  . PRO   D  1 217 ? 36.589  54.215  -32.846  1.00 45.38  ? 518  PRO   D CG  1 
ATOM   11964 C  CD  . PRO   D  1 217 ? 35.175  54.652  -33.052  1.00 42.21  ? 518  PRO   D CD  1 
ATOM   11965 N  N   . ARG   D  1 218 ? 35.911  57.139  -35.711  1.00 75.02  ? 519  ARG   D N   1 
ATOM   11966 C  CA  . ARG   D  1 218 ? 36.022  57.692  -37.061  1.00 77.14  ? 519  ARG   D CA  1 
ATOM   11967 C  C   . ARG   D  1 218 ? 37.365  57.317  -37.691  1.00 76.84  ? 519  ARG   D C   1 
ATOM   11968 O  O   . ARG   D  1 218 ? 38.215  58.158  -37.988  1.00 81.50  ? 519  ARG   D O   1 
ATOM   11969 C  CB  . ARG   D  1 218 ? 35.807  59.204  -37.058  1.00 71.28  ? 519  ARG   D CB  1 
ATOM   11970 C  CG  . ARG   D  1 218 ? 34.614  59.654  -36.234  1.00 71.11  ? 519  ARG   D CG  1 
ATOM   11971 C  CD  . ARG   D  1 218 ? 34.104  60.997  -36.718  1.00 77.30  ? 519  ARG   D CD  1 
ATOM   11972 N  NE  . ARG   D  1 218 ? 33.349  60.843  -37.956  1.00 89.87  ? 519  ARG   D NE  1 
ATOM   11973 C  CZ  . ARG   D  1 218 ? 32.022  60.884  -38.027  1.00 93.46  ? 519  ARG   D CZ  1 
ATOM   11974 N  NH1 . ARG   D  1 218 ? 31.408  60.722  -39.199  1.00 92.52  ? 519  ARG   D NH1 1 
ATOM   11975 N  NH2 . ARG   D  1 218 ? 31.314  61.100  -36.922  1.00 89.59  ? 519  ARG   D NH2 1 
ATOM   11976 N  N   . GLY   D  1 219 ? 37.545  56.010  -37.872  1.00 68.33  ? 520  GLY   D N   1 
ATOM   11977 C  CA  . GLY   D  1 219 ? 38.709  55.475  -38.539  1.00 66.90  ? 520  GLY   D CA  1 
ATOM   11978 C  C   . GLY   D  1 219 ? 38.297  54.611  -39.711  1.00 74.29  ? 520  GLY   D C   1 
ATOM   11979 O  O   . GLY   D  1 219 ? 37.124  54.593  -40.098  1.00 74.71  ? 520  GLY   D O   1 
ATOM   11980 N  N   . ARG   D  1 220 ? 39.243  53.876  -40.287  1.00 74.14  ? 521  ARG   D N   1 
ATOM   11981 C  CA  . ARG   D  1 220 ? 38.903  53.031  -41.422  1.00 61.88  ? 521  ARG   D CA  1 
ATOM   11982 C  C   . ARG   D  1 220 ? 38.368  51.669  -41.011  1.00 56.77  ? 521  ARG   D C   1 
ATOM   11983 O  O   . ARG   D  1 220 ? 37.516  51.122  -41.713  1.00 55.39  ? 521  ARG   D O   1 
ATOM   11984 C  CB  . ARG   D  1 220 ? 40.117  52.838  -42.328  1.00 66.36  ? 521  ARG   D CB  1 
ATOM   11985 C  CG  . ARG   D  1 220 ? 39.818  52.062  -43.605  1.00 76.76  ? 521  ARG   D CG  1 
ATOM   11986 C  CD  . ARG   D  1 220 ? 39.597  52.991  -44.799  1.00 82.67  ? 521  ARG   D CD  1 
ATOM   11987 N  NE  . ARG   D  1 220 ? 39.850  52.290  -46.057  1.00 82.76  ? 521  ARG   D NE  1 
ATOM   11988 C  CZ  . ARG   D  1 220 ? 41.023  52.273  -46.682  1.00 82.57  ? 521  ARG   D CZ  1 
ATOM   11989 N  NH1 . ARG   D  1 220 ? 42.047  52.945  -46.174  1.00 81.62  ? 521  ARG   D NH1 1 
ATOM   11990 N  NH2 . ARG   D  1 220 ? 41.169  51.595  -47.820  1.00 81.09  ? 521  ARG   D NH2 1 
ATOM   11991 N  N   . PHE   D  1 221 ? 38.842  51.101  -39.901  1.00 67.02  ? 522  PHE   D N   1 
ATOM   11992 C  CA  . PHE   D  1 221 ? 38.482  49.736  -39.521  1.00 60.45  ? 522  PHE   D CA  1 
ATOM   11993 C  C   . PHE   D  1 221 ? 38.034  49.677  -38.063  1.00 59.83  ? 522  PHE   D C   1 
ATOM   11994 O  O   . PHE   D  1 221 ? 38.487  48.857  -37.264  1.00 66.68  ? 522  PHE   D O   1 
ATOM   11995 C  CB  . PHE   D  1 221 ? 39.635  48.785  -39.825  1.00 60.81  ? 522  PHE   D CB  1 
ATOM   11996 C  CG  . PHE   D  1 221 ? 40.001  48.740  -41.289  1.00 62.62  ? 522  PHE   D CG  1 
ATOM   11997 C  CD1 . PHE   D  1 221 ? 41.287  49.039  -41.712  1.00 66.84  ? 522  PHE   D CD1 1 
ATOM   11998 C  CD2 . PHE   D  1 221 ? 39.048  48.429  -42.244  1.00 55.96  ? 522  PHE   D CD2 1 
ATOM   11999 C  CE1 . PHE   D  1 221 ? 41.614  49.017  -43.063  1.00 55.13  ? 522  PHE   D CE1 1 
ATOM   12000 C  CE2 . PHE   D  1 221 ? 39.368  48.404  -43.580  1.00 51.72  ? 522  PHE   D CE2 1 
ATOM   12001 C  CZ  . PHE   D  1 221 ? 40.651  48.698  -43.990  1.00 51.93  ? 522  PHE   D CZ  1 
ATOM   12002 N  N   . ASP   D  1 222 ? 37.099  50.556  -37.719  1.00 49.71  ? 523  ASP   D N   1 
ATOM   12003 C  CA  . ASP   D  1 222 ? 36.402  50.504  -36.444  1.00 44.81  ? 523  ASP   D CA  1 
ATOM   12004 C  C   . ASP   D  1 222 ? 35.459  49.314  -36.429  1.00 53.43  ? 523  ASP   D C   1 
ATOM   12005 O  O   . ASP   D  1 222 ? 34.606  49.202  -37.309  1.00 61.48  ? 523  ASP   D O   1 
ATOM   12006 C  CB  . ASP   D  1 222 ? 35.612  51.795  -36.242  1.00 35.04  ? 523  ASP   D CB  1 
ATOM   12007 C  CG  . ASP   D  1 222 ? 36.466  53.040  -36.415  1.00 54.25  ? 523  ASP   D CG  1 
ATOM   12008 O  OD1 . ASP   D  1 222 ? 37.677  52.936  -36.738  1.00 60.76  ? 523  ASP   D OD1 1 
ATOM   12009 O  OD2 . ASP   D  1 222 ? 35.911  54.137  -36.226  1.00 63.15  ? 523  ASP   D OD2 1 
ATOM   12010 N  N   . VAL   D  1 223 ? 35.593  48.418  -35.446  1.00 58.88  ? 524  VAL   D N   1 
ATOM   12011 C  CA  . VAL   D  1 223 ? 34.584  47.375  -35.274  1.00 46.91  ? 524  VAL   D CA  1 
ATOM   12012 C  C   . VAL   D  1 223 ? 33.320  48.002  -34.714  1.00 48.41  ? 524  VAL   D C   1 
ATOM   12013 O  O   . VAL   D  1 223 ? 33.370  48.759  -33.738  1.00 49.35  ? 524  VAL   D O   1 
ATOM   12014 C  CB  . VAL   D  1 223 ? 35.077  46.260  -34.346  1.00 36.48  ? 524  VAL   D CB  1 
ATOM   12015 C  CG1 . VAL   D  1 223 ? 33.939  45.303  -34.103  1.00 31.58  ? 524  VAL   D CG1 1 
ATOM   12016 C  CG2 . VAL   D  1 223 ? 36.273  45.536  -34.945  1.00 27.12  ? 524  VAL   D CG2 1 
ATOM   12017 N  N   . LEU   D  1 224 ? 32.187  47.707  -35.328  1.00 39.13  ? 525  LEU   D N   1 
ATOM   12018 C  CA  . LEU   D  1 224 ? 30.969  48.341  -34.866  1.00 40.50  ? 525  LEU   D CA  1 
ATOM   12019 C  C   . LEU   D  1 224 ? 30.535  47.759  -33.535  1.00 44.12  ? 525  LEU   D C   1 
ATOM   12020 O  O   . LEU   D  1 224 ? 30.973  46.677  -33.148  1.00 54.59  ? 525  LEU   D O   1 
ATOM   12021 C  CB  . LEU   D  1 224 ? 29.859  48.151  -35.880  1.00 42.23  ? 525  LEU   D CB  1 
ATOM   12022 C  CG  . LEU   D  1 224 ? 29.910  49.056  -37.099  1.00 42.71  ? 525  LEU   D CG  1 
ATOM   12023 C  CD1 . LEU   D  1 224 ? 29.234  48.278  -38.165  1.00 26.71  ? 525  LEU   D CD1 1 
ATOM   12024 C  CD2 . LEU   D  1 224 ? 29.198  50.370  -36.824  1.00 34.06  ? 525  LEU   D CD2 1 
ATOM   12025 N  N   . PRO   D  1 225 ? 29.664  48.451  -32.815  1.00 38.86  ? 526  PRO   D N   1 
ATOM   12026 C  CA  . PRO   D  1 225 ? 29.118  47.889  -31.582  1.00 46.56  ? 526  PRO   D CA  1 
ATOM   12027 C  C   . PRO   D  1 225 ? 27.951  46.978  -31.910  1.00 46.35  ? 526  PRO   D C   1 
ATOM   12028 O  O   . PRO   D  1 225 ? 27.343  47.078  -32.970  1.00 50.18  ? 526  PRO   D O   1 
ATOM   12029 C  CB  . PRO   D  1 225 ? 28.640  49.128  -30.816  1.00 43.09  ? 526  PRO   D CB  1 
ATOM   12030 C  CG  . PRO   D  1 225 ? 28.242  50.078  -31.904  1.00 44.49  ? 526  PRO   D CG  1 
ATOM   12031 C  CD  . PRO   D  1 225 ? 29.217  49.840  -33.026  1.00 46.35  ? 526  PRO   D CD  1 
ATOM   12032 N  N   . LEU   D  1 226 ? 27.656  46.075  -30.984  1.00 34.40  ? 527  LEU   D N   1 
ATOM   12033 C  CA  . LEU   D  1 226 ? 26.433  45.310  -31.111  1.00 36.30  ? 527  LEU   D CA  1 
ATOM   12034 C  C   . LEU   D  1 226 ? 25.255  46.206  -30.782  1.00 45.08  ? 527  LEU   D C   1 
ATOM   12035 O  O   . LEU   D  1 226 ? 25.353  47.114  -29.962  1.00 60.74  ? 527  LEU   D O   1 
ATOM   12036 C  CB  . LEU   D  1 226 ? 26.451  44.100  -30.191  1.00 45.98  ? 527  LEU   D CB  1 
ATOM   12037 C  CG  . LEU   D  1 226 ? 27.459  43.052  -30.652  1.00 45.87  ? 527  LEU   D CG  1 
ATOM   12038 C  CD1 . LEU   D  1 226 ? 27.462  41.795  -29.751  1.00 41.31  ? 527  LEU   D CD1 1 
ATOM   12039 C  CD2 . LEU   D  1 226 ? 27.145  42.709  -32.093  1.00 37.94  ? 527  LEU   D CD2 1 
ATOM   12040 N  N   . LEU   D  1 227 ? 24.146  45.972  -31.471  1.00 55.77  ? 528  LEU   D N   1 
ATOM   12041 C  CA  . LEU   D  1 227 ? 22.885  46.667  -31.225  1.00 52.98  ? 528  LEU   D CA  1 
ATOM   12042 C  C   . LEU   D  1 227 ? 21.870  45.556  -31.025  1.00 51.54  ? 528  LEU   D C   1 
ATOM   12043 O  O   . LEU   D  1 227 ? 21.433  44.928  -31.994  1.00 53.00  ? 528  LEU   D O   1 
ATOM   12044 C  CB  . LEU   D  1 227 ? 22.502  47.578  -32.382  1.00 52.20  ? 528  LEU   D CB  1 
ATOM   12045 C  CG  . LEU   D  1 227 ? 21.983  48.964  -32.008  1.00 47.15  ? 528  LEU   D CG  1 
ATOM   12046 C  CD1 . LEU   D  1 227 ? 20.966  49.374  -33.015  1.00 41.41  ? 528  LEU   D CD1 1 
ATOM   12047 C  CD2 . LEU   D  1 227 ? 21.390  48.959  -30.627  1.00 42.21  ? 528  LEU   D CD2 1 
ATOM   12048 N  N   . LEU   D  1 228 ? 21.534  45.279  -29.777  1.00 42.63  ? 529  LEU   D N   1 
ATOM   12049 C  CA  . LEU   D  1 228 ? 20.777  44.084  -29.445  1.00 45.83  ? 529  LEU   D CA  1 
ATOM   12050 C  C   . LEU   D  1 228 ? 19.415  44.460  -28.894  1.00 48.64  ? 529  LEU   D C   1 
ATOM   12051 O  O   . LEU   D  1 228 ? 19.286  45.416  -28.123  1.00 46.51  ? 529  LEU   D O   1 
ATOM   12052 C  CB  . LEU   D  1 228 ? 21.517  43.237  -28.437  1.00 51.76  ? 529  LEU   D CB  1 
ATOM   12053 C  CG  . LEU   D  1 228 ? 22.901  42.848  -28.919  1.00 48.16  ? 529  LEU   D CG  1 
ATOM   12054 C  CD1 . LEU   D  1 228 ? 23.596  42.117  -27.802  1.00 55.16  ? 529  LEU   D CD1 1 
ATOM   12055 C  CD2 . LEU   D  1 228 ? 22.782  41.971  -30.126  1.00 39.18  ? 529  LEU   D CD2 1 
ATOM   12056 N  N   . GLN   D  1 229 ? 18.412  43.687  -29.287  1.00 45.09  ? 530  GLN   D N   1 
ATOM   12057 C  CA  . GLN   D  1 229 ? 17.042  43.908  -28.878  1.00 45.96  ? 530  GLN   D CA  1 
ATOM   12058 C  C   . GLN   D  1 229 ? 16.494  42.594  -28.366  1.00 42.39  ? 530  GLN   D C   1 
ATOM   12059 O  O   . GLN   D  1 229 ? 16.691  41.549  -28.988  1.00 44.80  ? 530  GLN   D O   1 
ATOM   12060 C  CB  . GLN   D  1 229 ? 16.217  44.435  -30.046  1.00 50.64  ? 530  GLN   D CB  1 
ATOM   12061 C  CG  . GLN   D  1 229 ? 14.726  44.136  -30.008  1.00 41.35  ? 530  GLN   D CG  1 
ATOM   12062 C  CD  . GLN   D  1 229 ? 13.983  44.740  -31.210  1.00 46.32  ? 530  GLN   D CD  1 
ATOM   12063 O  OE1 . GLN   D  1 229 ? 14.372  44.547  -32.375  1.00 48.66  ? 530  GLN   D OE1 1 
ATOM   12064 N  NE2 . GLN   D  1 229 ? 12.917  45.478  -30.929  1.00 41.77  ? 530  GLN   D NE2 1 
ATOM   12065 N  N   . ALA   D  1 230 ? 15.816  42.656  -27.229  1.00 46.30  ? 531  ALA   D N   1 
ATOM   12066 C  CA  . ALA   D  1 230 ? 15.239  41.490  -26.580  1.00 49.48  ? 531  ALA   D CA  1 
ATOM   12067 C  C   . ALA   D  1 230 ? 13.781  41.773  -26.260  1.00 46.70  ? 531  ALA   D C   1 
ATOM   12068 O  O   . ALA   D  1 230 ? 13.460  42.830  -25.710  1.00 54.05  ? 531  ALA   D O   1 
ATOM   12069 C  CB  . ALA   D  1 230 ? 16.009  41.143  -25.298  1.00 49.97  ? 531  ALA   D CB  1 
ATOM   12070 N  N   . ASN   D  1 231 ? 12.902  40.845  -26.627  1.00 43.07  ? 532  ASN   D N   1 
ATOM   12071 C  CA  . ASN   D  1 231 ? 11.496  40.912  -26.226  1.00 44.52  ? 532  ASN   D CA  1 
ATOM   12072 C  C   . ASN   D  1 231 ? 10.841  42.215  -26.686  1.00 45.65  ? 532  ASN   D C   1 
ATOM   12073 O  O   . ASN   D  1 231 ? 10.064  42.837  -25.955  1.00 50.29  ? 532  ASN   D O   1 
ATOM   12074 C  CB  . ASN   D  1 231 ? 11.362  40.731  -24.713  1.00 44.25  ? 532  ASN   D CB  1 
ATOM   12075 C  CG  . ASN   D  1 231 ? 10.145  39.921  -24.332  1.00 60.28  ? 532  ASN   D CG  1 
ATOM   12076 O  OD1 . ASN   D  1 231 ? 9.149   40.467  -23.863  1.00 78.80  ? 532  ASN   D OD1 1 
ATOM   12077 N  ND2 . ASN   D  1 231 ? 10.214  38.611  -24.536  1.00 64.87  ? 532  ASN   D ND2 1 
ATOM   12078 N  N   . GLY   D  1 232 ? 11.163  42.627  -27.914  1.00 52.64  ? 533  GLY   D N   1 
ATOM   12079 C  CA  . GLY   D  1 232 ? 10.591  43.814  -28.528  1.00 49.30  ? 533  GLY   D CA  1 
ATOM   12080 C  C   . GLY   D  1 232 ? 10.917  45.124  -27.849  1.00 46.39  ? 533  GLY   D C   1 
ATOM   12081 O  O   . GLY   D  1 232 ? 10.221  46.121  -28.065  1.00 41.58  ? 533  GLY   D O   1 
ATOM   12082 N  N   . ASN   D  1 233 ? 11.936  45.161  -27.010  1.00 54.28  ? 534  ASN   D N   1 
ATOM   12083 C  CA  . ASN   D  1 233 ? 12.277  46.431  -26.400  1.00 50.80  ? 534  ASN   D CA  1 
ATOM   12084 C  C   . ASN   D  1 233 ? 13.213  47.202  -27.318  1.00 54.65  ? 534  ASN   D C   1 
ATOM   12085 O  O   . ASN   D  1 233 ? 13.763  46.650  -28.277  1.00 44.36  ? 534  ASN   D O   1 
ATOM   12086 C  CB  . ASN   D  1 233 ? 12.879  46.195  -25.026  1.00 61.30  ? 534  ASN   D CB  1 
ATOM   12087 C  CG  . ASN   D  1 233 ? 11.848  45.649  -24.050  1.00 70.18  ? 534  ASN   D CG  1 
ATOM   12088 O  OD1 . ASN   D  1 233 ? 10.712  46.135  -24.010  1.00 74.24  ? 534  ASN   D OD1 1 
ATOM   12089 N  ND2 . ASN   D  1 233 ? 12.223  44.622  -23.281  1.00 66.21  ? 534  ASN   D ND2 1 
ATOM   12090 N  N   . ASP   D  1 234 ? 13.330  48.507  -27.067  1.00 61.86  ? 535  ASP   D N   1 
ATOM   12091 C  CA  . ASP   D  1 234 ? 14.311  49.290  -27.803  1.00 57.70  ? 535  ASP   D CA  1 
ATOM   12092 C  C   . ASP   D  1 234 ? 15.657  48.587  -27.682  1.00 50.99  ? 535  ASP   D C   1 
ATOM   12093 O  O   . ASP   D  1 234 ? 15.935  47.973  -26.647  1.00 53.55  ? 535  ASP   D O   1 
ATOM   12094 C  CB  . ASP   D  1 234 ? 14.422  50.728  -27.266  1.00 65.38  ? 535  ASP   D CB  1 
ATOM   12095 C  CG  . ASP   D  1 234 ? 13.118  51.521  -27.372  1.00 69.72  ? 535  ASP   D CG  1 
ATOM   12096 O  OD1 . ASP   D  1 234 ? 13.044  52.629  -26.795  1.00 72.60  ? 535  ASP   D OD1 1 
ATOM   12097 O  OD2 . ASP   D  1 234 ? 12.162  51.041  -28.014  1.00 71.18  ? 535  ASP   D OD2 1 
ATOM   12098 N  N   . PRO   D  1 235 ? 16.481  48.589  -28.715  1.00 52.23  ? 536  PRO   D N   1 
ATOM   12099 C  CA  . PRO   D  1 235 ? 17.742  47.853  -28.643  1.00 51.57  ? 536  PRO   D CA  1 
ATOM   12100 C  C   . PRO   D  1 235 ? 18.777  48.651  -27.862  1.00 45.68  ? 536  PRO   D C   1 
ATOM   12101 O  O   . PRO   D  1 235 ? 18.592  49.836  -27.572  1.00 40.53  ? 536  PRO   D O   1 
ATOM   12102 C  CB  . PRO   D  1 235 ? 18.127  47.692  -30.113  1.00 47.72  ? 536  PRO   D CB  1 
ATOM   12103 C  CG  . PRO   D  1 235 ? 17.600  48.931  -30.731  1.00 38.10  ? 536  PRO   D CG  1 
ATOM   12104 C  CD  . PRO   D  1 235 ? 16.303  49.237  -30.025  1.00 40.62  ? 536  PRO   D CD  1 
ATOM   12105 N  N   . GLU   D  1 236 ? 19.882  47.974  -27.516  1.00 49.79  ? 537  GLU   D N   1 
ATOM   12106 C  CA  . GLU   D  1 236 ? 20.903  48.532  -26.627  1.00 52.84  ? 537  GLU   D CA  1 
ATOM   12107 C  C   . GLU   D  1 236 ? 22.307  48.251  -27.164  1.00 49.79  ? 537  GLU   D C   1 
ATOM   12108 O  O   . GLU   D  1 236 ? 22.577  47.159  -27.676  1.00 42.25  ? 537  GLU   D O   1 
ATOM   12109 C  CB  . GLU   D  1 236 ? 20.755  47.961  -25.194  1.00 48.18  ? 537  GLU   D CB  1 
ATOM   12110 C  CG  . GLU   D  1 236 ? 19.409  48.278  -24.536  1.00 49.09  ? 537  GLU   D CG  1 
ATOM   12111 C  CD  . GLU   D  1 236 ? 19.046  47.324  -23.402  1.00 61.54  ? 537  GLU   D CD  1 
ATOM   12112 O  OE1 . GLU   D  1 236 ? 19.851  47.163  -22.449  1.00 65.69  ? 537  GLU   D OE1 1 
ATOM   12113 O  OE2 . GLU   D  1 236 ? 17.945  46.729  -23.471  1.00 60.08  ? 537  GLU   D OE2 1 
ATOM   12114 N  N   . LEU   D  1 237 ? 23.203  49.236  -27.037  1.00 42.10  ? 538  LEU   D N   1 
ATOM   12115 C  CA  . LEU   D  1 237 ? 24.564  49.106  -27.549  1.00 40.32  ? 538  LEU   D CA  1 
ATOM   12116 C  C   . LEU   D  1 237 ? 25.433  48.280  -26.602  1.00 54.69  ? 538  LEU   D C   1 
ATOM   12117 O  O   . LEU   D  1 237 ? 25.190  48.228  -25.397  1.00 57.70  ? 538  LEU   D O   1 
ATOM   12118 C  CB  . LEU   D  1 237 ? 25.197  50.488  -27.755  1.00 31.04  ? 538  LEU   D CB  1 
ATOM   12119 C  CG  . LEU   D  1 237 ? 24.503  51.464  -28.706  1.00 47.27  ? 538  LEU   D CG  1 
ATOM   12120 C  CD1 . LEU   D  1 237 ? 25.182  52.813  -28.688  1.00 56.97  ? 538  LEU   D CD1 1 
ATOM   12121 C  CD2 . LEU   D  1 237 ? 24.470  50.915  -30.137  1.00 47.42  ? 538  LEU   D CD2 1 
ATOM   12122 N  N   . PHE   D  1 238 ? 26.449  47.618  -27.167  1.00 58.62  ? 539  PHE   D N   1 
ATOM   12123 C  CA  . PHE   D  1 238 ? 27.506  46.969  -26.393  1.00 53.39  ? 539  PHE   D CA  1 
ATOM   12124 C  C   . PHE   D  1 238 ? 28.771  46.931  -27.237  1.00 59.99  ? 539  PHE   D C   1 
ATOM   12125 O  O   . PHE   D  1 238 ? 28.704  46.779  -28.458  1.00 59.08  ? 539  PHE   D O   1 
ATOM   12126 C  CB  . PHE   D  1 238 ? 27.145  45.536  -25.985  1.00 42.44  ? 539  PHE   D CB  1 
ATOM   12127 C  CG  . PHE   D  1 238 ? 25.868  45.431  -25.250  1.00 43.65  ? 539  PHE   D CG  1 
ATOM   12128 C  CD1 . PHE   D  1 238 ? 24.714  45.085  -25.910  1.00 37.40  ? 539  PHE   D CD1 1 
ATOM   12129 C  CD2 . PHE   D  1 238 ? 25.813  45.714  -23.891  1.00 51.00  ? 539  PHE   D CD2 1 
ATOM   12130 C  CE1 . PHE   D  1 238 ? 23.518  44.999  -25.233  1.00 46.14  ? 539  PHE   D CE1 1 
ATOM   12131 C  CE2 . PHE   D  1 238 ? 24.626  45.643  -23.210  1.00 47.36  ? 539  PHE   D CE2 1 
ATOM   12132 C  CZ  . PHE   D  1 238 ? 23.471  45.280  -23.881  1.00 48.91  ? 539  PHE   D CZ  1 
ATOM   12133 N  N   . GLN   D  1 239 ? 29.928  47.054  -26.583  1.00 57.77  ? 540  GLN   D N   1 
ATOM   12134 C  CA  . GLN   D  1 239 ? 31.219  46.950  -27.261  1.00 60.97  ? 540  GLN   D CA  1 
ATOM   12135 C  C   . GLN   D  1 239 ? 31.747  45.531  -27.090  1.00 56.24  ? 540  GLN   D C   1 
ATOM   12136 O  O   . GLN   D  1 239 ? 32.085  45.132  -25.975  1.00 58.81  ? 540  GLN   D O   1 
ATOM   12137 C  CB  . GLN   D  1 239 ? 32.216  47.967  -26.703  1.00 68.49  ? 540  GLN   D CB  1 
ATOM   12138 C  CG  . GLN   D  1 239 ? 33.606  47.935  -27.362  1.00 73.30  ? 540  GLN   D CG  1 
ATOM   12139 C  CD  . GLN   D  1 239 ? 34.761  48.104  -26.359  1.00 80.50  ? 540  GLN   D CD  1 
ATOM   12140 O  OE1 . GLN   D  1 239 ? 34.890  47.337  -25.390  1.00 81.83  ? 540  GLN   D OE1 1 
ATOM   12141 N  NE2 . GLN   D  1 239 ? 35.601  49.109  -26.593  1.00 74.85  ? 540  GLN   D NE2 1 
ATOM   12142 N  N   . ILE   D  1 240 ? 31.798  44.768  -28.184  1.00 58.09  ? 541  ILE   D N   1 
ATOM   12143 C  CA  . ILE   D  1 240 ? 32.489  43.471  -28.222  1.00 56.22  ? 541  ILE   D CA  1 
ATOM   12144 C  C   . ILE   D  1 240 ? 33.911  43.666  -27.711  1.00 57.66  ? 541  ILE   D C   1 
ATOM   12145 O  O   . ILE   D  1 240 ? 34.652  44.482  -28.277  1.00 64.27  ? 541  ILE   D O   1 
ATOM   12146 C  CB  . ILE   D  1 240 ? 32.543  42.874  -29.642  1.00 43.04  ? 541  ILE   D CB  1 
ATOM   12147 C  CG1 . ILE   D  1 240 ? 31.163  42.777  -30.275  1.00 49.61  ? 541  ILE   D CG1 1 
ATOM   12148 C  CG2 . ILE   D  1 240 ? 33.170  41.493  -29.612  1.00 35.45  ? 541  ILE   D CG2 1 
ATOM   12149 C  CD1 . ILE   D  1 240 ? 31.158  42.019  -31.613  1.00 50.02  ? 541  ILE   D CD1 1 
ATOM   12150 N  N   . PRO   D  1 241 ? 34.347  42.952  -26.682  1.00 56.80  ? 542  PRO   D N   1 
ATOM   12151 C  CA  . PRO   D  1 241 ? 35.673  43.212  -26.133  1.00 54.99  ? 542  PRO   D CA  1 
ATOM   12152 C  C   . PRO   D  1 241 ? 36.734  42.972  -27.192  1.00 50.94  ? 542  PRO   D C   1 
ATOM   12153 O  O   . PRO   D  1 241 ? 36.734  41.938  -27.882  1.00 44.18  ? 542  PRO   D O   1 
ATOM   12154 C  CB  . PRO   D  1 241 ? 35.779  42.214  -24.972  1.00 45.26  ? 542  PRO   D CB  1 
ATOM   12155 C  CG  . PRO   D  1 241 ? 34.360  41.879  -24.654  1.00 46.86  ? 542  PRO   D CG  1 
ATOM   12156 C  CD  . PRO   D  1 241 ? 33.686  41.842  -25.983  1.00 50.97  ? 542  PRO   D CD  1 
ATOM   12157 N  N   . PRO   D  1 242 ? 37.638  43.928  -27.370  1.00 41.40  ? 543  PRO   D N   1 
ATOM   12158 C  CA  . PRO   D  1 242 ? 38.518  43.893  -28.542  1.00 46.43  ? 543  PRO   D CA  1 
ATOM   12159 C  C   . PRO   D  1 242 ? 39.381  42.648  -28.600  1.00 53.62  ? 543  PRO   D C   1 
ATOM   12160 O  O   . PRO   D  1 242 ? 39.774  42.226  -29.695  1.00 59.28  ? 543  PRO   D O   1 
ATOM   12161 C  CB  . PRO   D  1 242 ? 39.362  45.165  -28.382  1.00 46.39  ? 543  PRO   D CB  1 
ATOM   12162 C  CG  . PRO   D  1 242 ? 38.636  46.006  -27.374  1.00 42.39  ? 543  PRO   D CG  1 
ATOM   12163 C  CD  . PRO   D  1 242 ? 37.931  45.053  -26.475  1.00 34.27  ? 543  PRO   D CD  1 
ATOM   12164 N  N   . GLU   D  1 243 ? 39.671  42.029  -27.457  1.00 48.19  ? 544  GLU   D N   1 
ATOM   12165 C  CA  . GLU   D  1 243 ? 40.476  40.816  -27.477  1.00 44.58  ? 544  GLU   D CA  1 
ATOM   12166 C  C   . GLU   D  1 243 ? 39.728  39.636  -28.082  1.00 40.52  ? 544  GLU   D C   1 
ATOM   12167 O  O   . GLU   D  1 243 ? 40.333  38.581  -28.305  1.00 39.45  ? 544  GLU   D O   1 
ATOM   12168 C  CB  . GLU   D  1 243 ? 40.972  40.480  -26.054  1.00 45.62  ? 544  GLU   D CB  1 
ATOM   12169 C  CG  . GLU   D  1 243 ? 39.907  40.069  -25.025  1.00 51.85  ? 544  GLU   D CG  1 
ATOM   12170 C  CD  . GLU   D  1 243 ? 39.334  41.229  -24.201  1.00 55.55  ? 544  GLU   D CD  1 
ATOM   12171 O  OE1 . GLU   D  1 243 ? 39.651  42.395  -24.508  1.00 52.65  ? 544  GLU   D OE1 1 
ATOM   12172 O  OE2 . GLU   D  1 243 ? 38.564  40.966  -23.240  1.00 61.18  ? 544  GLU   D OE2 1 
ATOM   12173 N  N   . LEU   D  1 244 ? 38.433  39.778  -28.340  1.00 36.05  ? 545  LEU   D N   1 
ATOM   12174 C  CA  . LEU   D  1 244 ? 37.660  38.706  -28.941  1.00 34.00  ? 545  LEU   D CA  1 
ATOM   12175 C  C   . LEU   D  1 244 ? 37.465  38.865  -30.450  1.00 34.81  ? 545  LEU   D C   1 
ATOM   12176 O  O   . LEU   D  1 244 ? 36.969  37.933  -31.086  1.00 41.67  ? 545  LEU   D O   1 
ATOM   12177 C  CB  . LEU   D  1 244 ? 36.284  38.611  -28.276  1.00 25.57  ? 545  LEU   D CB  1 
ATOM   12178 C  CG  . LEU   D  1 244 ? 36.087  38.220  -26.823  1.00 37.15  ? 545  LEU   D CG  1 
ATOM   12179 C  CD1 . LEU   D  1 244 ? 34.624  37.979  -26.638  1.00 36.79  ? 545  LEU   D CD1 1 
ATOM   12180 C  CD2 . LEU   D  1 244 ? 36.885  36.978  -26.495  1.00 45.24  ? 545  LEU   D CD2 1 
ATOM   12181 N  N   . VAL   D  1 245 ? 37.817  40.019  -31.032  1.00 32.88  ? 546  VAL   D N   1 
ATOM   12182 C  CA  . VAL   D  1 245 ? 37.694  40.278  -32.467  1.00 38.67  ? 546  VAL   D CA  1 
ATOM   12183 C  C   . VAL   D  1 245 ? 39.046  39.982  -33.103  1.00 43.98  ? 546  VAL   D C   1 
ATOM   12184 O  O   . VAL   D  1 245 ? 39.942  40.841  -33.132  1.00 41.87  ? 546  VAL   D O   1 
ATOM   12185 C  CB  . VAL   D  1 245 ? 37.265  41.717  -32.761  1.00 42.77  ? 546  VAL   D CB  1 
ATOM   12186 C  CG1 . VAL   D  1 245 ? 37.004  41.890  -34.264  1.00 49.40  ? 546  VAL   D CG1 1 
ATOM   12187 C  CG2 . VAL   D  1 245 ? 36.043  42.097  -31.959  1.00 38.23  ? 546  VAL   D CG2 1 
ATOM   12188 N  N   . LEU   D  1 246 ? 39.196  38.766  -33.624  1.00 38.21  ? 547  LEU   D N   1 
ATOM   12189 C  CA  . LEU   D  1 246 ? 40.420  38.390  -34.312  1.00 40.76  ? 547  LEU   D CA  1 
ATOM   12190 C  C   . LEU   D  1 246 ? 40.437  39.021  -35.696  1.00 49.19  ? 547  LEU   D C   1 
ATOM   12191 O  O   . LEU   D  1 246 ? 39.432  38.988  -36.417  1.00 48.57  ? 547  LEU   D O   1 
ATOM   12192 C  CB  . LEU   D  1 246 ? 40.522  36.873  -34.424  1.00 38.28  ? 547  LEU   D CB  1 
ATOM   12193 C  CG  . LEU   D  1 246 ? 41.609  36.363  -35.359  1.00 35.77  ? 547  LEU   D CG  1 
ATOM   12194 C  CD1 . LEU   D  1 246 ? 42.946  36.799  -34.826  1.00 40.54  ? 547  LEU   D CD1 1 
ATOM   12195 C  CD2 . LEU   D  1 246 ? 41.560  34.863  -35.470  1.00 39.35  ? 547  LEU   D CD2 1 
ATOM   12196 N  N   . GLU   D  1 247 ? 41.578  39.592  -36.069  1.00 42.46  ? 548  GLU   D N   1 
ATOM   12197 C  CA  . GLU   D  1 247 ? 41.709  40.313  -37.320  1.00 38.18  ? 548  GLU   D CA  1 
ATOM   12198 C  C   . GLU   D  1 247 ? 43.005  39.909  -38.007  1.00 48.13  ? 548  GLU   D C   1 
ATOM   12199 O  O   . GLU   D  1 247 ? 43.983  39.526  -37.362  1.00 51.80  ? 548  GLU   D O   1 
ATOM   12200 C  CB  . GLU   D  1 247 ? 41.692  41.820  -37.102  1.00 33.14  ? 548  GLU   D CB  1 
ATOM   12201 C  CG  . GLU   D  1 247 ? 40.356  42.377  -36.691  1.00 31.27  ? 548  GLU   D CG  1 
ATOM   12202 C  CD  . GLU   D  1 247 ? 40.433  43.868  -36.418  1.00 41.72  ? 548  GLU   D CD  1 
ATOM   12203 O  OE1 . GLU   D  1 247 ? 41.425  44.323  -35.804  1.00 40.32  ? 548  GLU   D OE1 1 
ATOM   12204 O  OE2 . GLU   D  1 247 ? 39.519  44.604  -36.832  1.00 42.60  ? 548  GLU   D OE2 1 
ATOM   12205 N  N   . VAL   D  1 248 ? 43.011  40.011  -39.331  1.00 43.81  ? 549  VAL   D N   1 
ATOM   12206 C  CA  . VAL   D  1 248 ? 44.166  39.642  -40.136  1.00 48.11  ? 549  VAL   D CA  1 
ATOM   12207 C  C   . VAL   D  1 248 ? 44.633  40.868  -40.912  1.00 42.35  ? 549  VAL   D C   1 
ATOM   12208 O  O   . VAL   D  1 248 ? 43.886  41.394  -41.740  1.00 38.72  ? 549  VAL   D O   1 
ATOM   12209 C  CB  . VAL   D  1 248 ? 43.844  38.489  -41.099  1.00 41.60  ? 549  VAL   D CB  1 
ATOM   12210 C  CG1 . VAL   D  1 248 ? 45.069  38.131  -41.880  1.00 39.89  ? 549  VAL   D CG1 1 
ATOM   12211 C  CG2 . VAL   D  1 248 ? 43.288  37.284  -40.324  1.00 37.84  ? 549  VAL   D CG2 1 
ATOM   12212 N  N   . PRO   D  1 249 ? 45.838  41.369  -40.681  1.00 38.57  ? 550  PRO   D N   1 
ATOM   12213 C  CA  . PRO   D  1 249 ? 46.375  42.396  -41.576  1.00 45.97  ? 550  PRO   D CA  1 
ATOM   12214 C  C   . PRO   D  1 249 ? 46.702  41.755  -42.912  1.00 56.44  ? 550  PRO   D C   1 
ATOM   12215 O  O   . PRO   D  1 249 ? 47.192  40.625  -42.962  1.00 62.06  ? 550  PRO   D O   1 
ATOM   12216 C  CB  . PRO   D  1 249 ? 47.641  42.877  -40.857  1.00 33.84  ? 550  PRO   D CB  1 
ATOM   12217 C  CG  . PRO   D  1 249 ? 48.089  41.666  -40.070  1.00 41.67  ? 550  PRO   D CG  1 
ATOM   12218 C  CD  . PRO   D  1 249 ? 46.829  40.913  -39.680  1.00 42.04  ? 550  PRO   D CD  1 
ATOM   12219 N  N   . ILE   D  1 250 ? 46.414  42.467  -43.998  1.00 57.82  ? 551  ILE   D N   1 
ATOM   12220 C  CA  . ILE   D  1 250 ? 46.542  41.907  -45.345  1.00 50.53  ? 551  ILE   D CA  1 
ATOM   12221 C  C   . ILE   D  1 250 ? 47.837  42.411  -45.963  1.00 43.12  ? 551  ILE   D C   1 
ATOM   12222 O  O   . ILE   D  1 250 ? 48.004  43.620  -46.174  1.00 50.13  ? 551  ILE   D O   1 
ATOM   12223 C  CB  . ILE   D  1 250 ? 45.326  42.245  -46.225  1.00 41.79  ? 551  ILE   D CB  1 
ATOM   12224 C  CG1 . ILE   D  1 250 ? 44.033  41.886  -45.489  1.00 40.87  ? 551  ILE   D CG1 1 
ATOM   12225 C  CG2 . ILE   D  1 250 ? 45.386  41.482  -47.530  1.00 42.57  ? 551  ILE   D CG2 1 
ATOM   12226 C  CD1 . ILE   D  1 250 ? 43.991  40.460  -44.967  1.00 31.50  ? 551  ILE   D CD1 1 
ATOM   12227 N  N   . ARG   D  1 251 ? 48.767  41.484  -46.209  1.00 43.11  ? 552  ARG   D N   1 
ATOM   12228 C  CA  . ARG   D  1 251 ? 49.990  41.745  -46.958  1.00 52.54  ? 552  ARG   D CA  1 
ATOM   12229 C  C   . ARG   D  1 251 ? 50.097  40.763  -48.124  1.00 50.52  ? 552  ARG   D C   1 
ATOM   12230 O  O   . ARG   D  1 251 ? 49.328  39.807  -48.231  1.00 50.97  ? 552  ARG   D O   1 
ATOM   12231 C  CB  . ARG   D  1 251 ? 51.224  41.640  -46.066  1.00 51.85  ? 552  ARG   D CB  1 
ATOM   12232 C  CG  . ARG   D  1 251 ? 51.412  40.285  -45.424  1.00 57.42  ? 552  ARG   D CG  1 
ATOM   12233 C  CD  . ARG   D  1 251 ? 50.842  40.262  -44.006  1.00 53.52  ? 552  ARG   D CD  1 
ATOM   12234 N  NE  . ARG   D  1 251 ? 51.040  38.966  -43.376  1.00 55.60  ? 552  ARG   D NE  1 
ATOM   12235 C  CZ  . ARG   D  1 251 ? 50.276  38.493  -42.401  1.00 59.64  ? 552  ARG   D CZ  1 
ATOM   12236 N  NH1 . ARG   D  1 251 ? 50.516  37.296  -41.897  1.00 63.83  ? 552  ARG   D NH1 1 
ATOM   12237 N  NH2 . ARG   D  1 251 ? 49.268  39.214  -41.941  1.00 59.30  ? 552  ARG   D NH2 1 
ATOM   12238 N  N   . HIS   D  1 252 ? 51.068  40.998  -49.005  1.00 52.83  ? 553  HIS   D N   1 
ATOM   12239 C  CA  . HIS   D  1 252 ? 51.190  40.218  -50.230  1.00 57.14  ? 553  HIS   D CA  1 
ATOM   12240 C  C   . HIS   D  1 252 ? 52.557  39.547  -50.280  1.00 61.75  ? 553  HIS   D C   1 
ATOM   12241 O  O   . HIS   D  1 252 ? 53.543  40.137  -49.829  1.00 70.03  ? 553  HIS   D O   1 
ATOM   12242 C  CB  . HIS   D  1 252 ? 51.006  41.122  -51.460  1.00 54.65  ? 553  HIS   D CB  1 
ATOM   12243 C  CG  . HIS   D  1 252 ? 50.825  40.386  -52.751  1.00 53.86  ? 553  HIS   D CG  1 
ATOM   12244 N  ND1 . HIS   D  1 252 ? 51.883  39.904  -53.491  1.00 56.11  ? 553  HIS   D ND1 1 
ATOM   12245 C  CD2 . HIS   D  1 252 ? 49.711  40.093  -53.460  1.00 51.06  ? 553  HIS   D CD2 1 
ATOM   12246 C  CE1 . HIS   D  1 252 ? 51.427  39.317  -54.584  1.00 47.49  ? 553  HIS   D CE1 1 
ATOM   12247 N  NE2 . HIS   D  1 252 ? 50.111  39.416  -54.586  1.00 53.49  ? 553  HIS   D NE2 1 
ATOM   12248 N  N   . PRO   D  1 253 ? 52.652  38.317  -50.803  1.00 60.22  ? 554  PRO   D N   1 
ATOM   12249 C  CA  . PRO   D  1 253 ? 53.947  37.606  -50.766  1.00 57.41  ? 554  PRO   D CA  1 
ATOM   12250 C  C   . PRO   D  1 253 ? 55.004  38.217  -51.655  1.00 61.35  ? 554  PRO   D C   1 
ATOM   12251 O  O   . PRO   D  1 253 ? 56.188  38.178  -51.300  1.00 75.86  ? 554  PRO   D O   1 
ATOM   12252 C  CB  . PRO   D  1 253 ? 53.596  36.185  -51.228  1.00 45.61  ? 554  PRO   D CB  1 
ATOM   12253 C  CG  . PRO   D  1 253 ? 52.282  36.313  -51.919  1.00 47.25  ? 554  PRO   D CG  1 
ATOM   12254 C  CD  . PRO   D  1 253 ? 51.554  37.456  -51.269  1.00 48.03  ? 554  PRO   D CD  1 
ATOM   12255 N  N   . LYS   D  1 254 ? 54.621  38.774  -52.798  1.00 65.99  ? 555  LYS   D N   1 
ATOM   12256 C  CA  . LYS   D  1 254 ? 55.565  39.345  -53.749  1.00 71.77  ? 555  LYS   D CA  1 
ATOM   12257 C  C   . LYS   D  1 254 ? 55.711  40.847  -53.591  1.00 64.85  ? 555  LYS   D C   1 
ATOM   12258 O  O   . LYS   D  1 254 ? 56.826  41.370  -53.681  1.00 67.85  ? 555  LYS   D O   1 
ATOM   12259 C  CB  . LYS   D  1 254 ? 55.120  39.044  -55.190  1.00 88.05  ? 555  LYS   D CB  1 
ATOM   12260 C  CG  . LYS   D  1 254 ? 54.503  37.667  -55.404  1.00 96.64  ? 555  LYS   D CG  1 
ATOM   12261 C  CD  . LYS   D  1 254 ? 55.551  36.572  -55.319  1.00 101.30 ? 555  LYS   D CD  1 
ATOM   12262 C  CE  . LYS   D  1 254 ? 54.942  35.212  -55.617  1.00 103.25 ? 555  LYS   D CE  1 
ATOM   12263 N  NZ  . LYS   D  1 254 ? 55.979  34.148  -55.694  1.00 107.14 ? 555  LYS   D NZ  1 
ATOM   12264 N  N   . PHE   D  1 255 ? 54.609  41.556  -53.362  1.00 60.98  ? 556  PHE   D N   1 
ATOM   12265 C  CA  . PHE   D  1 255 ? 54.611  43.014  -53.351  1.00 66.34  ? 556  PHE   D CA  1 
ATOM   12266 C  C   . PHE   D  1 255 ? 54.733  43.475  -51.901  1.00 72.54  ? 556  PHE   D C   1 
ATOM   12267 O  O   . PHE   D  1 255 ? 53.811  43.288  -51.095  1.00 74.93  ? 556  PHE   D O   1 
ATOM   12268 C  CB  . PHE   D  1 255 ? 53.352  43.586  -54.013  1.00 70.52  ? 556  PHE   D CB  1 
ATOM   12269 C  CG  . PHE   D  1 255 ? 53.093  43.078  -55.416  1.00 68.60  ? 556  PHE   D CG  1 
ATOM   12270 C  CD1 . PHE   D  1 255 ? 51.815  43.100  -55.945  1.00 59.57  ? 556  PHE   D CD1 1 
ATOM   12271 C  CD2 . PHE   D  1 255 ? 54.116  42.580  -56.195  1.00 78.38  ? 556  PHE   D CD2 1 
ATOM   12272 C  CE1 . PHE   D  1 255 ? 51.568  42.635  -57.207  1.00 58.85  ? 556  PHE   D CE1 1 
ATOM   12273 C  CE2 . PHE   D  1 255 ? 53.866  42.109  -57.467  1.00 76.68  ? 556  PHE   D CE2 1 
ATOM   12274 C  CZ  . PHE   D  1 255 ? 52.592  42.143  -57.970  1.00 68.81  ? 556  PHE   D CZ  1 
ATOM   12275 N  N   . GLU   D  1 256 ? 55.875  44.066  -51.566  1.00 72.42  ? 557  GLU   D N   1 
ATOM   12276 C  CA  . GLU   D  1 256 ? 56.060  44.585  -50.226  1.00 68.39  ? 557  GLU   D CA  1 
ATOM   12277 C  C   . GLU   D  1 256 ? 55.285  45.876  -50.001  1.00 71.08  ? 557  GLU   D C   1 
ATOM   12278 O  O   . GLU   D  1 256 ? 54.947  46.187  -48.858  1.00 83.79  ? 557  GLU   D O   1 
ATOM   12279 C  CB  . GLU   D  1 256 ? 57.543  44.796  -49.965  1.00 81.74  ? 557  GLU   D CB  1 
ATOM   12280 C  CG  . GLU   D  1 256 ? 58.410  43.770  -50.665  1.00 96.39  ? 557  GLU   D CG  1 
ATOM   12281 C  CD  . GLU   D  1 256 ? 59.528  44.414  -51.457  1.00 115.12 ? 557  GLU   D CD  1 
ATOM   12282 O  OE1 . GLU   D  1 256 ? 60.159  45.352  -50.923  1.00 126.08 ? 557  GLU   D OE1 1 
ATOM   12283 O  OE2 . GLU   D  1 256 ? 59.768  43.998  -52.613  1.00 116.43 ? 557  GLU   D OE2 1 
ATOM   12284 N  N   . TRP   D  1 257 ? 54.979  46.628  -51.061  1.00 70.49  ? 558  TRP   D N   1 
ATOM   12285 C  CA  . TRP   D  1 257 ? 54.159  47.823  -50.893  1.00 65.58  ? 558  TRP   D CA  1 
ATOM   12286 C  C   . TRP   D  1 257 ? 52.758  47.504  -50.411  1.00 67.76  ? 558  TRP   D C   1 
ATOM   12287 O  O   . TRP   D  1 257 ? 52.024  48.431  -50.053  1.00 74.39  ? 558  TRP   D O   1 
ATOM   12288 C  CB  . TRP   D  1 257 ? 54.058  48.625  -52.203  1.00 70.99  ? 558  TRP   D CB  1 
ATOM   12289 C  CG  . TRP   D  1 257 ? 53.712  47.830  -53.452  1.00 62.00  ? 558  TRP   D CG  1 
ATOM   12290 C  CD1 . TRP   D  1 257 ? 54.596  47.301  -54.352  1.00 66.18  ? 558  TRP   D CD1 1 
ATOM   12291 C  CD2 . TRP   D  1 257 ? 52.404  47.507  -53.946  1.00 67.90  ? 558  TRP   D CD2 1 
ATOM   12292 N  NE1 . TRP   D  1 257 ? 53.924  46.651  -55.359  1.00 73.77  ? 558  TRP   D NE1 1 
ATOM   12293 C  CE2 . TRP   D  1 257 ? 52.576  46.765  -55.138  1.00 71.75  ? 558  TRP   D CE2 1 
ATOM   12294 C  CE3 . TRP   D  1 257 ? 51.105  47.765  -53.498  1.00 68.20  ? 558  TRP   D CE3 1 
ATOM   12295 C  CZ2 . TRP   D  1 257 ? 51.497  46.284  -55.888  1.00 62.08  ? 558  TRP   D CZ2 1 
ATOM   12296 C  CZ3 . TRP   D  1 257 ? 50.031  47.274  -54.244  1.00 63.47  ? 558  TRP   D CZ3 1 
ATOM   12297 C  CH2 . TRP   D  1 257 ? 50.238  46.541  -55.421  1.00 57.19  ? 558  TRP   D CH2 1 
ATOM   12298 N  N   . PHE   D  1 258 ? 52.368  46.229  -50.384  1.00 61.07  ? 559  PHE   D N   1 
ATOM   12299 C  CA  . PHE   D  1 258 ? 50.963  45.909  -50.162  1.00 58.46  ? 559  PHE   D CA  1 
ATOM   12300 C  C   . PHE   D  1 258 ? 50.531  46.255  -48.748  1.00 64.33  ? 559  PHE   D C   1 
ATOM   12301 O  O   . PHE   D  1 258 ? 49.443  46.811  -48.549  1.00 61.30  ? 559  PHE   D O   1 
ATOM   12302 C  CB  . PHE   D  1 258 ? 50.698  44.440  -50.445  1.00 52.26  ? 559  PHE   D CB  1 
ATOM   12303 C  CG  . PHE   D  1 258 ? 49.292  44.171  -50.872  1.00 54.05  ? 559  PHE   D CG  1 
ATOM   12304 C  CD1 . PHE   D  1 258 ? 48.989  43.973  -52.213  1.00 56.90  ? 559  PHE   D CD1 1 
ATOM   12305 C  CD2 . PHE   D  1 258 ? 48.262  44.157  -49.943  1.00 54.10  ? 559  PHE   D CD2 1 
ATOM   12306 C  CE1 . PHE   D  1 258 ? 47.693  43.738  -52.613  1.00 53.72  ? 559  PHE   D CE1 1 
ATOM   12307 C  CE2 . PHE   D  1 258 ? 46.960  43.926  -50.333  1.00 52.37  ? 559  PHE   D CE2 1 
ATOM   12308 C  CZ  . PHE   D  1 258 ? 46.675  43.721  -51.673  1.00 54.06  ? 559  PHE   D CZ  1 
ATOM   12309 N  N   . LYS   D  1 259 ? 51.371  45.931  -47.758  1.00 59.48  ? 560  LYS   D N   1 
ATOM   12310 C  CA  . LYS   D  1 259 ? 51.074  46.285  -46.372  1.00 62.95  ? 560  LYS   D CA  1 
ATOM   12311 C  C   . LYS   D  1 259 ? 50.842  47.786  -46.200  1.00 62.72  ? 560  LYS   D C   1 
ATOM   12312 O  O   . LYS   D  1 259 ? 50.122  48.201  -45.281  1.00 64.96  ? 560  LYS   D O   1 
ATOM   12313 C  CB  . LYS   D  1 259 ? 52.201  45.807  -45.443  1.00 56.03  ? 560  LYS   D CB  1 
ATOM   12314 C  CG  . LYS   D  1 259 ? 53.601  46.212  -45.864  1.00 51.37  ? 560  LYS   D CG  1 
ATOM   12315 C  CD  . LYS   D  1 259 ? 54.602  46.023  -44.719  1.00 67.97  ? 560  LYS   D CD  1 
ATOM   12316 C  CE  . LYS   D  1 259 ? 55.954  46.689  -45.036  1.00 72.48  ? 560  LYS   D CE  1 
ATOM   12317 N  NZ  . LYS   D  1 259 ? 56.581  46.170  -46.288  1.00 72.01  ? 560  LYS   D NZ  1 
ATOM   12318 N  N   . ASP   D  1 260 ? 51.427  48.610  -47.073  1.00 59.77  ? 561  ASP   D N   1 
ATOM   12319 C  CA  . ASP   D  1 260 ? 51.254  50.053  -46.971  1.00 59.32  ? 561  ASP   D CA  1 
ATOM   12320 C  C   . ASP   D  1 260 ? 49.848  50.499  -47.342  1.00 53.79  ? 561  ASP   D C   1 
ATOM   12321 O  O   . ASP   D  1 260 ? 49.500  51.668  -47.134  1.00 52.21  ? 561  ASP   D O   1 
ATOM   12322 C  CB  . ASP   D  1 260 ? 52.278  50.776  -47.853  1.00 68.96  ? 561  ASP   D CB  1 
ATOM   12323 C  CG  . ASP   D  1 260 ? 53.699  50.277  -47.632  1.00 78.48  ? 561  ASP   D CG  1 
ATOM   12324 O  OD1 . ASP   D  1 260 ? 53.900  49.477  -46.694  1.00 87.41  ? 561  ASP   D OD1 1 
ATOM   12325 O  OD2 . ASP   D  1 260 ? 54.612  50.679  -48.396  1.00 78.42  ? 561  ASP   D OD2 1 
ATOM   12326 N  N   . LEU   D  1 261 ? 49.027  49.615  -47.896  1.00 52.14  ? 562  LEU   D N   1 
ATOM   12327 C  CA  . LEU   D  1 261 ? 47.655  50.018  -48.131  1.00 52.23  ? 562  LEU   D CA  1 
ATOM   12328 C  C   . LEU   D  1 261 ? 46.897  50.189  -46.820  1.00 61.93  ? 562  LEU   D C   1 
ATOM   12329 O  O   . LEU   D  1 261 ? 45.900  50.917  -46.781  1.00 63.57  ? 562  LEU   D O   1 
ATOM   12330 C  CB  . LEU   D  1 261 ? 46.987  49.004  -49.058  1.00 47.74  ? 562  LEU   D CB  1 
ATOM   12331 C  CG  . LEU   D  1 261 ? 47.840  48.775  -50.305  1.00 50.99  ? 562  LEU   D CG  1 
ATOM   12332 C  CD1 . LEU   D  1 261 ? 47.383  47.550  -51.059  1.00 58.12  ? 562  LEU   D CD1 1 
ATOM   12333 C  CD2 . LEU   D  1 261 ? 47.795  49.988  -51.211  1.00 54.56  ? 562  LEU   D CD2 1 
ATOM   12334 N  N   . GLY   D  1 262 ? 47.379  49.573  -45.739  1.00 64.78  ? 563  GLY   D N   1 
ATOM   12335 C  CA  . GLY   D  1 262 ? 46.753  49.694  -44.438  1.00 60.80  ? 563  GLY   D CA  1 
ATOM   12336 C  C   . GLY   D  1 262 ? 45.576  48.777  -44.234  1.00 62.70  ? 563  GLY   D C   1 
ATOM   12337 O  O   . GLY   D  1 262 ? 44.777  48.998  -43.321  1.00 62.96  ? 563  GLY   D O   1 
ATOM   12338 N  N   . LEU   D  1 263 ? 45.438  47.750  -45.058  1.00 59.56  ? 564  LEU   D N   1 
ATOM   12339 C  CA  . LEU   D  1 263 ? 44.235  46.945  -45.027  1.00 57.08  ? 564  LEU   D CA  1 
ATOM   12340 C  C   . LEU   D  1 263 ? 44.338  45.822  -43.999  1.00 53.84  ? 564  LEU   D C   1 
ATOM   12341 O  O   . LEU   D  1 263 ? 45.430  45.326  -43.678  1.00 38.84  ? 564  LEU   D O   1 
ATOM   12342 C  CB  . LEU   D  1 263 ? 43.942  46.365  -46.410  1.00 51.41  ? 564  LEU   D CB  1 
ATOM   12343 C  CG  . LEU   D  1 263 ? 43.853  47.373  -47.563  1.00 57.26  ? 564  LEU   D CG  1 
ATOM   12344 C  CD1 . LEU   D  1 263 ? 43.890  46.647  -48.912  1.00 43.55  ? 564  LEU   D CD1 1 
ATOM   12345 C  CD2 . LEU   D  1 263 ? 42.623  48.278  -47.458  1.00 58.15  ? 564  LEU   D CD2 1 
ATOM   12346 N  N   . LYS   D  1 264 ? 43.168  45.430  -43.496  1.00 49.70  ? 565  LYS   D N   1 
ATOM   12347 C  CA  . LYS   D  1 264 ? 42.984  44.286  -42.613  1.00 45.41  ? 565  LYS   D CA  1 
ATOM   12348 C  C   . LYS   D  1 264 ? 41.534  43.843  -42.749  1.00 51.83  ? 565  LYS   D C   1 
ATOM   12349 O  O   . LYS   D  1 264 ? 40.701  44.547  -43.326  1.00 62.02  ? 565  LYS   D O   1 
ATOM   12350 C  CB  . LYS   D  1 264 ? 43.320  44.629  -41.160  1.00 46.01  ? 565  LYS   D CB  1 
ATOM   12351 C  CG  . LYS   D  1 264 ? 42.419  45.699  -40.516  1.00 45.52  ? 565  LYS   D CG  1 
ATOM   12352 C  CD  . LYS   D  1 264 ? 42.777  45.835  -39.048  1.00 50.04  ? 565  LYS   D CD  1 
ATOM   12353 C  CE  . LYS   D  1 264 ? 42.356  47.154  -38.417  1.00 56.68  ? 565  LYS   D CE  1 
ATOM   12354 N  NZ  . LYS   D  1 264 ? 42.618  47.081  -36.930  1.00 63.62  ? 565  LYS   D NZ  1 
ATOM   12355 N  N   . TRP   D  1 265 ? 41.239  42.653  -42.232  1.00 45.33  ? 566  TRP   D N   1 
ATOM   12356 C  CA  . TRP   D  1 265 ? 39.861  42.181  -42.221  1.00 49.39  ? 566  TRP   D CA  1 
ATOM   12357 C  C   . TRP   D  1 265 ? 39.640  41.347  -40.961  1.00 58.95  ? 566  TRP   D C   1 
ATOM   12358 O  O   . TRP   D  1 265 ? 40.575  40.750  -40.413  1.00 68.51  ? 566  TRP   D O   1 
ATOM   12359 C  CB  . TRP   D  1 265 ? 39.511  41.391  -43.510  1.00 34.53  ? 566  TRP   D CB  1 
ATOM   12360 C  CG  . TRP   D  1 265 ? 38.032  41.358  -43.783  1.00 29.61  ? 566  TRP   D CG  1 
ATOM   12361 C  CD1 . TRP   D  1 265 ? 37.200  40.271  -43.705  1.00 29.23  ? 566  TRP   D CD1 1 
ATOM   12362 C  CD2 . TRP   D  1 265 ? 37.196  42.474  -44.117  1.00 30.49  ? 566  TRP   D CD2 1 
ATOM   12363 N  NE1 . TRP   D  1 265 ? 35.891  40.645  -43.981  1.00 26.73  ? 566  TRP   D NE1 1 
ATOM   12364 C  CE2 . TRP   D  1 265 ? 35.868  41.990  -44.242  1.00 30.45  ? 566  TRP   D CE2 1 
ATOM   12365 C  CE3 . TRP   D  1 265 ? 37.445  43.828  -44.357  1.00 35.45  ? 566  TRP   D CE3 1 
ATOM   12366 C  CZ2 . TRP   D  1 265 ? 34.801  42.812  -44.596  1.00 38.38  ? 566  TRP   D CZ2 1 
ATOM   12367 C  CZ3 . TRP   D  1 265 ? 36.376  44.652  -44.706  1.00 40.65  ? 566  TRP   D CZ3 1 
ATOM   12368 C  CH2 . TRP   D  1 265 ? 35.068  44.138  -44.816  1.00 45.94  ? 566  TRP   D CH2 1 
ATOM   12369 N  N   . TYR   D  1 266 ? 38.404  41.351  -40.473  1.00 44.75  ? 567  TYR   D N   1 
ATOM   12370 C  CA  . TYR   D  1 266 ? 38.063  40.473  -39.369  1.00 36.72  ? 567  TYR   D CA  1 
ATOM   12371 C  C   . TYR   D  1 266 ? 38.010  39.032  -39.853  1.00 41.65  ? 567  TYR   D C   1 
ATOM   12372 O  O   . TYR   D  1 266 ? 37.755  38.768  -41.022  1.00 52.84  ? 567  TYR   D O   1 
ATOM   12373 C  CB  . TYR   D  1 266 ? 36.728  40.876  -38.777  1.00 36.46  ? 567  TYR   D CB  1 
ATOM   12374 C  CG  . TYR   D  1 266 ? 35.621  40.956  -39.778  1.00 39.03  ? 567  TYR   D CG  1 
ATOM   12375 C  CD1 . TYR   D  1 266 ? 34.864  39.841  -40.081  1.00 50.37  ? 567  TYR   D CD1 1 
ATOM   12376 C  CD2 . TYR   D  1 266 ? 35.317  42.147  -40.412  1.00 36.82  ? 567  TYR   D CD2 1 
ATOM   12377 C  CE1 . TYR   D  1 266 ? 33.840  39.900  -40.997  1.00 43.45  ? 567  TYR   D CE1 1 
ATOM   12378 C  CE2 . TYR   D  1 266 ? 34.287  42.218  -41.329  1.00 41.01  ? 567  TYR   D CE2 1 
ATOM   12379 C  CZ  . TYR   D  1 266 ? 33.557  41.085  -41.620  1.00 45.81  ? 567  TYR   D CZ  1 
ATOM   12380 O  OH  . TYR   D  1 266 ? 32.527  41.125  -42.527  1.00 59.39  ? 567  TYR   D OH  1 
ATOM   12381 N  N   . GLY   D  1 267 ? 38.254  38.094  -38.946  1.00 44.33  ? 568  GLY   D N   1 
ATOM   12382 C  CA  . GLY   D  1 267 ? 38.410  36.710  -39.329  1.00 31.54  ? 568  GLY   D CA  1 
ATOM   12383 C  C   . GLY   D  1 267 ? 37.158  35.869  -39.273  1.00 34.66  ? 568  GLY   D C   1 
ATOM   12384 O  O   . GLY   D  1 267 ? 37.180  34.703  -39.670  1.00 40.39  ? 568  GLY   D O   1 
ATOM   12385 N  N   . LEU   D  1 268 ? 36.047  36.412  -38.794  1.00 33.95  ? 569  LEU   D N   1 
ATOM   12386 C  CA  . LEU   D  1 268 ? 34.915  35.595  -38.365  1.00 40.34  ? 569  LEU   D CA  1 
ATOM   12387 C  C   . LEU   D  1 268 ? 33.651  36.086  -39.055  1.00 48.43  ? 569  LEU   D C   1 
ATOM   12388 O  O   . LEU   D  1 268 ? 33.074  37.108  -38.643  1.00 53.54  ? 569  LEU   D O   1 
ATOM   12389 C  CB  . LEU   D  1 268 ? 34.752  35.637  -36.843  1.00 36.05  ? 569  LEU   D CB  1 
ATOM   12390 C  CG  . LEU   D  1 268 ? 33.523  34.831  -36.412  1.00 39.00  ? 569  LEU   D CG  1 
ATOM   12391 C  CD1 . LEU   D  1 268 ? 33.756  33.327  -36.525  1.00 38.78  ? 569  LEU   D CD1 1 
ATOM   12392 C  CD2 . LEU   D  1 268 ? 33.038  35.217  -35.029  1.00 32.40  ? 569  LEU   D CD2 1 
ATOM   12393 N  N   . PRO   D  1 269 ? 33.187  35.400  -40.101  1.00 39.88  ? 570  PRO   D N   1 
ATOM   12394 C  CA  . PRO   D  1 269 ? 31.949  35.824  -40.767  1.00 26.89  ? 570  PRO   D CA  1 
ATOM   12395 C  C   . PRO   D  1 269 ? 30.765  35.292  -39.981  1.00 29.84  ? 570  PRO   D C   1 
ATOM   12396 O  O   . PRO   D  1 269 ? 30.626  34.080  -39.803  1.00 32.39  ? 570  PRO   D O   1 
ATOM   12397 C  CB  . PRO   D  1 269 ? 32.043  35.159  -42.139  1.00 32.47  ? 570  PRO   D CB  1 
ATOM   12398 C  CG  . PRO   D  1 269 ? 32.836  33.864  -41.851  1.00 39.91  ? 570  PRO   D CG  1 
ATOM   12399 C  CD  . PRO   D  1 269 ? 33.794  34.206  -40.726  1.00 38.13  ? 570  PRO   D CD  1 
ATOM   12400 N  N   . ALA   D  1 270 ? 29.892  36.188  -39.527  1.00 32.31  ? 571  ALA   D N   1 
ATOM   12401 C  CA  . ALA   D  1 270 ? 28.794  35.770  -38.655  1.00 36.10  ? 571  ALA   D CA  1 
ATOM   12402 C  C   . ALA   D  1 270 ? 27.531  36.532  -39.039  1.00 37.93  ? 571  ALA   D C   1 
ATOM   12403 O  O   . ALA   D  1 270 ? 27.361  37.686  -38.638  1.00 49.35  ? 571  ALA   D O   1 
ATOM   12404 C  CB  . ALA   D  1 270 ? 29.169  35.991  -37.191  1.00 29.26  ? 571  ALA   D CB  1 
ATOM   12405 N  N   . VAL   D  1 271 ? 26.642  35.877  -39.790  1.00 33.67  ? 572  VAL   D N   1 
ATOM   12406 C  CA  . VAL   D  1 271 ? 25.404  36.504  -40.242  1.00 31.13  ? 572  VAL   D CA  1 
ATOM   12407 C  C   . VAL   D  1 271 ? 24.422  36.537  -39.088  1.00 28.01  ? 572  VAL   D C   1 
ATOM   12408 O  O   . VAL   D  1 271 ? 24.123  35.501  -38.487  1.00 37.97  ? 572  VAL   D O   1 
ATOM   12409 C  CB  . VAL   D  1 271 ? 24.798  35.740  -41.436  1.00 35.07  ? 572  VAL   D CB  1 
ATOM   12410 C  CG1 . VAL   D  1 271 ? 23.397  36.248  -41.727  1.00 25.54  ? 572  VAL   D CG1 1 
ATOM   12411 C  CG2 . VAL   D  1 271 ? 25.645  35.892  -42.646  1.00 29.15  ? 572  VAL   D CG2 1 
ATOM   12412 N  N   . SER   D  1 272 ? 23.864  37.708  -38.820  1.00 25.08  ? 573  SER   D N   1 
ATOM   12413 C  CA  . SER   D  1 272 ? 22.993  37.871  -37.674  1.00 34.64  ? 573  SER   D CA  1 
ATOM   12414 C  C   . SER   D  1 272 ? 21.610  38.413  -37.994  1.00 48.18  ? 573  SER   D C   1 
ATOM   12415 O  O   . SER   D  1 272 ? 20.796  38.562  -37.069  1.00 44.62  ? 573  SER   D O   1 
ATOM   12416 C  CB  . SER   D  1 272 ? 23.662  38.785  -36.640  1.00 36.49  ? 573  SER   D CB  1 
ATOM   12417 O  OG  . SER   D  1 272 ? 24.106  39.996  -37.218  1.00 37.30  ? 573  SER   D OG  1 
ATOM   12418 N  N   . ASN   D  1 273 ? 21.312  38.715  -39.257  1.00 44.02  ? 574  ASN   D N   1 
ATOM   12419 C  CA  . ASN   D  1 273 ? 20.088  39.426  -39.601  1.00 36.63  ? 574  ASN   D CA  1 
ATOM   12420 C  C   . ASN   D  1 273 ? 19.019  38.539  -40.215  1.00 39.15  ? 574  ASN   D C   1 
ATOM   12421 O  O   . ASN   D  1 273 ? 17.953  39.048  -40.567  1.00 46.96  ? 574  ASN   D O   1 
ATOM   12422 C  CB  . ASN   D  1 273 ? 20.391  40.575  -40.559  1.00 32.59  ? 574  ASN   D CB  1 
ATOM   12423 C  CG  . ASN   D  1 273 ? 21.036  40.097  -41.849  1.00 43.54  ? 574  ASN   D CG  1 
ATOM   12424 O  OD1 . ASN   D  1 273 ? 21.153  38.892  -42.099  1.00 51.12  ? 574  ASN   D OD1 1 
ATOM   12425 N  ND2 . ASN   D  1 273 ? 21.477  41.040  -42.670  1.00 37.36  ? 574  ASN   D ND2 1 
ATOM   12426 N  N   . MET   D  1 274 ? 19.258  37.239  -40.347  1.00 35.61  ? 575  MET   D N   1 
ATOM   12427 C  CA  . MET   D  1 274 ? 18.301  36.360  -41.001  1.00 36.15  ? 575  MET   D CA  1 
ATOM   12428 C  C   . MET   D  1 274 ? 17.319  35.778  -39.995  1.00 46.89  ? 575  MET   D C   1 
ATOM   12429 O  O   . MET   D  1 274 ? 17.254  36.201  -38.838  1.00 60.60  ? 575  MET   D O   1 
ATOM   12430 C  CB  . MET   D  1 274 ? 19.044  35.291  -41.781  1.00 32.91  ? 575  MET   D CB  1 
ATOM   12431 C  CG  . MET   D  1 274 ? 19.604  35.895  -43.068  1.00 43.23  ? 575  MET   D CG  1 
ATOM   12432 S  SD  . MET   D  1 274 ? 20.477  34.726  -44.071  1.00 47.82  ? 575  MET   D SD  1 
ATOM   12433 C  CE  . MET   D  1 274 ? 19.103  33.834  -44.756  1.00 44.77  ? 575  MET   D CE  1 
ATOM   12434 N  N   . LEU   D  1 275 ? 16.515  34.817  -40.435  1.00 40.69  ? 576  LEU   D N   1 
ATOM   12435 C  CA  . LEU   D  1 275 ? 15.469  34.272  -39.587  1.00 33.99  ? 576  LEU   D CA  1 
ATOM   12436 C  C   . LEU   D  1 275 ? 15.448  32.778  -39.801  1.00 40.20  ? 576  LEU   D C   1 
ATOM   12437 O  O   . LEU   D  1 275 ? 15.538  32.323  -40.937  1.00 56.73  ? 576  LEU   D O   1 
ATOM   12438 C  CB  . LEU   D  1 275 ? 14.106  34.887  -39.905  1.00 40.33  ? 576  LEU   D CB  1 
ATOM   12439 C  CG  . LEU   D  1 275 ? 12.972  34.617  -38.912  1.00 41.52  ? 576  LEU   D CG  1 
ATOM   12440 C  CD1 . LEU   D  1 275 ? 12.071  35.832  -38.784  1.00 38.20  ? 576  LEU   D CD1 1 
ATOM   12441 C  CD2 . LEU   D  1 275 ? 12.147  33.425  -39.337  1.00 41.81  ? 576  LEU   D CD2 1 
ATOM   12442 N  N   . LEU   D  1 276 ? 15.363  32.021  -38.714  1.00 45.67  ? 577  LEU   D N   1 
ATOM   12443 C  CA  . LEU   D  1 276 ? 15.446  30.568  -38.755  1.00 38.30  ? 577  LEU   D CA  1 
ATOM   12444 C  C   . LEU   D  1 276 ? 14.047  30.009  -38.560  1.00 51.67  ? 577  LEU   D C   1 
ATOM   12445 O  O   . LEU   D  1 276 ? 13.370  30.359  -37.585  1.00 53.02  ? 577  LEU   D O   1 
ATOM   12446 C  CB  . LEU   D  1 276 ? 16.391  30.053  -37.677  1.00 38.66  ? 577  LEU   D CB  1 
ATOM   12447 C  CG  . LEU   D  1 276 ? 16.373  28.547  -37.393  1.00 39.37  ? 577  LEU   D CG  1 
ATOM   12448 C  CD1 . LEU   D  1 276 ? 17.008  27.806  -38.543  1.00 24.27  ? 577  LEU   D CD1 1 
ATOM   12449 C  CD2 . LEU   D  1 276 ? 17.089  28.205  -36.059  1.00 29.29  ? 577  LEU   D CD2 1 
ATOM   12450 N  N   . GLU   D  1 277 ? 13.608  29.152  -39.489  1.00 46.71  ? 578  GLU   D N   1 
ATOM   12451 C  CA  . GLU   D  1 277 ? 12.251  28.612  -39.475  1.00 38.30  ? 578  GLU   D CA  1 
ATOM   12452 C  C   . GLU   D  1 277 ? 12.341  27.117  -39.229  1.00 41.30  ? 578  GLU   D C   1 
ATOM   12453 O  O   . GLU   D  1 277 ? 12.864  26.379  -40.069  1.00 40.36  ? 578  GLU   D O   1 
ATOM   12454 C  CB  . GLU   D  1 277 ? 11.522  28.908  -40.778  1.00 38.13  ? 578  GLU   D CB  1 
ATOM   12455 C  CG  . GLU   D  1 277 ? 10.014  28.793  -40.703  1.00 45.99  ? 578  GLU   D CG  1 
ATOM   12456 C  CD  . GLU   D  1 277 ? 9.473   27.426  -41.116  1.00 64.28  ? 578  GLU   D CD  1 
ATOM   12457 O  OE1 . GLU   D  1 277 ? 10.184  26.415  -40.971  1.00 70.28  ? 578  GLU   D OE1 1 
ATOM   12458 O  OE2 . GLU   D  1 277 ? 8.317   27.355  -41.588  1.00 71.42  ? 578  GLU   D OE2 1 
ATOM   12459 N  N   . ILE   D  1 278 ? 11.815  26.672  -38.089  1.00 42.21  ? 579  ILE   D N   1 
ATOM   12460 C  CA  . ILE   D  1 278 ? 11.755  25.257  -37.734  1.00 39.38  ? 579  ILE   D CA  1 
ATOM   12461 C  C   . ILE   D  1 278 ? 10.323  24.945  -37.313  1.00 42.04  ? 579  ILE   D C   1 
ATOM   12462 O  O   . ILE   D  1 278 ? 9.825   25.520  -36.339  1.00 42.61  ? 579  ILE   D O   1 
ATOM   12463 C  CB  . ILE   D  1 278 ? 12.746  24.899  -36.609  1.00 30.08  ? 579  ILE   D CB  1 
ATOM   12464 C  CG1 . ILE   D  1 278 ? 14.124  25.497  -36.901  1.00 37.65  ? 579  ILE   D CG1 1 
ATOM   12465 C  CG2 . ILE   D  1 278 ? 12.891  23.408  -36.500  1.00 34.35  ? 579  ILE   D CG2 1 
ATOM   12466 C  CD1 . ILE   D  1 278 ? 15.177  25.225  -35.870  1.00 37.22  ? 579  ILE   D CD1 1 
ATOM   12467 N  N   . GLY   D  1 279 ? 9.657   24.062  -38.057  1.00 41.40  ? 580  GLY   D N   1 
ATOM   12468 C  CA  . GLY   D  1 279 ? 8.338   23.589  -37.668  1.00 33.06  ? 580  GLY   D CA  1 
ATOM   12469 C  C   . GLY   D  1 279 ? 7.289   24.673  -37.556  1.00 47.78  ? 580  GLY   D C   1 
ATOM   12470 O  O   . GLY   D  1 279 ? 6.362   24.556  -36.745  1.00 55.58  ? 580  GLY   D O   1 
ATOM   12471 N  N   . GLY   D  1 280 ? 7.392   25.720  -38.364  1.00 54.79  ? 581  GLY   D N   1 
ATOM   12472 C  CA  . GLY   D  1 280 ? 6.511   26.854  -38.226  1.00 52.84  ? 581  GLY   D CA  1 
ATOM   12473 C  C   . GLY   D  1 280 ? 6.971   27.872  -37.214  1.00 50.69  ? 581  GLY   D C   1 
ATOM   12474 O  O   . GLY   D  1 280 ? 6.429   28.981  -37.182  1.00 60.80  ? 581  GLY   D O   1 
ATOM   12475 N  N   . LEU   D  1 281 ? 7.957   27.547  -36.393  1.00 42.88  ? 582  LEU   D N   1 
ATOM   12476 C  CA  . LEU   D  1 281 ? 8.435   28.496  -35.405  1.00 44.92  ? 582  LEU   D CA  1 
ATOM   12477 C  C   . LEU   D  1 281 ? 9.480   29.410  -36.035  1.00 52.45  ? 582  LEU   D C   1 
ATOM   12478 O  O   . LEU   D  1 281 ? 10.321  28.970  -36.822  1.00 61.01  ? 582  LEU   D O   1 
ATOM   12479 C  CB  . LEU   D  1 281 ? 9.011   27.752  -34.198  1.00 47.68  ? 582  LEU   D CB  1 
ATOM   12480 C  CG  . LEU   D  1 281 ? 8.014   26.843  -33.474  1.00 42.43  ? 582  LEU   D CG  1 
ATOM   12481 C  CD1 . LEU   D  1 281 ? 8.726   26.036  -32.441  1.00 46.15  ? 582  LEU   D CD1 1 
ATOM   12482 C  CD2 . LEU   D  1 281 ? 6.916   27.650  -32.839  1.00 44.17  ? 582  LEU   D CD2 1 
ATOM   12483 N  N   . GLU   D  1 282 ? 9.424   30.687  -35.685  1.00 50.55  ? 583  GLU   D N   1 
ATOM   12484 C  CA  . GLU   D  1 282 ? 10.303  31.695  -36.260  1.00 50.93  ? 583  GLU   D CA  1 
ATOM   12485 C  C   . GLU   D  1 282 ? 11.281  32.206  -35.204  1.00 54.78  ? 583  GLU   D C   1 
ATOM   12486 O  O   . GLU   D  1 282 ? 10.868  32.828  -34.216  1.00 49.09  ? 583  GLU   D O   1 
ATOM   12487 C  CB  . GLU   D  1 282 ? 9.478   32.844  -36.836  1.00 46.13  ? 583  GLU   D CB  1 
ATOM   12488 C  CG  . GLU   D  1 282 ? 8.429   32.396  -37.846  1.00 49.29  ? 583  GLU   D CG  1 
ATOM   12489 C  CD  . GLU   D  1 282 ? 7.673   33.563  -38.430  1.00 51.42  ? 583  GLU   D CD  1 
ATOM   12490 O  OE1 . GLU   D  1 282 ? 7.650   33.686  -39.676  1.00 65.54  ? 583  GLU   D OE1 1 
ATOM   12491 O  OE2 . GLU   D  1 282 ? 7.114   34.369  -37.641  1.00 44.19  ? 583  GLU   D OE2 1 
ATOM   12492 N  N   . PHE   D  1 283 ? 12.575  31.968  -35.431  1.00 44.34  ? 584  PHE   D N   1 
ATOM   12493 C  CA  . PHE   D  1 283 ? 13.638  32.448  -34.552  1.00 24.35  ? 584  PHE   D CA  1 
ATOM   12494 C  C   . PHE   D  1 283 ? 14.260  33.706  -35.167  1.00 29.77  ? 584  PHE   D C   1 
ATOM   12495 O  O   . PHE   D  1 283 ? 15.249  33.650  -35.903  1.00 34.31  ? 584  PHE   D O   1 
ATOM   12496 C  CB  . PHE   D  1 283 ? 14.647  31.330  -34.314  1.00 26.21  ? 584  PHE   D CB  1 
ATOM   12497 C  CG  . PHE   D  1 283 ? 14.054  30.153  -33.570  1.00 38.71  ? 584  PHE   D CG  1 
ATOM   12498 C  CD1 . PHE   D  1 283 ? 13.648  29.012  -34.246  1.00 30.58  ? 584  PHE   D CD1 1 
ATOM   12499 C  CD2 . PHE   D  1 283 ? 13.857  30.215  -32.190  1.00 40.79  ? 584  PHE   D CD2 1 
ATOM   12500 C  CE1 . PHE   D  1 283 ? 13.058  27.940  -33.567  1.00 33.06  ? 584  PHE   D CE1 1 
ATOM   12501 C  CE2 . PHE   D  1 283 ? 13.280  29.140  -31.496  1.00 39.97  ? 584  PHE   D CE2 1 
ATOM   12502 C  CZ  . PHE   D  1 283 ? 12.886  28.000  -32.183  1.00 33.75  ? 584  PHE   D CZ  1 
ATOM   12503 N  N   . SER   D  1 284 ? 13.675  34.863  -34.849  1.00 27.38  ? 585  SER   D N   1 
ATOM   12504 C  CA  . SER   D  1 284 ? 14.081  36.116  -35.493  1.00 34.70  ? 585  SER   D CA  1 
ATOM   12505 C  C   . SER   D  1 284 ? 15.495  36.559  -35.139  1.00 34.41  ? 585  SER   D C   1 
ATOM   12506 O  O   . SER   D  1 284 ? 15.987  37.536  -35.714  1.00 34.20  ? 585  SER   D O   1 
ATOM   12507 C  CB  . SER   D  1 284 ? 13.104  37.245  -35.137  1.00 29.89  ? 585  SER   D CB  1 
ATOM   12508 O  OG  . SER   D  1 284 ? 12.753  37.210  -33.765  1.00 40.80  ? 585  SER   D OG  1 
ATOM   12509 N  N   . ALA   D  1 285 ? 16.156  35.911  -34.194  1.00 39.61  ? 586  ALA   D N   1 
ATOM   12510 C  CA  . ALA   D  1 285 ? 17.512  36.313  -33.845  1.00 36.93  ? 586  ALA   D CA  1 
ATOM   12511 C  C   . ALA   D  1 285 ? 18.295  35.044  -33.573  1.00 43.73  ? 586  ALA   D C   1 
ATOM   12512 O  O   . ALA   D  1 285 ? 18.101  34.411  -32.528  1.00 44.88  ? 586  ALA   D O   1 
ATOM   12513 C  CB  . ALA   D  1 285 ? 17.522  37.261  -32.655  1.00 31.23  ? 586  ALA   D CB  1 
ATOM   12514 N  N   . CYS   D  1 286 ? 19.172  34.680  -34.529  1.00 32.52  ? 587  CYS   D N   1 
ATOM   12515 C  CA  . CYS   D  1 286 ? 19.814  33.375  -34.608  1.00 33.07  ? 587  CYS   D CA  1 
ATOM   12516 C  C   . CYS   D  1 286 ? 21.230  33.417  -35.172  1.00 37.26  ? 587  CYS   D C   1 
ATOM   12517 O  O   . CYS   D  1 286 ? 21.561  32.575  -36.018  1.00 47.85  ? 587  CYS   D O   1 
ATOM   12518 C  CB  . CYS   D  1 286 ? 18.972  32.454  -35.492  1.00 35.60  ? 587  CYS   D CB  1 
ATOM   12519 S  SG  . CYS   D  1 286 ? 18.690  33.130  -37.199  1.00 41.73  ? 587  CYS   D SG  1 
ATOM   12520 N  N   . PRO   D  1 287 ? 22.098  34.331  -34.722  1.00 34.69  ? 588  PRO   D N   1 
ATOM   12521 C  CA  . PRO   D  1 287 ? 23.381  34.537  -35.412  1.00 26.59  ? 588  PRO   D CA  1 
ATOM   12522 C  C   . PRO   D  1 287 ? 24.134  33.236  -35.624  1.00 30.74  ? 588  PRO   D C   1 
ATOM   12523 O  O   . PRO   D  1 287 ? 24.167  32.370  -34.749  1.00 44.27  ? 588  PRO   D O   1 
ATOM   12524 C  CB  . PRO   D  1 287 ? 24.147  35.481  -34.478  1.00 21.62  ? 588  PRO   D CB  1 
ATOM   12525 C  CG  . PRO   D  1 287 ? 23.437  35.454  -33.205  1.00 43.85  ? 588  PRO   D CG  1 
ATOM   12526 C  CD  . PRO   D  1 287 ? 22.006  35.132  -33.493  1.00 44.56  ? 588  PRO   D CD  1 
ATOM   12527 N  N   . PHE   D  1 288 ? 24.727  33.093  -36.812  1.00 33.42  ? 589  PHE   D N   1 
ATOM   12528 C  CA  . PHE   D  1 288 ? 25.508  31.908  -37.160  1.00 30.50  ? 589  PHE   D CA  1 
ATOM   12529 C  C   . PHE   D  1 288 ? 26.798  32.328  -37.843  1.00 33.59  ? 589  PHE   D C   1 
ATOM   12530 O  O   . PHE   D  1 288 ? 26.920  33.439  -38.370  1.00 35.48  ? 589  PHE   D O   1 
ATOM   12531 C  CB  . PHE   D  1 288 ? 24.732  30.929  -38.069  1.00 46.50  ? 589  PHE   D CB  1 
ATOM   12532 C  CG  . PHE   D  1 288 ? 24.181  31.556  -39.323  1.00 48.83  ? 589  PHE   D CG  1 
ATOM   12533 C  CD1 . PHE   D  1 288 ? 24.925  31.570  -40.493  1.00 44.02  ? 589  PHE   D CD1 1 
ATOM   12534 C  CD2 . PHE   D  1 288 ? 22.915  32.127  -39.331  1.00 51.40  ? 589  PHE   D CD2 1 
ATOM   12535 C  CE1 . PHE   D  1 288 ? 24.417  32.143  -41.642  1.00 42.25  ? 589  PHE   D CE1 1 
ATOM   12536 C  CE2 . PHE   D  1 288 ? 22.401  32.704  -40.492  1.00 42.96  ? 589  PHE   D CE2 1 
ATOM   12537 C  CZ  . PHE   D  1 288 ? 23.158  32.713  -41.639  1.00 35.51  ? 589  PHE   D CZ  1 
ATOM   12538 N  N   . SER   D  1 289 ? 27.760  31.410  -37.848  1.00 27.34  ? 590  SER   D N   1 
ATOM   12539 C  CA  . SER   D  1 289 ? 29.090  31.761  -38.308  1.00 30.90  ? 590  SER   D CA  1 
ATOM   12540 C  C   . SER   D  1 289 ? 29.829  30.502  -38.731  1.00 43.12  ? 590  SER   D C   1 
ATOM   12541 O  O   . SER   D  1 289 ? 29.595  29.419  -38.187  1.00 48.64  ? 590  SER   D O   1 
ATOM   12542 C  CB  . SER   D  1 289 ? 29.866  32.470  -37.201  1.00 38.75  ? 590  SER   D CB  1 
ATOM   12543 O  OG  . SER   D  1 289 ? 30.083  31.545  -36.164  1.00 44.32  ? 590  SER   D OG  1 
ATOM   12544 N  N   . GLY   D  1 290 ? 30.736  30.666  -39.696  1.00 42.05  ? 591  GLY   D N   1 
ATOM   12545 C  CA  . GLY   D  1 290 ? 31.656  29.609  -40.071  1.00 38.80  ? 591  GLY   D CA  1 
ATOM   12546 C  C   . GLY   D  1 290 ? 33.049  30.151  -40.319  1.00 44.74  ? 591  GLY   D C   1 
ATOM   12547 O  O   . GLY   D  1 290 ? 33.706  30.630  -39.392  1.00 61.89  ? 591  GLY   D O   1 
ATOM   12548 N  N   . TRP   D  1 291 ? 33.515  30.087  -41.563  1.00 35.84  ? 592  TRP   D N   1 
ATOM   12549 C  CA  . TRP   D  1 291 ? 34.783  30.696  -41.936  1.00 40.36  ? 592  TRP   D CA  1 
ATOM   12550 C  C   . TRP   D  1 291 ? 34.707  31.146  -43.392  1.00 46.10  ? 592  TRP   D C   1 
ATOM   12551 O  O   . TRP   D  1 291 ? 33.862  30.685  -44.165  1.00 36.45  ? 592  TRP   D O   1 
ATOM   12552 C  CB  . TRP   D  1 291 ? 35.965  29.735  -41.722  1.00 43.67  ? 592  TRP   D CB  1 
ATOM   12553 C  CG  . TRP   D  1 291 ? 35.838  28.449  -42.469  1.00 49.13  ? 592  TRP   D CG  1 
ATOM   12554 C  CD1 . TRP   D  1 291 ? 36.069  28.236  -43.811  1.00 53.72  ? 592  TRP   D CD1 1 
ATOM   12555 C  CD2 . TRP   D  1 291 ? 35.440  27.195  -41.927  1.00 47.41  ? 592  TRP   D CD2 1 
ATOM   12556 N  NE1 . TRP   D  1 291 ? 35.835  26.918  -44.125  1.00 51.28  ? 592  TRP   D NE1 1 
ATOM   12557 C  CE2 . TRP   D  1 291 ? 35.445  26.261  -42.983  1.00 54.53  ? 592  TRP   D CE2 1 
ATOM   12558 C  CE3 . TRP   D  1 291 ? 35.064  26.770  -40.651  1.00 48.73  ? 592  TRP   D CE3 1 
ATOM   12559 C  CZ2 . TRP   D  1 291 ? 35.095  24.932  -42.795  1.00 58.94  ? 592  TRP   D CZ2 1 
ATOM   12560 C  CZ3 . TRP   D  1 291 ? 34.737  25.456  -40.465  1.00 44.43  ? 592  TRP   D CZ3 1 
ATOM   12561 C  CH2 . TRP   D  1 291 ? 34.749  24.548  -41.527  1.00 57.90  ? 592  TRP   D CH2 1 
ATOM   12562 N  N   . TYR   D  1 292 ? 35.632  32.031  -43.759  1.00 46.26  ? 593  TYR   D N   1 
ATOM   12563 C  CA  . TYR   D  1 292 ? 35.578  32.753  -45.024  1.00 41.09  ? 593  TYR   D CA  1 
ATOM   12564 C  C   . TYR   D  1 292 ? 36.113  31.946  -46.198  1.00 41.29  ? 593  TYR   D C   1 
ATOM   12565 O  O   . TYR   D  1 292 ? 37.120  31.234  -46.087  1.00 46.10  ? 593  TYR   D O   1 
ATOM   12566 C  CB  . TYR   D  1 292 ? 36.405  34.034  -44.934  1.00 43.40  ? 593  TYR   D CB  1 
ATOM   12567 C  CG  . TYR   D  1 292 ? 35.636  35.273  -44.567  1.00 49.72  ? 593  TYR   D CG  1 
ATOM   12568 C  CD1 . TYR   D  1 292 ? 35.962  36.026  -43.426  1.00 43.67  ? 593  TYR   D CD1 1 
ATOM   12569 C  CD2 . TYR   D  1 292 ? 34.583  35.703  -45.361  1.00 39.93  ? 593  TYR   D CD2 1 
ATOM   12570 C  CE1 . TYR   D  1 292 ? 35.264  37.190  -43.113  1.00 40.46  ? 593  TYR   D CE1 1 
ATOM   12571 C  CE2 . TYR   D  1 292 ? 33.870  36.839  -45.040  1.00 45.04  ? 593  TYR   D CE2 1 
ATOM   12572 C  CZ  . TYR   D  1 292 ? 34.212  37.580  -43.927  1.00 43.64  ? 593  TYR   D CZ  1 
ATOM   12573 O  OH  . TYR   D  1 292 ? 33.490  38.712  -43.659  1.00 54.82  ? 593  TYR   D OH  1 
ATOM   12574 N  N   . MET   D  1 293 ? 35.448  32.109  -47.338  1.00 38.10  ? 594  MET   D N   1 
ATOM   12575 C  CA  . MET   D  1 293 ? 36.066  31.890  -48.636  1.00 29.21  ? 594  MET   D CA  1 
ATOM   12576 C  C   . MET   D  1 293 ? 36.774  33.167  -49.046  1.00 31.31  ? 594  MET   D C   1 
ATOM   12577 O  O   . MET   D  1 293 ? 36.249  34.264  -48.848  1.00 32.11  ? 594  MET   D O   1 
ATOM   12578 C  CB  . MET   D  1 293 ? 35.009  31.526  -49.667  1.00 36.37  ? 594  MET   D CB  1 
ATOM   12579 C  CG  . MET   D  1 293 ? 35.531  31.103  -51.019  1.00 37.21  ? 594  MET   D CG  1 
ATOM   12580 S  SD  . MET   D  1 293 ? 34.160  30.310  -51.859  1.00 43.80  ? 594  MET   D SD  1 
ATOM   12581 C  CE  . MET   D  1 293 ? 33.205  31.775  -52.255  1.00 38.34  ? 594  MET   D CE  1 
ATOM   12582 N  N   . GLY   D  1 294 ? 37.970  33.027  -49.605  1.00 36.92  ? 595  GLY   D N   1 
ATOM   12583 C  CA  . GLY   D  1 294 ? 38.779  34.201  -49.923  1.00 46.98  ? 595  GLY   D CA  1 
ATOM   12584 C  C   . GLY   D  1 294 ? 38.057  35.262  -50.737  1.00 54.55  ? 595  GLY   D C   1 
ATOM   12585 O  O   . GLY   D  1 294 ? 38.190  36.458  -50.458  1.00 59.17  ? 595  GLY   D O   1 
ATOM   12586 N  N   . THR   D  1 295 ? 37.263  34.840  -51.741  1.00 45.68  ? 596  THR   D N   1 
ATOM   12587 C  CA  . THR   D  1 295 ? 36.659  35.776  -52.698  1.00 42.46  ? 596  THR   D CA  1 
ATOM   12588 C  C   . THR   D  1 295 ? 35.717  36.767  -52.039  1.00 40.65  ? 596  THR   D C   1 
ATOM   12589 O  O   . THR   D  1 295 ? 35.494  37.852  -52.588  1.00 45.72  ? 596  THR   D O   1 
ATOM   12590 C  CB  . THR   D  1 295 ? 35.854  35.053  -53.793  1.00 41.95  ? 596  THR   D CB  1 
ATOM   12591 O  OG1 . THR   D  1 295 ? 34.818  34.238  -53.204  1.00 36.13  ? 596  THR   D OG1 1 
ATOM   12592 C  CG2 . THR   D  1 295 ? 36.765  34.251  -54.760  1.00 26.22  ? 596  THR   D CG2 1 
ATOM   12593 N  N   . GLU   D  1 296 ? 35.102  36.397  -50.910  1.00 42.56  ? 597  GLU   D N   1 
ATOM   12594 C  CA  . GLU   D  1 296 ? 34.164  37.298  -50.243  1.00 34.64  ? 597  GLU   D CA  1 
ATOM   12595 C  C   . GLU   D  1 296 ? 34.845  38.591  -49.820  1.00 42.01  ? 597  GLU   D C   1 
ATOM   12596 O  O   . GLU   D  1 296 ? 34.272  39.673  -49.966  1.00 48.99  ? 597  GLU   D O   1 
ATOM   12597 C  CB  . GLU   D  1 296 ? 33.562  36.635  -49.013  1.00 45.51  ? 597  GLU   D CB  1 
ATOM   12598 C  CG  . GLU   D  1 296 ? 32.975  35.290  -49.237  1.00 49.74  ? 597  GLU   D CG  1 
ATOM   12599 C  CD  . GLU   D  1 296 ? 32.219  34.826  -48.026  1.00 48.69  ? 597  GLU   D CD  1 
ATOM   12600 O  OE1 . GLU   D  1 296 ? 31.395  35.616  -47.516  1.00 54.26  ? 597  GLU   D OE1 1 
ATOM   12601 O  OE2 . GLU   D  1 296 ? 32.453  33.689  -47.576  1.00 46.63  ? 597  GLU   D OE2 1 
ATOM   12602 N  N   . ILE   D  1 297 ? 36.038  38.490  -49.225  1.00 46.78  ? 598  ILE   D N   1 
ATOM   12603 C  CA  . ILE   D  1 297 ? 36.788  39.675  -48.815  1.00 46.42  ? 598  ILE   D CA  1 
ATOM   12604 C  C   . ILE   D  1 297 ? 37.443  40.310  -50.024  1.00 43.69  ? 598  ILE   D C   1 
ATOM   12605 O  O   . ILE   D  1 297 ? 37.296  41.514  -50.279  1.00 42.51  ? 598  ILE   D O   1 
ATOM   12606 C  CB  . ILE   D  1 297 ? 37.861  39.321  -47.757  1.00 41.29  ? 598  ILE   D CB  1 
ATOM   12607 C  CG1 . ILE   D  1 297 ? 37.280  38.625  -46.531  1.00 41.89  ? 598  ILE   D CG1 1 
ATOM   12608 C  CG2 . ILE   D  1 297 ? 38.680  40.557  -47.359  1.00 30.54  ? 598  ILE   D CG2 1 
ATOM   12609 C  CD1 . ILE   D  1 297 ? 38.194  37.532  -45.980  1.00 35.92  ? 598  ILE   D CD1 1 
ATOM   12610 N  N   . GLY   D  1 298 ? 38.182  39.493  -50.778  1.00 51.54  ? 599  GLY   D N   1 
ATOM   12611 C  CA  . GLY   D  1 298 ? 39.059  39.982  -51.828  1.00 65.18  ? 599  GLY   D CA  1 
ATOM   12612 C  C   . GLY   D  1 298 ? 38.362  40.446  -53.092  1.00 60.17  ? 599  GLY   D C   1 
ATOM   12613 O  O   . GLY   D  1 298 ? 38.940  41.243  -53.832  1.00 71.44  ? 599  GLY   D O   1 
ATOM   12614 N  N   . VAL   D  1 299 ? 37.147  39.973  -53.364  1.00 53.57  ? 600  VAL   D N   1 
ATOM   12615 C  CA  . VAL   D  1 299 ? 36.399  40.366  -54.557  1.00 53.02  ? 600  VAL   D CA  1 
ATOM   12616 C  C   . VAL   D  1 299 ? 35.225  41.269  -54.206  1.00 52.60  ? 600  VAL   D C   1 
ATOM   12617 O  O   . VAL   D  1 299 ? 35.062  42.339  -54.793  1.00 48.15  ? 600  VAL   D O   1 
ATOM   12618 C  CB  . VAL   D  1 299 ? 35.929  39.130  -55.357  1.00 50.88  ? 600  VAL   D CB  1 
ATOM   12619 C  CG1 . VAL   D  1 299 ? 35.316  39.541  -56.677  1.00 48.67  ? 600  VAL   D CG1 1 
ATOM   12620 C  CG2 . VAL   D  1 299 ? 37.083  38.181  -55.576  1.00 52.13  ? 600  VAL   D CG2 1 
ATOM   12621 N  N   . ARG   D  1 300 ? 34.412  40.870  -53.221  1.00 55.60  ? 601  ARG   D N   1 
ATOM   12622 C  CA  . ARG   D  1 300 ? 33.212  41.637  -52.901  1.00 52.68  ? 601  ARG   D CA  1 
ATOM   12623 C  C   . ARG   D  1 300 ? 33.489  42.801  -51.939  1.00 58.21  ? 601  ARG   D C   1 
ATOM   12624 O  O   . ARG   D  1 300 ? 33.141  43.950  -52.247  1.00 49.02  ? 601  ARG   D O   1 
ATOM   12625 C  CB  . ARG   D  1 300 ? 32.125  40.707  -52.344  1.00 41.18  ? 601  ARG   D CB  1 
ATOM   12626 C  CG  . ARG   D  1 300 ? 31.855  39.408  -53.172  1.00 33.58  ? 601  ARG   D CG  1 
ATOM   12627 C  CD  . ARG   D  1 300 ? 31.383  39.688  -54.637  1.00 46.35  ? 601  ARG   D CD  1 
ATOM   12628 N  NE  . ARG   D  1 300 ? 30.464  40.817  -54.688  1.00 37.27  ? 601  ARG   D NE  1 
ATOM   12629 C  CZ  . ARG   D  1 300 ? 29.169  40.704  -54.438  1.00 34.98  ? 601  ARG   D CZ  1 
ATOM   12630 N  NH1 . ARG   D  1 300 ? 28.642  39.505  -54.161  1.00 33.54  ? 601  ARG   D NH1 1 
ATOM   12631 N  NH2 . ARG   D  1 300 ? 28.403  41.778  -54.467  1.00 36.14  ? 601  ARG   D NH2 1 
ATOM   12632 N  N   . ASP   D  1 301 ? 34.141  42.526  -50.797  1.00 61.53  ? 602  ASP   D N   1 
ATOM   12633 C  CA  . ASP   D  1 301 ? 34.377  43.550  -49.771  1.00 59.84  ? 602  ASP   D CA  1 
ATOM   12634 C  C   . ASP   D  1 301 ? 35.284  44.663  -50.273  1.00 61.73  ? 602  ASP   D C   1 
ATOM   12635 O  O   . ASP   D  1 301 ? 34.950  45.854  -50.167  1.00 51.41  ? 602  ASP   D O   1 
ATOM   12636 C  CB  . ASP   D  1 301 ? 34.993  42.920  -48.520  1.00 50.09  ? 602  ASP   D CB  1 
ATOM   12637 C  CG  . ASP   D  1 301 ? 34.016  42.062  -47.773  1.00 51.40  ? 602  ASP   D CG  1 
ATOM   12638 O  OD1 . ASP   D  1 301 ? 32.842  42.466  -47.652  1.00 50.68  ? 602  ASP   D OD1 1 
ATOM   12639 O  OD2 . ASP   D  1 301 ? 34.418  40.976  -47.313  1.00 53.32  ? 602  ASP   D OD2 1 
ATOM   12640 N  N   . TYR   D  1 302 ? 36.457  44.295  -50.796  1.00 60.43  ? 603  TYR   D N   1 
ATOM   12641 C  CA  . TYR   D  1 302 ? 37.444  45.287  -51.204  1.00 66.47  ? 603  TYR   D CA  1 
ATOM   12642 C  C   . TYR   D  1 302 ? 37.213  45.865  -52.595  1.00 63.82  ? 603  TYR   D C   1 
ATOM   12643 O  O   . TYR   D  1 302 ? 37.760  46.937  -52.890  1.00 59.16  ? 603  TYR   D O   1 
ATOM   12644 C  CB  . TYR   D  1 302 ? 38.840  44.683  -51.171  1.00 69.44  ? 603  TYR   D CB  1 
ATOM   12645 C  CG  . TYR   D  1 302 ? 39.356  44.426  -49.793  1.00 60.74  ? 603  TYR   D CG  1 
ATOM   12646 C  CD1 . TYR   D  1 302 ? 40.376  43.514  -49.584  1.00 57.18  ? 603  TYR   D CD1 1 
ATOM   12647 C  CD2 . TYR   D  1 302 ? 38.829  45.094  -48.705  1.00 56.47  ? 603  TYR   D CD2 1 
ATOM   12648 C  CE1 . TYR   D  1 302 ? 40.856  43.271  -48.345  1.00 56.13  ? 603  TYR   D CE1 1 
ATOM   12649 C  CE2 . TYR   D  1 302 ? 39.312  44.865  -47.456  1.00 62.74  ? 603  TYR   D CE2 1 
ATOM   12650 C  CZ  . TYR   D  1 302 ? 40.331  43.947  -47.279  1.00 64.68  ? 603  TYR   D CZ  1 
ATOM   12651 O  OH  . TYR   D  1 302 ? 40.831  43.696  -46.028  1.00 69.10  ? 603  TYR   D OH  1 
ATOM   12652 N  N   . CYS   D  1 303 ? 36.426  45.196  -53.458  1.00 60.80  ? 604  CYS   D N   1 
ATOM   12653 C  CA  . CYS   D  1 303 ? 36.445  45.535  -54.876  1.00 56.90  ? 604  CYS   D CA  1 
ATOM   12654 C  C   . CYS   D  1 303 ? 35.121  45.998  -55.471  1.00 47.89  ? 604  CYS   D C   1 
ATOM   12655 O  O   . CYS   D  1 303 ? 35.159  46.806  -56.398  1.00 41.17  ? 604  CYS   D O   1 
ATOM   12656 C  CB  . CYS   D  1 303 ? 36.988  44.356  -55.680  1.00 53.81  ? 604  CYS   D CB  1 
ATOM   12657 S  SG  . CYS   D  1 303 ? 38.777  44.295  -55.569  1.00 54.99  ? 604  CYS   D SG  1 
ATOM   12658 N  N   . ASP   D  1 304 ? 33.966  45.545  -54.972  1.00 53.73  ? 605  ASP   D N   1 
ATOM   12659 C  CA  . ASP   D  1 304 ? 32.694  46.161  -55.357  1.00 53.70  ? 605  ASP   D CA  1 
ATOM   12660 C  C   . ASP   D  1 304 ? 32.802  47.683  -55.263  1.00 63.02  ? 605  ASP   D C   1 
ATOM   12661 O  O   . ASP   D  1 304 ? 33.435  48.215  -54.347  1.00 63.84  ? 605  ASP   D O   1 
ATOM   12662 C  CB  . ASP   D  1 304 ? 31.540  45.669  -54.458  1.00 40.26  ? 605  ASP   D CB  1 
ATOM   12663 C  CG  . ASP   D  1 304 ? 31.042  44.255  -54.810  1.00 50.72  ? 605  ASP   D CG  1 
ATOM   12664 O  OD1 . ASP   D  1 304 ? 31.727  43.503  -55.565  1.00 57.47  ? 605  ASP   D OD1 1 
ATOM   12665 O  OD2 . ASP   D  1 304 ? 29.936  43.904  -54.319  1.00 41.16  ? 605  ASP   D OD2 1 
ATOM   12666 N  N   . ASN   D  1 305 ? 32.194  48.384  -56.228  1.00 65.43  ? 606  ASN   D N   1 
ATOM   12667 C  CA  . ASN   D  1 305 ? 32.303  49.843  -56.250  1.00 73.01  ? 606  ASN   D CA  1 
ATOM   12668 C  C   . ASN   D  1 305 ? 31.568  50.476  -55.070  1.00 73.86  ? 606  ASN   D C   1 
ATOM   12669 O  O   . ASN   D  1 305 ? 32.055  51.449  -54.479  1.00 79.39  ? 606  ASN   D O   1 
ATOM   12670 C  CB  . ASN   D  1 305 ? 31.785  50.396  -57.582  1.00 87.75  ? 606  ASN   D CB  1 
ATOM   12671 C  CG  . ASN   D  1 305 ? 32.750  50.134  -58.753  1.00 97.73  ? 606  ASN   D CG  1 
ATOM   12672 O  OD1 . ASN   D  1 305 ? 33.755  50.836  -58.926  1.00 100.21 ? 606  ASN   D OD1 1 
ATOM   12673 N  ND2 . ASN   D  1 305 ? 32.432  49.129  -59.567  1.00 97.48  ? 606  ASN   D ND2 1 
ATOM   12674 N  N   . SER   D  1 306 ? 30.413  49.922  -54.690  1.00 71.02  ? 607  SER   D N   1 
ATOM   12675 C  CA  . SER   D  1 306 ? 29.680  50.387  -53.512  1.00 74.04  ? 607  SER   D CA  1 
ATOM   12676 C  C   . SER   D  1 306 ? 30.356  50.020  -52.191  1.00 76.93  ? 607  SER   D C   1 
ATOM   12677 O  O   . SER   D  1 306 ? 29.781  50.300  -51.134  1.00 77.86  ? 607  SER   D O   1 
ATOM   12678 C  CB  . SER   D  1 306 ? 28.252  49.821  -53.508  1.00 72.49  ? 607  SER   D CB  1 
ATOM   12679 O  OG  . SER   D  1 306 ? 27.507  50.250  -54.639  1.00 76.92  ? 607  SER   D OG  1 
ATOM   12680 N  N   . ARG   D  1 307 ? 31.534  49.391  -52.215  1.00 74.44  ? 608  ARG   D N   1 
ATOM   12681 C  CA  . ARG   D  1 307 ? 32.194  48.944  -50.991  1.00 69.54  ? 608  ARG   D CA  1 
ATOM   12682 C  C   . ARG   D  1 307 ? 33.568  49.599  -50.847  1.00 66.03  ? 608  ARG   D C   1 
ATOM   12683 O  O   . ARG   D  1 307 ? 33.688  50.821  -50.990  1.00 72.50  ? 608  ARG   D O   1 
ATOM   12684 C  CB  . ARG   D  1 307 ? 32.303  47.416  -50.971  1.00 60.85  ? 608  ARG   D CB  1 
ATOM   12685 C  CG  . ARG   D  1 307 ? 30.961  46.687  -51.076  1.00 50.41  ? 608  ARG   D CG  1 
ATOM   12686 C  CD  . ARG   D  1 307 ? 30.105  46.814  -49.800  1.00 55.29  ? 608  ARG   D CD  1 
ATOM   12687 N  NE  . ARG   D  1 307 ? 30.830  46.470  -48.577  1.00 53.42  ? 608  ARG   D NE  1 
ATOM   12688 C  CZ  . ARG   D  1 307 ? 31.237  45.240  -48.258  1.00 61.38  ? 608  ARG   D CZ  1 
ATOM   12689 N  NH1 . ARG   D  1 307 ? 31.006  44.220  -49.071  1.00 57.49  ? 608  ARG   D NH1 1 
ATOM   12690 N  NH2 . ARG   D  1 307 ? 31.891  45.020  -47.121  1.00 68.72  ? 608  ARG   D NH2 1 
ATOM   12691 N  N   . TYR   D  1 308 ? 34.616  48.812  -50.576  1.00 50.24  ? 609  TYR   D N   1 
ATOM   12692 C  CA  . TYR   D  1 308 ? 35.895  49.439  -50.254  1.00 55.73  ? 609  TYR   D CA  1 
ATOM   12693 C  C   . TYR   D  1 308 ? 36.653  49.935  -51.473  1.00 61.14  ? 609  TYR   D C   1 
ATOM   12694 O  O   . TYR   D  1 308 ? 37.542  50.779  -51.311  1.00 74.80  ? 609  TYR   D O   1 
ATOM   12695 C  CB  . TYR   D  1 308 ? 36.780  48.496  -49.446  1.00 61.31  ? 609  TYR   D CB  1 
ATOM   12696 C  CG  . TYR   D  1 308 ? 36.685  48.770  -47.956  1.00 62.19  ? 609  TYR   D CG  1 
ATOM   12697 C  CD1 . TYR   D  1 308 ? 35.753  48.107  -47.156  1.00 52.86  ? 609  TYR   D CD1 1 
ATOM   12698 C  CD2 . TYR   D  1 308 ? 37.511  49.709  -47.353  1.00 58.60  ? 609  TYR   D CD2 1 
ATOM   12699 C  CE1 . TYR   D  1 308 ? 35.666  48.363  -45.801  1.00 54.19  ? 609  TYR   D CE1 1 
ATOM   12700 C  CE2 . TYR   D  1 308 ? 37.429  49.967  -46.003  1.00 52.00  ? 609  TYR   D CE2 1 
ATOM   12701 C  CZ  . TYR   D  1 308 ? 36.502  49.296  -45.234  1.00 61.40  ? 609  TYR   D CZ  1 
ATOM   12702 O  OH  . TYR   D  1 308 ? 36.411  49.546  -43.885  1.00 72.32  ? 609  TYR   D OH  1 
ATOM   12703 N  N   . ASN   D  1 309 ? 36.352  49.405  -52.660  1.00 55.03  ? 610  ASN   D N   1 
ATOM   12704 C  CA  . ASN   D  1 309 ? 36.714  49.994  -53.960  1.00 61.81  ? 610  ASN   D CA  1 
ATOM   12705 C  C   . ASN   D  1 309 ? 38.198  50.379  -54.052  1.00 60.91  ? 610  ASN   D C   1 
ATOM   12706 O  O   . ASN   D  1 309 ? 38.568  51.524  -54.340  1.00 47.57  ? 610  ASN   D O   1 
ATOM   12707 C  CB  . ASN   D  1 309 ? 35.809  51.194  -54.270  1.00 58.92  ? 610  ASN   D CB  1 
ATOM   12708 C  CG  . ASN   D  1 309 ? 35.947  51.679  -55.703  1.00 59.77  ? 610  ASN   D CG  1 
ATOM   12709 O  OD1 . ASN   D  1 309 ? 36.295  50.908  -56.607  1.00 55.77  ? 610  ASN   D OD1 1 
ATOM   12710 N  ND2 . ASN   D  1 309 ? 35.696  52.966  -55.913  1.00 58.36  ? 610  ASN   D ND2 1 
ATOM   12711 N  N   . ILE   D  1 310 ? 39.056  49.376  -53.850  1.00 66.82  ? 611  ILE   D N   1 
ATOM   12712 C  CA  . ILE   D  1 310 ? 40.499  49.594  -53.800  1.00 73.51  ? 611  ILE   D CA  1 
ATOM   12713 C  C   . ILE   D  1 310 ? 41.189  49.187  -55.096  1.00 71.43  ? 611  ILE   D C   1 
ATOM   12714 O  O   . ILE   D  1 310 ? 42.416  49.050  -55.115  1.00 71.06  ? 611  ILE   D O   1 
ATOM   12715 C  CB  . ILE   D  1 310 ? 41.129  48.862  -52.608  1.00 73.13  ? 611  ILE   D CB  1 
ATOM   12716 C  CG1 . ILE   D  1 310 ? 40.856  47.366  -52.718  1.00 70.16  ? 611  ILE   D CG1 1 
ATOM   12717 C  CG2 . ILE   D  1 310 ? 40.581  49.404  -51.306  1.00 72.84  ? 611  ILE   D CG2 1 
ATOM   12718 C  CD1 . ILE   D  1 310 ? 41.848  46.529  -51.955  1.00 73.39  ? 611  ILE   D CD1 1 
ATOM   12719 N  N   . LEU   D  1 311 ? 40.435  48.997  -56.183  1.00 71.33  ? 612  LEU   D N   1 
ATOM   12720 C  CA  . LEU   D  1 311 ? 41.055  48.574  -57.435  1.00 60.87  ? 612  LEU   D CA  1 
ATOM   12721 C  C   . LEU   D  1 311 ? 41.933  49.677  -58.031  1.00 64.77  ? 612  LEU   D C   1 
ATOM   12722 O  O   . LEU   D  1 311 ? 43.063  49.413  -58.459  1.00 68.53  ? 612  LEU   D O   1 
ATOM   12723 C  CB  . LEU   D  1 311 ? 39.991  48.119  -58.440  1.00 49.71  ? 612  LEU   D CB  1 
ATOM   12724 C  CG  . LEU   D  1 311 ? 39.411  46.700  -58.349  1.00 49.29  ? 612  LEU   D CG  1 
ATOM   12725 C  CD1 . LEU   D  1 311 ? 38.209  46.580  -59.253  1.00 50.00  ? 612  LEU   D CD1 1 
ATOM   12726 C  CD2 . LEU   D  1 311 ? 40.421  45.620  -58.689  1.00 33.32  ? 612  LEU   D CD2 1 
ATOM   12727 N  N   . GLU   D  1 312 ? 41.435  50.920  -58.087  1.00 59.57  ? 613  GLU   D N   1 
ATOM   12728 C  CA  . GLU   D  1 312 ? 42.266  52.000  -58.619  1.00 69.94  ? 613  GLU   D CA  1 
ATOM   12729 C  C   . GLU   D  1 312 ? 43.570  52.112  -57.843  1.00 66.84  ? 613  GLU   D C   1 
ATOM   12730 O  O   . GLU   D  1 312 ? 44.646  52.252  -58.439  1.00 65.42  ? 613  GLU   D O   1 
ATOM   12731 C  CB  . GLU   D  1 312 ? 41.532  53.347  -58.586  1.00 84.72  ? 613  GLU   D CB  1 
ATOM   12732 C  CG  . GLU   D  1 312 ? 40.182  53.377  -59.272  1.00 91.26  ? 613  GLU   D CG  1 
ATOM   12733 C  CD  . GLU   D  1 312 ? 39.025  53.310  -58.277  1.00 94.63  ? 613  GLU   D CD  1 
ATOM   12734 O  OE1 . GLU   D  1 312 ? 38.116  54.161  -58.393  1.00 105.94 ? 613  GLU   D OE1 1 
ATOM   12735 O  OE2 . GLU   D  1 312 ? 39.029  52.424  -57.380  1.00 76.00  ? 613  GLU   D OE2 1 
ATOM   12736 N  N   . GLU   D  1 313 ? 43.503  52.028  -56.512  1.00 53.80  ? 614  GLU   D N   1 
ATOM   12737 C  CA  . GLU   D  1 313 ? 44.732  52.194  -55.750  1.00 68.11  ? 614  GLU   D CA  1 
ATOM   12738 C  C   . GLU   D  1 313 ? 45.684  51.035  -55.991  1.00 69.60  ? 614  GLU   D C   1 
ATOM   12739 O  O   . GLU   D  1 313 ? 46.893  51.243  -56.141  1.00 80.42  ? 614  GLU   D O   1 
ATOM   12740 C  CB  . GLU   D  1 313 ? 44.450  52.346  -54.254  1.00 71.12  ? 614  GLU   D CB  1 
ATOM   12741 C  CG  . GLU   D  1 313 ? 45.655  52.951  -53.529  1.00 81.16  ? 614  GLU   D CG  1 
ATOM   12742 C  CD  . GLU   D  1 313 ? 45.443  53.119  -52.052  1.00 87.59  ? 614  GLU   D CD  1 
ATOM   12743 O  OE1 . GLU   D  1 313 ? 46.338  52.714  -51.285  1.00 88.92  ? 614  GLU   D OE1 1 
ATOM   12744 O  OE2 . GLU   D  1 313 ? 44.387  53.656  -51.660  1.00 91.04  ? 614  GLU   D OE2 1 
ATOM   12745 N  N   . VAL   D  1 314 ? 45.168  49.810  -56.029  1.00 60.28  ? 615  VAL   D N   1 
ATOM   12746 C  CA  . VAL   D  1 314 ? 46.062  48.676  -56.213  1.00 56.85  ? 615  VAL   D CA  1 
ATOM   12747 C  C   . VAL   D  1 314 ? 46.643  48.688  -57.617  1.00 62.85  ? 615  VAL   D C   1 
ATOM   12748 O  O   . VAL   D  1 314 ? 47.838  48.440  -57.807  1.00 77.39  ? 615  VAL   D O   1 
ATOM   12749 C  CB  . VAL   D  1 314 ? 45.337  47.358  -55.899  1.00 59.23  ? 615  VAL   D CB  1 
ATOM   12750 C  CG1 . VAL   D  1 314 ? 46.204  46.179  -56.279  1.00 52.63  ? 615  VAL   D CG1 1 
ATOM   12751 C  CG2 . VAL   D  1 314 ? 44.997  47.285  -54.416  1.00 68.26  ? 615  VAL   D CG2 1 
ATOM   12752 N  N   . ALA   D  1 315 ? 45.828  49.018  -58.620  1.00 66.65  ? 616  ALA   D N   1 
ATOM   12753 C  CA  . ALA   D  1 315 ? 46.325  49.025  -59.992  1.00 56.01  ? 616  ALA   D CA  1 
ATOM   12754 C  C   . ALA   D  1 315 ? 47.368  50.114  -60.190  1.00 58.35  ? 616  ALA   D C   1 
ATOM   12755 O  O   . ALA   D  1 315 ? 48.344  49.919  -60.921  1.00 51.19  ? 616  ALA   D O   1 
ATOM   12756 C  CB  . ALA   D  1 315 ? 45.169  49.204  -60.975  1.00 56.33  ? 616  ALA   D CB  1 
ATOM   12757 N  N   . LYS   D  1 316 ? 47.186  51.272  -59.553  1.00 61.68  ? 617  LYS   D N   1 
ATOM   12758 C  CA  . LYS   D  1 316 ? 48.200  52.311  -59.667  1.00 62.14  ? 617  LYS   D CA  1 
ATOM   12759 C  C   . LYS   D  1 316 ? 49.518  51.800  -59.111  1.00 70.76  ? 617  LYS   D C   1 
ATOM   12760 O  O   . LYS   D  1 316 ? 50.527  51.755  -59.819  1.00 76.74  ? 617  LYS   D O   1 
ATOM   12761 C  CB  . LYS   D  1 316 ? 47.743  53.587  -58.956  1.00 55.73  ? 617  LYS   D CB  1 
ATOM   12762 C  CG  . LYS   D  1 316 ? 46.713  54.368  -59.742  1.00 64.26  ? 617  LYS   D CG  1 
ATOM   12763 C  CD  . LYS   D  1 316 ? 46.020  55.428  -58.908  1.00 76.62  ? 617  LYS   D CD  1 
ATOM   12764 C  CE  . LYS   D  1 316 ? 44.995  56.190  -59.749  1.00 84.02  ? 617  LYS   D CE  1 
ATOM   12765 N  NZ  . LYS   D  1 316 ? 44.391  57.325  -58.990  1.00 92.02  ? 617  LYS   D NZ  1 
ATOM   12766 N  N   . LYS   D  1 317 ? 49.499  51.322  -57.862  1.00 75.22  ? 618  LYS   D N   1 
ATOM   12767 C  CA  . LYS   D  1 317 ? 50.676  50.713  -57.250  1.00 73.79  ? 618  LYS   D CA  1 
ATOM   12768 C  C   . LYS   D  1 317 ? 51.207  49.524  -58.042  1.00 74.69  ? 618  LYS   D C   1 
ATOM   12769 O  O   . LYS   D  1 317 ? 52.314  49.056  -57.751  1.00 78.16  ? 618  LYS   D O   1 
ATOM   12770 C  CB  . LYS   D  1 317 ? 50.371  50.263  -55.817  1.00 66.41  ? 618  LYS   D CB  1 
ATOM   12771 C  CG  . LYS   D  1 317 ? 50.160  51.394  -54.816  1.00 66.41  ? 618  LYS   D CG  1 
ATOM   12772 C  CD  . LYS   D  1 317 ? 50.972  51.170  -53.563  1.00 64.57  ? 618  LYS   D CD  1 
ATOM   12773 C  CE  . LYS   D  1 317 ? 52.083  52.201  -53.429  1.00 76.06  ? 618  LYS   D CE  1 
ATOM   12774 N  NZ  . LYS   D  1 317 ? 51.532  53.585  -53.344  1.00 82.99  ? 618  LYS   D NZ  1 
ATOM   12775 N  N   . MET   D  1 318 ? 50.455  49.014  -59.022  1.00 67.13  ? 619  MET   D N   1 
ATOM   12776 C  CA  . MET   D  1 318 ? 50.962  47.961  -59.891  1.00 62.25  ? 619  MET   D CA  1 
ATOM   12777 C  C   . MET   D  1 318 ? 51.571  48.499  -61.175  1.00 66.39  ? 619  MET   D C   1 
ATOM   12778 O  O   . MET   D  1 318 ? 52.205  47.725  -61.894  1.00 78.63  ? 619  MET   D O   1 
ATOM   12779 C  CB  . MET   D  1 318 ? 49.861  46.933  -60.227  1.00 52.15  ? 619  MET   D CB  1 
ATOM   12780 C  CG  . MET   D  1 318 ? 49.466  46.031  -59.050  1.00 52.46  ? 619  MET   D CG  1 
ATOM   12781 S  SD  . MET   D  1 318 ? 48.352  44.625  -59.361  1.00 56.46  ? 619  MET   D SD  1 
ATOM   12782 C  CE  . MET   D  1 318 ? 49.322  43.740  -60.574  1.00 59.65  ? 619  MET   D CE  1 
ATOM   12783 N  N   . ASN   D  1 319 ? 51.432  49.806  -61.450  1.00 65.73  ? 620  ASN   D N   1 
ATOM   12784 C  CA  . ASN   D  1 319 ? 51.906  50.450  -62.693  1.00 66.60  ? 620  ASN   D CA  1 
ATOM   12785 C  C   . ASN   D  1 319 ? 51.107  49.986  -63.915  1.00 58.35  ? 620  ASN   D C   1 
ATOM   12786 O  O   . ASN   D  1 319 ? 51.667  49.730  -64.980  1.00 66.79  ? 620  ASN   D O   1 
ATOM   12787 C  CB  . ASN   D  1 319 ? 53.400  50.222  -62.923  1.00 73.94  ? 620  ASN   D CB  1 
ATOM   12788 C  CG  . ASN   D  1 319 ? 54.259  50.925  -61.907  1.00 88.25  ? 620  ASN   D CG  1 
ATOM   12789 O  OD1 . ASN   D  1 319 ? 54.061  52.108  -61.625  1.00 99.16  ? 620  ASN   D OD1 1 
ATOM   12790 N  ND2 . ASN   D  1 319 ? 55.231  50.202  -61.348  1.00 85.36  ? 620  ASN   D ND2 1 
ATOM   12791 N  N   . LEU   D  1 320 ? 49.793  49.886  -63.767  1.00 54.13  ? 621  LEU   D N   1 
ATOM   12792 C  CA  . LEU   D  1 320 ? 48.935  49.343  -64.804  1.00 65.25  ? 621  LEU   D CA  1 
ATOM   12793 C  C   . LEU   D  1 320 ? 48.365  50.465  -65.659  1.00 72.64  ? 621  LEU   D C   1 
ATOM   12794 O  O   . LEU   D  1 320 ? 48.206  51.603  -65.201  1.00 78.66  ? 621  LEU   D O   1 
ATOM   12795 C  CB  . LEU   D  1 320 ? 47.805  48.523  -64.187  1.00 58.18  ? 621  LEU   D CB  1 
ATOM   12796 C  CG  . LEU   D  1 320 ? 48.312  47.293  -63.441  1.00 56.77  ? 621  LEU   D CG  1 
ATOM   12797 C  CD1 . LEU   D  1 320 ? 47.158  46.377  -63.013  1.00 48.34  ? 621  LEU   D CD1 1 
ATOM   12798 C  CD2 . LEU   D  1 320 ? 49.346  46.558  -64.276  1.00 52.86  ? 621  LEU   D CD2 1 
ATOM   12799 N  N   . ASP   D  1 321 ? 48.067  50.136  -66.913  1.00 70.24  ? 622  ASP   D N   1 
ATOM   12800 C  CA  . ASP   D  1 321 ? 47.439  51.097  -67.809  1.00 72.32  ? 622  ASP   D CA  1 
ATOM   12801 C  C   . ASP   D  1 321 ? 45.949  51.079  -67.536  1.00 69.32  ? 622  ASP   D C   1 
ATOM   12802 O  O   . ASP   D  1 321 ? 45.266  50.104  -67.859  1.00 78.44  ? 622  ASP   D O   1 
ATOM   12803 C  CB  . ASP   D  1 321 ? 47.738  50.780  -69.270  1.00 85.13  ? 622  ASP   D CB  1 
ATOM   12804 C  CG  . ASP   D  1 321 ? 46.956  51.667  -70.225  1.00 93.84  ? 622  ASP   D CG  1 
ATOM   12805 O  OD1 . ASP   D  1 321 ? 46.425  51.142  -71.230  1.00 97.37  ? 622  ASP   D OD1 1 
ATOM   12806 O  OD2 . ASP   D  1 321 ? 46.850  52.883  -69.952  1.00 91.90  ? 622  ASP   D OD2 1 
ATOM   12807 N  N   . MET   D  1 322 ? 45.450  52.142  -66.912  1.00 70.79  ? 623  MET   D N   1 
ATOM   12808 C  CA  . MET   D  1 322 ? 44.040  52.261  -66.570  1.00 75.47  ? 623  MET   D CA  1 
ATOM   12809 C  C   . MET   D  1 322 ? 43.300  53.212  -67.507  1.00 83.37  ? 623  MET   D C   1 
ATOM   12810 O  O   . MET   D  1 322 ? 42.298  53.825  -67.118  1.00 90.53  ? 623  MET   D O   1 
ATOM   12811 C  CB  . MET   D  1 322 ? 43.907  52.690  -65.118  1.00 74.78  ? 623  MET   D CB  1 
ATOM   12812 C  CG  . MET   D  1 322 ? 44.509  51.667  -64.178  1.00 73.01  ? 623  MET   D CG  1 
ATOM   12813 S  SD  . MET   D  1 322 ? 45.068  52.371  -62.637  1.00 71.10  ? 623  MET   D SD  1 
ATOM   12814 C  CE  . MET   D  1 322 ? 43.590  53.206  -62.074  1.00 70.99  ? 623  MET   D CE  1 
ATOM   12815 N  N   . ARG   D  1 323 ? 43.789  53.343  -68.740  1.00 71.56  ? 624  ARG   D N   1 
ATOM   12816 C  CA  . ARG   D  1 323 ? 43.088  54.045  -69.802  1.00 82.54  ? 624  ARG   D CA  1 
ATOM   12817 C  C   . ARG   D  1 323 ? 42.097  53.124  -70.509  1.00 98.45  ? 624  ARG   D C   1 
ATOM   12818 O  O   . ARG   D  1 323 ? 40.909  53.446  -70.623  1.00 110.32 ? 624  ARG   D O   1 
ATOM   12819 C  CB  . ARG   D  1 323 ? 44.088  54.608  -70.819  1.00 85.52  ? 624  ARG   D CB  1 
ATOM   12820 C  CG  . ARG   D  1 323 ? 44.937  55.780  -70.350  1.00 90.65  ? 624  ARG   D CG  1 
ATOM   12821 C  CD  . ARG   D  1 323 ? 46.063  56.053  -71.349  1.00 100.64 ? 624  ARG   D CD  1 
ATOM   12822 N  NE  . ARG   D  1 323 ? 47.224  55.208  -71.083  1.00 113.26 ? 624  ARG   D NE  1 
ATOM   12823 C  CZ  . ARG   D  1 323 ? 48.448  55.666  -70.836  1.00 124.09 ? 624  ARG   D CZ  1 
ATOM   12824 N  NH1 . ARG   D  1 323 ? 48.689  56.973  -70.851  1.00 125.04 ? 624  ARG   D NH1 1 
ATOM   12825 N  NH2 . ARG   D  1 323 ? 49.439  54.814  -70.592  1.00 128.86 ? 624  ARG   D NH2 1 
ATOM   12826 N  N   . LYS   D  1 324 ? 42.566  51.972  -70.980  1.00 93.89  ? 625  LYS   D N   1 
ATOM   12827 C  CA  . LYS   D  1 324 ? 41.748  51.049  -71.757  1.00 86.22  ? 625  LYS   D CA  1 
ATOM   12828 C  C   . LYS   D  1 324 ? 41.269  49.915  -70.857  1.00 82.49  ? 625  LYS   D C   1 
ATOM   12829 O  O   . LYS   D  1 324 ? 42.085  49.213  -70.249  1.00 82.37  ? 625  LYS   D O   1 
ATOM   12830 C  CB  . LYS   D  1 324 ? 42.536  50.497  -72.943  1.00 75.55  ? 625  LYS   D CB  1 
ATOM   12831 C  CG  . LYS   D  1 324 ? 43.239  51.567  -73.763  1.00 82.96  ? 625  LYS   D CG  1 
ATOM   12832 C  CD  . LYS   D  1 324 ? 44.645  51.129  -74.184  1.00 90.63  ? 625  LYS   D CD  1 
ATOM   12833 C  CE  . LYS   D  1 324 ? 44.729  49.620  -74.416  1.00 83.78  ? 625  LYS   D CE  1 
ATOM   12834 N  NZ  . LYS   D  1 324 ? 45.841  49.002  -73.640  1.00 80.20  ? 625  LYS   D NZ  1 
ATOM   12835 N  N   . THR   D  1 325 ? 39.946  49.745  -70.774  1.00 74.09  ? 626  THR   D N   1 
ATOM   12836 C  CA  . THR   D  1 325 ? 39.387  48.604  -70.055  1.00 63.92  ? 626  THR   D CA  1 
ATOM   12837 C  C   . THR   D  1 325 ? 39.993  47.297  -70.547  1.00 62.31  ? 626  THR   D C   1 
ATOM   12838 O  O   . THR   D  1 325 ? 40.292  46.400  -69.749  1.00 45.97  ? 626  THR   D O   1 
ATOM   12839 C  CB  . THR   D  1 325 ? 37.864  48.576  -70.213  1.00 62.51  ? 626  THR   D CB  1 
ATOM   12840 O  OG1 . THR   D  1 325 ? 37.515  48.585  -71.608  1.00 61.06  ? 626  THR   D OG1 1 
ATOM   12841 C  CG2 . THR   D  1 325 ? 37.243  49.777  -69.534  1.00 56.21  ? 626  THR   D CG2 1 
ATOM   12842 N  N   . SER   D  1 326 ? 40.205  47.184  -71.862  1.00 64.67  ? 627  SER   D N   1 
ATOM   12843 C  CA  . SER   D  1 326 ? 40.658  45.951  -72.493  1.00 61.91  ? 627  SER   D CA  1 
ATOM   12844 C  C   . SER   D  1 326 ? 42.103  45.595  -72.156  1.00 61.02  ? 627  SER   D C   1 
ATOM   12845 O  O   . SER   D  1 326 ? 42.563  44.541  -72.605  1.00 64.44  ? 627  SER   D O   1 
ATOM   12846 C  CB  . SER   D  1 326 ? 40.473  46.035  -74.017  1.00 60.70  ? 627  SER   D CB  1 
ATOM   12847 O  OG  . SER   D  1 326 ? 41.155  47.154  -74.561  1.00 59.81  ? 627  SER   D OG  1 
ATOM   12848 N  N   . SER   D  1 327 ? 42.835  46.422  -71.404  1.00 59.84  ? 628  SER   D N   1 
ATOM   12849 C  CA  . SER   D  1 327 ? 44.069  45.912  -70.819  1.00 57.89  ? 628  SER   D CA  1 
ATOM   12850 C  C   . SER   D  1 327 ? 43.793  44.987  -69.645  1.00 49.04  ? 628  SER   D C   1 
ATOM   12851 O  O   . SER   D  1 327 ? 44.708  44.291  -69.195  1.00 52.80  ? 628  SER   D O   1 
ATOM   12852 C  CB  . SER   D  1 327 ? 44.979  47.054  -70.366  1.00 58.69  ? 628  SER   D CB  1 
ATOM   12853 O  OG  . SER   D  1 327 ? 44.534  47.604  -69.147  1.00 54.20  ? 628  SER   D OG  1 
ATOM   12854 N  N   . LEU   D  1 328 ? 42.561  44.969  -69.147  1.00 43.06  ? 629  LEU   D N   1 
ATOM   12855 C  CA  . LEU   D  1 328 ? 42.154  44.096  -68.045  1.00 53.43  ? 629  LEU   D CA  1 
ATOM   12856 C  C   . LEU   D  1 328 ? 42.914  44.401  -66.755  1.00 63.75  ? 629  LEU   D C   1 
ATOM   12857 O  O   . LEU   D  1 328 ? 43.260  43.498  -65.990  1.00 70.10  ? 629  LEU   D O   1 
ATOM   12858 C  CB  . LEU   D  1 328 ? 42.298  42.623  -68.434  1.00 60.20  ? 629  LEU   D CB  1 
ATOM   12859 C  CG  . LEU   D  1 328 ? 41.545  42.215  -69.709  1.00 54.86  ? 629  LEU   D CG  1 
ATOM   12860 C  CD1 . LEU   D  1 328 ? 41.476  40.704  -69.870  1.00 43.38  ? 629  LEU   D CD1 1 
ATOM   12861 C  CD2 . LEU   D  1 328 ? 40.141  42.801  -69.716  1.00 58.62  ? 629  LEU   D CD2 1 
ATOM   12862 N  N   . TRP   D  1 329 ? 43.160  45.689  -66.491  1.00 66.77  ? 630  TRP   D N   1 
ATOM   12863 C  CA  . TRP   D  1 329 ? 43.802  46.061  -65.231  1.00 59.90  ? 630  TRP   D CA  1 
ATOM   12864 C  C   . TRP   D  1 329 ? 42.917  45.726  -64.028  1.00 62.50  ? 630  TRP   D C   1 
ATOM   12865 O  O   . TRP   D  1 329 ? 43.405  45.206  -63.017  1.00 66.17  ? 630  TRP   D O   1 
ATOM   12866 C  CB  . TRP   D  1 329 ? 44.174  47.549  -65.238  1.00 54.36  ? 630  TRP   D CB  1 
ATOM   12867 C  CG  . TRP   D  1 329 ? 43.017  48.515  -65.329  1.00 58.16  ? 630  TRP   D CG  1 
ATOM   12868 C  CD1 . TRP   D  1 329 ? 42.487  49.054  -66.467  1.00 58.07  ? 630  TRP   D CD1 1 
ATOM   12869 C  CD2 . TRP   D  1 329 ? 42.263  49.068  -64.238  1.00 59.18  ? 630  TRP   D CD2 1 
ATOM   12870 N  NE1 . TRP   D  1 329 ? 41.447  49.901  -66.156  1.00 57.32  ? 630  TRP   D NE1 1 
ATOM   12871 C  CE2 . TRP   D  1 329 ? 41.290  49.927  -64.793  1.00 60.75  ? 630  TRP   D CE2 1 
ATOM   12872 C  CE3 . TRP   D  1 329 ? 42.312  48.917  -62.847  1.00 58.98  ? 630  TRP   D CE3 1 
ATOM   12873 C  CZ2 . TRP   D  1 329 ? 40.370  50.630  -64.001  1.00 54.57  ? 630  TRP   D CZ2 1 
ATOM   12874 C  CZ3 . TRP   D  1 329 ? 41.404  49.624  -62.063  1.00 54.91  ? 630  TRP   D CZ3 1 
ATOM   12875 C  CH2 . TRP   D  1 329 ? 40.445  50.466  -62.643  1.00 55.80  ? 630  TRP   D CH2 1 
ATOM   12876 N  N   . LYS   D  1 330 ? 41.617  46.019  -64.111  1.00 63.10  ? 631  LYS   D N   1 
ATOM   12877 C  CA  . LYS   D  1 330 ? 40.698  45.628  -63.046  1.00 54.87  ? 631  LYS   D CA  1 
ATOM   12878 C  C   . LYS   D  1 330 ? 40.815  44.142  -62.755  1.00 57.33  ? 631  LYS   D C   1 
ATOM   12879 O  O   . LYS   D  1 330 ? 40.944  43.729  -61.596  1.00 63.06  ? 631  LYS   D O   1 
ATOM   12880 C  CB  . LYS   D  1 330 ? 39.258  45.973  -63.425  1.00 47.58  ? 631  LYS   D CB  1 
ATOM   12881 C  CG  . LYS   D  1 330 ? 38.871  47.404  -63.181  1.00 52.05  ? 631  LYS   D CG  1 
ATOM   12882 C  CD  . LYS   D  1 330 ? 37.389  47.588  -63.443  1.00 46.08  ? 631  LYS   D CD  1 
ATOM   12883 C  CE  . LYS   D  1 330 ? 36.945  49.006  -63.112  1.00 48.36  ? 631  LYS   D CE  1 
ATOM   12884 N  NZ  . LYS   D  1 330 ? 35.591  49.004  -62.472  1.00 56.92  ? 631  LYS   D NZ  1 
ATOM   12885 N  N   . ASP   D  1 331 ? 40.776  43.323  -63.808  1.00 54.15  ? 632  ASP   D N   1 
ATOM   12886 C  CA  . ASP   D  1 331 ? 40.897  41.876  -63.646  1.00 56.06  ? 632  ASP   D CA  1 
ATOM   12887 C  C   . ASP   D  1 331 ? 42.230  41.493  -63.010  1.00 52.44  ? 632  ASP   D C   1 
ATOM   12888 O  O   . ASP   D  1 331 ? 42.288  40.615  -62.138  1.00 54.10  ? 632  ASP   D O   1 
ATOM   12889 C  CB  . ASP   D  1 331 ? 40.754  41.192  -65.010  1.00 52.02  ? 632  ASP   D CB  1 
ATOM   12890 C  CG  . ASP   D  1 331 ? 39.516  41.642  -65.767  1.00 49.37  ? 632  ASP   D CG  1 
ATOM   12891 O  OD1 . ASP   D  1 331 ? 39.563  42.707  -66.419  1.00 48.11  ? 632  ASP   D OD1 1 
ATOM   12892 O  OD2 . ASP   D  1 331 ? 38.491  40.933  -65.704  1.00 50.32  ? 632  ASP   D OD2 1 
ATOM   12893 N  N   . GLN   D  1 332 ? 43.313  42.141  -63.440  1.00 45.53  ? 633  GLN   D N   1 
ATOM   12894 C  CA  . GLN   D  1 332 ? 44.644  41.754  -62.993  1.00 49.68  ? 633  GLN   D CA  1 
ATOM   12895 C  C   . GLN   D  1 332 ? 44.854  42.104  -61.524  1.00 55.52  ? 633  GLN   D C   1 
ATOM   12896 O  O   . GLN   D  1 332 ? 45.412  41.308  -60.762  1.00 60.95  ? 633  GLN   D O   1 
ATOM   12897 C  CB  . GLN   D  1 332 ? 45.684  42.449  -63.853  1.00 48.67  ? 633  GLN   D CB  1 
ATOM   12898 C  CG  . GLN   D  1 332 ? 46.728  41.583  -64.477  1.00 50.35  ? 633  GLN   D CG  1 
ATOM   12899 C  CD  . GLN   D  1 332 ? 47.566  42.408  -65.436  1.00 63.05  ? 633  GLN   D CD  1 
ATOM   12900 O  OE1 . GLN   D  1 332 ? 47.436  43.632  -65.481  1.00 66.00  ? 633  GLN   D OE1 1 
ATOM   12901 N  NE2 . GLN   D  1 332 ? 48.417  41.750  -66.213  1.00 71.62  ? 633  GLN   D NE2 1 
ATOM   12902 N  N   . ALA   D  1 333 ? 44.413  43.294  -61.113  1.00 52.79  ? 634  ALA   D N   1 
ATOM   12903 C  CA  . ALA   D  1 333 ? 44.592  43.711  -59.727  1.00 54.65  ? 634  ALA   D CA  1 
ATOM   12904 C  C   . ALA   D  1 333 ? 43.723  42.890  -58.780  1.00 55.68  ? 634  ALA   D C   1 
ATOM   12905 O  O   . ALA   D  1 333 ? 44.162  42.535  -57.681  1.00 61.82  ? 634  ALA   D O   1 
ATOM   12906 C  CB  . ALA   D  1 333 ? 44.289  45.204  -59.596  1.00 50.46  ? 634  ALA   D CB  1 
ATOM   12907 N  N   . LEU   D  1 334 ? 42.495  42.568  -59.197  1.00 53.21  ? 635  LEU   D N   1 
ATOM   12908 C  CA  . LEU   D  1 334 ? 41.612  41.741  -58.377  1.00 41.87  ? 635  LEU   D CA  1 
ATOM   12909 C  C   . LEU   D  1 334 ? 42.265  40.423  -57.979  1.00 47.43  ? 635  LEU   D C   1 
ATOM   12910 O  O   . LEU   D  1 334 ? 42.112  39.974  -56.836  1.00 58.14  ? 635  LEU   D O   1 
ATOM   12911 C  CB  . LEU   D  1 334 ? 40.307  41.469  -59.118  1.00 36.07  ? 635  LEU   D CB  1 
ATOM   12912 C  CG  . LEU   D  1 334 ? 39.322  40.488  -58.482  1.00 38.55  ? 635  LEU   D CG  1 
ATOM   12913 C  CD1 . LEU   D  1 334 ? 38.647  41.126  -57.320  1.00 47.28  ? 635  LEU   D CD1 1 
ATOM   12914 C  CD2 . LEU   D  1 334 ? 38.289  40.053  -59.502  1.00 47.07  ? 635  LEU   D CD2 1 
ATOM   12915 N  N   . VAL   D  1 335 ? 42.984  39.776  -58.899  1.00 49.00  ? 636  VAL   D N   1 
ATOM   12916 C  CA  . VAL   D  1 335 ? 43.614  38.505  -58.550  1.00 48.03  ? 636  VAL   D CA  1 
ATOM   12917 C  C   . VAL   D  1 335 ? 44.660  38.714  -57.464  1.00 52.68  ? 636  VAL   D C   1 
ATOM   12918 O  O   . VAL   D  1 335 ? 44.707  37.976  -56.476  1.00 53.23  ? 636  VAL   D O   1 
ATOM   12919 C  CB  . VAL   D  1 335 ? 44.229  37.830  -59.783  1.00 46.03  ? 636  VAL   D CB  1 
ATOM   12920 C  CG1 . VAL   D  1 335 ? 45.023  36.586  -59.347  1.00 34.46  ? 636  VAL   D CG1 1 
ATOM   12921 C  CG2 . VAL   D  1 335 ? 43.150  37.461  -60.778  1.00 44.96  ? 636  VAL   D CG2 1 
ATOM   12922 N  N   . GLU   D  1 336 ? 45.520  39.719  -57.637  1.00 52.50  ? 637  GLU   D N   1 
ATOM   12923 C  CA  . GLU   D  1 336 ? 46.566  39.973  -56.650  1.00 51.17  ? 637  GLU   D CA  1 
ATOM   12924 C  C   . GLU   D  1 336 ? 45.979  40.195  -55.259  1.00 61.71  ? 637  GLU   D C   1 
ATOM   12925 O  O   . GLU   D  1 336 ? 46.486  39.659  -54.263  1.00 57.33  ? 637  GLU   D O   1 
ATOM   12926 C  CB  . GLU   D  1 336 ? 47.400  41.183  -57.076  1.00 46.45  ? 637  GLU   D CB  1 
ATOM   12927 C  CG  . GLU   D  1 336 ? 48.174  41.001  -58.369  1.00 49.82  ? 637  GLU   D CG  1 
ATOM   12928 C  CD  . GLU   D  1 336 ? 49.207  39.875  -58.306  1.00 55.98  ? 637  GLU   D CD  1 
ATOM   12929 O  OE1 . GLU   D  1 336 ? 49.311  39.163  -57.283  1.00 55.05  ? 637  GLU   D OE1 1 
ATOM   12930 O  OE2 . GLU   D  1 336 ? 49.921  39.694  -59.308  1.00 63.87  ? 637  GLU   D OE2 1 
ATOM   12931 N  N   . ILE   D  1 337 ? 44.907  40.983  -55.177  1.00 60.79  ? 638  ILE   D N   1 
ATOM   12932 C  CA  . ILE   D  1 337 ? 44.238  41.228  -53.907  1.00 48.01  ? 638  ILE   D CA  1 
ATOM   12933 C  C   . ILE   D  1 337 ? 43.840  39.913  -53.261  1.00 57.03  ? 638  ILE   D C   1 
ATOM   12934 O  O   . ILE   D  1 337 ? 44.056  39.696  -52.063  1.00 66.63  ? 638  ILE   D O   1 
ATOM   12935 C  CB  . ILE   D  1 337 ? 43.020  42.145  -54.123  1.00 41.21  ? 638  ILE   D CB  1 
ATOM   12936 C  CG1 . ILE   D  1 337 ? 43.480  43.552  -54.490  1.00 45.20  ? 638  ILE   D CG1 1 
ATOM   12937 C  CG2 . ILE   D  1 337 ? 42.169  42.206  -52.881  1.00 40.22  ? 638  ILE   D CG2 1 
ATOM   12938 C  CD1 . ILE   D  1 337 ? 42.347  44.432  -54.927  1.00 50.33  ? 638  ILE   D CD1 1 
ATOM   12939 N  N   . ASN   D  1 338 ? 43.285  39.001  -54.048  1.00 54.91  ? 639  ASN   D N   1 
ATOM   12940 C  CA  . ASN   D  1 338 ? 42.805  37.744  -53.494  1.00 53.16  ? 639  ASN   D CA  1 
ATOM   12941 C  C   . ASN   D  1 338 ? 43.928  36.794  -53.121  1.00 47.80  ? 639  ASN   D C   1 
ATOM   12942 O  O   . ASN   D  1 338 ? 43.687  35.870  -52.337  1.00 41.27  ? 639  ASN   D O   1 
ATOM   12943 C  CB  . ASN   D  1 338 ? 41.857  37.086  -54.488  1.00 44.91  ? 639  ASN   D CB  1 
ATOM   12944 C  CG  . ASN   D  1 338 ? 40.495  37.668  -54.403  1.00 51.30  ? 639  ASN   D CG  1 
ATOM   12945 O  OD1 . ASN   D  1 338 ? 39.734  37.336  -53.501  1.00 61.99  ? 639  ASN   D OD1 1 
ATOM   12946 N  ND2 . ASN   D  1 338 ? 40.191  38.598  -55.292  1.00 48.31  ? 639  ASN   D ND2 1 
ATOM   12947 N  N   . ILE   D  1 339 ? 45.119  36.977  -53.707  1.00 47.45  ? 640  ILE   D N   1 
ATOM   12948 C  CA  . ILE   D  1 339 ? 46.308  36.245  -53.278  1.00 49.08  ? 640  ILE   D CA  1 
ATOM   12949 C  C   . ILE   D  1 339 ? 46.733  36.729  -51.910  1.00 51.82  ? 640  ILE   D C   1 
ATOM   12950 O  O   . ILE   D  1 339 ? 47.036  35.935  -51.009  1.00 54.81  ? 640  ILE   D O   1 
ATOM   12951 C  CB  . ILE   D  1 339 ? 47.453  36.421  -54.294  1.00 41.59  ? 640  ILE   D CB  1 
ATOM   12952 C  CG1 . ILE   D  1 339 ? 47.195  35.603  -55.553  1.00 42.71  ? 640  ILE   D CG1 1 
ATOM   12953 C  CG2 . ILE   D  1 339 ? 48.790  36.032  -53.670  1.00 48.10  ? 640  ILE   D CG2 1 
ATOM   12954 C  CD1 . ILE   D  1 339 ? 47.650  36.304  -56.790  1.00 36.68  ? 640  ILE   D CD1 1 
ATOM   12955 N  N   . ALA   D  1 340 ? 46.760  38.055  -51.752  1.00 50.44  ? 641  ALA   D N   1 
ATOM   12956 C  CA  . ALA   D  1 340 ? 47.092  38.675  -50.479  1.00 68.00  ? 641  ALA   D CA  1 
ATOM   12957 C  C   . ALA   D  1 340 ? 46.194  38.158  -49.364  1.00 65.14  ? 641  ALA   D C   1 
ATOM   12958 O  O   . ALA   D  1 340 ? 46.678  37.688  -48.329  1.00 57.65  ? 641  ALA   D O   1 
ATOM   12959 C  CB  . ALA   D  1 340 ? 46.977  40.195  -50.612  1.00 71.56  ? 641  ALA   D CB  1 
ATOM   12960 N  N   . VAL   D  1 341 ? 44.876  38.227  -49.575  1.00 57.61  ? 642  VAL   D N   1 
ATOM   12961 C  CA  . VAL   D  1 341 ? 43.916  37.739  -48.590  1.00 41.67  ? 642  VAL   D CA  1 
ATOM   12962 C  C   . VAL   D  1 341 ? 44.240  36.306  -48.194  1.00 45.79  ? 642  VAL   D C   1 
ATOM   12963 O  O   . VAL   D  1 341 ? 44.375  35.982  -47.009  1.00 40.41  ? 642  VAL   D O   1 
ATOM   12964 C  CB  . VAL   D  1 341 ? 42.484  37.854  -49.141  1.00 29.29  ? 642  VAL   D CB  1 
ATOM   12965 C  CG1 . VAL   D  1 341 ? 41.535  37.017  -48.306  1.00 41.55  ? 642  VAL   D CG1 1 
ATOM   12966 C  CG2 . VAL   D  1 341 ? 42.033  39.318  -49.159  1.00 33.87  ? 642  VAL   D CG2 1 
ATOM   12967 N  N   . LEU   D  1 342 ? 44.356  35.420  -49.181  1.00 50.10  ? 643  LEU   D N   1 
ATOM   12968 C  CA  . LEU   D  1 342 ? 44.582  34.016  -48.856  1.00 52.09  ? 643  LEU   D CA  1 
ATOM   12969 C  C   . LEU   D  1 342 ? 45.908  33.830  -48.133  1.00 56.21  ? 643  LEU   D C   1 
ATOM   12970 O  O   . LEU   D  1 342 ? 45.998  33.057  -47.177  1.00 48.03  ? 643  LEU   D O   1 
ATOM   12971 C  CB  . LEU   D  1 342 ? 44.527  33.158  -50.123  1.00 37.69  ? 643  LEU   D CB  1 
ATOM   12972 C  CG  . LEU   D  1 342 ? 43.103  33.009  -50.663  1.00 41.26  ? 643  LEU   D CG  1 
ATOM   12973 C  CD1 . LEU   D  1 342 ? 43.011  32.402  -52.094  1.00 39.12  ? 643  LEU   D CD1 1 
ATOM   12974 C  CD2 . LEU   D  1 342 ? 42.272  32.229  -49.698  1.00 28.66  ? 643  LEU   D CD2 1 
ATOM   12975 N  N   . TYR   D  1 343 ? 46.946  34.534  -48.577  1.00 65.26  ? 644  TYR   D N   1 
ATOM   12976 C  CA  . TYR   D  1 343 ? 48.264  34.381  -47.973  1.00 50.84  ? 644  TYR   D CA  1 
ATOM   12977 C  C   . TYR   D  1 343 ? 48.312  35.006  -46.596  1.00 59.04  ? 644  TYR   D C   1 
ATOM   12978 O  O   . TYR   D  1 343 ? 49.095  34.581  -45.733  1.00 53.12  ? 644  TYR   D O   1 
ATOM   12979 C  CB  . TYR   D  1 343 ? 49.302  35.022  -48.883  1.00 36.85  ? 644  TYR   D CB  1 
ATOM   12980 C  CG  . TYR   D  1 343 ? 50.638  35.368  -48.258  1.00 39.48  ? 644  TYR   D CG  1 
ATOM   12981 C  CD1 . TYR   D  1 343 ? 51.629  34.413  -48.125  1.00 37.57  ? 644  TYR   D CD1 1 
ATOM   12982 C  CD2 . TYR   D  1 343 ? 50.932  36.666  -47.869  1.00 39.60  ? 644  TYR   D CD2 1 
ATOM   12983 C  CE1 . TYR   D  1 343 ? 52.855  34.728  -47.583  1.00 50.82  ? 644  TYR   D CE1 1 
ATOM   12984 C  CE2 . TYR   D  1 343 ? 52.165  36.991  -47.327  1.00 54.82  ? 644  TYR   D CE2 1 
ATOM   12985 C  CZ  . TYR   D  1 343 ? 53.124  36.015  -47.184  1.00 58.91  ? 644  TYR   D CZ  1 
ATOM   12986 O  OH  . TYR   D  1 343 ? 54.362  36.324  -46.648  1.00 66.85  ? 644  TYR   D OH  1 
ATOM   12987 N  N   . SER   D  1 344 ? 47.480  36.011  -46.374  1.00 55.52  ? 645  SER   D N   1 
ATOM   12988 C  CA  . SER   D  1 344 ? 47.527  36.699  -45.106  1.00 37.70  ? 645  SER   D CA  1 
ATOM   12989 C  C   . SER   D  1 344 ? 46.829  35.894  -44.028  1.00 43.55  ? 645  SER   D C   1 
ATOM   12990 O  O   . SER   D  1 344 ? 47.335  35.806  -42.908  1.00 42.73  ? 645  SER   D O   1 
ATOM   12991 C  CB  . SER   D  1 344 ? 46.935  38.090  -45.268  1.00 36.87  ? 645  SER   D CB  1 
ATOM   12992 O  OG  . SER   D  1 344 ? 47.887  38.904  -45.948  1.00 37.74  ? 645  SER   D OG  1 
ATOM   12993 N  N   . PHE   D  1 345 ? 45.685  35.275  -44.349  1.00 41.20  ? 646  PHE   D N   1 
ATOM   12994 C  CA  . PHE   D  1 345 ? 45.027  34.402  -43.377  1.00 41.05  ? 646  PHE   D CA  1 
ATOM   12995 C  C   . PHE   D  1 345 ? 45.857  33.151  -43.104  1.00 54.06  ? 646  PHE   D C   1 
ATOM   12996 O  O   . PHE   D  1 345 ? 45.990  32.727  -41.952  1.00 70.24  ? 646  PHE   D O   1 
ATOM   12997 C  CB  . PHE   D  1 345 ? 43.630  34.017  -43.858  1.00 27.61  ? 646  PHE   D CB  1 
ATOM   12998 C  CG  . PHE   D  1 345 ? 42.588  35.097  -43.637  1.00 44.76  ? 646  PHE   D CG  1 
ATOM   12999 C  CD1 . PHE   D  1 345 ? 42.843  36.416  -44.000  1.00 27.34  ? 646  PHE   D CD1 1 
ATOM   13000 C  CD2 . PHE   D  1 345 ? 41.364  34.792  -43.054  1.00 34.06  ? 646  PHE   D CD2 1 
ATOM   13001 C  CE1 . PHE   D  1 345 ? 41.884  37.399  -43.816  1.00 31.84  ? 646  PHE   D CE1 1 
ATOM   13002 C  CE2 . PHE   D  1 345 ? 40.409  35.776  -42.836  1.00 32.20  ? 646  PHE   D CE2 1 
ATOM   13003 C  CZ  . PHE   D  1 345 ? 40.662  37.074  -43.227  1.00 37.99  ? 646  PHE   D CZ  1 
ATOM   13004 N  N   . GLN   D  1 346 ? 46.437  32.555  -44.141  1.00 44.50  ? 647  GLN   D N   1 
ATOM   13005 C  CA  . GLN   D  1 346 ? 47.162  31.310  -43.941  1.00 48.37  ? 647  GLN   D CA  1 
ATOM   13006 C  C   . GLN   D  1 346 ? 48.419  31.529  -43.118  1.00 56.37  ? 647  GLN   D C   1 
ATOM   13007 O  O   . GLN   D  1 346 ? 48.839  30.629  -42.387  1.00 61.95  ? 647  GLN   D O   1 
ATOM   13008 C  CB  . GLN   D  1 346 ? 47.494  30.675  -45.293  1.00 50.34  ? 647  GLN   D CB  1 
ATOM   13009 C  CG  . GLN   D  1 346 ? 46.336  29.891  -45.888  1.00 52.44  ? 647  GLN   D CG  1 
ATOM   13010 C  CD  . GLN   D  1 346 ? 46.431  29.753  -47.391  1.00 59.16  ? 647  GLN   D CD  1 
ATOM   13011 O  OE1 . GLN   D  1 346 ? 47.249  30.408  -48.038  1.00 59.66  ? 647  GLN   D OE1 1 
ATOM   13012 N  NE2 . GLN   D  1 346 ? 45.600  28.890  -47.954  1.00 58.05  ? 647  GLN   D NE2 1 
ATOM   13013 N  N   . SER   D  1 347 ? 49.023  32.714  -43.218  1.00 53.75  ? 648  SER   D N   1 
ATOM   13014 C  CA  . SER   D  1 347 ? 50.225  33.005  -42.446  1.00 49.31  ? 648  SER   D CA  1 
ATOM   13015 C  C   . SER   D  1 347 ? 49.896  33.189  -40.967  1.00 60.66  ? 648  SER   D C   1 
ATOM   13016 O  O   . SER   D  1 347 ? 50.688  32.826  -40.085  1.00 60.24  ? 648  SER   D O   1 
ATOM   13017 C  CB  . SER   D  1 347 ? 50.890  34.250  -43.015  1.00 42.68  ? 648  SER   D CB  1 
ATOM   13018 O  OG  . SER   D  1 347 ? 51.237  34.031  -44.367  1.00 57.55  ? 648  SER   D OG  1 
ATOM   13019 N  N   . ASP   D  1 348 ? 48.726  33.743  -40.680  1.00 47.40  ? 649  ASP   D N   1 
ATOM   13020 C  CA  . ASP   D  1 348 ? 48.256  33.914  -39.321  1.00 44.67  ? 649  ASP   D CA  1 
ATOM   13021 C  C   . ASP   D  1 348 ? 47.409  32.739  -38.850  1.00 54.10  ? 649  ASP   D C   1 
ATOM   13022 O  O   . ASP   D  1 348 ? 46.629  32.892  -37.910  1.00 61.18  ? 649  ASP   D O   1 
ATOM   13023 C  CB  . ASP   D  1 348 ? 47.488  35.229  -39.220  1.00 31.48  ? 649  ASP   D CB  1 
ATOM   13024 C  CG  . ASP   D  1 348 ? 48.379  36.424  -39.489  1.00 43.24  ? 649  ASP   D CG  1 
ATOM   13025 O  OD1 . ASP   D  1 348 ? 49.574  36.206  -39.784  1.00 45.57  ? 649  ASP   D OD1 1 
ATOM   13026 O  OD2 . ASP   D  1 348 ? 47.902  37.575  -39.399  1.00 52.80  ? 649  ASP   D OD2 1 
ATOM   13027 N  N   . LYS   D  1 349 ? 47.559  31.575  -39.485  1.00 56.14  ? 650  LYS   D N   1 
ATOM   13028 C  CA  . LYS   D  1 349 ? 46.803  30.355  -39.204  1.00 55.26  ? 650  LYS   D CA  1 
ATOM   13029 C  C   . LYS   D  1 349 ? 45.361  30.629  -38.764  1.00 51.90  ? 650  LYS   D C   1 
ATOM   13030 O  O   . LYS   D  1 349 ? 44.855  30.056  -37.792  1.00 52.27  ? 650  LYS   D O   1 
ATOM   13031 C  CB  . LYS   D  1 349 ? 47.582  29.511  -38.198  1.00 56.78  ? 650  LYS   D CB  1 
ATOM   13032 C  CG  . LYS   D  1 349 ? 48.854  28.928  -38.842  1.00 54.95  ? 650  LYS   D CG  1 
ATOM   13033 C  CD  . LYS   D  1 349 ? 49.917  28.555  -37.825  1.00 66.81  ? 650  LYS   D CD  1 
ATOM   13034 C  CE  . LYS   D  1 349 ? 49.740  27.136  -37.316  1.00 79.41  ? 650  LYS   D CE  1 
ATOM   13035 N  NZ  . LYS   D  1 349 ? 50.925  26.676  -36.521  1.00 87.64  ? 650  LYS   D NZ  1 
ATOM   13036 N  N   . VAL   D  1 350 ? 44.700  31.512  -39.509  1.00 39.54  ? 651  VAL   D N   1 
ATOM   13037 C  CA  . VAL   D  1 350 ? 43.273  31.771  -39.402  1.00 42.10  ? 651  VAL   D CA  1 
ATOM   13038 C  C   . VAL   D  1 350 ? 42.574  31.064  -40.557  1.00 48.13  ? 651  VAL   D C   1 
ATOM   13039 O  O   . VAL   D  1 350 ? 42.914  31.283  -41.731  1.00 40.65  ? 651  VAL   D O   1 
ATOM   13040 C  CB  . VAL   D  1 350 ? 42.990  33.281  -39.427  1.00 38.62  ? 651  VAL   D CB  1 
ATOM   13041 C  CG1 . VAL   D  1 350 ? 41.507  33.554  -39.315  1.00 36.96  ? 651  VAL   D CG1 1 
ATOM   13042 C  CG2 . VAL   D  1 350 ? 43.753  33.974  -38.329  1.00 39.42  ? 651  VAL   D CG2 1 
ATOM   13043 N  N   . THR   D  1 351 ? 41.585  30.233  -40.229  1.00 45.08  ? 652  THR   D N   1 
ATOM   13044 C  CA  . THR   D  1 351 ? 40.938  29.403  -41.234  1.00 42.34  ? 652  THR   D CA  1 
ATOM   13045 C  C   . THR   D  1 351 ? 40.388  30.241  -42.379  1.00 45.68  ? 652  THR   D C   1 
ATOM   13046 O  O   . THR   D  1 351 ? 39.734  31.268  -42.166  1.00 43.64  ? 652  THR   D O   1 
ATOM   13047 C  CB  . THR   D  1 351 ? 39.806  28.588  -40.614  1.00 41.46  ? 652  THR   D CB  1 
ATOM   13048 O  OG1 . THR   D  1 351 ? 40.331  27.719  -39.598  1.00 48.76  ? 652  THR   D OG1 1 
ATOM   13049 C  CG2 . THR   D  1 351 ? 39.098  27.755  -41.718  1.00 35.32  ? 652  THR   D CG2 1 
ATOM   13050 N  N   . ILE   D  1 352 ? 40.656  29.785  -43.603  1.00 47.83  ? 653  ILE   D N   1 
ATOM   13051 C  CA  . ILE   D  1 352 ? 40.063  30.360  -44.803  1.00 36.80  ? 653  ILE   D CA  1 
ATOM   13052 C  C   . ILE   D  1 352 ? 40.076  29.271  -45.853  1.00 43.48  ? 653  ILE   D C   1 
ATOM   13053 O  O   . ILE   D  1 352 ? 40.849  28.304  -45.756  1.00 46.25  ? 653  ILE   D O   1 
ATOM   13054 C  CB  . ILE   D  1 352 ? 40.858  31.604  -45.262  1.00 33.51  ? 653  ILE   D CB  1 
ATOM   13055 C  CG1 . ILE   D  1 352 ? 40.030  32.463  -46.225  1.00 31.83  ? 653  ILE   D CG1 1 
ATOM   13056 C  CG2 . ILE   D  1 352 ? 42.180  31.169  -45.839  1.00 27.91  ? 653  ILE   D CG2 1 
ATOM   13057 C  CD1 . ILE   D  1 352 ? 40.609  33.912  -46.437  1.00 25.47  ? 653  ILE   D CD1 1 
ATOM   13058 N  N   . VAL   D  1 353 ? 39.222  29.418  -46.872  1.00 45.40  ? 654  VAL   D N   1 
ATOM   13059 C  CA  . VAL   D  1 353 ? 39.230  28.530  -48.041  1.00 47.99  ? 654  VAL   D CA  1 
ATOM   13060 C  C   . VAL   D  1 353 ? 39.213  29.361  -49.326  1.00 48.93  ? 654  VAL   D C   1 
ATOM   13061 O  O   . VAL   D  1 353 ? 38.511  30.373  -49.427  1.00 47.27  ? 654  VAL   D O   1 
ATOM   13062 C  CB  . VAL   D  1 353 ? 38.052  27.525  -48.001  1.00 43.05  ? 654  VAL   D CB  1 
ATOM   13063 C  CG1 . VAL   D  1 353 ? 36.725  28.198  -48.340  1.00 35.42  ? 654  VAL   D CG1 1 
ATOM   13064 C  CG2 . VAL   D  1 353 ? 38.303  26.347  -48.920  1.00 44.74  ? 654  VAL   D CG2 1 
ATOM   13065 N  N   . ASP   D  1 354 ? 40.020  28.950  -50.299  1.00 47.34  ? 655  ASP   D N   1 
ATOM   13066 C  CA  . ASP   D  1 354 ? 40.004  29.595  -51.602  1.00 50.60  ? 655  ASP   D CA  1 
ATOM   13067 C  C   . ASP   D  1 354 ? 38.787  29.140  -52.392  1.00 47.44  ? 655  ASP   D C   1 
ATOM   13068 O  O   . ASP   D  1 354 ? 38.206  28.079  -52.133  1.00 43.19  ? 655  ASP   D O   1 
ATOM   13069 C  CB  . ASP   D  1 354 ? 41.273  29.270  -52.388  1.00 54.46  ? 655  ASP   D CB  1 
ATOM   13070 C  CG  . ASP   D  1 354 ? 41.497  27.776  -52.526  1.00 69.91  ? 655  ASP   D CG  1 
ATOM   13071 O  OD1 . ASP   D  1 354 ? 41.867  27.129  -51.517  1.00 82.63  ? 655  ASP   D OD1 1 
ATOM   13072 O  OD2 . ASP   D  1 354 ? 41.274  27.241  -53.629  1.00 73.87  ? 655  ASP   D OD2 1 
ATOM   13073 N  N   . HIS   D  1 355 ? 38.411  29.940  -53.390  1.00 50.89  ? 656  HIS   D N   1 
ATOM   13074 C  CA  . HIS   D  1 355 ? 37.213  29.585  -54.149  1.00 39.81  ? 656  HIS   D CA  1 
ATOM   13075 C  C   . HIS   D  1 355 ? 37.376  28.274  -54.905  1.00 36.36  ? 656  HIS   D C   1 
ATOM   13076 O  O   . HIS   D  1 355 ? 36.383  27.570  -55.120  1.00 35.93  ? 656  HIS   D O   1 
ATOM   13077 C  CB  . HIS   D  1 355 ? 36.802  30.721  -55.083  1.00 26.69  ? 656  HIS   D CB  1 
ATOM   13078 C  CG  . HIS   D  1 355 ? 37.886  31.217  -55.992  1.00 40.28  ? 656  HIS   D CG  1 
ATOM   13079 N  ND1 . HIS   D  1 355 ? 38.912  32.038  -55.564  1.00 37.51  ? 656  HIS   D ND1 1 
ATOM   13080 C  CD2 . HIS   D  1 355 ? 38.064  31.058  -57.326  1.00 37.89  ? 656  HIS   D CD2 1 
ATOM   13081 C  CE1 . HIS   D  1 355 ? 39.688  32.339  -56.590  1.00 42.23  ? 656  HIS   D CE1 1 
ATOM   13082 N  NE2 . HIS   D  1 355 ? 39.198  31.753  -57.670  1.00 41.40  ? 656  HIS   D NE2 1 
ATOM   13083 N  N   . HIS   D  1 356 ? 38.605  27.883  -55.236  1.00 35.90  ? 657  HIS   D N   1 
ATOM   13084 C  CA  . HIS   D  1 356 ? 38.790  26.601  -55.907  1.00 35.69  ? 657  HIS   D CA  1 
ATOM   13085 C  C   . HIS   D  1 356 ? 38.503  25.445  -54.975  1.00 45.34  ? 657  HIS   D C   1 
ATOM   13086 O  O   . HIS   D  1 356 ? 37.667  24.585  -55.284  1.00 43.82  ? 657  HIS   D O   1 
ATOM   13087 C  CB  . HIS   D  1 356 ? 40.193  26.504  -56.468  1.00 38.84  ? 657  HIS   D CB  1 
ATOM   13088 C  CG  . HIS   D  1 356 ? 40.454  27.522  -57.518  1.00 44.11  ? 657  HIS   D CG  1 
ATOM   13089 N  ND1 . HIS   D  1 356 ? 39.934  27.421  -58.789  1.00 47.06  ? 657  HIS   D ND1 1 
ATOM   13090 C  CD2 . HIS   D  1 356 ? 41.121  28.695  -57.468  1.00 43.85  ? 657  HIS   D CD2 1 
ATOM   13091 C  CE1 . HIS   D  1 356 ? 40.309  28.474  -59.490  1.00 52.14  ? 657  HIS   D CE1 1 
ATOM   13092 N  NE2 . HIS   D  1 356 ? 41.024  29.265  -58.707  1.00 48.01  ? 657  HIS   D NE2 1 
ATOM   13093 N  N   . SER   D  1 357 ? 39.182  25.411  -53.824  1.00 52.52  ? 658  SER   D N   1 
ATOM   13094 C  CA  . SER   D  1 357 ? 38.955  24.328  -52.875  1.00 41.77  ? 658  SER   D CA  1 
ATOM   13095 C  C   . SER   D  1 357 ? 37.484  24.262  -52.477  1.00 40.69  ? 658  SER   D C   1 
ATOM   13096 O  O   . SER   D  1 357 ? 36.882  23.178  -52.475  1.00 40.66  ? 658  SER   D O   1 
ATOM   13097 C  CB  . SER   D  1 357 ? 39.862  24.500  -51.652  1.00 52.77  ? 658  SER   D CB  1 
ATOM   13098 O  OG  . SER   D  1 357 ? 39.643  23.473  -50.691  1.00 66.04  ? 658  SER   D OG  1 
ATOM   13099 N  N   . ALA   D  1 358 ? 36.878  25.425  -52.194  1.00 25.00  ? 659  ALA   D N   1 
ATOM   13100 C  CA  . ALA   D  1 358 ? 35.477  25.479  -51.781  1.00 32.32  ? 659  ALA   D CA  1 
ATOM   13101 C  C   . ALA   D  1 358 ? 34.553  24.842  -52.818  1.00 47.24  ? 659  ALA   D C   1 
ATOM   13102 O  O   . ALA   D  1 358 ? 33.703  24.004  -52.476  1.00 49.98  ? 659  ALA   D O   1 
ATOM   13103 C  CB  . ALA   D  1 358 ? 35.073  26.934  -51.526  1.00 23.33  ? 659  ALA   D CB  1 
ATOM   13104 N  N   . THR   D  1 359 ? 34.689  25.241  -54.098  1.00 47.13  ? 660  THR   D N   1 
ATOM   13105 C  CA  . THR   D  1 359 ? 33.736  24.763  -55.097  1.00 39.52  ? 660  THR   D CA  1 
ATOM   13106 C  C   . THR   D  1 359 ? 33.910  23.277  -55.336  1.00 37.47  ? 660  THR   D C   1 
ATOM   13107 O  O   . THR   D  1 359 ? 32.922  22.550  -55.479  1.00 36.74  ? 660  THR   D O   1 
ATOM   13108 C  CB  . THR   D  1 359 ? 33.865  25.527  -56.408  1.00 35.29  ? 660  THR   D CB  1 
ATOM   13109 O  OG1 . THR   D  1 359 ? 35.238  25.593  -56.806  1.00 43.08  ? 660  THR   D OG1 1 
ATOM   13110 C  CG2 . THR   D  1 359 ? 33.319  26.916  -56.260  1.00 36.28  ? 660  THR   D CG2 1 
ATOM   13111 N  N   . GLU   D  1 360 ? 35.158  22.810  -55.367  1.00 40.36  ? 661  GLU   D N   1 
ATOM   13112 C  CA  . GLU   D  1 360 ? 35.418  21.383  -55.516  1.00 39.03  ? 661  GLU   D CA  1 
ATOM   13113 C  C   . GLU   D  1 360 ? 34.750  20.593  -54.395  1.00 48.27  ? 661  GLU   D C   1 
ATOM   13114 O  O   . GLU   D  1 360 ? 34.076  19.585  -54.642  1.00 45.52  ? 661  GLU   D O   1 
ATOM   13115 C  CB  . GLU   D  1 360 ? 36.926  21.151  -55.544  1.00 36.87  ? 661  GLU   D CB  1 
ATOM   13116 C  CG  . GLU   D  1 360 ? 37.364  19.700  -55.543  1.00 57.71  ? 661  GLU   D CG  1 
ATOM   13117 C  CD  . GLU   D  1 360 ? 38.890  19.558  -55.411  1.00 81.01  ? 661  GLU   D CD  1 
ATOM   13118 O  OE1 . GLU   D  1 360 ? 39.566  20.567  -55.094  1.00 84.62  ? 661  GLU   D OE1 1 
ATOM   13119 O  OE2 . GLU   D  1 360 ? 39.415  18.437  -55.625  1.00 87.92  ? 661  GLU   D OE2 1 
ATOM   13120 N  N   . SER   D  1 361 ? 34.904  21.058  -53.148  1.00 51.63  ? 662  SER   D N   1 
ATOM   13121 C  CA  A SER   D  1 361 ? 34.283  20.357  -52.030  0.53 47.23  ? 662  SER   D CA  1 
ATOM   13122 C  CA  B SER   D  1 361 ? 34.280  20.370  -52.021  0.47 47.15  ? 662  SER   D CA  1 
ATOM   13123 C  C   . SER   D  1 361 ? 32.768  20.346  -52.173  1.00 45.16  ? 662  SER   D C   1 
ATOM   13124 O  O   . SER   D  1 361 ? 32.123  19.324  -51.908  1.00 47.35  ? 662  SER   D O   1 
ATOM   13125 C  CB  A SER   D  1 361 ? 34.706  20.985  -50.699  0.53 43.70  ? 662  SER   D CB  1 
ATOM   13126 C  CB  B SER   D  1 361 ? 34.679  21.038  -50.700  0.47 43.79  ? 662  SER   D CB  1 
ATOM   13127 O  OG  A SER   D  1 361 ? 36.061  20.687  -50.398  0.53 42.25  ? 662  SER   D OG  1 
ATOM   13128 O  OG  B SER   D  1 361 ? 33.821  22.126  -50.374  0.47 42.49  ? 662  SER   D OG  1 
ATOM   13129 N  N   . PHE   D  1 362 ? 32.186  21.461  -52.621  1.00 45.94  ? 663  PHE   D N   1 
ATOM   13130 C  CA  . PHE   D  1 362 ? 30.737  21.503  -52.795  1.00 47.15  ? 663  PHE   D CA  1 
ATOM   13131 C  C   . PHE   D  1 362 ? 30.251  20.485  -53.827  1.00 51.95  ? 663  PHE   D C   1 
ATOM   13132 O  O   . PHE   D  1 362 ? 29.223  19.833  -53.615  1.00 57.98  ? 663  PHE   D O   1 
ATOM   13133 C  CB  . PHE   D  1 362 ? 30.283  22.899  -53.192  1.00 46.18  ? 663  PHE   D CB  1 
ATOM   13134 C  CG  . PHE   D  1 362 ? 28.817  22.984  -53.448  1.00 37.79  ? 663  PHE   D CG  1 
ATOM   13135 C  CD1 . PHE   D  1 362 ? 27.930  23.027  -52.383  1.00 27.42  ? 663  PHE   D CD1 1 
ATOM   13136 C  CD2 . PHE   D  1 362 ? 28.319  22.993  -54.753  1.00 35.59  ? 663  PHE   D CD2 1 
ATOM   13137 C  CE1 . PHE   D  1 362 ? 26.553  23.088  -52.595  1.00 36.34  ? 663  PHE   D CE1 1 
ATOM   13138 C  CE2 . PHE   D  1 362 ? 26.946  23.068  -54.984  1.00 48.46  ? 663  PHE   D CE2 1 
ATOM   13139 C  CZ  . PHE   D  1 362 ? 26.058  23.110  -53.907  1.00 52.84  ? 663  PHE   D CZ  1 
ATOM   13140 N  N   . ILE   D  1 363 ? 30.958  20.346  -54.958  1.00 48.64  ? 664  ILE   D N   1 
ATOM   13141 C  CA  . ILE   D  1 363 ? 30.589  19.320  -55.937  1.00 38.64  ? 664  ILE   D CA  1 
ATOM   13142 C  C   . ILE   D  1 363 ? 30.599  17.938  -55.284  1.00 50.22  ? 664  ILE   D C   1 
ATOM   13143 O  O   . ILE   D  1 363 ? 29.638  17.167  -55.413  1.00 40.82  ? 664  ILE   D O   1 
ATOM   13144 C  CB  . ILE   D  1 363 ? 31.514  19.369  -57.166  1.00 36.23  ? 664  ILE   D CB  1 
ATOM   13145 C  CG1 . ILE   D  1 363 ? 31.262  20.630  -57.990  1.00 40.81  ? 664  ILE   D CG1 1 
ATOM   13146 C  CG2 . ILE   D  1 363 ? 31.250  18.183  -58.057  1.00 32.44  ? 664  ILE   D CG2 1 
ATOM   13147 C  CD1 . ILE   D  1 363 ? 29.860  20.717  -58.504  1.00 32.60  ? 664  ILE   D CD1 1 
ATOM   13148 N  N   . LYS   D  1 364 ? 31.676  17.619  -54.543  1.00 50.92  ? 665  LYS   D N   1 
ATOM   13149 C  CA  . LYS   D  1 364 ? 31.723  16.364  -53.787  1.00 50.30  ? 665  LYS   D CA  1 
ATOM   13150 C  C   . LYS   D  1 364 ? 30.534  16.246  -52.838  1.00 50.00  ? 665  LYS   D C   1 
ATOM   13151 O  O   . LYS   D  1 364 ? 29.910  15.179  -52.742  1.00 49.84  ? 665  LYS   D O   1 
ATOM   13152 C  CB  . LYS   D  1 364 ? 33.028  16.258  -52.995  1.00 46.15  ? 665  LYS   D CB  1 
ATOM   13153 C  CG  . LYS   D  1 364 ? 34.287  16.152  -53.826  1.00 51.93  ? 665  LYS   D CG  1 
ATOM   13154 C  CD  . LYS   D  1 364 ? 34.423  14.768  -54.453  1.00 69.66  ? 665  LYS   D CD  1 
ATOM   13155 C  CE  . LYS   D  1 364 ? 34.987  13.732  -53.477  1.00 74.97  ? 665  LYS   D CE  1 
ATOM   13156 N  NZ  . LYS   D  1 364 ? 36.439  13.474  -53.712  1.00 73.93  ? 665  LYS   D NZ  1 
ATOM   13157 N  N   . HIS   D  1 365 ? 30.197  17.335  -52.139  1.00 40.69  ? 666  HIS   D N   1 
ATOM   13158 C  CA  . HIS   D  1 365 ? 29.060  17.306  -51.221  1.00 47.30  ? 666  HIS   D CA  1 
ATOM   13159 C  C   . HIS   D  1 365 ? 27.761  17.083  -51.977  1.00 51.74  ? 666  HIS   D C   1 
ATOM   13160 O  O   . HIS   D  1 365 ? 26.873  16.351  -51.520  1.00 51.68  ? 666  HIS   D O   1 
ATOM   13161 C  CB  . HIS   D  1 365 ? 29.009  18.611  -50.427  1.00 32.48  ? 666  HIS   D CB  1 
ATOM   13162 C  CG  . HIS   D  1 365 ? 27.697  18.877  -49.760  1.00 30.77  ? 666  HIS   D CG  1 
ATOM   13163 N  ND1 . HIS   D  1 365 ? 27.207  18.091  -48.741  1.00 40.80  ? 666  HIS   D ND1 1 
ATOM   13164 C  CD2 . HIS   D  1 365 ? 26.791  19.868  -49.942  1.00 40.83  ? 666  HIS   D CD2 1 
ATOM   13165 C  CE1 . HIS   D  1 365 ? 26.050  18.583  -48.330  1.00 46.06  ? 666  HIS   D CE1 1 
ATOM   13166 N  NE2 . HIS   D  1 365 ? 25.764  19.647  -49.060  1.00 40.36  ? 666  HIS   D NE2 1 
ATOM   13167 N  N   . MET   D  1 366 ? 27.645  17.697  -53.149  1.00 53.21  ? 667  MET   D N   1 
ATOM   13168 C  CA  . MET   D  1 366 ? 26.435  17.560  -53.937  1.00 49.66  ? 667  MET   D CA  1 
ATOM   13169 C  C   . MET   D  1 366 ? 26.188  16.112  -54.333  1.00 44.37  ? 667  MET   D C   1 
ATOM   13170 O  O   . MET   D  1 366 ? 25.095  15.580  -54.105  1.00 45.25  ? 667  MET   D O   1 
ATOM   13171 C  CB  . MET   D  1 366 ? 26.527  18.443  -55.166  1.00 55.65  ? 667  MET   D CB  1 
ATOM   13172 C  CG  . MET   D  1 366 ? 25.224  18.591  -55.897  1.00 53.32  ? 667  MET   D CG  1 
ATOM   13173 S  SD  . MET   D  1 366 ? 25.500  19.796  -57.178  1.00 46.76  ? 667  MET   D SD  1 
ATOM   13174 C  CE  . MET   D  1 366 ? 23.807  20.252  -57.546  1.00 52.20  ? 667  MET   D CE  1 
ATOM   13175 N  N   . GLU   D  1 367 ? 27.186  15.452  -54.936  1.00 43.53  ? 668  GLU   D N   1 
ATOM   13176 C  CA  . GLU   D  1 367 ? 26.966  14.064  -55.347  1.00 56.91  ? 668  GLU   D CA  1 
ATOM   13177 C  C   . GLU   D  1 367 ? 26.524  13.227  -54.152  1.00 56.76  ? 668  GLU   D C   1 
ATOM   13178 O  O   . GLU   D  1 367 ? 25.544  12.471  -54.223  1.00 50.29  ? 668  GLU   D O   1 
ATOM   13179 C  CB  . GLU   D  1 367 ? 28.223  13.456  -55.996  1.00 63.86  ? 668  GLU   D CB  1 
ATOM   13180 C  CG  . GLU   D  1 367 ? 29.306  14.442  -56.412  1.00 74.35  ? 668  GLU   D CG  1 
ATOM   13181 C  CD  . GLU   D  1 367 ? 29.773  14.282  -57.863  1.00 76.85  ? 668  GLU   D CD  1 
ATOM   13182 O  OE1 . GLU   D  1 367 ? 28.916  14.060  -58.743  1.00 77.10  ? 668  GLU   D OE1 1 
ATOM   13183 O  OE2 . GLU   D  1 367 ? 30.999  14.391  -58.118  1.00 77.08  ? 668  GLU   D OE2 1 
ATOM   13184 N  N   . ASN   D  1 368 ? 27.215  13.404  -53.023  1.00 61.95  ? 669  ASN   D N   1 
ATOM   13185 C  CA  . ASN   D  1 368 ? 26.900  12.652  -51.818  1.00 54.33  ? 669  ASN   D CA  1 
ATOM   13186 C  C   . ASN   D  1 368 ? 25.449  12.866  -51.411  1.00 53.17  ? 669  ASN   D C   1 
ATOM   13187 O  O   . ASN   D  1 368 ? 24.718  11.899  -51.141  1.00 46.32  ? 669  ASN   D O   1 
ATOM   13188 C  CB  . ASN   D  1 368 ? 27.855  13.061  -50.696  1.00 62.89  ? 669  ASN   D CB  1 
ATOM   13189 C  CG  . ASN   D  1 368 ? 27.674  12.234  -49.455  1.00 59.39  ? 669  ASN   D CG  1 
ATOM   13190 O  OD1 . ASN   D  1 368 ? 27.706  10.998  -49.504  1.00 57.39  ? 669  ASN   D OD1 1 
ATOM   13191 N  ND2 . ASN   D  1 368 ? 27.439  12.907  -48.334  1.00 59.24  ? 669  ASN   D ND2 1 
ATOM   13192 N  N   . GLU   D  1 369 ? 25.003  14.133  -51.401  1.00 46.74  ? 670  GLU   D N   1 
ATOM   13193 C  CA  . GLU   D  1 369 ? 23.604  14.448  -51.109  1.00 36.17  ? 670  GLU   D CA  1 
ATOM   13194 C  C   . GLU   D  1 369 ? 22.619  13.798  -52.088  1.00 47.24  ? 670  GLU   D C   1 
ATOM   13195 O  O   . GLU   D  1 369 ? 21.502  13.450  -51.689  1.00 54.73  ? 670  GLU   D O   1 
ATOM   13196 C  CB  . GLU   D  1 369 ? 23.410  15.959  -51.108  1.00 38.47  ? 670  GLU   D CB  1 
ATOM   13197 C  CG  . GLU   D  1 369 ? 24.114  16.639  -49.973  1.00 52.38  ? 670  GLU   D CG  1 
ATOM   13198 C  CD  . GLU   D  1 369 ? 23.358  16.525  -48.673  1.00 44.18  ? 670  GLU   D CD  1 
ATOM   13199 O  OE1 . GLU   D  1 369 ? 22.683  17.505  -48.314  1.00 45.70  ? 670  GLU   D OE1 1 
ATOM   13200 O  OE2 . GLU   D  1 369 ? 23.427  15.457  -48.030  1.00 45.18  ? 670  GLU   D OE2 1 
ATOM   13201 N  N   . TYR   D  1 370 ? 22.973  13.647  -53.369  1.00 46.55  ? 671  TYR   D N   1 
ATOM   13202 C  CA  . TYR   D  1 370 ? 22.031  12.968  -54.255  1.00 53.11  ? 671  TYR   D CA  1 
ATOM   13203 C  C   . TYR   D  1 370 ? 21.974  11.482  -53.941  1.00 65.51  ? 671  TYR   D C   1 
ATOM   13204 O  O   . TYR   D  1 370 ? 20.892  10.885  -53.932  1.00 66.18  ? 671  TYR   D O   1 
ATOM   13205 C  CB  . TYR   D  1 370 ? 22.387  13.199  -55.726  1.00 54.55  ? 671  TYR   D CB  1 
ATOM   13206 C  CG  . TYR   D  1 370 ? 21.804  14.474  -56.292  1.00 50.53  ? 671  TYR   D CG  1 
ATOM   13207 C  CD1 . TYR   D  1 370 ? 22.380  15.695  -56.008  1.00 48.61  ? 671  TYR   D CD1 1 
ATOM   13208 C  CD2 . TYR   D  1 370 ? 20.683  14.453  -57.113  1.00 53.16  ? 671  TYR   D CD2 1 
ATOM   13209 C  CE1 . TYR   D  1 370 ? 21.859  16.863  -56.511  1.00 53.77  ? 671  TYR   D CE1 1 
ATOM   13210 C  CE2 . TYR   D  1 370 ? 20.153  15.626  -57.629  1.00 49.68  ? 671  TYR   D CE2 1 
ATOM   13211 C  CZ  . TYR   D  1 370 ? 20.745  16.827  -57.315  1.00 49.56  ? 671  TYR   D CZ  1 
ATOM   13212 O  OH  . TYR   D  1 370 ? 20.235  17.998  -57.804  1.00 43.24  ? 671  TYR   D OH  1 
ATOM   13213 N  N   . ARG   D  1 371 ? 23.129  10.873  -53.665  1.00 74.71  ? 672  ARG   D N   1 
ATOM   13214 C  CA  . ARG   D  1 371 ? 23.166  9.450   -53.350  1.00 77.17  ? 672  ARG   D CA  1 
ATOM   13215 C  C   . ARG   D  1 371 ? 22.309  9.126   -52.127  1.00 80.97  ? 672  ARG   D C   1 
ATOM   13216 O  O   . ARG   D  1 371 ? 21.404  8.284   -52.194  1.00 93.54  ? 672  ARG   D O   1 
ATOM   13217 C  CB  . ARG   D  1 371 ? 24.613  9.010   -53.131  1.00 91.30  ? 672  ARG   D CB  1 
ATOM   13218 C  CG  . ARG   D  1 371 ? 24.840  7.511   -53.255  1.00 107.49 ? 672  ARG   D CG  1 
ATOM   13219 C  CD  . ARG   D  1 371 ? 26.306  7.133   -53.030  1.00 119.59 ? 672  ARG   D CD  1 
ATOM   13220 N  NE  . ARG   D  1 371 ? 27.237  7.906   -53.861  1.00 123.41 ? 672  ARG   D NE  1 
ATOM   13221 C  CZ  . ARG   D  1 371 ? 28.152  8.750   -53.383  1.00 120.36 ? 672  ARG   D CZ  1 
ATOM   13222 N  NH1 . ARG   D  1 371 ? 28.271  8.931   -52.071  1.00 118.97 ? 672  ARG   D NH1 1 
ATOM   13223 N  NH2 . ARG   D  1 371 ? 28.955  9.408   -54.216  1.00 115.15 ? 672  ARG   D NH2 1 
ATOM   13224 N  N   . CYS   D  1 372 ? 22.556  9.805   -51.006  1.00 70.13  ? 673  CYS   D N   1 
ATOM   13225 C  CA  . CYS   D  1 372 ? 21.956  9.409   -49.738  1.00 67.73  ? 673  CYS   D CA  1 
ATOM   13226 C  C   . CYS   D  1 372 ? 20.673  10.159  -49.391  1.00 66.88  ? 673  CYS   D C   1 
ATOM   13227 O  O   . CYS   D  1 372 ? 19.841  9.622   -48.655  1.00 69.24  ? 673  CYS   D O   1 
ATOM   13228 C  CB  . CYS   D  1 372 ? 22.974  9.586   -48.604  1.00 62.06  ? 673  CYS   D CB  1 
ATOM   13229 S  SG  . CYS   D  1 372 ? 23.199  11.286  -48.023  1.00 67.43  ? 673  CYS   D SG  1 
ATOM   13230 N  N   . ARG   D  1 373 ? 20.486  11.383  -49.890  1.00 61.59  ? 674  ARG   D N   1 
ATOM   13231 C  CA  . ARG   D  1 373 ? 19.294  12.171  -49.589  1.00 50.19  ? 674  ARG   D CA  1 
ATOM   13232 C  C   . ARG   D  1 373 ? 18.340  12.331  -50.767  1.00 54.39  ? 674  ARG   D C   1 
ATOM   13233 O  O   . ARG   D  1 373 ? 17.169  12.671  -50.554  1.00 49.30  ? 674  ARG   D O   1 
ATOM   13234 C  CB  . ARG   D  1 373 ? 19.690  13.572  -49.094  1.00 38.50  ? 674  ARG   D CB  1 
ATOM   13235 C  CG  . ARG   D  1 373 ? 18.586  14.337  -48.345  1.00 36.27  ? 674  ARG   D CG  1 
ATOM   13236 C  CD  . ARG   D  1 373 ? 18.972  15.796  -48.087  1.00 37.26  ? 674  ARG   D CD  1 
ATOM   13237 N  NE  . ARG   D  1 373 ? 18.006  16.479  -47.228  1.00 36.40  ? 674  ARG   D NE  1 
ATOM   13238 C  CZ  . ARG   D  1 373 ? 17.957  17.801  -47.081  1.00 44.57  ? 674  ARG   D CZ  1 
ATOM   13239 N  NH1 . ARG   D  1 373 ? 18.800  18.566  -47.755  1.00 53.62  ? 674  ARG   D NH1 1 
ATOM   13240 N  NH2 . ARG   D  1 373 ? 17.074  18.365  -46.271  1.00 46.90  ? 674  ARG   D NH2 1 
ATOM   13241 N  N   . GLY   D  1 374 ? 18.795  12.107  -51.995  1.00 51.18  ? 675  GLY   D N   1 
ATOM   13242 C  CA  . GLY   D  1 374 ? 17.912  12.243  -53.132  1.00 58.16  ? 675  GLY   D CA  1 
ATOM   13243 C  C   . GLY   D  1 374 ? 17.880  13.620  -53.742  1.00 56.61  ? 675  GLY   D C   1 
ATOM   13244 O  O   . GLY   D  1 374 ? 16.935  13.942  -54.471  1.00 55.54  ? 675  GLY   D O   1 
ATOM   13245 N  N   . GLY   D  1 375 ? 18.878  14.434  -53.477  1.00 50.72  ? 676  GLY   D N   1 
ATOM   13246 C  CA  . GLY   D  1 375 ? 18.942  15.752  -54.067  1.00 56.23  ? 676  GLY   D CA  1 
ATOM   13247 C  C   . GLY   D  1 375 ? 19.663  16.706  -53.140  1.00 53.24  ? 676  GLY   D C   1 
ATOM   13248 O  O   . GLY   D  1 375 ? 20.122  16.340  -52.061  1.00 55.96  ? 676  GLY   D O   1 
ATOM   13249 N  N   . CYS   D  1 376 ? 19.741  17.944  -53.593  1.00 43.19  ? 677  CYS   D N   1 
ATOM   13250 C  CA  . CYS   D  1 376 ? 20.407  19.000  -52.864  1.00 43.13  ? 677  CYS   D CA  1 
ATOM   13251 C  C   . CYS   D  1 376 ? 20.086  20.327  -53.543  1.00 51.04  ? 677  CYS   D C   1 
ATOM   13252 O  O   . CYS   D  1 376 ? 20.630  20.633  -54.608  1.00 55.94  ? 677  CYS   D O   1 
ATOM   13253 C  CB  . CYS   D  1 376 ? 21.907  18.738  -52.816  1.00 38.74  ? 677  CYS   D CB  1 
ATOM   13254 S  SG  . CYS   D  1 376 ? 22.827  20.124  -52.210  1.00 47.10  ? 677  CYS   D SG  1 
ATOM   13255 N  N   . PRO   D  1 377 ? 19.189  21.130  -52.984  1.00 44.94  ? 678  PRO   D N   1 
ATOM   13256 C  CA  . PRO   D  1 377 ? 18.839  22.392  -53.640  1.00 44.45  ? 678  PRO   D CA  1 
ATOM   13257 C  C   . PRO   D  1 377 ? 20.018  23.359  -53.646  1.00 48.81  ? 678  PRO   D C   1 
ATOM   13258 O  O   . PRO   D  1 377 ? 20.649  23.602  -52.616  1.00 51.52  ? 678  PRO   D O   1 
ATOM   13259 C  CB  . PRO   D  1 377 ? 17.673  22.912  -52.794  1.00 50.13  ? 678  PRO   D CB  1 
ATOM   13260 C  CG  . PRO   D  1 377 ? 17.897  22.301  -51.435  1.00 40.42  ? 678  PRO   D CG  1 
ATOM   13261 C  CD  . PRO   D  1 377 ? 18.432  20.922  -51.736  1.00 42.55  ? 678  PRO   D CD  1 
ATOM   13262 N  N   . ALA   D  1 378 ? 20.305  23.918  -54.821  1.00 52.12  ? 679  ALA   D N   1 
ATOM   13263 C  CA  . ALA   D  1 378 ? 21.451  24.799  -55.008  1.00 42.63  ? 679  ALA   D CA  1 
ATOM   13264 C  C   . ALA   D  1 378 ? 21.088  25.930  -55.960  1.00 43.26  ? 679  ALA   D C   1 
ATOM   13265 O  O   . ALA   D  1 378 ? 20.240  25.781  -56.848  1.00 40.87  ? 679  ALA   D O   1 
ATOM   13266 C  CB  . ALA   D  1 378 ? 22.670  24.037  -55.547  1.00 35.37  ? 679  ALA   D CB  1 
ATOM   13267 N  N   . ASP   D  1 379 ? 21.764  27.058  -55.772  1.00 40.09  ? 680  ASP   D N   1 
ATOM   13268 C  CA  . ASP   D  1 379 ? 21.458  28.338  -56.412  1.00 38.99  ? 680  ASP   D CA  1 
ATOM   13269 C  C   . ASP   D  1 379 ? 22.730  28.754  -57.146  1.00 47.50  ? 680  ASP   D C   1 
ATOM   13270 O  O   . ASP   D  1 379 ? 23.574  29.460  -56.581  1.00 49.84  ? 680  ASP   D O   1 
ATOM   13271 C  CB  . ASP   D  1 379 ? 21.025  29.371  -55.342  1.00 40.08  ? 680  ASP   D CB  1 
ATOM   13272 C  CG  . ASP   D  1 379 ? 20.531  30.676  -55.920  1.00 42.55  ? 680  ASP   D CG  1 
ATOM   13273 O  OD1 . ASP   D  1 379 ? 19.569  31.223  -55.346  1.00 46.07  ? 680  ASP   D OD1 1 
ATOM   13274 O  OD2 . ASP   D  1 379 ? 21.097  31.163  -56.919  1.00 49.46  ? 680  ASP   D OD2 1 
ATOM   13275 N  N   . TRP   D  1 380 ? 22.872  28.277  -58.389  1.00 52.61  ? 681  TRP   D N   1 
ATOM   13276 C  CA  . TRP   D  1 380 ? 23.995  28.562  -59.282  1.00 34.63  ? 681  TRP   D CA  1 
ATOM   13277 C  C   . TRP   D  1 380 ? 24.426  30.031  -59.217  1.00 27.10  ? 681  TRP   D C   1 
ATOM   13278 O  O   . TRP   D  1 380 ? 25.618  30.337  -59.229  1.00 34.13  ? 681  TRP   D O   1 
ATOM   13279 C  CB  . TRP   D  1 380 ? 23.593  28.182  -60.722  1.00 39.91  ? 681  TRP   D CB  1 
ATOM   13280 C  CG  . TRP   D  1 380 ? 24.747  28.030  -61.684  1.00 33.07  ? 681  TRP   D CG  1 
ATOM   13281 C  CD1 . TRP   D  1 380 ? 25.384  26.865  -62.024  1.00 29.74  ? 681  TRP   D CD1 1 
ATOM   13282 C  CD2 . TRP   D  1 380 ? 25.434  29.078  -62.379  1.00 27.59  ? 681  TRP   D CD2 1 
ATOM   13283 N  NE1 . TRP   D  1 380 ? 26.418  27.130  -62.892  1.00 38.53  ? 681  TRP   D NE1 1 
ATOM   13284 C  CE2 . TRP   D  1 380 ? 26.461  28.478  -63.138  1.00 30.25  ? 681  TRP   D CE2 1 
ATOM   13285 C  CE3 . TRP   D  1 380 ? 25.270  30.459  -62.446  1.00 26.64  ? 681  TRP   D CE3 1 
ATOM   13286 C  CZ2 . TRP   D  1 380 ? 27.325  29.214  -63.946  1.00 31.77  ? 681  TRP   D CZ2 1 
ATOM   13287 C  CZ3 . TRP   D  1 380 ? 26.113  31.187  -63.261  1.00 33.35  ? 681  TRP   D CZ3 1 
ATOM   13288 C  CH2 . TRP   D  1 380 ? 27.136  30.566  -63.997  1.00 34.08  ? 681  TRP   D CH2 1 
ATOM   13289 N  N   . VAL   D  1 381 ? 23.457  30.949  -59.198  1.00 31.25  ? 682  VAL   D N   1 
ATOM   13290 C  CA  . VAL   D  1 381 ? 23.741  32.384  -59.224  1.00 27.59  ? 682  VAL   D CA  1 
ATOM   13291 C  C   . VAL   D  1 381 ? 24.575  32.790  -58.020  1.00 42.79  ? 682  VAL   D C   1 
ATOM   13292 O  O   . VAL   D  1 381 ? 25.314  33.785  -58.060  1.00 48.45  ? 682  VAL   D O   1 
ATOM   13293 C  CB  . VAL   D  1 381 ? 22.404  33.165  -59.288  1.00 27.89  ? 682  VAL   D CB  1 
ATOM   13294 C  CG1 . VAL   D  1 381 ? 22.634  34.651  -59.181  1.00 30.11  ? 682  VAL   D CG1 1 
ATOM   13295 C  CG2 . VAL   D  1 381 ? 21.638  32.828  -60.563  1.00 36.76  ? 682  VAL   D CG2 1 
ATOM   13296 N  N   . TRP   D  1 382 ? 24.462  32.039  -56.930  1.00 49.54  ? 683  TRP   D N   1 
ATOM   13297 C  CA  . TRP   D  1 382 ? 25.193  32.270  -55.695  1.00 45.74  ? 683  TRP   D CA  1 
ATOM   13298 C  C   . TRP   D  1 382 ? 26.341  31.293  -55.475  1.00 48.73  ? 683  TRP   D C   1 
ATOM   13299 O  O   . TRP   D  1 382 ? 27.382  31.701  -54.948  1.00 47.33  ? 683  TRP   D O   1 
ATOM   13300 C  CB  . TRP   D  1 382 ? 24.225  32.197  -54.509  1.00 45.48  ? 683  TRP   D CB  1 
ATOM   13301 C  CG  . TRP   D  1 382 ? 23.409  33.439  -54.343  1.00 51.43  ? 683  TRP   D CG  1 
ATOM   13302 C  CD1 . TRP   D  1 382 ? 22.470  33.929  -55.198  1.00 52.68  ? 683  TRP   D CD1 1 
ATOM   13303 C  CD2 . TRP   D  1 382 ? 23.479  34.361  -53.253  1.00 54.59  ? 683  TRP   D CD2 1 
ATOM   13304 N  NE1 . TRP   D  1 382 ? 21.952  35.102  -54.712  1.00 52.24  ? 683  TRP   D NE1 1 
ATOM   13305 C  CE2 . TRP   D  1 382 ? 22.549  35.384  -53.512  1.00 52.92  ? 683  TRP   D CE2 1 
ATOM   13306 C  CE3 . TRP   D  1 382 ? 24.234  34.414  -52.074  1.00 47.53  ? 683  TRP   D CE3 1 
ATOM   13307 C  CZ2 . TRP   D  1 382 ? 22.361  36.452  -52.645  1.00 55.73  ? 683  TRP   D CZ2 1 
ATOM   13308 C  CZ3 . TRP   D  1 382 ? 24.040  35.472  -51.208  1.00 49.11  ? 683  TRP   D CZ3 1 
ATOM   13309 C  CH2 . TRP   D  1 382 ? 23.115  36.479  -51.500  1.00 54.85  ? 683  TRP   D CH2 1 
ATOM   13310 N  N   . ILE   D  1 383 ? 26.188  30.020  -55.879  1.00 36.97  ? 684  ILE   D N   1 
ATOM   13311 C  CA  . ILE   D  1 383 ? 27.261  29.038  -55.691  1.00 28.08  ? 684  ILE   D CA  1 
ATOM   13312 C  C   . ILE   D  1 383 ? 28.507  29.433  -56.473  1.00 32.69  ? 684  ILE   D C   1 
ATOM   13313 O  O   . ILE   D  1 383 ? 29.629  29.231  -56.008  1.00 42.88  ? 684  ILE   D O   1 
ATOM   13314 C  CB  . ILE   D  1 383 ? 26.789  27.628  -56.090  1.00 22.90  ? 684  ILE   D CB  1 
ATOM   13315 C  CG1 . ILE   D  1 383 ? 25.617  27.188  -55.223  1.00 27.60  ? 684  ILE   D CG1 1 
ATOM   13316 C  CG2 . ILE   D  1 383 ? 27.911  26.623  -55.891  1.00 22.20  ? 684  ILE   D CG2 1 
ATOM   13317 C  CD1 . ILE   D  1 383 ? 25.824  27.511  -53.773  1.00 33.18  ? 684  ILE   D CD1 1 
ATOM   13318 N  N   . VAL   D  1 384 ? 28.337  29.987  -57.670  1.00 38.43  ? 685  VAL   D N   1 
ATOM   13319 C  CA  . VAL   D  1 384 ? 29.488  30.294  -58.530  1.00 37.75  ? 685  VAL   D CA  1 
ATOM   13320 C  C   . VAL   D  1 384 ? 30.276  31.461  -57.932  1.00 40.82  ? 685  VAL   D C   1 
ATOM   13321 O  O   . VAL   D  1 384 ? 29.678  32.480  -57.540  1.00 42.73  ? 685  VAL   D O   1 
ATOM   13322 C  CB  . VAL   D  1 384 ? 29.011  30.580  -59.964  1.00 37.54  ? 685  VAL   D CB  1 
ATOM   13323 C  CG1 . VAL   D  1 384 ? 30.167  30.788  -60.928  1.00 24.97  ? 685  VAL   D CG1 1 
ATOM   13324 C  CG2 . VAL   D  1 384 ? 28.252  29.393  -60.456  1.00 44.90  ? 685  VAL   D CG2 1 
ATOM   13325 N  N   . PRO   D  1 385 ? 31.593  31.334  -57.775  1.00 38.23  ? 686  PRO   D N   1 
ATOM   13326 C  CA  . PRO   D  1 385 ? 32.367  32.414  -57.173  1.00 32.99  ? 686  PRO   D CA  1 
ATOM   13327 C  C   . PRO   D  1 385 ? 32.289  33.667  -58.018  1.00 43.20  ? 686  PRO   D C   1 
ATOM   13328 O  O   . PRO   D  1 385 ? 32.145  33.593  -59.250  1.00 56.89  ? 686  PRO   D O   1 
ATOM   13329 C  CB  . PRO   D  1 385 ? 33.795  31.852  -57.144  1.00 38.09  ? 686  PRO   D CB  1 
ATOM   13330 C  CG  . PRO   D  1 385 ? 33.613  30.379  -57.126  1.00 36.85  ? 686  PRO   D CG  1 
ATOM   13331 C  CD  . PRO   D  1 385 ? 32.367  30.089  -57.889  1.00 42.67  ? 686  PRO   D CD  1 
ATOM   13332 N  N   . PRO   D  1 386 ? 32.442  34.853  -57.402  1.00 46.95  ? 687  PRO   D N   1 
ATOM   13333 C  CA  . PRO   D  1 386 ? 32.265  36.107  -58.154  1.00 40.18  ? 687  PRO   D CA  1 
ATOM   13334 C  C   . PRO   D  1 386 ? 33.452  36.506  -59.027  1.00 48.21  ? 687  PRO   D C   1 
ATOM   13335 O  O   . PRO   D  1 386 ? 33.555  37.668  -59.442  1.00 55.54  ? 687  PRO   D O   1 
ATOM   13336 C  CB  . PRO   D  1 386 ? 32.046  37.132  -57.041  1.00 39.75  ? 687  PRO   D CB  1 
ATOM   13337 C  CG  . PRO   D  1 386 ? 32.909  36.610  -55.921  1.00 30.60  ? 687  PRO   D CG  1 
ATOM   13338 C  CD  . PRO   D  1 386 ? 32.905  35.099  -56.024  1.00 34.87  ? 687  PRO   D CD  1 
ATOM   13339 N  N   . MET   D  1 387 ? 34.372  35.575  -59.280  1.00 41.24  ? 688  MET   D N   1 
ATOM   13340 C  CA  . MET   D  1 387 ? 35.557  35.826  -60.088  1.00 38.95  ? 688  MET   D CA  1 
ATOM   13341 C  C   . MET   D  1 387 ? 36.064  34.468  -60.522  1.00 44.53  ? 688  MET   D C   1 
ATOM   13342 O  O   . MET   D  1 387 ? 35.890  33.497  -59.792  1.00 41.87  ? 688  MET   D O   1 
ATOM   13343 C  CB  . MET   D  1 387 ? 36.660  36.572  -59.329  1.00 48.37  ? 688  MET   D CB  1 
ATOM   13344 C  CG  . MET   D  1 387 ? 37.341  35.747  -58.239  1.00 52.96  ? 688  MET   D CG  1 
ATOM   13345 S  SD  . MET   D  1 387 ? 39.014  36.310  -57.830  1.00 52.35  ? 688  MET   D SD  1 
ATOM   13346 C  CE  . MET   D  1 387 ? 39.956  35.902  -59.300  1.00 55.74  ? 688  MET   D CE  1 
ATOM   13347 N  N   . SER   D  1 388 ? 36.649  34.399  -61.718  1.00 46.50  ? 689  SER   D N   1 
ATOM   13348 C  CA  . SER   D  1 388 ? 37.169  33.140  -62.254  1.00 43.28  ? 689  SER   D CA  1 
ATOM   13349 C  C   . SER   D  1 388 ? 36.121  32.022  -62.231  1.00 44.63  ? 689  SER   D C   1 
ATOM   13350 O  O   . SER   D  1 388 ? 36.442  30.856  -61.980  1.00 52.83  ? 689  SER   D O   1 
ATOM   13351 C  CB  . SER   D  1 388 ? 38.419  32.700  -61.491  1.00 42.23  ? 689  SER   D CB  1 
ATOM   13352 O  OG  . SER   D  1 388 ? 39.443  33.660  -61.629  1.00 48.36  ? 689  SER   D OG  1 
ATOM   13353 N  N   . GLY   D  1 389 ? 34.860  32.373  -62.497  1.00 39.49  ? 690  GLY   D N   1 
ATOM   13354 C  CA  . GLY   D  1 389 ? 33.759  31.428  -62.472  1.00 38.02  ? 690  GLY   D CA  1 
ATOM   13355 C  C   . GLY   D  1 389 ? 33.922  30.123  -63.247  1.00 56.10  ? 690  GLY   D C   1 
ATOM   13356 O  O   . GLY   D  1 389 ? 33.779  29.047  -62.654  1.00 64.28  ? 690  GLY   D O   1 
ATOM   13357 N  N   . SER   D  1 390 ? 34.205  30.178  -64.563  1.00 43.05  ? 691  SER   D N   1 
ATOM   13358 C  CA  . SER   D  1 390 ? 34.161  28.959  -65.371  1.00 50.49  ? 691  SER   D CA  1 
ATOM   13359 C  C   . SER   D  1 390 ? 35.371  28.044  -65.194  1.00 45.80  ? 691  SER   D C   1 
ATOM   13360 O  O   . SER   D  1 390 ? 35.332  26.902  -65.672  1.00 44.23  ? 691  SER   D O   1 
ATOM   13361 C  CB  . SER   D  1 390 ? 33.989  29.276  -66.873  1.00 56.20  ? 691  SER   D CB  1 
ATOM   13362 O  OG  . SER   D  1 390 ? 35.201  29.642  -67.516  1.00 48.53  ? 691  SER   D OG  1 
ATOM   13363 N  N   . ILE   D  1 391 ? 36.441  28.495  -64.530  1.00 46.03  ? 692  ILE   D N   1 
ATOM   13364 C  CA  . ILE   D  1 391 ? 37.538  27.595  -64.191  1.00 48.70  ? 692  ILE   D CA  1 
ATOM   13365 C  C   . ILE   D  1 391 ? 37.351  26.903  -62.840  1.00 45.18  ? 692  ILE   D C   1 
ATOM   13366 O  O   . ILE   D  1 391 ? 38.251  26.171  -62.401  1.00 44.42  ? 692  ILE   D O   1 
ATOM   13367 C  CB  . ILE   D  1 391 ? 38.892  28.326  -64.201  1.00 49.53  ? 692  ILE   D CB  1 
ATOM   13368 C  CG1 . ILE   D  1 391 ? 39.067  29.152  -62.944  1.00 41.89  ? 692  ILE   D CG1 1 
ATOM   13369 C  CG2 . ILE   D  1 391 ? 39.010  29.218  -65.411  1.00 42.82  ? 692  ILE   D CG2 1 
ATOM   13370 C  CD1 . ILE   D  1 391 ? 40.357  29.936  -62.984  1.00 45.90  ? 692  ILE   D CD1 1 
ATOM   13371 N  N   . THR   D  1 392 ? 36.188  27.099  -62.162  1.00 45.10  ? 693  THR   D N   1 
ATOM   13372 C  CA  . THR   D  1 392 ? 35.805  26.284  -61.014  1.00 47.27  ? 693  THR   D CA  1 
ATOM   13373 C  C   . THR   D  1 392 ? 34.725  25.298  -61.427  1.00 46.66  ? 693  THR   D C   1 
ATOM   13374 O  O   . THR   D  1 392 ? 33.894  25.612  -62.281  1.00 54.16  ? 693  THR   D O   1 
ATOM   13375 C  CB  . THR   D  1 392 ? 35.269  27.140  -59.867  1.00 48.14  ? 693  THR   D CB  1 
ATOM   13376 O  OG1 . THR   D  1 392 ? 34.043  27.742  -60.281  1.00 47.10  ? 693  THR   D OG1 1 
ATOM   13377 C  CG2 . THR   D  1 392 ? 36.261  28.220  -59.480  1.00 40.33  ? 693  THR   D CG2 1 
ATOM   13378 N  N   . PRO   D  1 393 ? 34.696  24.102  -60.832  1.00 43.94  ? 694  PRO   D N   1 
ATOM   13379 C  CA  . PRO   D  1 393 ? 33.800  23.045  -61.343  1.00 46.89  ? 694  PRO   D CA  1 
ATOM   13380 C  C   . PRO   D  1 393 ? 32.311  23.348  -61.218  1.00 46.23  ? 694  PRO   D C   1 
ATOM   13381 O  O   . PRO   D  1 393 ? 31.537  22.792  -61.996  1.00 46.24  ? 694  PRO   D O   1 
ATOM   13382 C  CB  . PRO   D  1 393 ? 34.178  21.826  -60.493  1.00 41.90  ? 694  PRO   D CB  1 
ATOM   13383 C  CG  . PRO   D  1 393 ? 34.690  22.425  -59.229  1.00 48.77  ? 694  PRO   D CG  1 
ATOM   13384 C  CD  . PRO   D  1 393 ? 35.446  23.657  -59.650  1.00 48.13  ? 694  PRO   D CD  1 
ATOM   13385 N  N   . VAL   D  1 394 ? 31.872  24.189  -60.276  1.00 47.10  ? 695  VAL   D N   1 
ATOM   13386 C  CA  . VAL   D  1 394 ? 30.436  24.415  -60.129  1.00 46.48  ? 695  VAL   D CA  1 
ATOM   13387 C  C   . VAL   D  1 394 ? 29.862  25.089  -61.360  1.00 43.74  ? 695  VAL   D C   1 
ATOM   13388 O  O   . VAL   D  1 394 ? 28.659  24.974  -61.624  1.00 38.34  ? 695  VAL   D O   1 
ATOM   13389 C  CB  . VAL   D  1 394 ? 30.085  25.257  -58.878  1.00 44.70  ? 695  VAL   D CB  1 
ATOM   13390 C  CG1 . VAL   D  1 394 ? 30.250  24.448  -57.598  1.00 40.73  ? 695  VAL   D CG1 1 
ATOM   13391 C  CG2 . VAL   D  1 394 ? 30.886  26.560  -58.832  1.00 35.69  ? 695  VAL   D CG2 1 
ATOM   13392 N  N   . PHE   D  1 395 ? 30.701  25.776  -62.131  1.00 36.57  ? 696  PHE   D N   1 
ATOM   13393 C  CA  . PHE   D  1 395 ? 30.205  26.504  -63.291  1.00 40.47  ? 696  PHE   D CA  1 
ATOM   13394 C  C   . PHE   D  1 395 ? 29.487  25.573  -64.263  1.00 48.05  ? 696  PHE   D C   1 
ATOM   13395 O  O   . PHE   D  1 395 ? 28.400  25.897  -64.764  1.00 42.45  ? 696  PHE   D O   1 
ATOM   13396 C  CB  . PHE   D  1 395 ? 31.368  27.218  -63.973  1.00 42.35  ? 696  PHE   D CB  1 
ATOM   13397 C  CG  . PHE   D  1 395 ? 30.950  28.092  -65.094  1.00 45.72  ? 696  PHE   D CG  1 
ATOM   13398 C  CD1 . PHE   D  1 395 ? 30.698  29.427  -64.877  1.00 45.04  ? 696  PHE   D CD1 1 
ATOM   13399 C  CD2 . PHE   D  1 395 ? 30.800  27.572  -66.378  1.00 52.11  ? 696  PHE   D CD2 1 
ATOM   13400 C  CE1 . PHE   D  1 395 ? 30.296  30.232  -65.922  1.00 47.69  ? 696  PHE   D CE1 1 
ATOM   13401 C  CE2 . PHE   D  1 395 ? 30.389  28.364  -67.415  1.00 43.76  ? 696  PHE   D CE2 1 
ATOM   13402 C  CZ  . PHE   D  1 395 ? 30.146  29.693  -67.193  1.00 47.58  ? 696  PHE   D CZ  1 
ATOM   13403 N  N   . HIS   D  1 396 ? 30.061  24.402  -64.513  1.00 44.93  ? 697  HIS   D N   1 
ATOM   13404 C  CA  . HIS   D  1 396 ? 29.557  23.435  -65.476  1.00 42.36  ? 697  HIS   D CA  1 
ATOM   13405 C  C   . HIS   D  1 396 ? 28.591  22.441  -64.862  1.00 49.85  ? 697  HIS   D C   1 
ATOM   13406 O  O   . HIS   D  1 396 ? 28.240  21.448  -65.518  1.00 49.27  ? 697  HIS   D O   1 
ATOM   13407 C  CB  . HIS   D  1 396 ? 30.744  22.715  -66.095  1.00 43.25  ? 697  HIS   D CB  1 
ATOM   13408 C  CG  . HIS   D  1 396 ? 31.901  23.624  -66.320  1.00 43.97  ? 697  HIS   D CG  1 
ATOM   13409 N  ND1 . HIS   D  1 396 ? 32.084  24.313  -67.498  1.00 43.64  ? 697  HIS   D ND1 1 
ATOM   13410 C  CD2 . HIS   D  1 396 ? 32.886  24.027  -65.487  1.00 47.20  ? 697  HIS   D CD2 1 
ATOM   13411 C  CE1 . HIS   D  1 396 ? 33.154  25.079  -67.390  1.00 49.53  ? 697  HIS   D CE1 1 
ATOM   13412 N  NE2 . HIS   D  1 396 ? 33.660  24.923  -66.179  1.00 48.77  ? 697  HIS   D NE2 1 
ATOM   13413 N  N   . GLN   D  1 397 ? 28.177  22.681  -63.616  1.00 43.59  ? 698  GLN   D N   1 
ATOM   13414 C  CA  . GLN   D  1 397 ? 27.296  21.797  -62.866  1.00 41.64  ? 698  GLN   D CA  1 
ATOM   13415 C  C   . GLN   D  1 397 ? 25.868  22.335  -62.899  1.00 42.44  ? 698  GLN   D C   1 
ATOM   13416 O  O   . GLN   D  1 397 ? 25.600  23.442  -62.421  1.00 46.86  ? 698  GLN   D O   1 
ATOM   13417 C  CB  . GLN   D  1 397 ? 27.762  21.668  -61.416  1.00 37.50  ? 698  GLN   D CB  1 
ATOM   13418 C  CG  . GLN   D  1 397 ? 26.770  20.895  -60.579  1.00 38.45  ? 698  GLN   D CG  1 
ATOM   13419 C  CD  . GLN   D  1 397 ? 26.713  19.441  -60.971  1.00 45.38  ? 698  GLN   D CD  1 
ATOM   13420 O  OE1 . GLN   D  1 397 ? 27.745  18.754  -61.009  1.00 43.56  ? 698  GLN   D OE1 1 
ATOM   13421 N  NE2 . GLN   D  1 397 ? 25.510  18.956  -61.277  1.00 46.97  ? 698  GLN   D NE2 1 
ATOM   13422 N  N   . GLU   D  1 398 ? 24.956  21.550  -63.448  1.00 42.75  ? 699  GLU   D N   1 
ATOM   13423 C  CA  . GLU   D  1 398 ? 23.554  21.921  -63.409  1.00 45.43  ? 699  GLU   D CA  1 
ATOM   13424 C  C   . GLU   D  1 398 ? 23.024  21.722  -62.000  1.00 45.98  ? 699  GLU   D C   1 
ATOM   13425 O  O   . GLU   D  1 398 ? 23.328  20.713  -61.349  1.00 38.90  ? 699  GLU   D O   1 
ATOM   13426 C  CB  . GLU   D  1 398 ? 22.755  21.075  -64.403  1.00 43.31  ? 699  GLU   D CB  1 
ATOM   13427 C  CG  . GLU   D  1 398 ? 22.594  21.707  -65.775  1.00 35.53  ? 699  GLU   D CG  1 
ATOM   13428 C  CD  . GLU   D  1 398 ? 22.002  20.744  -66.788  1.00 44.50  ? 699  GLU   D CD  1 
ATOM   13429 O  OE1 . GLU   D  1 398 ? 21.916  21.106  -67.991  1.00 49.24  ? 699  GLU   D OE1 1 
ATOM   13430 O  OE2 . GLU   D  1 398 ? 21.628  19.624  -66.396  1.00 43.61  ? 699  GLU   D OE2 1 
ATOM   13431 N  N   . MET   D  1 399 ? 22.235  22.694  -61.525  1.00 47.78  ? 700  MET   D N   1 
ATOM   13432 C  CA  . MET   D  1 399 ? 21.683  22.668  -60.168  1.00 48.34  ? 700  MET   D CA  1 
ATOM   13433 C  C   . MET   D  1 399 ? 20.203  23.011  -60.180  1.00 50.64  ? 700  MET   D C   1 
ATOM   13434 O  O   . MET   D  1 399 ? 19.795  24.011  -60.781  1.00 64.78  ? 700  MET   D O   1 
ATOM   13435 C  CB  . MET   D  1 399 ? 22.395  23.652  -59.235  1.00 39.07  ? 700  MET   D CB  1 
ATOM   13436 C  CG  . MET   D  1 399 ? 23.908  23.530  -59.166  1.00 43.99  ? 700  MET   D CG  1 
ATOM   13437 S  SD  . MET   D  1 399 ? 24.612  25.112  -58.670  1.00 51.33  ? 700  MET   D SD  1 
ATOM   13438 C  CE  . MET   D  1 399 ? 26.381  24.745  -58.671  1.00 31.76  ? 700  MET   D CE  1 
ATOM   13439 N  N   . LEU   D  1 400 ? 19.413  22.191  -59.496  1.00 46.40  ? 701  LEU   D N   1 
ATOM   13440 C  CA  . LEU   D  1 400 ? 17.999  22.458  -59.265  1.00 50.48  ? 701  LEU   D CA  1 
ATOM   13441 C  C   . LEU   D  1 400 ? 17.821  23.243  -57.971  1.00 52.32  ? 701  LEU   D C   1 
ATOM   13442 O  O   . LEU   D  1 400 ? 18.474  22.953  -56.954  1.00 34.17  ? 701  LEU   D O   1 
ATOM   13443 C  CB  . LEU   D  1 400 ? 17.207  21.149  -59.181  1.00 42.57  ? 701  LEU   D CB  1 
ATOM   13444 C  CG  . LEU   D  1 400 ? 17.073  20.375  -60.478  1.00 45.93  ? 701  LEU   D CG  1 
ATOM   13445 C  CD1 . LEU   D  1 400 ? 16.419  19.077  -60.155  1.00 50.52  ? 701  LEU   D CD1 1 
ATOM   13446 C  CD2 . LEU   D  1 400 ? 16.252  21.173  -61.476  1.00 46.73  ? 701  LEU   D CD2 1 
ATOM   13447 N  N   . ASN   D  1 401 ? 16.932  24.237  -58.015  1.00 50.45  ? 702  ASN   D N   1 
ATOM   13448 C  CA  . ASN   D  1 401 ? 16.712  25.156  -56.907  1.00 51.61  ? 702  ASN   D CA  1 
ATOM   13449 C  C   . ASN   D  1 401 ? 15.286  24.997  -56.404  1.00 52.95  ? 702  ASN   D C   1 
ATOM   13450 O  O   . ASN   D  1 401 ? 14.343  24.994  -57.201  1.00 51.23  ? 702  ASN   D O   1 
ATOM   13451 C  CB  . ASN   D  1 401 ? 16.970  26.607  -57.322  1.00 45.16  ? 702  ASN   D CB  1 
ATOM   13452 C  CG  . ASN   D  1 401 ? 17.181  27.517  -56.138  1.00 44.50  ? 702  ASN   D CG  1 
ATOM   13453 O  OD1 . ASN   D  1 401 ? 17.549  27.064  -55.070  1.00 53.14  ? 702  ASN   D OD1 1 
ATOM   13454 N  ND2 . ASN   D  1 401 ? 16.944  28.804  -56.318  1.00 44.29  ? 702  ASN   D ND2 1 
ATOM   13455 N  N   . TYR   D  1 402 ? 15.138  24.852  -55.085  1.00 44.40  ? 703  TYR   D N   1 
ATOM   13456 C  CA  . TYR   D  1 402 ? 13.839  24.697  -54.440  1.00 43.98  ? 703  TYR   D CA  1 
ATOM   13457 C  C   . TYR   D  1 402 ? 14.027  24.855  -52.938  1.00 53.89  ? 703  TYR   D C   1 
ATOM   13458 O  O   . TYR   D  1 402 ? 15.137  24.721  -52.417  1.00 52.48  ? 703  TYR   D O   1 
ATOM   13459 C  CB  . TYR   D  1 402 ? 13.178  23.353  -54.771  1.00 41.57  ? 703  TYR   D CB  1 
ATOM   13460 C  CG  . TYR   D  1 402 ? 14.074  22.141  -54.635  1.00 45.14  ? 703  TYR   D CG  1 
ATOM   13461 C  CD1 . TYR   D  1 402 ? 14.154  21.440  -53.446  1.00 52.13  ? 703  TYR   D CD1 1 
ATOM   13462 C  CD2 . TYR   D  1 402 ? 14.817  21.681  -55.710  1.00 49.72  ? 703  TYR   D CD2 1 
ATOM   13463 C  CE1 . TYR   D  1 402 ? 14.971  20.314  -53.317  1.00 51.59  ? 703  TYR   D CE1 1 
ATOM   13464 C  CE2 . TYR   D  1 402 ? 15.631  20.559  -55.594  1.00 53.87  ? 703  TYR   D CE2 1 
ATOM   13465 C  CZ  . TYR   D  1 402 ? 15.702  19.879  -54.395  1.00 54.39  ? 703  TYR   D CZ  1 
ATOM   13466 O  OH  . TYR   D  1 402 ? 16.515  18.768  -54.291  1.00 48.62  ? 703  TYR   D OH  1 
ATOM   13467 N  N   . ARG   D  1 403 ? 12.921  25.142  -52.252  1.00 55.65  ? 704  ARG   D N   1 
ATOM   13468 C  CA  . ARG   D  1 403 ? 12.943  25.638  -50.882  1.00 49.77  ? 704  ARG   D CA  1 
ATOM   13469 C  C   . ARG   D  1 403 ? 12.408  24.554  -49.946  1.00 51.75  ? 704  ARG   D C   1 
ATOM   13470 O  O   . ARG   D  1 403 ? 11.193  24.404  -49.791  1.00 50.59  ? 704  ARG   D O   1 
ATOM   13471 C  CB  . ARG   D  1 403 ? 12.129  26.927  -50.782  1.00 51.84  ? 704  ARG   D CB  1 
ATOM   13472 C  CG  . ARG   D  1 403 ? 12.244  27.623  -49.440  1.00 63.59  ? 704  ARG   D CG  1 
ATOM   13473 C  CD  . ARG   D  1 403 ? 12.158  29.125  -49.596  1.00 75.45  ? 704  ARG   D CD  1 
ATOM   13474 N  NE  . ARG   D  1 403 ? 10.878  29.648  -49.125  1.00 85.87  ? 704  ARG   D NE  1 
ATOM   13475 C  CZ  . ARG   D  1 403 ? 10.494  30.917  -49.258  1.00 92.32  ? 704  ARG   D CZ  1 
ATOM   13476 N  NH1 . ARG   D  1 403 ? 11.297  31.792  -49.857  1.00 95.67  ? 704  ARG   D NH1 1 
ATOM   13477 N  NH2 . ARG   D  1 403 ? 9.310   31.313  -48.797  1.00 84.39  ? 704  ARG   D NH2 1 
ATOM   13478 N  N   . LEU   D  1 404 ? 13.321  23.792  -49.342  1.00 41.45  ? 705  LEU   D N   1 
ATOM   13479 C  CA  . LEU   D  1 404 ? 13.003  22.857  -48.273  1.00 47.09  ? 705  LEU   D CA  1 
ATOM   13480 C  C   . LEU   D  1 404 ? 13.004  23.571  -46.926  1.00 47.38  ? 705  LEU   D C   1 
ATOM   13481 O  O   . LEU   D  1 404 ? 13.766  24.517  -46.700  1.00 44.68  ? 705  LEU   D O   1 
ATOM   13482 C  CB  . LEU   D  1 404 ? 14.021  21.735  -48.196  1.00 44.10  ? 705  LEU   D CB  1 
ATOM   13483 C  CG  . LEU   D  1 404 ? 14.388  20.954  -49.430  1.00 42.42  ? 705  LEU   D CG  1 
ATOM   13484 C  CD1 . LEU   D  1 404 ? 15.724  20.305  -49.146  1.00 36.19  ? 705  LEU   D CD1 1 
ATOM   13485 C  CD2 . LEU   D  1 404 ? 13.340  19.910  -49.697  1.00 41.61  ? 705  LEU   D CD2 1 
ATOM   13486 N  N   . THR   D  1 405 ? 12.174  23.082  -46.013  1.00 48.93  ? 706  THR   D N   1 
ATOM   13487 C  CA  . THR   D  1 405 ? 12.206  23.594  -44.651  1.00 47.26  ? 706  THR   D CA  1 
ATOM   13488 C  C   . THR   D  1 405 ? 12.573  22.479  -43.667  1.00 49.66  ? 706  THR   D C   1 
ATOM   13489 O  O   . THR   D  1 405 ? 12.231  21.311  -43.896  1.00 53.32  ? 706  THR   D O   1 
ATOM   13490 C  CB  . THR   D  1 405 ? 10.848  24.210  -44.299  1.00 46.89  ? 706  THR   D CB  1 
ATOM   13491 O  OG1 . THR   D  1 405 ? 11.025  25.214  -43.297  1.00 59.83  ? 706  THR   D OG1 1 
ATOM   13492 C  CG2 . THR   D  1 405 ? 9.855   23.154  -43.835  1.00 31.14  ? 706  THR   D CG2 1 
ATOM   13493 N  N   . PRO   D  1 406 ? 13.274  22.792  -42.553  1.00 49.84  ? 707  PRO   D N   1 
ATOM   13494 C  CA  . PRO   D  1 406 ? 13.688  24.090  -42.011  1.00 45.70  ? 707  PRO   D CA  1 
ATOM   13495 C  C   . PRO   D  1 406 ? 14.576  24.870  -42.956  1.00 45.84  ? 707  PRO   D C   1 
ATOM   13496 O  O   . PRO   D  1 406 ? 15.251  24.256  -43.777  1.00 45.04  ? 707  PRO   D O   1 
ATOM   13497 C  CB  . PRO   D  1 406 ? 14.459  23.716  -40.739  1.00 42.36  ? 707  PRO   D CB  1 
ATOM   13498 C  CG  . PRO   D  1 406 ? 14.008  22.348  -40.396  1.00 37.05  ? 707  PRO   D CG  1 
ATOM   13499 C  CD  . PRO   D  1 406 ? 13.738  21.681  -41.697  1.00 42.15  ? 707  PRO   D CD  1 
ATOM   13500 N  N   . SER   D  1 407 ? 14.563  26.195  -42.843  1.00 41.91  ? 708  SER   D N   1 
ATOM   13501 C  CA  . SER   D  1 407 ? 15.326  27.029  -43.749  1.00 53.40  ? 708  SER   D CA  1 
ATOM   13502 C  C   . SER   D  1 407 ? 15.655  28.346  -43.068  1.00 43.15  ? 708  SER   D C   1 
ATOM   13503 O  O   . SER   D  1 407 ? 14.955  28.774  -42.152  1.00 49.73  ? 708  SER   D O   1 
ATOM   13504 C  CB  . SER   D  1 407 ? 14.547  27.280  -45.046  1.00 68.03  ? 708  SER   D CB  1 
ATOM   13505 O  OG  . SER   D  1 407 ? 13.356  28.000  -44.782  1.00 71.89  ? 708  SER   D OG  1 
ATOM   13506 N  N   . PHE   D  1 408 ? 16.738  28.982  -43.533  1.00 42.59  ? 709  PHE   D N   1 
ATOM   13507 C  CA  . PHE   D  1 408 ? 17.058  30.364  -43.185  1.00 33.96  ? 709  PHE   D CA  1 
ATOM   13508 C  C   . PHE   D  1 408 ? 16.390  31.292  -44.184  1.00 42.37  ? 709  PHE   D C   1 
ATOM   13509 O  O   . PHE   D  1 408 ? 16.492  31.080  -45.393  1.00 57.98  ? 709  PHE   D O   1 
ATOM   13510 C  CB  . PHE   D  1 408 ? 18.570  30.614  -43.162  1.00 31.79  ? 709  PHE   D CB  1 
ATOM   13511 C  CG  . PHE   D  1 408 ? 19.263  29.948  -42.012  1.00 32.04  ? 709  PHE   D CG  1 
ATOM   13512 C  CD1 . PHE   D  1 408 ? 19.994  28.771  -42.203  1.00 34.04  ? 709  PHE   D CD1 1 
ATOM   13513 C  CD2 . PHE   D  1 408 ? 19.138  30.457  -40.724  1.00 29.88  ? 709  PHE   D CD2 1 
ATOM   13514 C  CE1 . PHE   D  1 408 ? 20.608  28.134  -41.135  1.00 46.66  ? 709  PHE   D CE1 1 
ATOM   13515 C  CE2 . PHE   D  1 408 ? 19.744  29.814  -39.634  1.00 26.32  ? 709  PHE   D CE2 1 
ATOM   13516 C  CZ  . PHE   D  1 408 ? 20.487  28.660  -39.842  1.00 37.23  ? 709  PHE   D CZ  1 
ATOM   13517 N  N   . GLU   D  1 409 ? 15.702  32.303  -43.668  1.00 42.61  ? 710  GLU   D N   1 
ATOM   13518 C  CA  . GLU   D  1 409 ? 14.907  33.242  -44.435  1.00 38.44  ? 710  GLU   D CA  1 
ATOM   13519 C  C   . GLU   D  1 409 ? 15.426  34.643  -44.165  1.00 42.93  ? 710  GLU   D C   1 
ATOM   13520 O  O   . GLU   D  1 409 ? 16.085  34.889  -43.156  1.00 45.68  ? 710  GLU   D O   1 
ATOM   13521 C  CB  . GLU   D  1 409 ? 13.419  33.179  -44.041  1.00 45.30  ? 710  GLU   D CB  1 
ATOM   13522 C  CG  . GLU   D  1 409 ? 12.725  31.832  -44.230  1.00 55.82  ? 710  GLU   D CG  1 
ATOM   13523 C  CD  . GLU   D  1 409 ? 12.389  31.530  -45.684  1.00 69.82  ? 710  GLU   D CD  1 
ATOM   13524 O  OE1 . GLU   D  1 409 ? 12.280  32.485  -46.494  1.00 68.22  ? 710  GLU   D OE1 1 
ATOM   13525 O  OE2 . GLU   D  1 409 ? 12.238  30.330  -46.017  1.00 75.25  ? 710  GLU   D OE2 1 
ATOM   13526 N  N   . TYR   D  1 410 ? 15.098  35.567  -45.065  1.00 44.18  ? 711  TYR   D N   1 
ATOM   13527 C  CA  . TYR   D  1 410 ? 15.338  36.981  -44.839  1.00 42.85  ? 711  TYR   D CA  1 
ATOM   13528 C  C   . TYR   D  1 410 ? 14.209  37.574  -44.008  1.00 48.71  ? 711  TYR   D C   1 
ATOM   13529 O  O   . TYR   D  1 410 ? 13.161  36.961  -43.795  1.00 53.20  ? 711  TYR   D O   1 
ATOM   13530 C  CB  . TYR   D  1 410 ? 15.441  37.731  -46.161  1.00 45.55  ? 711  TYR   D CB  1 
ATOM   13531 C  CG  . TYR   D  1 410 ? 16.646  37.369  -46.984  1.00 50.78  ? 711  TYR   D CG  1 
ATOM   13532 C  CD1 . TYR   D  1 410 ? 16.586  36.366  -47.933  1.00 59.50  ? 711  TYR   D CD1 1 
ATOM   13533 C  CD2 . TYR   D  1 410 ? 17.848  38.027  -46.804  1.00 57.25  ? 711  TYR   D CD2 1 
ATOM   13534 C  CE1 . TYR   D  1 410 ? 17.689  36.039  -48.687  1.00 66.42  ? 711  TYR   D CE1 1 
ATOM   13535 C  CE2 . TYR   D  1 410 ? 18.955  37.699  -47.547  1.00 60.61  ? 711  TYR   D CE2 1 
ATOM   13536 C  CZ  . TYR   D  1 410 ? 18.866  36.713  -48.485  1.00 64.37  ? 711  TYR   D CZ  1 
ATOM   13537 O  OH  . TYR   D  1 410 ? 19.968  36.404  -49.223  1.00 70.02  ? 711  TYR   D OH  1 
ATOM   13538 N  N   . GLN   D  1 411 ? 14.427  38.792  -43.531  1.00 48.06  ? 712  GLN   D N   1 
ATOM   13539 C  CA  . GLN   D  1 411 ? 13.386  39.485  -42.789  1.00 52.59  ? 712  GLN   D CA  1 
ATOM   13540 C  C   . GLN   D  1 411 ? 13.684  40.966  -42.853  1.00 43.12  ? 712  GLN   D C   1 
ATOM   13541 O  O   . GLN   D  1 411 ? 14.834  41.349  -43.084  1.00 60.73  ? 712  GLN   D O   1 
ATOM   13542 C  CB  . GLN   D  1 411 ? 13.312  39.005  -41.327  1.00 58.47  ? 712  GLN   D CB  1 
ATOM   13543 C  CG  . GLN   D  1 411 ? 14.639  39.028  -40.607  1.00 57.68  ? 712  GLN   D CG  1 
ATOM   13544 C  CD  . GLN   D  1 411 ? 14.529  38.661  -39.135  1.00 49.62  ? 712  GLN   D CD  1 
ATOM   13545 O  OE1 . GLN   D  1 411 ? 13.438  38.468  -38.599  1.00 40.10  ? 712  GLN   D OE1 1 
ATOM   13546 N  NE2 . GLN   D  1 411 ? 15.667  38.586  -38.476  1.00 32.39  ? 712  GLN   D NE2 1 
ATOM   13547 N  N   . PRO   D  1 412 ? 12.686  41.817  -42.681  1.00 39.13  ? 713  PRO   D N   1 
ATOM   13548 C  CA  . PRO   D  1 412 ? 12.935  43.258  -42.741  1.00 53.68  ? 713  PRO   D CA  1 
ATOM   13549 C  C   . PRO   D  1 412 ? 13.960  43.732  -41.709  1.00 55.97  ? 713  PRO   D C   1 
ATOM   13550 O  O   . PRO   D  1 412 ? 14.081  43.179  -40.615  1.00 56.95  ? 713  PRO   D O   1 
ATOM   13551 C  CB  . PRO   D  1 412 ? 11.551  43.862  -42.483  1.00 53.45  ? 713  PRO   D CB  1 
ATOM   13552 C  CG  . PRO   D  1 412 ? 10.675  42.703  -42.034  1.00 47.00  ? 713  PRO   D CG  1 
ATOM   13553 C  CD  . PRO   D  1 412 ? 11.250  41.511  -42.691  1.00 41.80  ? 713  PRO   D CD  1 
ATOM   13554 N  N   . ASP   D  1 413 ? 14.722  44.757  -42.099  1.00 59.33  ? 714  ASP   D N   1 
ATOM   13555 C  CA  . ASP   D  1 413 ? 15.584  45.473  -41.174  1.00 52.13  ? 714  ASP   D CA  1 
ATOM   13556 C  C   . ASP   D  1 413 ? 14.747  46.022  -40.019  1.00 55.91  ? 714  ASP   D C   1 
ATOM   13557 O  O   . ASP   D  1 413 ? 13.651  46.550  -40.250  1.00 59.11  ? 714  ASP   D O   1 
ATOM   13558 C  CB  . ASP   D  1 413 ? 16.300  46.628  -41.883  1.00 53.31  ? 714  ASP   D CB  1 
ATOM   13559 C  CG  . ASP   D  1 413 ? 17.312  46.165  -42.918  1.00 59.33  ? 714  ASP   D CG  1 
ATOM   13560 O  OD1 . ASP   D  1 413 ? 17.870  45.052  -42.775  1.00 47.33  ? 714  ASP   D OD1 1 
ATOM   13561 O  OD2 . ASP   D  1 413 ? 17.553  46.933  -43.879  1.00 70.66  ? 714  ASP   D OD2 1 
ATOM   13562 N  N   . PRO   D  1 414 ? 15.240  45.948  -38.777  1.00 47.46  ? 715  PRO   D N   1 
ATOM   13563 C  CA  . PRO   D  1 414 ? 14.387  46.283  -37.631  1.00 47.05  ? 715  PRO   D CA  1 
ATOM   13564 C  C   . PRO   D  1 414 ? 14.029  47.749  -37.558  1.00 58.14  ? 715  PRO   D C   1 
ATOM   13565 O  O   . PRO   D  1 414 ? 12.966  48.089  -37.024  1.00 61.61  ? 715  PRO   D O   1 
ATOM   13566 C  CB  . PRO   D  1 414 ? 15.235  45.860  -36.423  1.00 44.48  ? 715  PRO   D CB  1 
ATOM   13567 C  CG  . PRO   D  1 414 ? 16.401  45.066  -36.987  1.00 44.18  ? 715  PRO   D CG  1 
ATOM   13568 C  CD  . PRO   D  1 414 ? 16.607  45.599  -38.358  1.00 52.83  ? 715  PRO   D CD  1 
ATOM   13569 N  N   . TRP   D  1 415 ? 14.876  48.634  -38.075  1.00 57.46  ? 716  TRP   D N   1 
ATOM   13570 C  CA  . TRP   D  1 415 ? 14.517  50.041  -38.013  1.00 53.97  ? 716  TRP   D CA  1 
ATOM   13571 C  C   . TRP   D  1 415 ? 13.419  50.401  -38.983  1.00 61.33  ? 716  TRP   D C   1 
ATOM   13572 O  O   . TRP   D  1 415 ? 13.033  51.574  -39.042  1.00 63.25  ? 716  TRP   D O   1 
ATOM   13573 C  CB  . TRP   D  1 415 ? 15.737  50.910  -38.274  1.00 57.56  ? 716  TRP   D CB  1 
ATOM   13574 C  CG  . TRP   D  1 415 ? 16.485  50.509  -39.467  1.00 64.95  ? 716  TRP   D CG  1 
ATOM   13575 C  CD1 . TRP   D  1 415 ? 16.272  50.932  -40.743  1.00 69.09  ? 716  TRP   D CD1 1 
ATOM   13576 C  CD2 . TRP   D  1 415 ? 17.590  49.601  -39.521  1.00 64.56  ? 716  TRP   D CD2 1 
ATOM   13577 N  NE1 . TRP   D  1 415 ? 17.178  50.341  -41.595  1.00 61.54  ? 716  TRP   D NE1 1 
ATOM   13578 C  CE2 . TRP   D  1 415 ? 17.996  49.517  -40.869  1.00 62.66  ? 716  TRP   D CE2 1 
ATOM   13579 C  CE3 . TRP   D  1 415 ? 18.273  48.849  -38.565  1.00 58.47  ? 716  TRP   D CE3 1 
ATOM   13580 C  CZ2 . TRP   D  1 415 ? 19.054  48.714  -41.282  1.00 55.73  ? 716  TRP   D CZ2 1 
ATOM   13581 C  CZ3 . TRP   D  1 415 ? 19.320  48.051  -38.980  1.00 61.72  ? 716  TRP   D CZ3 1 
ATOM   13582 C  CH2 . TRP   D  1 415 ? 19.703  47.992  -40.327  1.00 60.41  ? 716  TRP   D CH2 1 
ATOM   13583 N  N   . ASN   D  1 416 ? 12.917  49.438  -39.753  1.00 66.65  ? 717  ASN   D N   1 
ATOM   13584 C  CA  . ASN   D  1 416 ? 11.755  49.671  -40.597  1.00 64.42  ? 717  ASN   D CA  1 
ATOM   13585 C  C   . ASN   D  1 416 ? 10.459  49.236  -39.933  1.00 65.77  ? 717  ASN   D C   1 
ATOM   13586 O  O   . ASN   D  1 416 ? 9.393   49.731  -40.308  1.00 79.10  ? 717  ASN   D O   1 
ATOM   13587 C  CB  . ASN   D  1 416 ? 11.916  48.947  -41.946  1.00 65.01  ? 717  ASN   D CB  1 
ATOM   13588 C  CG  . ASN   D  1 416 ? 13.079  49.500  -42.782  1.00 59.51  ? 717  ASN   D CG  1 
ATOM   13589 O  OD1 . ASN   D  1 416 ? 13.417  50.686  -42.699  1.00 64.39  ? 717  ASN   D OD1 1 
ATOM   13590 N  ND2 . ASN   D  1 416 ? 13.694  48.632  -43.592  1.00 45.25  ? 717  ASN   D ND2 1 
ATOM   13591 N  N   . THR   D  1 417 ? 10.526  48.347  -38.945  1.00 64.56  ? 718  THR   D N   1 
ATOM   13592 C  CA  . THR   D  1 417 ? 9.341   47.818  -38.288  1.00 59.91  ? 718  THR   D CA  1 
ATOM   13593 C  C   . THR   D  1 417 ? 9.203   48.238  -36.838  1.00 62.75  ? 718  THR   D C   1 
ATOM   13594 O  O   . THR   D  1 417 ? 8.075   48.411  -36.370  1.00 72.47  ? 718  THR   D O   1 
ATOM   13595 C  CB  . THR   D  1 417 ? 9.342   46.289  -38.336  1.00 63.83  ? 718  THR   D CB  1 
ATOM   13596 O  OG1 . THR   D  1 417 ? 10.454  45.841  -39.115  1.00 69.17  ? 718  THR   D OG1 1 
ATOM   13597 C  CG2 . THR   D  1 417 ? 8.049   45.770  -38.940  1.00 65.12  ? 718  THR   D CG2 1 
ATOM   13598 N  N   . HIS   D  1 418 ? 10.312  48.404  -36.121  1.00 59.35  ? 719  HIS   D N   1 
ATOM   13599 C  CA  . HIS   D  1 418 ? 10.245  48.634  -34.682  1.00 64.53  ? 719  HIS   D CA  1 
ATOM   13600 C  C   . HIS   D  1 418 ? 9.651   49.999  -34.371  1.00 62.77  ? 719  HIS   D C   1 
ATOM   13601 O  O   . HIS   D  1 418 ? 9.958   50.994  -35.030  1.00 68.51  ? 719  HIS   D O   1 
ATOM   13602 C  CB  . HIS   D  1 418 ? 11.633  48.528  -34.047  1.00 65.07  ? 719  HIS   D CB  1 
ATOM   13603 C  CG  . HIS   D  1 418 ? 11.641  48.810  -32.576  1.00 67.60  ? 719  HIS   D CG  1 
ATOM   13604 N  ND1 . HIS   D  1 418 ? 11.328  47.856  -31.632  1.00 66.48  ? 719  HIS   D ND1 1 
ATOM   13605 C  CD2 . HIS   D  1 418 ? 11.912  49.944  -31.887  1.00 66.78  ? 719  HIS   D CD2 1 
ATOM   13606 C  CE1 . HIS   D  1 418 ? 11.414  48.387  -30.425  1.00 66.57  ? 719  HIS   D CE1 1 
ATOM   13607 N  NE2 . HIS   D  1 418 ? 11.763  49.654  -30.552  1.00 66.97  ? 719  HIS   D NE2 1 
ATOM   13608 N  N   . VAL   D  1 419 ? 8.796   50.042  -33.354  1.00 66.37  ? 720  VAL   D N   1 
ATOM   13609 C  CA  . VAL   D  1 419 ? 8.259   51.287  -32.824  1.00 70.84  ? 720  VAL   D CA  1 
ATOM   13610 C  C   . VAL   D  1 419 ? 8.927   51.567  -31.483  1.00 69.46  ? 720  VAL   D C   1 
ATOM   13611 O  O   . VAL   D  1 419 ? 8.932   50.711  -30.585  1.00 63.02  ? 720  VAL   D O   1 
ATOM   13612 C  CB  . VAL   D  1 419 ? 6.731   51.229  -32.687  1.00 74.93  ? 720  VAL   D CB  1 
ATOM   13613 C  CG1 . VAL   D  1 419 ? 6.083   52.279  -33.597  1.00 79.22  ? 720  VAL   D CG1 1 
ATOM   13614 C  CG2 . VAL   D  1 419 ? 6.241   49.823  -33.015  1.00 71.80  ? 720  VAL   D CG2 1 
ATOM   13615 N  N   . TRP   D  1 420 ? 9.480   52.769  -31.352  1.00 72.03  ? 721  TRP   D N   1 
ATOM   13616 C  CA  . TRP   D  1 420 ? 10.289  53.129  -30.199  1.00 84.55  ? 721  TRP   D CA  1 
ATOM   13617 C  C   . TRP   D  1 420 ? 9.412   53.555  -29.027  1.00 93.84  ? 721  TRP   D C   1 
ATOM   13618 O  O   . TRP   D  1 420 ? 8.334   54.133  -29.209  1.00 100.14 ? 721  TRP   D O   1 
ATOM   13619 C  CB  . TRP   D  1 420 ? 11.264  54.247  -30.577  1.00 82.21  ? 721  TRP   D CB  1 
ATOM   13620 C  CG  . TRP   D  1 420 ? 12.277  53.810  -31.600  1.00 74.47  ? 721  TRP   D CG  1 
ATOM   13621 C  CD1 . TRP   D  1 420 ? 12.087  53.684  -32.947  1.00 71.72  ? 721  TRP   D CD1 1 
ATOM   13622 C  CD2 . TRP   D  1 420 ? 13.630  53.423  -31.352  1.00 66.19  ? 721  TRP   D CD2 1 
ATOM   13623 N  NE1 . TRP   D  1 420 ? 13.237  53.243  -33.551  1.00 59.66  ? 721  TRP   D NE1 1 
ATOM   13624 C  CE2 . TRP   D  1 420 ? 14.202  53.079  -32.593  1.00 67.05  ? 721  TRP   D CE2 1 
ATOM   13625 C  CE3 . TRP   D  1 420 ? 14.414  53.337  -30.203  1.00 67.93  ? 721  TRP   D CE3 1 
ATOM   13626 C  CZ2 . TRP   D  1 420 ? 15.522  52.658  -32.714  1.00 74.20  ? 721  TRP   D CZ2 1 
ATOM   13627 C  CZ3 . TRP   D  1 420 ? 15.720  52.916  -30.323  1.00 72.44  ? 721  TRP   D CZ3 1 
ATOM   13628 C  CH2 . TRP   D  1 420 ? 16.263  52.582  -31.569  1.00 73.97  ? 721  TRP   D CH2 1 
ATOM   13629 N  N   . LYS   D  1 421 ? 9.891   53.267  -27.815  1.00 92.32  ? 722  LYS   D N   1 
ATOM   13630 C  CA  . LYS   D  1 421 ? 9.138   53.583  -26.597  1.00 88.22  ? 722  LYS   D CA  1 
ATOM   13631 C  C   . LYS   D  1 421 ? 9.896   54.489  -25.607  1.00 77.66  ? 722  LYS   D C   1 
ATOM   13632 O  O   . LYS   D  1 421 ? 10.977  55.026  -25.864  1.00 69.76  ? 722  LYS   D O   1 
ATOM   13633 C  CB  . LYS   D  1 421 ? 8.705   52.282  -25.905  1.00 86.92  ? 722  LYS   D CB  1 
ATOM   13634 C  CG  . LYS   D  1 421 ? 9.777   51.206  -25.834  1.00 84.52  ? 722  LYS   D CG  1 
ATOM   13635 C  CD  . LYS   D  1 421 ? 9.166   49.824  -25.606  1.00 83.15  ? 722  LYS   D CD  1 
ATOM   13636 C  CE  . LYS   D  1 421 ? 8.414   49.346  -26.853  1.00 78.69  ? 722  LYS   D CE  1 
ATOM   13637 N  NZ  . LYS   D  1 421 ? 7.742   48.035  -26.631  1.00 71.18  ? 722  LYS   D NZ  1 
HETATM 13638 C  CHA . HEM   E  2 .   ? -33.449 9.420   -34.113  1.00 48.81  ? 801  HEM   A CHA 1 
HETATM 13639 C  CHB . HEM   E  2 .   ? -28.966 11.172  -34.603  1.00 49.35  ? 801  HEM   A CHB 1 
HETATM 13640 C  CHC . HEM   E  2 .   ? -30.349 12.994  -38.970  1.00 55.43  ? 801  HEM   A CHC 1 
HETATM 13641 C  CHD . HEM   E  2 .   ? -34.917 11.762  -38.182  1.00 46.95  ? 801  HEM   A CHD 1 
HETATM 13642 C  C1A . HEM   E  2 .   ? -32.087 9.591   -33.916  1.00 44.88  ? 801  HEM   A C1A 1 
HETATM 13643 C  C2A . HEM   E  2 .   ? -31.196 8.884   -33.006  1.00 48.30  ? 801  HEM   A C2A 1 
HETATM 13644 C  C3A . HEM   E  2 .   ? -29.966 9.385   -33.153  1.00 47.33  ? 801  HEM   A C3A 1 
HETATM 13645 C  C4A . HEM   E  2 .   ? -30.019 10.417  -34.146  1.00 49.88  ? 801  HEM   A C4A 1 
HETATM 13646 C  CMA . HEM   E  2 .   ? -28.688 8.961   -32.421  1.00 41.00  ? 801  HEM   A CMA 1 
HETATM 13647 C  CAA . HEM   E  2 .   ? -31.580 7.736   -32.054  1.00 49.15  ? 801  HEM   A CAA 1 
HETATM 13648 C  CBA . HEM   E  2 .   ? -31.909 6.529   -32.930  1.00 47.37  ? 801  HEM   A CBA 1 
HETATM 13649 C  CGA . HEM   E  2 .   ? -31.844 5.245   -32.143  1.00 58.92  ? 801  HEM   A CGA 1 
HETATM 13650 O  O1A . HEM   E  2 .   ? -31.066 5.153   -31.147  1.00 60.40  ? 801  HEM   A O1A 1 
HETATM 13651 O  O2A . HEM   E  2 .   ? -32.575 4.296   -32.524  1.00 60.18  ? 801  HEM   A O2A 1 
HETATM 13652 C  C1B . HEM   E  2 .   ? -28.971 11.837  -35.823  1.00 53.16  ? 801  HEM   A C1B 1 
HETATM 13653 C  C2B . HEM   E  2 .   ? -27.863 12.606  -36.358  1.00 54.09  ? 801  HEM   A C2B 1 
HETATM 13654 C  C3B . HEM   E  2 .   ? -28.230 13.108  -37.544  1.00 50.84  ? 801  HEM   A C3B 1 
HETATM 13655 C  C4B . HEM   E  2 .   ? -29.603 12.688  -37.832  1.00 50.77  ? 801  HEM   A C4B 1 
HETATM 13656 C  CMB . HEM   E  2 .   ? -26.491 12.816  -35.675  1.00 41.19  ? 801  HEM   A CMB 1 
HETATM 13657 C  CAB . HEM   E  2 .   ? -27.281 13.974  -38.393  1.00 50.83  ? 801  HEM   A CAB 1 
HETATM 13658 C  CBB . HEM   E  2 .   ? -27.694 14.674  -39.450  1.00 55.07  ? 801  HEM   A CBB 1 
HETATM 13659 C  C1C . HEM   E  2 .   ? -31.701 12.800  -39.198  1.00 51.26  ? 801  HEM   A C1C 1 
HETATM 13660 C  C2C . HEM   E  2 .   ? -32.451 13.082  -40.418  1.00 53.46  ? 801  HEM   A C2C 1 
HETATM 13661 C  C3C . HEM   E  2 .   ? -33.733 12.732  -40.198  1.00 58.28  ? 801  HEM   A C3C 1 
HETATM 13662 C  C4C . HEM   E  2 .   ? -33.813 12.234  -38.833  1.00 45.92  ? 801  HEM   A C4C 1 
HETATM 13663 C  CMC . HEM   E  2 .   ? -31.852 13.676  -41.719  1.00 45.37  ? 801  HEM   A CMC 1 
HETATM 13664 C  CAC . HEM   E  2 .   ? -34.961 12.847  -41.151  1.00 59.46  ? 801  HEM   A CAC 1 
HETATM 13665 C  CBC . HEM   E  2 .   ? -34.980 13.525  -42.306  1.00 53.23  ? 801  HEM   A CBC 1 
HETATM 13666 C  C1D . HEM   E  2 .   ? -34.883 11.025  -37.021  1.00 46.49  ? 801  HEM   A C1D 1 
HETATM 13667 C  C2D . HEM   E  2 .   ? -36.038 10.408  -36.421  1.00 44.55  ? 801  HEM   A C2D 1 
HETATM 13668 C  C3D . HEM   E  2 .   ? -35.642 9.774   -35.316  1.00 54.12  ? 801  HEM   A C3D 1 
HETATM 13669 C  C4D . HEM   E  2 .   ? -34.213 9.941   -35.153  1.00 52.07  ? 801  HEM   A C4D 1 
HETATM 13670 C  CMD . HEM   E  2 .   ? -37.458 10.504  -36.981  1.00 41.78  ? 801  HEM   A CMD 1 
HETATM 13671 C  CAD . HEM   E  2 .   ? -36.551 9.002   -34.366  1.00 48.86  ? 801  HEM   A CAD 1 
HETATM 13672 C  CBD . HEM   E  2 .   ? -36.226 7.525   -34.472  1.00 47.94  ? 801  HEM   A CBD 1 
HETATM 13673 C  CGD . HEM   E  2 .   ? -37.502 6.853   -34.055  1.00 58.79  ? 801  HEM   A CGD 1 
HETATM 13674 O  O1D . HEM   E  2 .   ? -38.498 7.568   -33.740  1.00 64.89  ? 801  HEM   A O1D 1 
HETATM 13675 O  O2D . HEM   E  2 .   ? -37.544 5.603   -34.031  1.00 54.07  ? 801  HEM   A O2D 1 
HETATM 13676 N  NA  . HEM   E  2 .   ? -31.327 10.518  -34.591  1.00 52.01  ? 801  HEM   A NA  1 
HETATM 13677 N  NB  . HEM   E  2 .   ? -30.019 11.914  -36.748  1.00 43.23  ? 801  HEM   A NB  1 
HETATM 13678 N  NC  . HEM   E  2 .   ? -32.572 12.285  -38.262  1.00 45.94  ? 801  HEM   A NC  1 
HETATM 13679 N  ND  . HEM   E  2 .   ? -33.783 10.717  -36.231  1.00 35.37  ? 801  HEM   A ND  1 
HETATM 13680 FE FE  . HEM   E  2 .   ? -31.991 11.579  -36.361  1.00 37.80  ? 801  HEM   A FE  1 
HETATM 13681 N  N1  . H4B   F  3 .   ? -33.245 5.647   -26.993  1.00 69.87  ? 802  H4B   A N1  1 
HETATM 13682 C  C2  . H4B   F  3 .   ? -32.746 5.438   -28.236  1.00 62.75  ? 802  H4B   A C2  1 
HETATM 13683 N  N2  . H4B   F  3 .   ? -32.031 6.425   -28.833  1.00 60.19  ? 802  H4B   A N2  1 
HETATM 13684 N  N3  . H4B   F  3 .   ? -32.947 4.260   -28.882  1.00 53.62  ? 802  H4B   A N3  1 
HETATM 13685 C  C4  . H4B   F  3 .   ? -33.658 3.275   -28.292  1.00 58.67  ? 802  H4B   A C4  1 
HETATM 13686 O  O4  . H4B   F  3 .   ? -33.860 2.179   -28.865  1.00 62.05  ? 802  H4B   A O4  1 
HETATM 13687 C  C4A . H4B   F  3 .   ? -34.186 3.481   -27.034  1.00 64.57  ? 802  H4B   A C4A 1 
HETATM 13688 C  C8A . H4B   F  3 .   ? -33.962 4.678   -26.376  1.00 67.43  ? 802  H4B   A C8A 1 
HETATM 13689 N  N5  . H4B   F  3 .   ? -34.901 2.513   -26.424  1.00 64.13  ? 802  H4B   A N5  1 
HETATM 13690 N  N8  . H4B   F  3 .   ? -34.463 4.872   -25.123  1.00 57.73  ? 802  H4B   A N8  1 
HETATM 13691 C  C6  . H4B   F  3 .   ? -35.819 2.904   -25.365  1.00 57.41  ? 802  H4B   A C6  1 
HETATM 13692 C  C7  . H4B   F  3 .   ? -35.125 3.809   -24.362  1.00 51.20  ? 802  H4B   A C7  1 
HETATM 13693 C  C9  . H4B   F  3 .   ? -36.450 1.667   -24.734  1.00 51.86  ? 802  H4B   A C9  1 
HETATM 13694 O  O9  . H4B   F  3 .   ? -35.439 0.727   -24.381  1.00 58.00  ? 802  H4B   A O9  1 
HETATM 13695 C  C10 . H4B   F  3 .   ? -37.325 1.963   -23.531  1.00 51.34  ? 802  H4B   A C10 1 
HETATM 13696 C  C11 . H4B   F  3 .   ? -38.193 0.747   -23.255  1.00 47.64  ? 802  H4B   A C11 1 
HETATM 13697 O  O10 . H4B   F  3 .   ? -38.184 3.059   -23.830  1.00 61.24  ? 802  H4B   A O10 1 
HETATM 13698 C  C14 . A1AZ9 G  4 .   ? -32.344 3.430   -36.180  1.00 55.09  ? 803  A1AZ9 A C14 1 
HETATM 13699 C  C13 . A1AZ9 G  4 .   ? -30.999 3.431   -36.553  1.00 56.16  ? 803  A1AZ9 A C13 1 
HETATM 13700 C  C12 . A1AZ9 G  4 .   ? -30.389 4.602   -36.944  1.00 51.07  ? 803  A1AZ9 A C12 1 
HETATM 13701 C  C11 . A1AZ9 G  4 .   ? -31.104 5.776   -36.968  1.00 35.85  ? 803  A1AZ9 A C11 1 
HETATM 13702 C  C15 . A1AZ9 G  4 .   ? -33.070 4.621   -36.206  1.00 50.49  ? 803  A1AZ9 A C15 1 
HETATM 13703 C  C16 . A1AZ9 G  4 .   ? -32.442 5.796   -36.602  1.00 32.41  ? 803  A1AZ9 A C16 1 
HETATM 13704 C  C17 . A1AZ9 G  4 .   ? -34.531 4.668   -35.806  1.00 54.05  ? 803  A1AZ9 A C17 1 
HETATM 13705 C  C19 . A1AZ9 G  4 .   ? -35.879 3.213   -34.456  1.00 68.03  ? 803  A1AZ9 A C19 1 
HETATM 13706 C  C20 . A1AZ9 G  4 .   ? -35.488 1.811   -34.902  1.00 78.84  ? 803  A1AZ9 A C20 1 
HETATM 13707 C  C02 . A1AZ9 G  4 .   ? -28.749 8.606   -37.343  1.00 36.75  ? 803  A1AZ9 A C02 1 
HETATM 13708 C  C03 . A1AZ9 G  4 .   ? -29.333 9.322   -38.380  1.00 47.52  ? 803  A1AZ9 A C03 1 
HETATM 13709 C  C04 . A1AZ9 G  4 .   ? -30.503 8.872   -38.956  1.00 52.54  ? 803  A1AZ9 A C04 1 
HETATM 13710 C  C05 . A1AZ9 G  4 .   ? -31.067 7.705   -38.465  1.00 51.30  ? 803  A1AZ9 A C05 1 
HETATM 13711 C  C06 . A1AZ9 G  4 .   ? -30.454 7.020   -37.425  1.00 32.31  ? 803  A1AZ9 A C06 1 
HETATM 13712 C  C07 . A1AZ9 G  4 .   ? -31.156 9.626   -40.089  1.00 51.88  ? 803  A1AZ9 A C07 1 
HETATM 13713 F  F12 . A1AZ9 G  4 .   ? -29.095 4.600   -37.297  1.00 62.62  ? 803  A1AZ9 A F12 1 
HETATM 13714 F  F13 . A1AZ9 G  4 .   ? -30.267 2.304   -36.539  1.00 66.74  ? 803  A1AZ9 A F13 1 
HETATM 13715 F  F21 . A1AZ9 G  4 .   ? -34.891 1.174   -33.846  1.00 86.18  ? 803  A1AZ9 A F21 1 
HETATM 13716 N  N01 . A1AZ9 G  4 .   ? -29.300 7.459   -36.910  1.00 34.58  ? 803  A1AZ9 A N01 1 
HETATM 13717 N  N02 . A1AZ9 G  4 .   ? -27.599 9.048   -36.789  1.00 39.69  ? 803  A1AZ9 A N02 1 
HETATM 13718 N  N18 . A1AZ9 G  4 .   ? -34.715 4.119   -34.461  1.00 54.78  ? 803  A1AZ9 A N18 1 
HETATM 13719 C  C1  . GOL   H  5 .   ? -46.753 25.673  -35.845  1.00 68.96  ? 804  GOL   A C1  1 
HETATM 13720 O  O1  . GOL   H  5 .   ? -47.201 24.399  -36.247  1.00 68.70  ? 804  GOL   A O1  1 
HETATM 13721 C  C2  . GOL   H  5 .   ? -45.454 25.959  -36.580  1.00 72.05  ? 804  GOL   A C2  1 
HETATM 13722 O  O2  . GOL   H  5 .   ? -44.817 24.742  -36.903  1.00 65.59  ? 804  GOL   A O2  1 
HETATM 13723 C  C3  . GOL   H  5 .   ? -44.529 26.832  -35.739  1.00 79.03  ? 804  GOL   A C3  1 
HETATM 13724 O  O3  . GOL   H  5 .   ? -43.287 26.957  -36.406  1.00 83.72  ? 804  GOL   A O3  1 
HETATM 13725 C  C1  . GOL   I  5 .   ? -32.223 21.805  -50.612  1.00 67.05  ? 805  GOL   A C1  1 
HETATM 13726 O  O1  . GOL   I  5 .   ? -32.194 23.000  -49.853  1.00 69.09  ? 805  GOL   A O1  1 
HETATM 13727 C  C2  . GOL   I  5 .   ? -33.645 21.252  -50.592  1.00 66.35  ? 805  GOL   A C2  1 
HETATM 13728 O  O2  . GOL   I  5 .   ? -33.779 20.059  -51.346  1.00 63.28  ? 805  GOL   A O2  1 
HETATM 13729 C  C3  . GOL   I  5 .   ? -34.569 22.356  -51.085  1.00 72.21  ? 805  GOL   A C3  1 
HETATM 13730 O  O3  . GOL   I  5 .   ? -34.372 23.500  -50.278  1.00 72.28  ? 805  GOL   A O3  1 
HETATM 13731 ZN ZN  . ZN    J  6 .   ? -45.746 11.433  -19.816  1.00 49.50  ? 806  ZN    A ZN  1 
HETATM 13732 C  CHA . HEM   K  2 .   ? -34.502 7.689   -5.154   1.00 52.32  ? 801  HEM   B CHA 1 
HETATM 13733 C  CHB . HEM   K  2 .   ? -31.576 3.849   -4.668   1.00 64.72  ? 801  HEM   B CHB 1 
HETATM 13734 C  CHC . HEM   K  2 .   ? -33.522 2.980   -0.278   1.00 42.80  ? 801  HEM   B CHC 1 
HETATM 13735 C  CHD . HEM   K  2 .   ? -36.912 6.258   -1.146   1.00 46.70  ? 801  HEM   B CHD 1 
HETATM 13736 C  C1A . HEM   K  2 .   ? -33.433 6.830   -5.362   1.00 45.77  ? 801  HEM   B C1A 1 
HETATM 13737 C  C2A . HEM   K  2 .   ? -32.345 6.949   -6.320   1.00 54.66  ? 801  HEM   B C2A 1 
HETATM 13738 C  C3A . HEM   K  2 .   ? -31.540 5.896   -6.187   1.00 59.74  ? 801  HEM   B C3A 1 
HETATM 13739 C  C4A . HEM   K  2 .   ? -32.091 5.049   -5.142   1.00 60.30  ? 801  HEM   B C4A 1 
HETATM 13740 C  CMA . HEM   K  2 .   ? -30.252 5.642   -7.006   1.00 49.84  ? 801  HEM   B CMA 1 
HETATM 13741 C  CAA . HEM   K  2 .   ? -32.097 8.100   -7.307   1.00 56.92  ? 801  HEM   B CAA 1 
HETATM 13742 C  CBA . HEM   K  2 .   ? -31.847 9.341   -6.451   1.00 61.22  ? 801  HEM   B CBA 1 
HETATM 13743 C  CGA . HEM   K  2 .   ? -30.840 10.236  -7.116   1.00 67.92  ? 801  HEM   B CGA 1 
HETATM 13744 O  O1A . HEM   K  2 .   ? -30.054 9.745   -7.975   1.00 71.24  ? 801  HEM   B O1A 1 
HETATM 13745 O  O2A . HEM   K  2 .   ? -30.832 11.444  -6.769   1.00 67.47  ? 801  HEM   B O2A 1 
HETATM 13746 C  C1B . HEM   K  2 .   ? -31.843 3.279   -3.425   1.00 51.39  ? 801  HEM   B C1B 1 
HETATM 13747 C  C2B . HEM   K  2 .   ? -31.198 2.105   -2.871   1.00 47.96  ? 801  HEM   B C2B 1 
HETATM 13748 C  C3B . HEM   K  2 .   ? -31.737 1.855   -1.671   1.00 53.90  ? 801  HEM   B C3B 1 
HETATM 13749 C  C4B . HEM   K  2 .   ? -32.752 2.866   -1.413   1.00 48.16  ? 801  HEM   B C4B 1 
HETATM 13750 C  CMB . HEM   K  2 .   ? -30.084 1.274   -3.550   1.00 42.40  ? 801  HEM   B CMB 1 
HETATM 13751 C  CAB . HEM   K  2 .   ? -31.300 0.687   -0.751   1.00 54.33  ? 801  HEM   B CAB 1 
HETATM 13752 C  CBB . HEM   K  2 .   ? -31.944 0.361   0.373    1.00 44.70  ? 801  HEM   B CBB 1 
HETATM 13753 C  C1C . HEM   K  2 .   ? -34.608 3.793   -0.090   1.00 38.15  ? 801  HEM   B C1C 1 
HETATM 13754 C  C2C . HEM   K  2 .   ? -35.443 3.891   1.095    1.00 49.80  ? 801  HEM   B C2C 1 
HETATM 13755 C  C3C . HEM   K  2 .   ? -36.379 4.820   0.847    1.00 54.65  ? 801  HEM   B C3C 1 
HETATM 13756 C  C4C . HEM   K  2 .   ? -36.152 5.323   -0.486   1.00 48.55  ? 801  HEM   B C4C 1 
HETATM 13757 C  CMC . HEM   K  2 .   ? -35.247 3.065   2.394    1.00 40.07  ? 801  HEM   B CMC 1 
HETATM 13758 C  CAC . HEM   K  2 .   ? -37.539 5.311   1.750    1.00 54.38  ? 801  HEM   B CAC 1 
HETATM 13759 C  CBC . HEM   K  2 .   ? -37.832 4.752   2.930    1.00 55.96  ? 801  HEM   B CBC 1 
HETATM 13760 C  C1D . HEM   K  2 .   ? -36.554 6.937   -2.286   1.00 40.14  ? 801  HEM   B C1D 1 
HETATM 13761 C  C2D . HEM   K  2 .   ? -37.244 8.086   -2.812   1.00 44.12  ? 801  HEM   B C2D 1 
HETATM 13762 C  C3D . HEM   K  2 .   ? -36.585 8.479   -3.901   1.00 47.17  ? 801  HEM   B C3D 1 
HETATM 13763 C  C4D . HEM   K  2 .   ? -35.439 7.610   -4.121   1.00 49.40  ? 801  HEM   B C4D 1 
HETATM 13764 C  CMD . HEM   K  2 .   ? -38.518 8.725   -2.223   1.00 47.62  ? 801  HEM   B CMD 1 
HETATM 13765 C  CAD . HEM   K  2 .   ? -36.975 9.668   -4.766   1.00 33.26  ? 801  HEM   B CAD 1 
HETATM 13766 C  CBD . HEM   K  2 .   ? -35.879 10.668  -4.418   1.00 42.48  ? 801  HEM   B CBD 1 
HETATM 13767 C  CGD . HEM   K  2 .   ? -36.342 12.003  -4.927   1.00 58.89  ? 801  HEM   B CGD 1 
HETATM 13768 O  O1D . HEM   K  2 .   ? -37.424 12.060  -5.588   1.00 57.94  ? 801  HEM   B O1D 1 
HETATM 13769 O  O2D . HEM   K  2 .   ? -35.660 13.028  -4.692   1.00 52.98  ? 801  HEM   B O2D 1 
HETATM 13770 N  NA  . HEM   K  2 .   ? -33.245 5.652   -4.675   1.00 48.03  ? 801  HEM   B NA  1 
HETATM 13771 N  NB  . HEM   K  2 .   ? -32.788 3.715   -2.506   1.00 41.49  ? 801  HEM   B NB  1 
HETATM 13772 N  NC  . HEM   K  2 .   ? -35.068 4.678   -1.018   1.00 46.23  ? 801  HEM   B NC  1 
HETATM 13773 N  ND  . HEM   K  2 .   ? -35.472 6.669   -3.105   1.00 33.69  ? 801  HEM   B ND  1 
HETATM 13774 FE FE  . HEM   K  2 .   ? -34.413 4.935   -2.995   1.00 43.11  ? 801  HEM   B FE  1 
HETATM 13775 N  N1  . H4B   L  3 .   ? -32.213 10.526  -12.379  1.00 63.59  ? 802  H4B   B N1  1 
HETATM 13776 C  C2  . H4B   L  3 .   ? -31.753 10.348  -11.129  1.00 63.08  ? 802  H4B   B C2  1 
HETATM 13777 N  N2  . H4B   L  3 .   ? -31.724 9.084   -10.646  1.00 64.30  ? 802  H4B   B N2  1 
HETATM 13778 N  N3  . H4B   L  3 .   ? -31.334 11.411  -10.384  1.00 51.78  ? 802  H4B   B N3  1 
HETATM 13779 C  C4  . H4B   L  3 .   ? -31.381 12.666  -10.882  1.00 52.66  ? 802  H4B   B C4  1 
HETATM 13780 O  O4  . H4B   L  3 .   ? -31.002 13.636  -10.191  1.00 51.79  ? 802  H4B   B O4  1 
HETATM 13781 C  C4A . H4B   L  3 .   ? -31.862 12.859  -12.172  1.00 56.53  ? 802  H4B   B C4A 1 
HETATM 13782 C  C8A . H4B   L  3 .   ? -32.275 11.761  -12.914  1.00 54.64  ? 802  H4B   B C8A 1 
HETATM 13783 N  N5  . H4B   L  3 .   ? -31.940 14.087  -12.725  1.00 54.71  ? 802  H4B   B N5  1 
HETATM 13784 N  N8  . H4B   L  3 .   ? -32.743 11.899  -14.179  1.00 50.58  ? 802  H4B   B N8  1 
HETATM 13785 C  C6  . H4B   L  3 .   ? -32.966 14.236  -13.753  1.00 56.52  ? 802  H4B   B C6  1 
HETATM 13786 C  C7  . H4B   L  3 .   ? -32.787 13.192  -14.841  1.00 43.16  ? 802  H4B   B C7  1 
HETATM 13787 C  C9  . H4B   L  3 .   ? -33.002 15.616  -14.388  1.00 58.20  ? 802  H4B   B C9  1 
HETATM 13788 O  O9  . H4B   L  3 .   ? -31.690 15.954  -14.849  1.00 56.95  ? 802  H4B   B O9  1 
HETATM 13789 C  C10 . H4B   L  3 .   ? -34.012 15.568  -15.525  1.00 62.44  ? 802  H4B   B C10 1 
HETATM 13790 C  C11 . H4B   L  3 .   ? -34.104 16.902  -16.253  1.00 59.93  ? 802  H4B   B C11 1 
HETATM 13791 O  O10 . H4B   L  3 .   ? -35.287 15.195  -14.975  1.00 69.79  ? 802  H4B   B O10 1 
HETATM 13792 C  C14 . A1AZ9 M  4 .   ? -30.374 12.184  -3.099   1.00 58.07  ? 803  A1AZ9 B C14 1 
HETATM 13793 C  C13 . A1AZ9 M  4 .   ? -29.221 11.503  -2.731   1.00 57.02  ? 803  A1AZ9 B C13 1 
HETATM 13794 C  C12 . A1AZ9 M  4 .   ? -29.304 10.191  -2.347   1.00 48.59  ? 803  A1AZ9 B C12 1 
HETATM 13795 C  C11 . A1AZ9 M  4 .   ? -30.519 9.543   -2.332   1.00 39.18  ? 803  A1AZ9 B C11 1 
HETATM 13796 C  C15 . A1AZ9 M  4 .   ? -31.613 11.547  -3.084   1.00 53.29  ? 803  A1AZ9 B C15 1 
HETATM 13797 C  C16 . A1AZ9 M  4 .   ? -31.679 10.213  -2.697   1.00 39.47  ? 803  A1AZ9 B C16 1 
HETATM 13798 C  C17 . A1AZ9 M  4 .   ? -32.866 12.299  -3.495   1.00 56.95  ? 803  A1AZ9 B C17 1 
HETATM 13799 C  C19 . A1AZ9 M  4 .   ? -33.078 14.195  -5.051   1.00 68.06  ? 803  A1AZ9 B C19 1 
HETATM 13800 C  C20 . A1AZ9 M  4 .   ? -32.473 15.013  -3.923   1.00 75.86  ? 803  A1AZ9 B C20 1 
HETATM 13801 C  C02 . A1AZ9 M  4 .   ? -29.852 5.906   -1.854   1.00 36.16  ? 803  A1AZ9 B C02 1 
HETATM 13802 C  C03 . A1AZ9 M  4 .   ? -30.785 5.605   -0.880   1.00 39.04  ? 803  A1AZ9 B C03 1 
HETATM 13803 C  C04 . A1AZ9 M  4 .   ? -31.610 6.592   -0.398   1.00 40.65  ? 803  A1AZ9 B C04 1 
HETATM 13804 C  C05 . A1AZ9 M  4 .   ? -31.498 7.857   -0.903   1.00 37.49  ? 803  A1AZ9 B C05 1 
HETATM 13805 C  C06 . A1AZ9 M  4 .   ? -30.571 8.134   -1.880   1.00 33.46  ? 803  A1AZ9 B C06 1 
HETATM 13806 C  C07 . A1AZ9 M  4 .   ? -32.632 6.319   0.662    1.00 53.70  ? 803  A1AZ9 B C07 1 
HETATM 13807 F  F12 . A1AZ9 M  4 .   ? -28.193 9.538   -1.992   1.00 49.46  ? 803  A1AZ9 B F12 1 
HETATM 13808 F  F13 . A1AZ9 M  4 .   ? -28.020 12.099  -2.750   1.00 70.25  ? 803  A1AZ9 B F13 1 
HETATM 13809 F  F21 . A1AZ9 M  4 .   ? -31.626 15.927  -4.483   1.00 87.36  ? 803  A1AZ9 B F21 1 
HETATM 13810 N  N01 . A1AZ9 M  4 .   ? -29.740 7.172   -2.323   1.00 30.76  ? 803  A1AZ9 B N01 1 
HETATM 13811 N  N02 . A1AZ9 M  4 .   ? -29.047 4.910   -2.298   1.00 38.64  ? 803  A1AZ9 B N02 1 
HETATM 13812 N  N18 . A1AZ9 M  4 .   ? -32.775 12.756  -4.901   1.00 65.84  ? 803  A1AZ9 B N18 1 
HETATM 13813 C  C1  . GOL   N  5 .   ? -53.134 1.195   -3.775   1.00 92.90  ? 804  GOL   B C1  1 
HETATM 13814 O  O1  . GOL   N  5 .   ? -52.687 2.361   -3.110   1.00 88.41  ? 804  GOL   B O1  1 
HETATM 13815 C  C2  . GOL   N  5 .   ? -53.204 -0.002  -2.823   1.00 90.69  ? 804  GOL   B C2  1 
HETATM 13816 O  O2  . GOL   N  5 .   ? -51.937 -0.622  -2.686   1.00 80.98  ? 804  GOL   B O2  1 
HETATM 13817 C  C3  . GOL   N  5 .   ? -54.262 -0.983  -3.339   1.00 91.80  ? 804  GOL   B C3  1 
HETATM 13818 O  O3  . GOL   N  5 .   ? -53.882 -2.330  -3.136   1.00 88.62  ? 804  GOL   B O3  1 
HETATM 13819 C  CHA . HEM   O  2 .   ? 24.888  33.724  -77.117  1.00 44.27  ? 801  HEM   C CHA 1 
HETATM 13820 C  CHB . HEM   O  2 .   ? 27.865  37.520  -77.597  1.00 60.44  ? 801  HEM   C CHB 1 
HETATM 13821 C  CHC . HEM   O  2 .   ? 25.920  38.434  -81.981  1.00 44.10  ? 801  HEM   C CHC 1 
HETATM 13822 C  CHD . HEM   O  2 .   ? 22.526  35.119  -81.145  1.00 43.90  ? 801  HEM   C CHD 1 
HETATM 13823 C  C1A . HEM   O  2 .   ? 25.966  34.566  -76.906  1.00 50.35  ? 801  HEM   C C1A 1 
HETATM 13824 C  C2A . HEM   O  2 .   ? 27.061  34.417  -75.942  1.00 54.89  ? 801  HEM   C C2A 1 
HETATM 13825 C  C3A . HEM   O  2 .   ? 27.883  35.455  -76.077  1.00 55.41  ? 801  HEM   C C3A 1 
HETATM 13826 C  C4A . HEM   O  2 .   ? 27.341  36.323  -77.123  1.00 60.75  ? 801  HEM   C C4A 1 
HETATM 13827 C  CMA . HEM   O  2 .   ? 29.173  35.657  -75.251  1.00 39.50  ? 801  HEM   C CMA 1 
HETATM 13828 C  CAA . HEM   O  2 .   ? 27.297  33.250  -74.964  1.00 48.75  ? 801  HEM   C CAA 1 
HETATM 13829 C  CBA . HEM   O  2 .   ? 27.410  32.006  -75.850  1.00 48.84  ? 801  HEM   C CBA 1 
HETATM 13830 C  CGA . HEM   O  2 .   ? 28.455  31.038  -75.383  1.00 61.34  ? 801  HEM   C CGA 1 
HETATM 13831 O  O1A . HEM   O  2 .   ? 29.318  31.417  -74.542  1.00 78.53  ? 801  HEM   C O1A 1 
HETATM 13832 O  O2A . HEM   O  2 .   ? 28.413  29.878  -75.859  1.00 53.22  ? 801  HEM   C O2A 1 
HETATM 13833 C  C1B . HEM   O  2 .   ? 27.594  38.103  -78.827  1.00 51.86  ? 801  HEM   C C1B 1 
HETATM 13834 C  C2B . HEM   O  2 .   ? 28.245  39.278  -79.371  1.00 50.57  ? 801  HEM   C C2B 1 
HETATM 13835 C  C3B . HEM   O  2 .   ? 27.711  39.541  -80.568  1.00 51.27  ? 801  HEM   C C3B 1 
HETATM 13836 C  C4B . HEM   O  2 .   ? 26.694  38.534  -80.842  1.00 49.11  ? 801  HEM   C C4B 1 
HETATM 13837 C  CMB . HEM   O  2 .   ? 29.357  40.103  -78.685  1.00 50.92  ? 801  HEM   C CMB 1 
HETATM 13838 C  CAB . HEM   O  2 .   ? 28.154  40.723  -81.464  1.00 53.51  ? 801  HEM   C CAB 1 
HETATM 13839 C  CBB . HEM   O  2 .   ? 27.563  41.007  -82.633  1.00 57.29  ? 801  HEM   C CBB 1 
HETATM 13840 C  C1C . HEM   O  2 .   ? 24.854  37.592  -82.182  1.00 43.98  ? 801  HEM   C C1C 1 
HETATM 13841 C  C2C . HEM   O  2 .   ? 24.054  37.446  -83.390  1.00 53.49  ? 801  HEM   C C2C 1 
HETATM 13842 C  C3C . HEM   O  2 .   ? 23.130  36.504  -83.165  1.00 56.37  ? 801  HEM   C C3C 1 
HETATM 13843 C  C4C . HEM   O  2 .   ? 23.297  36.050  -81.799  1.00 47.58  ? 801  HEM   C C4C 1 
HETATM 13844 C  CMC . HEM   O  2 .   ? 24.259  38.214  -84.713  1.00 43.71  ? 801  HEM   C CMC 1 
HETATM 13845 C  CAC . HEM   O  2 .   ? 22.017  36.006  -84.119  1.00 50.34  ? 801  HEM   C CAC 1 
HETATM 13846 C  CBC . HEM   O  2 .   ? 21.446  36.800  -85.030  1.00 51.74  ? 801  HEM   C CBC 1 
HETATM 13847 C  C1D . HEM   O  2 .   ? 22.866  34.460  -79.991  1.00 38.51  ? 801  HEM   C C1D 1 
HETATM 13848 C  C2D . HEM   O  2 .   ? 22.144  33.347  -79.424  1.00 44.11  ? 801  HEM   C C2D 1 
HETATM 13849 C  C3D . HEM   O  2 .   ? 22.797  32.958  -78.325  1.00 44.69  ? 801  HEM   C C3D 1 
HETATM 13850 C  C4D . HEM   O  2 .   ? 23.964  33.803  -78.150  1.00 45.88  ? 801  HEM   C C4D 1 
HETATM 13851 C  CMD . HEM   O  2 .   ? 20.847  32.715  -79.973  1.00 46.05  ? 801  HEM   C CMD 1 
HETATM 13852 C  CAD . HEM   O  2 .   ? 22.372  31.806  -77.409  1.00 33.59  ? 801  HEM   C CAD 1 
HETATM 13853 C  CBD . HEM   O  2 .   ? 23.457  30.758  -77.607  1.00 43.64  ? 801  HEM   C CBD 1 
HETATM 13854 C  CGD . HEM   O  2 .   ? 22.924  29.445  -77.111  1.00 51.19  ? 801  HEM   C CGD 1 
HETATM 13855 O  O1D . HEM   O  2 .   ? 21.723  29.388  -76.690  1.00 52.51  ? 801  HEM   C O1D 1 
HETATM 13856 O  O2D . HEM   O  2 .   ? 23.687  28.437  -77.124  1.00 43.23  ? 801  HEM   C O2D 1 
HETATM 13857 N  NA  . HEM   O  2 .   ? 26.174  35.744  -77.594  1.00 51.72  ? 801  HEM   C NA  1 
HETATM 13858 N  NB  . HEM   O  2 .   ? 26.648  37.680  -79.748  1.00 47.08  ? 801  HEM   C NB  1 
HETATM 13859 N  NC  . HEM   O  2 .   ? 24.362  36.724  -81.242  1.00 43.65  ? 801  HEM   C NC  1 
HETATM 13860 N  ND  . HEM   O  2 .   ? 23.962  34.716  -79.194  1.00 35.27  ? 801  HEM   C ND  1 
HETATM 13861 FE FE  . HEM   O  2 .   ? 25.051  36.443  -79.234  1.00 43.44  ? 801  HEM   C FE  1 
HETATM 13862 N  N1  . H4B   P  3 .   ? 27.200  30.685  -69.984  1.00 66.41  ? 802  H4B   C N1  1 
HETATM 13863 C  C2  . H4B   P  3 .   ? 27.657  30.822  -71.244  1.00 62.66  ? 802  H4B   C C2  1 
HETATM 13864 N  N2  . H4B   P  3 .   ? 27.704  32.065  -71.792  1.00 64.91  ? 802  H4B   C N2  1 
HETATM 13865 N  N3  . H4B   P  3 .   ? 28.058  29.730  -71.940  1.00 60.21  ? 802  H4B   C N3  1 
HETATM 13866 C  C4  . H4B   P  3 .   ? 28.009  28.493  -71.388  1.00 63.02  ? 802  H4B   C C4  1 
HETATM 13867 O  O4  . H4B   P  3 .   ? 28.385  27.493  -72.042  1.00 65.52  ? 802  H4B   C O4  1 
HETATM 13868 C  C4A . H4B   P  3 .   ? 27.529  28.346  -70.094  1.00 64.55  ? 802  H4B   C C4A 1 
HETATM 13869 C  C8A . H4B   P  3 .   ? 27.126  29.471  -69.392  1.00 64.50  ? 802  H4B   C C8A 1 
HETATM 13870 N  N5  . H4B   P  3 .   ? 27.438  27.138  -69.492  1.00 65.43  ? 802  H4B   C N5  1 
HETATM 13871 N  N8  . H4B   P  3 .   ? 26.657  29.371  -68.115  1.00 58.04  ? 802  H4B   C N8  1 
HETATM 13872 C  C6  . H4B   P  3 .   ? 26.429  27.031  -68.440  1.00 61.13  ? 802  H4B   C C6  1 
HETATM 13873 C  C7  . H4B   P  3 .   ? 26.656  28.104  -67.392  1.00 50.76  ? 802  H4B   C C7  1 
HETATM 13874 C  C9  . H4B   P  3 .   ? 26.385  25.657  -67.786  1.00 61.32  ? 802  H4B   C C9  1 
HETATM 13875 O  O9  . H4B   P  3 .   ? 27.709  25.219  -67.467  1.00 60.47  ? 802  H4B   C O9  1 
HETATM 13876 C  C10 . H4B   P  3 .   ? 25.530  25.722  -66.532  1.00 56.09  ? 802  H4B   C C10 1 
HETATM 13877 C  C11 . H4B   P  3 .   ? 25.304  24.332  -65.951  1.00 50.67  ? 802  H4B   C C11 1 
HETATM 13878 O  O10 . H4B   P  3 .   ? 24.270  26.305  -66.878  1.00 59.44  ? 802  H4B   C O10 1 
HETATM 13879 C  C14 . A1AZ9 Q  4 .   ? 28.998  29.036  -79.268  1.00 50.17  ? 803  A1AZ9 C C14 1 
HETATM 13880 C  C13 . A1AZ9 Q  4 .   ? 30.139  29.768  -79.605  1.00 48.63  ? 803  A1AZ9 C C13 1 
HETATM 13881 C  C12 . A1AZ9 Q  4 .   ? 30.004  31.104  -79.918  1.00 39.08  ? 803  A1AZ9 C C12 1 
HETATM 13882 C  C11 . A1AZ9 Q  4 .   ? 28.781  31.714  -79.878  1.00 36.67  ? 803  A1AZ9 C C11 1 
HETATM 13883 C  C15 . A1AZ9 Q  4 .   ? 27.739  29.647  -79.233  1.00 47.95  ? 803  A1AZ9 C C15 1 
HETATM 13884 C  C16 . A1AZ9 Q  4 .   ? 27.634  30.997  -79.560  1.00 39.74  ? 803  A1AZ9 C C16 1 
HETATM 13885 C  C17 . A1AZ9 Q  4 .   ? 26.484  28.864  -78.883  1.00 55.17  ? 803  A1AZ9 C C17 1 
HETATM 13886 C  C19 . A1AZ9 Q  4 .   ? 26.670  27.520  -76.865  1.00 81.33  ? 803  A1AZ9 C C19 1 
HETATM 13887 C  C20 . A1AZ9 Q  4 .   ? 26.675  26.365  -77.861  1.00 82.83  ? 803  A1AZ9 C C20 1 
HETATM 13888 C  C02 . A1AZ9 Q  4 .   ? 29.501  35.353  -80.304  1.00 40.20  ? 803  A1AZ9 C C02 1 
HETATM 13889 C  C03 . A1AZ9 Q  4 .   ? 28.635  35.662  -81.346  1.00 43.10  ? 803  A1AZ9 C C03 1 
HETATM 13890 C  C04 . A1AZ9 Q  4 .   ? 27.837  34.674  -81.887  1.00 47.56  ? 803  A1AZ9 C C04 1 
HETATM 13891 C  C05 . A1AZ9 Q  4 .   ? 27.911  33.407  -81.367  1.00 44.12  ? 803  A1AZ9 C C05 1 
HETATM 13892 C  C06 . A1AZ9 Q  4 .   ? 28.762  33.132  -80.304  1.00 39.30  ? 803  A1AZ9 C C06 1 
HETATM 13893 C  C07 . A1AZ9 Q  4 .   ? 26.891  34.957  -83.016  1.00 56.02  ? 803  A1AZ9 C C07 1 
HETATM 13894 F  F12 . A1AZ9 Q  4 .   ? 31.052  31.863  -80.261  1.00 39.37  ? 803  A1AZ9 C F12 1 
HETATM 13895 F  F13 . A1AZ9 Q  4 .   ? 31.365  29.206  -79.625  1.00 55.00  ? 803  A1AZ9 C F13 1 
HETATM 13896 F  F21 . A1AZ9 Q  4 .   ? 27.981  26.022  -78.108  1.00 87.43  ? 803  A1AZ9 C F21 1 
HETATM 13897 N  N01 . A1AZ9 Q  4 .   ? 29.574  34.086  -79.811  1.00 31.85  ? 803  A1AZ9 C N01 1 
HETATM 13898 N  N02 . A1AZ9 Q  4 .   ? 30.275  36.353  -79.807  1.00 42.91  ? 803  A1AZ9 C N02 1 
HETATM 13899 N  N18 . A1AZ9 Q  4 .   ? 26.152  28.776  -77.455  1.00 68.63  ? 803  A1AZ9 C N18 1 
HETATM 13900 C  C1  . GOL   R  5 .   ? 5.107   41.064  -79.157  1.00 91.62  ? 804  GOL   C C1  1 
HETATM 13901 O  O1  . GOL   R  5 .   ? 6.000   40.337  -78.336  1.00 89.31  ? 804  GOL   C O1  1 
HETATM 13902 C  C2  . GOL   R  5 .   ? 5.781   42.308  -79.743  1.00 88.40  ? 804  GOL   C C2  1 
HETATM 13903 O  O2  . GOL   R  5 .   ? 7.077   42.498  -79.202  1.00 80.43  ? 804  GOL   C O2  1 
HETATM 13904 C  C3  . GOL   R  5 .   ? 4.879   43.533  -79.556  1.00 87.71  ? 804  GOL   C C3  1 
HETATM 13905 O  O3  . GOL   R  5 .   ? 5.624   44.732  -79.509  1.00 87.93  ? 804  GOL   C O3  1 
HETATM 13906 C  C1  . GOL   S  5 .   ? 19.864  45.337  -92.785  1.00 73.05  ? 805  GOL   C C1  1 
HETATM 13907 O  O1  . GOL   S  5 .   ? 19.664  46.068  -91.584  1.00 81.98  ? 805  GOL   C O1  1 
HETATM 13908 C  C2  . GOL   S  5 .   ? 18.724  44.335  -92.959  1.00 63.35  ? 805  GOL   C C2  1 
HETATM 13909 O  O2  . GOL   S  5 .   ? 19.091  43.247  -93.785  1.00 59.79  ? 805  GOL   C O2  1 
HETATM 13910 C  C3  . GOL   S  5 .   ? 17.522  45.080  -93.506  1.00 59.43  ? 805  GOL   C C3  1 
HETATM 13911 O  O3  . GOL   S  5 .   ? 17.686  46.432  -93.131  1.00 64.24  ? 805  GOL   C O3  1 
HETATM 13912 ZN ZN  . ZN    T  6 .   ? 13.696  29.857  -62.457  1.00 52.67  ? 806  ZN    C ZN  1 
HETATM 13913 C  CHA . HEM   U  2 .   ? 25.871  32.010  -48.006  1.00 53.12  ? 801  HEM   D CHA 1 
HETATM 13914 C  CHB . HEM   U  2 .   ? 30.337  30.158  -47.607  1.00 58.32  ? 801  HEM   D CHB 1 
HETATM 13915 C  CHC . HEM   U  2 .   ? 28.978  28.344  -43.297  1.00 51.89  ? 801  HEM   D CHC 1 
HETATM 13916 C  CHD . HEM   U  2 .   ? 24.372  29.502  -44.089  1.00 47.87  ? 801  HEM   D CHD 1 
HETATM 13917 C  C1A . HEM   U  2 .   ? 27.221  31.774  -48.211  1.00 51.09  ? 801  HEM   D C1A 1 
HETATM 13918 C  C2A . HEM   U  2 .   ? 28.093  32.427  -49.168  1.00 43.68  ? 801  HEM   D C2A 1 
HETATM 13919 C  C3A . HEM   U  2 .   ? 29.313  31.920  -49.047  1.00 44.24  ? 801  HEM   D C3A 1 
HETATM 13920 C  C4A . HEM   U  2 .   ? 29.275  30.917  -48.030  1.00 50.17  ? 801  HEM   D C4A 1 
HETATM 13921 C  CMA . HEM   U  2 .   ? 30.560  32.298  -49.852  1.00 48.19  ? 801  HEM   D CMA 1 
HETATM 13922 C  CAA . HEM   U  2 .   ? 27.689  33.549  -50.130  1.00 40.19  ? 801  HEM   D CAA 1 
HETATM 13923 C  CBA . HEM   U  2 .   ? 27.778  34.784  -49.245  1.00 39.01  ? 801  HEM   D CBA 1 
HETATM 13924 C  CGA . HEM   U  2 .   ? 27.651  36.031  -50.070  1.00 53.71  ? 801  HEM   D CGA 1 
HETATM 13925 O  O1A . HEM   U  2 .   ? 28.436  36.206  -51.051  1.00 53.17  ? 801  HEM   D O1A 1 
HETATM 13926 O  O2A . HEM   U  2 .   ? 26.767  36.855  -49.717  1.00 54.09  ? 801  HEM   D O2A 1 
HETATM 13927 C  C1B . HEM   U  2 .   ? 30.360  29.517  -46.385  1.00 57.36  ? 801  HEM   D C1B 1 
HETATM 13928 C  C2B . HEM   U  2 .   ? 31.499  28.842  -45.817  1.00 52.99  ? 801  HEM   D C2B 1 
HETATM 13929 C  C3B . HEM   U  2 .   ? 31.131  28.327  -44.633  1.00 55.07  ? 801  HEM   D C3B 1 
HETATM 13930 C  C4B . HEM   U  2 .   ? 29.739  28.672  -44.402  1.00 53.36  ? 801  HEM   D C4B 1 
HETATM 13931 C  CMB . HEM   U  2 .   ? 32.874  28.736  -46.507  1.00 40.48  ? 801  HEM   D CMB 1 
HETATM 13932 C  CAB . HEM   U  2 .   ? 32.058  27.529  -43.696  1.00 55.76  ? 801  HEM   D CAB 1 
HETATM 13933 C  CBB . HEM   U  2 .   ? 31.588  26.685  -42.777  1.00 53.03  ? 801  HEM   D CBB 1 
HETATM 13934 C  C1C . HEM   U  2 .   ? 27.622  28.523  -43.094  1.00 50.01  ? 801  HEM   D C1C 1 
HETATM 13935 C  C2C . HEM   U  2 .   ? 26.897  28.232  -41.876  1.00 52.07  ? 801  HEM   D C2C 1 
HETATM 13936 C  C3C . HEM   U  2 .   ? 25.611  28.556  -42.091  1.00 62.76  ? 801  HEM   D C3C 1 
HETATM 13937 C  C4C . HEM   U  2 .   ? 25.503  29.057  -43.451  1.00 50.41  ? 801  HEM   D C4C 1 
HETATM 13938 C  CMC . HEM   U  2 .   ? 27.545  27.652  -40.594  1.00 46.44  ? 801  HEM   D CMC 1 
HETATM 13939 C  CAC . HEM   U  2 .   ? 24.398  28.429  -41.124  1.00 71.74  ? 801  HEM   D CAC 1 
HETATM 13940 C  CBC . HEM   U  2 .   ? 24.434  27.836  -39.921  1.00 70.21  ? 801  HEM   D CBC 1 
HETATM 13941 C  C1D . HEM   U  2 .   ? 24.384  30.291  -45.214  1.00 44.04  ? 801  HEM   D C1D 1 
HETATM 13942 C  C2D . HEM   U  2 .   ? 23.235  30.922  -45.819  1.00 37.54  ? 801  HEM   D C2D 1 
HETATM 13943 C  C3D . HEM   U  2 .   ? 23.652  31.599  -46.886  1.00 52.83  ? 801  HEM   D C3D 1 
HETATM 13944 C  C4D . HEM   U  2 .   ? 25.084  31.448  -47.014  1.00 54.22  ? 801  HEM   D C4D 1 
HETATM 13945 C  CMD . HEM   U  2 .   ? 21.785  30.806  -45.324  1.00 28.32  ? 801  HEM   D CMD 1 
HETATM 13946 C  CAD . HEM   U  2 .   ? 22.769  32.415  -47.830  1.00 53.76  ? 801  HEM   D CAD 1 
HETATM 13947 C  CBD . HEM   U  2 .   ? 23.054  33.873  -47.530  1.00 51.96  ? 801  HEM   D CBD 1 
HETATM 13948 C  CGD . HEM   U  2 .   ? 21.924  34.655  -48.123  1.00 59.60  ? 801  HEM   D CGD 1 
HETATM 13949 O  O1D . HEM   U  2 .   ? 20.904  34.039  -48.529  1.00 66.69  ? 801  HEM   D O1D 1 
HETATM 13950 O  O2D . HEM   U  2 .   ? 22.030  35.900  -48.193  1.00 58.56  ? 801  HEM   D O2D 1 
HETATM 13951 N  NA  . HEM   U  2 .   ? 27.982  30.843  -47.538  1.00 49.73  ? 801  HEM   D NA  1 
HETATM 13952 N  NB  . HEM   U  2 .   ? 29.298  29.393  -45.502  1.00 50.51  ? 801  HEM   D NB  1 
HETATM 13953 N  NC  . HEM   U  2 .   ? 26.739  29.022  -44.027  1.00 48.67  ? 801  HEM   D NC  1 
HETATM 13954 N  ND  . HEM   U  2 .   ? 25.496  30.631  -45.970  1.00 39.73  ? 801  HEM   D ND  1 
HETATM 13955 FE FE  . HEM   U  2 .   ? 27.251  29.656  -45.966  1.00 41.87  ? 801  HEM   D FE  1 
HETATM 13956 N  N1  . H4B   V  3 .   ? 26.215  35.667  -55.361  1.00 65.09  ? 802  H4B   D N1  1 
HETATM 13957 C  C2  . H4B   V  3 .   ? 26.731  35.816  -54.130  1.00 58.69  ? 802  H4B   D C2  1 
HETATM 13958 N  N2  . H4B   V  3 .   ? 27.471  34.800  -53.637  1.00 66.22  ? 802  H4B   D N2  1 
HETATM 13959 N  N3  . H4B   V  3 .   ? 26.515  36.947  -53.411  1.00 46.88  ? 802  H4B   D N3  1 
HETATM 13960 C  C4  . H4B   V  3 .   ? 25.764  37.952  -53.922  1.00 52.63  ? 802  H4B   D C4  1 
HETATM 13961 O  O4  . H4B   V  3 .   ? 25.547  38.988  -53.248  1.00 49.62  ? 802  H4B   D O4  1 
HETATM 13962 C  C4A . H4B   V  3 .   ? 25.218  37.810  -55.191  1.00 58.15  ? 802  H4B   D C4A 1 
HETATM 13963 C  C8A . H4B   V  3 .   ? 25.470  36.650  -55.912  1.00 62.13  ? 802  H4B   D C8A 1 
HETATM 13964 N  N5  . H4B   V  3 .   ? 24.462  38.786  -55.759  1.00 65.76  ? 802  H4B   D N5  1 
HETATM 13965 N  N8  . H4B   V  3 .   ? 24.973  36.484  -57.172  1.00 52.37  ? 802  H4B   D N8  1 
HETATM 13966 C  C6  . H4B   V  3 .   ? 23.587  38.433  -56.888  1.00 55.61  ? 802  H4B   D C6  1 
HETATM 13967 C  C7  . H4B   V  3 .   ? 24.316  37.567  -57.902  1.00 46.59  ? 802  H4B   D C7  1 
HETATM 13968 C  C9  . H4B   V  3 .   ? 22.941  39.651  -57.552  1.00 43.52  ? 802  H4B   D C9  1 
HETATM 13969 O  O9  . H4B   V  3 .   ? 23.942  40.533  -58.053  1.00 55.04  ? 802  H4B   D O9  1 
HETATM 13970 C  C10 . H4B   V  3 .   ? 21.976  39.319  -58.683  1.00 48.45  ? 802  H4B   D C10 1 
HETATM 13971 C  C11 . H4B   V  3 .   ? 21.081  40.530  -58.920  1.00 36.19  ? 802  H4B   D C11 1 
HETATM 13972 O  O10 . H4B   V  3 .   ? 21.145  38.205  -58.345  1.00 60.18  ? 802  H4B   D O10 1 
HETATM 13973 C  C14 . A1AZ9 W  4 .   ? 26.925  37.932  -46.089  1.00 63.30  ? 803  A1AZ9 D C14 1 
HETATM 13974 C  C13 . A1AZ9 W  4 .   ? 28.249  37.914  -45.669  1.00 61.54  ? 803  A1AZ9 D C13 1 
HETATM 13975 C  C12 . A1AZ9 W  4 .   ? 28.808  36.727  -45.269  1.00 51.12  ? 803  A1AZ9 D C12 1 
HETATM 13976 C  C11 . A1AZ9 W  4 .   ? 28.075  35.568  -45.273  1.00 48.58  ? 803  A1AZ9 D C11 1 
HETATM 13977 C  C15 . A1AZ9 W  4 .   ? 26.173  36.760  -46.096  1.00 59.65  ? 803  A1AZ9 D C15 1 
HETATM 13978 C  C16 . A1AZ9 W  4 .   ? 26.753  35.563  -45.703  1.00 42.45  ? 803  A1AZ9 D C16 1 
HETATM 13979 C  C17 . A1AZ9 W  4 .   ? 24.737  36.798  -46.561  1.00 70.77  ? 803  A1AZ9 D C17 1 
HETATM 13980 C  C19 . A1AZ9 W  4 .   ? 23.976  38.223  -48.422  1.00 83.64  ? 803  A1AZ9 D C19 1 
HETATM 13981 C  C20 . A1AZ9 W  4 .   ? 23.892  39.265  -47.318  1.00 90.16  ? 803  A1AZ9 D C20 1 
HETATM 13982 C  C02 . A1AZ9 W  4 .   ? 30.575  32.883  -44.878  1.00 37.48  ? 803  A1AZ9 D C02 1 
HETATM 13983 C  C03 . A1AZ9 W  4 .   ? 30.006  32.083  -43.896  1.00 44.07  ? 803  A1AZ9 D C03 1 
HETATM 13984 C  C04 . A1AZ9 W  4 .   ? 28.781  32.440  -43.349  1.00 45.61  ? 803  A1AZ9 D C04 1 
HETATM 13985 C  C05 . A1AZ9 W  4 .   ? 28.149  33.582  -43.814  1.00 42.66  ? 803  A1AZ9 D C05 1 
HETATM 13986 C  C06 . A1AZ9 W  4 .   ? 28.758  34.338  -44.802  1.00 40.86  ? 803  A1AZ9 D C06 1 
HETATM 13987 C  C07 . A1AZ9 W  4 .   ? 28.121  31.615  -42.279  1.00 43.84  ? 803  A1AZ9 D C07 1 
HETATM 13988 F  F12 . A1AZ9 W  4 .   ? 30.080  36.671  -44.873  1.00 49.67  ? 803  A1AZ9 D F12 1 
HETATM 13989 F  F13 . A1AZ9 W  4 .   ? 29.000  39.029  -45.644  1.00 75.16  ? 803  A1AZ9 D F13 1 
HETATM 13990 F  F21 . A1AZ9 W  4 .   ? 24.919  40.164  -47.437  1.00 96.33  ? 803  A1AZ9 D F21 1 
HETATM 13991 N  N01 . A1AZ9 W  4 .   ? 29.960  33.997  -45.288  1.00 35.59  ? 803  A1AZ9 D N01 1 
HETATM 13992 N  N02 . A1AZ9 W  4 .   ? 31.763  32.570  -45.439  1.00 38.96  ? 803  A1AZ9 D N02 1 
HETATM 13993 N  N18 . A1AZ9 W  4 .   ? 24.769  37.044  -48.012  1.00 79.60  ? 803  A1AZ9 D N18 1 
HETATM 13994 C  C1  . GOL   X  5 .   ? 12.354  16.029  -46.317  1.00 71.51  ? 804  GOL   D C1  1 
HETATM 13995 O  O1  . GOL   X  5 .   ? 12.292  17.420  -46.069  1.00 77.32  ? 804  GOL   D O1  1 
HETATM 13996 C  C2  . GOL   X  5 .   ? 13.614  15.450  -45.676  1.00 63.10  ? 804  GOL   D C2  1 
HETATM 13997 O  O2  . GOL   X  5 .   ? 14.575  16.454  -45.443  1.00 52.15  ? 804  GOL   D O2  1 
HETATM 13998 C  C3  . GOL   X  5 .   ? 14.270  14.363  -46.515  1.00 65.06  ? 804  GOL   D C3  1 
HETATM 13999 O  O3  . GOL   X  5 .   ? 15.605  14.251  -46.058  1.00 68.33  ? 804  GOL   D O3  1 
HETATM 14000 O  O   . HOH   Y  7 .   ? -32.984 9.576   -54.954  1.00 39.38  ? 901  HOH   A O   1 
HETATM 14001 O  O   . HOH   Y  7 .   ? -21.027 -10.436 -32.857  1.00 54.44  ? 902  HOH   A O   1 
HETATM 14002 O  O   . HOH   Y  7 .   ? -30.942 24.876  -21.387  1.00 38.89  ? 903  HOH   A O   1 
HETATM 14003 O  O   . HOH   Y  7 .   ? -43.161 16.727  -32.713  1.00 31.00  ? 904  HOH   A O   1 
HETATM 14004 O  O   . HOH   Y  7 .   ? -59.977 7.101   -41.540  1.00 54.42  ? 905  HOH   A O   1 
HETATM 14005 O  O   . HOH   Y  7 .   ? -31.378 -26.694 -34.351  1.00 43.24  ? 906  HOH   A O   1 
HETATM 14006 O  O   . HOH   Y  7 .   ? -41.396 13.312  -36.822  1.00 46.14  ? 907  HOH   A O   1 
HETATM 14007 O  O   . HOH   Y  7 .   ? -41.296 -14.161 -47.487  1.00 65.93  ? 908  HOH   A O   1 
HETATM 14008 O  O   . HOH   Y  7 .   ? -29.825 3.912   -27.862  1.00 58.12  ? 909  HOH   A O   1 
HETATM 14009 O  O   . HOH   Y  7 .   ? -22.562 4.479   -48.726  1.00 28.69  ? 910  HOH   A O   1 
HETATM 14010 O  O   . HOH   Y  7 .   ? -21.370 8.499   -40.255  1.00 41.12  ? 911  HOH   A O   1 
HETATM 14011 O  O   . HOH   Y  7 .   ? -20.550 -8.019  -7.799   1.00 54.41  ? 912  HOH   A O   1 
HETATM 14012 O  O   . HOH   Y  7 .   ? -19.657 16.420  -53.474  1.00 53.39  ? 913  HOH   A O   1 
HETATM 14013 O  O   . HOH   Y  7 .   ? -24.356 -8.953  -49.367  1.00 45.59  ? 914  HOH   A O   1 
HETATM 14014 O  O   . HOH   Y  7 .   ? -20.410 15.572  -43.624  1.00 48.93  ? 915  HOH   A O   1 
HETATM 14015 O  O   . HOH   Y  7 .   ? -46.135 7.541   -59.409  1.00 34.93  ? 916  HOH   A O   1 
HETATM 14016 O  O   . HOH   Y  7 .   ? -42.938 -7.678  -37.132  1.00 54.05  ? 917  HOH   A O   1 
HETATM 14017 O  O   . HOH   Y  7 .   ? -40.701 -0.548  -44.265  1.00 49.71  ? 918  HOH   A O   1 
HETATM 14018 O  O   . HOH   Y  7 .   ? -59.896 22.326  -46.715  1.00 53.07  ? 919  HOH   A O   1 
HETATM 14019 O  O   . HOH   Y  7 .   ? -38.983 4.887   -25.955  1.00 43.16  ? 920  HOH   A O   1 
HETATM 14020 O  O   . HOH   Y  7 .   ? -22.890 18.474  -33.598  1.00 60.85  ? 921  HOH   A O   1 
HETATM 14021 O  O   . HOH   Y  7 .   ? -6.866  -2.169  -33.886  1.00 61.19  ? 922  HOH   A O   1 
HETATM 14022 O  O   . HOH   Y  7 .   ? -39.598 -3.478  -61.230  1.00 45.58  ? 923  HOH   A O   1 
HETATM 14023 O  O   . HOH   Y  7 .   ? -28.605 -3.276  -46.880  1.00 37.91  ? 924  HOH   A O   1 
HETATM 14024 O  O   . HOH   Y  7 .   ? -18.751 -11.449 -27.142  1.00 51.56  ? 925  HOH   A O   1 
HETATM 14025 O  O   . HOH   Y  7 .   ? -3.969  2.951   -35.580  1.00 57.35  ? 926  HOH   A O   1 
HETATM 14026 O  O   . HOH   Y  7 .   ? -40.287 7.505   -25.583  1.00 37.63  ? 927  HOH   A O   1 
HETATM 14027 O  O   . HOH   Y  7 .   ? -38.841 20.574  -24.632  1.00 41.59  ? 928  HOH   A O   1 
HETATM 14028 O  O   . HOH   Y  7 .   ? -24.268 -4.764  -51.945  1.00 37.31  ? 929  HOH   A O   1 
HETATM 14029 O  O   . HOH   Y  7 .   ? -41.104 2.196   -46.090  1.00 54.59  ? 930  HOH   A O   1 
HETATM 14030 O  O   . HOH   Y  7 .   ? -29.390 10.557  -28.576  1.00 39.25  ? 931  HOH   A O   1 
HETATM 14031 O  O   . HOH   Y  7 .   ? -47.611 4.836   -51.278  1.00 39.34  ? 932  HOH   A O   1 
HETATM 14032 O  O   . HOH   Y  7 .   ? -28.511 4.690   -30.225  1.00 50.05  ? 933  HOH   A O   1 
HETATM 14033 O  O   . HOH   Y  7 .   ? -49.648 -4.467  -49.869  1.00 50.91  ? 934  HOH   A O   1 
HETATM 14034 O  O   . HOH   Y  7 .   ? -25.782 27.146  -24.712  1.00 56.43  ? 935  HOH   A O   1 
HETATM 14035 O  O   . HOH   Y  7 .   ? -51.070 -2.071  -50.074  1.00 51.45  ? 936  HOH   A O   1 
HETATM 14036 O  O   . HOH   Y  7 .   ? -31.416 11.005  -30.794  1.00 53.68  ? 937  HOH   A O   1 
HETATM 14037 O  O   . HOH   Y  7 .   ? -42.023 2.186   -38.662  1.00 49.79  ? 938  HOH   A O   1 
HETATM 14038 O  O   . HOH   Y  7 .   ? -17.072 15.016  -32.688  1.00 42.94  ? 939  HOH   A O   1 
HETATM 14039 O  O   . HOH   Y  7 .   ? -22.698 3.193   -46.014  1.00 34.77  ? 940  HOH   A O   1 
HETATM 14040 O  O   . HOH   Y  7 .   ? -33.477 0.650   -38.519  1.00 56.74  ? 941  HOH   A O   1 
HETATM 14041 O  O   . HOH   Y  7 .   ? -15.678 13.751  -44.092  1.00 54.70  ? 942  HOH   A O   1 
HETATM 14042 O  O   . HOH   Y  7 .   ? -18.594 6.159   -29.994  1.00 35.86  ? 943  HOH   A O   1 
HETATM 14043 O  O   . HOH   Y  7 .   ? -44.582 31.000  -38.547  1.00 57.16  ? 944  HOH   A O   1 
HETATM 14044 O  O   . HOH   Y  7 .   ? -52.307 2.987   -28.011  1.00 52.81  ? 945  HOH   A O   1 
HETATM 14045 O  O   . HOH   Y  7 .   ? -37.808 31.428  -23.949  1.00 49.70  ? 946  HOH   A O   1 
HETATM 14046 O  O   . HOH   Y  7 .   ? -49.899 21.006  -58.458  1.00 58.69  ? 947  HOH   A O   1 
HETATM 14047 O  O   . HOH   Y  7 .   ? -16.679 18.917  -29.097  1.00 57.13  ? 948  HOH   A O   1 
HETATM 14048 O  O   . HOH   Y  7 .   ? -24.250 6.300   -60.269  1.00 39.33  ? 949  HOH   A O   1 
HETATM 14049 O  O   . HOH   Y  7 .   ? -12.130 1.956   -20.472  1.00 48.35  ? 950  HOH   A O   1 
HETATM 14050 O  O   . HOH   Y  7 .   ? -54.323 3.823   -56.419  1.00 47.91  ? 951  HOH   A O   1 
HETATM 14051 O  O   . HOH   Y  7 .   ? -27.567 18.044  -47.123  1.00 41.77  ? 952  HOH   A O   1 
HETATM 14052 O  O   . HOH   Y  7 .   ? -33.287 25.193  -20.270  1.00 42.69  ? 953  HOH   A O   1 
HETATM 14053 O  O   . HOH   Y  7 .   ? -64.792 10.220  -47.993  1.00 54.62  ? 954  HOH   A O   1 
HETATM 14054 O  O   . HOH   Y  7 .   ? -19.150 -10.206 -44.912  1.00 58.45  ? 955  HOH   A O   1 
HETATM 14055 O  O   . HOH   Y  7 .   ? -52.174 3.022   -51.351  1.00 47.42  ? 956  HOH   A O   1 
HETATM 14056 O  O   . HOH   Y  7 .   ? -30.024 6.391   -26.599  1.00 51.45  ? 957  HOH   A O   1 
HETATM 14057 O  O   . HOH   Y  7 .   ? -51.184 29.950  -55.311  1.00 52.47  ? 958  HOH   A O   1 
HETATM 14058 O  O   . HOH   Y  7 .   ? -22.820 18.668  -18.943  1.00 58.14  ? 959  HOH   A O   1 
HETATM 14059 O  O   . HOH   Y  7 .   ? -48.908 3.624   -31.330  1.00 62.06  ? 960  HOH   A O   1 
HETATM 14060 O  O   . HOH   Y  7 .   ? -53.156 17.006  -59.599  1.00 47.49  ? 961  HOH   A O   1 
HETATM 14061 O  O   . HOH   Y  7 .   ? -39.664 14.166  -21.998  1.00 50.72  ? 962  HOH   A O   1 
HETATM 14062 O  O   . HOH   Y  7 .   ? -15.977 13.752  -34.787  1.00 60.41  ? 963  HOH   A O   1 
HETATM 14063 O  O   . HOH   Y  7 .   ? -26.687 11.576  -56.917  1.00 46.89  ? 964  HOH   A O   1 
HETATM 14064 O  O   . HOH   Y  7 .   ? -53.246 21.351  -27.394  1.00 61.80  ? 965  HOH   A O   1 
HETATM 14065 O  O   . HOH   Y  7 .   ? -19.756 8.508   -29.684  1.00 44.03  ? 966  HOH   A O   1 
HETATM 14066 O  O   . HOH   Y  7 .   ? -5.441  3.931   -38.429  1.00 47.33  ? 967  HOH   A O   1 
HETATM 14067 O  O   . HOH   Y  7 .   ? -49.926 7.999   -55.266  1.00 39.35  ? 968  HOH   A O   1 
HETATM 14068 O  O   . HOH   Y  7 .   ? -59.260 38.860  -56.705  1.00 53.59  ? 969  HOH   A O   1 
HETATM 14069 O  O   . HOH   Y  7 .   ? -34.567 -8.633  -28.812  1.00 57.42  ? 970  HOH   A O   1 
HETATM 14070 O  O   . HOH   Y  7 .   ? -24.333 -24.768 -36.190  1.00 41.91  ? 971  HOH   A O   1 
HETATM 14071 O  O   . HOH   Y  7 .   ? -47.881 5.405   -59.269  1.00 37.51  ? 972  HOH   A O   1 
HETATM 14072 O  O   . HOH   Y  7 .   ? -18.399 16.822  -34.138  1.00 50.57  ? 973  HOH   A O   1 
HETATM 14073 O  O   . HOH   Y  7 .   ? -4.412  -5.544  -23.833  1.00 42.00  ? 974  HOH   A O   1 
HETATM 14074 O  O   . HOH   Y  7 .   ? -23.216 -12.184 -33.341  1.00 57.48  ? 975  HOH   A O   1 
HETATM 14075 O  O   . HOH   Y  7 .   ? -45.385 21.810  -58.210  1.00 48.04  ? 976  HOH   A O   1 
HETATM 14076 O  O   . HOH   Y  7 .   ? -52.479 -10.614 -43.099  1.00 64.11  ? 977  HOH   A O   1 
HETATM 14077 O  O   . HOH   Y  7 .   ? -47.683 19.333  -57.998  1.00 51.63  ? 978  HOH   A O   1 
HETATM 14078 O  O   . HOH   Y  7 .   ? -24.154 16.965  -35.834  1.00 42.30  ? 979  HOH   A O   1 
HETATM 14079 O  O   . HOH   Y  7 .   ? -43.982 24.141  -15.551  1.00 53.04  ? 980  HOH   A O   1 
HETATM 14080 O  O   . HOH   Y  7 .   ? -22.938 3.251   -59.704  1.00 36.53  ? 981  HOH   A O   1 
HETATM 14081 O  O   . HOH   Y  7 .   ? -48.800 -3.155  -47.513  1.00 49.85  ? 982  HOH   A O   1 
HETATM 14082 O  O   . HOH   Y  7 .   ? -16.476 18.639  -32.905  1.00 48.24  ? 983  HOH   A O   1 
HETATM 14083 O  O   . HOH   Y  7 .   ? -19.477 16.652  -36.944  1.00 50.99  ? 984  HOH   A O   1 
HETATM 14084 O  O   . HOH   Y  7 .   ? -41.401 33.709  -29.580  1.00 57.26  ? 985  HOH   A O   1 
HETATM 14085 O  O   . HOH   Y  7 .   ? -18.167 -14.584 -33.933  1.00 62.00  ? 986  HOH   A O   1 
HETATM 14086 O  O   . HOH   Y  7 .   ? -43.236 10.699  -32.143  1.00 61.80  ? 987  HOH   A O   1 
HETATM 14087 O  O   . HOH   Y  7 .   ? -18.319 -13.676 -31.815  1.00 59.62  ? 988  HOH   A O   1 
HETATM 14088 O  O   . HOH   Y  7 .   ? -21.142 18.677  -42.081  1.00 62.17  ? 989  HOH   A O   1 
HETATM 14089 O  O   . HOH   Y  7 .   ? -49.766 10.846  -58.966  1.00 53.45  ? 990  HOH   A O   1 
HETATM 14090 O  O   . HOH   Y  7 .   ? -38.870 27.457  -42.885  1.00 46.80  ? 991  HOH   A O   1 
HETATM 14091 O  O   . HOH   Y  7 .   ? -28.579 13.179  -57.378  1.00 31.48  ? 992  HOH   A O   1 
HETATM 14092 O  O   . HOH   Y  7 .   ? -54.886 6.843   -37.655  1.00 52.25  ? 993  HOH   A O   1 
HETATM 14093 O  O   . HOH   Y  7 .   ? -52.120 1.320   -25.524  1.00 60.12  ? 994  HOH   A O   1 
HETATM 14094 O  O   . HOH   Z  7 .   ? -46.249 -1.608  -7.014   1.00 46.94  ? 901  HOH   B O   1 
HETATM 14095 O  O   . HOH   Z  7 .   ? -33.584 4.842   -8.411   1.00 49.32  ? 902  HOH   B O   1 
HETATM 14096 O  O   . HOH   Z  7 .   ? -41.420 -6.541  -18.765  1.00 52.36  ? 903  HOH   B O   1 
HETATM 14097 O  O   . HOH   Z  7 .   ? -34.503 7.599   15.494   1.00 48.41  ? 904  HOH   B O   1 
HETATM 14098 O  O   . HOH   Z  7 .   ? -30.588 16.126  -9.829   1.00 49.13  ? 905  HOH   B O   1 
HETATM 14099 O  O   . HOH   Z  7 .   ? -43.462 5.860   -18.695  1.00 54.37  ? 906  HOH   B O   1 
HETATM 14100 O  O   . HOH   Z  7 .   ? -26.271 17.824  5.813    1.00 42.14  ? 907  HOH   B O   1 
HETATM 14101 O  O   . HOH   Z  7 .   ? -11.305 18.467  -11.718  1.00 49.57  ? 908  HOH   B O   1 
HETATM 14102 O  O   . HOH   Z  7 .   ? -47.758 12.862  14.216   1.00 51.41  ? 909  HOH   B O   1 
HETATM 14103 O  O   . HOH   Z  7 .   ? -55.995 -6.688  -11.340  1.00 40.26  ? 910  HOH   B O   1 
HETATM 14104 O  O   . HOH   Z  7 .   ? -22.595 6.625   9.549    1.00 37.05  ? 911  HOH   B O   1 
HETATM 14105 O  O   . HOH   Z  7 .   ? -54.389 6.658   19.401   1.00 66.21  ? 912  HOH   B O   1 
HETATM 14106 O  O   . HOH   Z  7 .   ? -44.676 3.622   18.039   1.00 42.00  ? 913  HOH   B O   1 
HETATM 14107 O  O   . HOH   Z  7 .   ? -25.315 16.064  -8.586   1.00 47.98  ? 914  HOH   B O   1 
HETATM 14108 O  O   . HOH   Z  7 .   ? -37.148 13.467  4.000    1.00 36.56  ? 915  HOH   B O   1 
HETATM 14109 O  O   . HOH   Z  7 .   ? -26.559 -4.485  4.413    1.00 43.09  ? 916  HOH   B O   1 
HETATM 14110 O  O   . HOH   Z  7 .   ? -39.297 20.707  -12.320  1.00 44.81  ? 917  HOH   B O   1 
HETATM 14111 O  O   . HOH   Z  7 .   ? -46.816 20.260  13.506   1.00 48.52  ? 918  HOH   B O   1 
HETATM 14112 O  O   . HOH   Z  7 .   ? -23.867 3.113   1.061    1.00 36.66  ? 919  HOH   B O   1 
HETATM 14113 O  O   . HOH   Z  7 .   ? -28.344 21.246  1.744    1.00 55.74  ? 920  HOH   B O   1 
HETATM 14114 O  O   . HOH   Z  7 .   ? -37.615 18.039  6.775    1.00 47.30  ? 921  HOH   B O   1 
HETATM 14115 O  O   . HOH   Z  7 .   ? -19.757 15.516  12.150   1.00 41.31  ? 922  HOH   B O   1 
HETATM 14116 O  O   . HOH   Z  7 .   ? -27.210 7.438   -9.798   1.00 39.82  ? 923  HOH   B O   1 
HETATM 14117 O  O   . HOH   Z  7 .   ? -37.820 15.319  6.486    1.00 53.93  ? 924  HOH   B O   1 
HETATM 14118 O  O   . HOH   Z  7 .   ? -33.800 -6.149  -20.127  1.00 56.80  ? 925  HOH   B O   1 
HETATM 14119 O  O   . HOH   Z  7 .   ? -40.222 -7.721  -4.824   1.00 39.54  ? 926  HOH   B O   1 
HETATM 14120 O  O   . HOH   Z  7 .   ? -29.333 -4.950  5.560    1.00 59.50  ? 927  HOH   B O   1 
HETATM 14121 O  O   . HOH   Z  7 .   ? -38.248 18.479  -0.864   1.00 46.95  ? 928  HOH   B O   1 
HETATM 14122 O  O   . HOH   Z  7 .   ? -40.358 6.529   20.954   1.00 71.05  ? 929  HOH   B O   1 
HETATM 14123 O  O   . HOH   Z  7 .   ? -44.476 -0.434  -27.333  1.00 47.92  ? 930  HOH   B O   1 
HETATM 14124 O  O   . HOH   Z  7 .   ? -20.007 2.906   -8.988   1.00 45.33  ? 931  HOH   B O   1 
HETATM 14125 O  O   . HOH   Z  7 .   ? -22.129 7.827   6.800    1.00 38.04  ? 932  HOH   B O   1 
HETATM 14126 O  O   . HOH   Z  7 .   ? -23.162 18.227  -15.243  1.00 50.18  ? 933  HOH   B O   1 
HETATM 14127 O  O   . HOH   Z  7 .   ? -26.215 6.159   -19.473  1.00 47.58  ? 934  HOH   B O   1 
HETATM 14128 O  O   . HOH   Z  7 .   ? -53.149 5.043   -4.229   1.00 43.71  ? 935  HOH   B O   1 
HETATM 14129 O  O   . HOH   Z  7 .   ? -21.916 1.173   -9.456   1.00 38.86  ? 936  HOH   B O   1 
HETATM 14130 O  O   . HOH   Z  7 .   ? -55.624 7.701   17.286   1.00 52.12  ? 937  HOH   B O   1 
HETATM 14131 O  O   . HOH   Z  7 .   ? -39.112 12.713  -13.819  1.00 46.84  ? 938  HOH   B O   1 
HETATM 14132 O  O   . HOH   Z  7 .   ? 0.395   12.292  -21.200  1.00 61.84  ? 939  HOH   B O   1 
HETATM 14133 O  O   . HOH   Z  7 .   ? -29.980 16.761  -12.486  1.00 51.76  ? 940  HOH   B O   1 
HETATM 14134 O  O   . HOH   Z  7 .   ? -42.431 30.152  9.504    1.00 60.29  ? 941  HOH   B O   1 
HETATM 14135 O  O   . HOH   Z  7 .   ? -29.314 3.100   17.615   1.00 47.25  ? 942  HOH   B O   1 
HETATM 14136 O  O   . HOH   Z  7 .   ? -41.002 -3.865  10.791   1.00 39.02  ? 943  HOH   B O   1 
HETATM 14137 O  O   . HOH   Z  7 .   ? -28.597 9.636   -11.452  1.00 49.51  ? 944  HOH   B O   1 
HETATM 14138 O  O   . HOH   Z  7 .   ? -41.434 6.081   -17.217  1.00 48.95  ? 945  HOH   B O   1 
HETATM 14139 O  O   . HOH   Z  7 .   ? -16.778 19.116  9.668    1.00 47.20  ? 946  HOH   B O   1 
HETATM 14140 O  O   . HOH   Z  7 .   ? -14.857 12.779  -23.577  1.00 40.59  ? 947  HOH   B O   1 
HETATM 14141 O  O   . HOH   Z  7 .   ? -20.946 17.976  11.832   1.00 47.31  ? 948  HOH   B O   1 
HETATM 14142 O  O   . HOH   Z  7 .   ? -50.776 2.415   18.597   1.00 41.36  ? 949  HOH   B O   1 
HETATM 14143 O  O   . HOH   Z  7 .   ? -7.415  -1.235  -0.082   1.00 48.86  ? 950  HOH   B O   1 
HETATM 14144 O  O   . HOH   Z  7 .   ? -11.794 17.942  5.077    1.00 52.01  ? 951  HOH   B O   1 
HETATM 14145 O  O   . HOH   Z  7 .   ? -15.089 7.744   9.296    1.00 50.68  ? 952  HOH   B O   1 
HETATM 14146 O  O   . HOH   Z  7 .   ? -39.291 22.307  -3.798   1.00 52.45  ? 953  HOH   B O   1 
HETATM 14147 O  O   . HOH   Z  7 .   ? -31.939 22.308  -1.655   1.00 50.30  ? 954  HOH   B O   1 
HETATM 14148 O  O   . HOH   Z  7 .   ? -5.820  19.417  -34.335  1.00 52.71  ? 955  HOH   B O   1 
HETATM 14149 O  O   . HOH   Z  7 .   ? -34.518 -7.729  -17.919  1.00 51.14  ? 956  HOH   B O   1 
HETATM 14150 O  O   . HOH   Z  7 .   ? -34.950 24.449  22.727   1.00 58.10  ? 957  HOH   B O   1 
HETATM 14151 O  O   . HOH   Z  7 .   ? -30.115 -6.277  8.423    1.00 65.32  ? 958  HOH   B O   1 
HETATM 14152 O  O   . HOH   Z  7 .   ? -51.267 16.538  0.564    1.00 62.34  ? 959  HOH   B O   1 
HETATM 14153 O  O   . HOH   Z  7 .   ? -42.001 10.724  -7.554   1.00 46.77  ? 960  HOH   B O   1 
HETATM 14154 O  O   . HOH   Z  7 .   ? -48.950 9.619   18.792   1.00 41.09  ? 961  HOH   B O   1 
HETATM 14155 O  O   . HOH   Z  7 .   ? -30.652 -3.565  -3.558   1.00 49.59  ? 962  HOH   B O   1 
HETATM 14156 O  O   . HOH   Z  7 .   ? -44.783 9.115   -6.835   1.00 61.62  ? 963  HOH   B O   1 
HETATM 14157 O  O   . HOH   Z  7 .   ? -44.758 18.576  -4.897   1.00 53.04  ? 964  HOH   B O   1 
HETATM 14158 O  O   . HOH   Z  7 .   ? -35.595 20.492  -3.190   1.00 60.72  ? 965  HOH   B O   1 
HETATM 14159 O  O   . HOH   Z  7 .   ? -37.643 -6.631  8.465    1.00 47.56  ? 966  HOH   B O   1 
HETATM 14160 O  O   . HOH   AA 7 .   ? 59.256  28.790  -61.114  1.00 64.02  ? 901  HOH   C O   1 
HETATM 14161 O  O   . HOH   AA 7 .   ? 16.748  42.927  -76.629  1.00 38.78  ? 902  HOH   C O   1 
HETATM 14162 O  O   . HOH   AA 7 .   ? 20.485  49.359  -80.054  1.00 43.56  ? 903  HOH   C O   1 
HETATM 14163 O  O   . HOH   AA 7 .   ? 36.715  34.547  -91.946  1.00 33.25  ? 904  HOH   C O   1 
HETATM 14164 O  O   . HOH   AA 7 .   ? 14.941  37.928  -100.493 1.00 43.27  ? 905  HOH   C O   1 
HETATM 14165 O  O   . HOH   AA 7 .   ? 8.699   32.214  -70.848  1.00 54.30  ? 906  HOH   C O   1 
HETATM 14166 O  O   . HOH   AA 7 .   ? 16.205  13.197  -100.226 1.00 61.43  ? 907  HOH   C O   1 
HETATM 14167 O  O   . HOH   AA 7 .   ? 2.518   38.942  -61.568  1.00 56.61  ? 908  HOH   C O   1 
HETATM 14168 O  O   . HOH   AA 7 .   ? 17.828  47.683  -63.050  1.00 38.79  ? 909  HOH   C O   1 
HETATM 14169 O  O   . HOH   AA 7 .   ? 19.363  48.880  -77.354  1.00 39.43  ? 910  HOH   C O   1 
HETATM 14170 O  O   . HOH   AA 7 .   ? 28.164  24.891  -72.308  1.00 53.46  ? 911  HOH   C O   1 
HETATM 14171 O  O   . HOH   AA 7 .   ? 33.856  25.402  -73.866  1.00 46.02  ? 912  HOH   C O   1 
HETATM 14172 O  O   . HOH   AA 7 .   ? 30.722  31.474  -70.962  1.00 40.12  ? 913  HOH   C O   1 
HETATM 14173 O  O   . HOH   AA 7 .   ? 26.075  36.234  -73.629  1.00 37.97  ? 914  HOH   C O   1 
HETATM 14174 O  O   . HOH   AA 7 .   ? 5.835   51.647  -59.654  1.00 52.79  ? 915  HOH   C O   1 
HETATM 14175 O  O   . HOH   AA 7 .   ? 46.804  35.547  -89.569  1.00 47.44  ? 916  HOH   C O   1 
HETATM 14176 O  O   . HOH   AA 7 .   ? 50.272  9.148   -78.417  1.00 49.49  ? 917  HOH   C O   1 
HETATM 14177 O  O   . HOH   AA 7 .   ? 21.726  23.212  -88.944  1.00 47.70  ? 918  HOH   C O   1 
HETATM 14178 O  O   . HOH   AA 7 .   ? -5.231  20.418  -91.691  1.00 54.04  ? 919  HOH   C O   1 
HETATM 14179 O  O   . HOH   AA 7 .   ? 24.991  34.203  -102.360 1.00 57.06  ? 920  HOH   C O   1 
HETATM 14180 O  O   . HOH   AA 7 .   ? 12.658  21.092  -95.869  1.00 39.13  ? 921  HOH   C O   1 
HETATM 14181 O  O   . HOH   AA 7 .   ? 35.591  38.358  -83.098  1.00 41.32  ? 922  HOH   C O   1 
HETATM 14182 O  O   . HOH   AA 7 .   ? 11.951  28.418  -96.603  1.00 51.21  ? 923  HOH   C O   1 
HETATM 14183 O  O   . HOH   AA 7 .   ? 33.364  23.494  -88.073  1.00 39.53  ? 924  HOH   C O   1 
HETATM 14184 O  O   . HOH   AA 7 .   ? 25.514  47.254  -62.359  1.00 60.14  ? 925  HOH   C O   1 
HETATM 14185 O  O   . HOH   AA 7 .   ? 21.258  26.232  -88.384  1.00 57.13  ? 926  HOH   C O   1 
HETATM 14186 O  O   . HOH   AA 7 .   ? 3.583   26.888  -99.207  1.00 55.01  ? 927  HOH   C O   1 
HETATM 14187 O  O   . HOH   AA 7 .   ? 23.857  20.947  -86.499  1.00 50.59  ? 928  HOH   C O   1 
HETATM 14188 O  O   . HOH   AA 7 .   ? 16.443  10.926  -91.809  1.00 58.41  ? 929  HOH   C O   1 
HETATM 14189 O  O   . HOH   AA 7 .   ? 28.149  36.582  -71.478  1.00 41.77  ? 930  HOH   C O   1 
HETATM 14190 O  O   . HOH   AA 7 .   ? 14.863  41.496  -55.106  1.00 53.10  ? 931  HOH   C O   1 
HETATM 14191 O  O   . HOH   AA 7 .   ? 18.117  35.562  -65.382  1.00 43.72  ? 932  HOH   C O   1 
HETATM 14192 O  O   . HOH   AA 7 .   ? 4.516   34.659  -102.162 1.00 46.58  ? 933  HOH   C O   1 
HETATM 14193 O  O   . HOH   AA 7 .   ? 32.881  46.104  -86.526  1.00 51.40  ? 934  HOH   C O   1 
HETATM 14194 O  O   . HOH   AA 7 .   ? 12.681  35.500  -75.212  1.00 46.04  ? 935  HOH   C O   1 
HETATM 14195 O  O   . HOH   AA 7 .   ? 21.068  22.899  -81.389  1.00 44.97  ? 936  HOH   C O   1 
HETATM 14196 O  O   . HOH   AA 7 .   ? 20.222  28.794  -68.510  1.00 45.39  ? 937  HOH   C O   1 
HETATM 14197 O  O   . HOH   AA 7 .   ? 30.217  46.426  -87.825  1.00 53.23  ? 938  HOH   C O   1 
HETATM 14198 O  O   . HOH   AA 7 .   ? -3.504  33.384  -83.401  1.00 50.46  ? 939  HOH   C O   1 
HETATM 14199 O  O   . HOH   AA 7 .   ? 5.393   44.459  -95.817  1.00 45.97  ? 940  HOH   C O   1 
HETATM 14200 O  O   . HOH   AA 7 .   ? 35.021  26.822  -80.532  1.00 58.69  ? 941  HOH   C O   1 
HETATM 14201 O  O   . HOH   AA 7 .   ? 0.686   14.772  -90.335  1.00 51.33  ? 942  HOH   C O   1 
HETATM 14202 O  O   . HOH   AA 7 .   ? 15.530  33.122  -74.952  1.00 62.11  ? 943  HOH   C O   1 
HETATM 14203 O  O   . HOH   AA 7 .   ? 37.274  33.433  -89.078  1.00 37.16  ? 944  HOH   C O   1 
HETATM 14204 O  O   . HOH   AA 7 .   ? 8.873   38.624  -100.761 1.00 54.30  ? 945  HOH   C O   1 
HETATM 14205 O  O   . HOH   AA 7 .   ? 34.284  35.388  -103.334 1.00 47.13  ? 946  HOH   C O   1 
HETATM 14206 O  O   . HOH   AA 7 .   ? 33.135  35.126  -62.751  1.00 54.45  ? 947  HOH   C O   1 
HETATM 14207 O  O   . HOH   AA 7 .   ? 41.385  7.606   -87.441  1.00 52.08  ? 948  HOH   C O   1 
HETATM 14208 O  O   . HOH   AA 7 .   ? 22.725  17.387  -101.912 1.00 49.18  ? 949  HOH   C O   1 
HETATM 14209 O  O   . HOH   AA 7 .   ? 43.510  24.781  -91.178  1.00 55.78  ? 950  HOH   C O   1 
HETATM 14210 O  O   . HOH   AA 7 .   ? 32.266  33.892  -72.343  1.00 41.29  ? 951  HOH   C O   1 
HETATM 14211 O  O   . HOH   AA 7 .   ? 53.680  21.438  -47.688  1.00 47.99  ? 952  HOH   C O   1 
HETATM 14212 O  O   . HOH   AA 7 .   ? 42.609  22.199  -91.784  1.00 52.18  ? 953  HOH   C O   1 
HETATM 14213 O  O   . HOH   AA 7 .   ? 27.260  18.560  -80.682  1.00 52.54  ? 954  HOH   C O   1 
HETATM 14214 O  O   . HOH   AA 7 .   ? 7.786   24.837  -82.685  1.00 61.79  ? 955  HOH   C O   1 
HETATM 14215 O  O   . HOH   AA 7 .   ? 48.517  23.438  -71.049  1.00 57.27  ? 956  HOH   C O   1 
HETATM 14216 O  O   . HOH   AA 7 .   ? 36.528  46.390  -76.184  1.00 58.87  ? 957  HOH   C O   1 
HETATM 14217 O  O   . HOH   AA 7 .   ? 10.311  35.384  -101.193 1.00 48.59  ? 958  HOH   C O   1 
HETATM 14218 O  O   . HOH   AA 7 .   ? 22.334  50.676  -64.094  1.00 47.40  ? 959  HOH   C O   1 
HETATM 14219 O  O   . HOH   AA 7 .   ? 6.272   36.671  -78.161  1.00 38.92  ? 960  HOH   C O   1 
HETATM 14220 O  O   . HOH   AA 7 .   ? 26.202  45.343  -54.273  1.00 50.13  ? 961  HOH   C O   1 
HETATM 14221 O  O   . HOH   AA 7 .   ? 11.080  27.911  -100.448 1.00 61.39  ? 962  HOH   C O   1 
HETATM 14222 O  O   . HOH   AA 7 .   ? 3.298   48.412  -71.085  1.00 50.09  ? 963  HOH   C O   1 
HETATM 14223 O  O   . HOH   AA 7 .   ? 20.059  27.338  -60.136  1.00 48.77  ? 964  HOH   C O   1 
HETATM 14224 O  O   . HOH   AA 7 .   ? 17.272  32.176  -78.074  1.00 45.68  ? 965  HOH   C O   1 
HETATM 14225 O  O   . HOH   AA 7 .   ? 8.935   41.872  -58.828  1.00 53.99  ? 966  HOH   C O   1 
HETATM 14226 O  O   . HOH   AA 7 .   ? 34.254  49.759  -86.837  1.00 57.74  ? 967  HOH   C O   1 
HETATM 14227 O  O   . HOH   AA 7 .   ? 55.228  39.070  -79.060  1.00 40.40  ? 968  HOH   C O   1 
HETATM 14228 O  O   . HOH   AA 7 .   ? 52.222  42.572  -82.387  1.00 45.97  ? 969  HOH   C O   1 
HETATM 14229 O  O   . HOH   AA 7 .   ? 13.898  46.472  -90.154  1.00 51.39  ? 970  HOH   C O   1 
HETATM 14230 O  O   . HOH   AA 7 .   ? 21.749  48.839  -90.518  1.00 40.56  ? 971  HOH   C O   1 
HETATM 14231 O  O   . HOH   AA 7 .   ? 29.249  44.373  -78.581  1.00 49.95  ? 972  HOH   C O   1 
HETATM 14232 O  O   . HOH   AA 7 .   ? 18.906  31.669  -75.962  1.00 51.87  ? 973  HOH   C O   1 
HETATM 14233 O  O   . HOH   AA 7 .   ? 30.048  35.001  -71.403  1.00 35.29  ? 974  HOH   C O   1 
HETATM 14234 O  O   . HOH   AA 7 .   ? 19.576  51.466  -86.778  1.00 58.49  ? 975  HOH   C O   1 
HETATM 14235 O  O   . HOH   AA 7 .   ? 39.631  8.276   -85.714  1.00 67.54  ? 976  HOH   C O   1 
HETATM 14236 O  O   . HOH   AA 7 .   ? 30.121  47.496  -90.678  1.00 55.91  ? 977  HOH   C O   1 
HETATM 14237 O  O   . HOH   AA 7 .   ? 2.279   35.498  -68.047  1.00 62.78  ? 978  HOH   C O   1 
HETATM 14238 O  O   . HOH   AA 7 .   ? 17.159  30.066  -74.601  1.00 50.97  ? 979  HOH   C O   1 
HETATM 14239 O  O   . HOH   AA 7 .   ? 0.878   33.641  -69.915  1.00 64.45  ? 980  HOH   C O   1 
HETATM 14240 O  O   . HOH   AA 7 .   ? 39.380  49.183  -87.545  1.00 53.30  ? 981  HOH   C O   1 
HETATM 14241 O  O   . HOH   AA 7 .   ? 12.228  55.579  -77.179  1.00 54.04  ? 982  HOH   C O   1 
HETATM 14242 O  O   . HOH   AA 7 .   ? 30.929  47.627  -85.546  1.00 52.72  ? 983  HOH   C O   1 
HETATM 14243 O  O   . HOH   BA 7 .   ? 43.870  52.069  -45.377  1.00 48.55  ? 901  HOH   D O   1 
HETATM 14244 O  O   . HOH   BA 7 .   ? 35.531  65.934  -45.845  1.00 51.43  ? 902  HOH   D O   1 
HETATM 14245 O  O   . HOH   BA 7 .   ? 40.057  46.770  -36.132  1.00 58.16  ? 903  HOH   D O   1 
HETATM 14246 O  O   . HOH   BA 7 .   ? 40.643  52.527  -54.826  1.00 50.79  ? 904  HOH   D O   1 
HETATM 14247 O  O   . HOH   BA 7 .   ? 18.832  31.235  -59.034  1.00 53.64  ? 905  HOH   D O   1 
HETATM 14248 O  O   . HOH   BA 7 .   ? 35.820  21.618  -30.759  1.00 53.61  ? 906  HOH   D O   1 
HETATM 14249 O  O   . HOH   BA 7 .   ? 16.499  30.235  -58.207  1.00 43.55  ? 907  HOH   D O   1 
HETATM 14250 O  O   . HOH   BA 7 .   ? 33.154  23.967  -37.316  1.00 40.44  ? 908  HOH   D O   1 
HETATM 14251 O  O   . HOH   BA 7 .   ? 19.986  18.237  -67.523  1.00 57.46  ? 909  HOH   D O   1 
HETATM 14252 O  O   . HOH   BA 7 .   ? 22.908  19.948  -48.527  1.00 36.23  ? 910  HOH   D O   1 
HETATM 14253 O  O   . HOH   BA 7 .   ? 18.443  25.973  -61.453  1.00 53.83  ? 911  HOH   D O   1 
HETATM 14254 O  O   . HOH   BA 7 .   ? 38.577  49.044  -73.868  1.00 49.37  ? 912  HOH   D O   1 
HETATM 14255 O  O   . HOH   BA 7 .   ? 14.838  33.753  -31.868  1.00 46.29  ? 913  HOH   D O   1 
HETATM 14256 O  O   . HOH   BA 7 .   ? 47.651  48.854  -71.854  1.00 61.84  ? 914  HOH   D O   1 
HETATM 14257 O  O   . HOH   BA 7 .   ? 51.341  37.633  -57.474  1.00 48.02  ? 915  HOH   D O   1 
HETATM 14258 O  O   . HOH   BA 7 .   ? 19.067  36.734  -36.657  1.00 40.34  ? 916  HOH   D O   1 
HETATM 14259 O  O   . HOH   BA 7 .   ? 37.185  37.032  -33.480  1.00 34.62  ? 917  HOH   D O   1 
HETATM 14260 O  O   . HOH   BA 7 .   ? 19.318  33.517  -56.484  1.00 42.25  ? 918  HOH   D O   1 
HETATM 14261 O  O   . HOH   BA 7 .   ? 30.944  22.670  -49.312  1.00 56.33  ? 919  HOH   D O   1 
HETATM 14262 O  O   . HOH   BA 7 .   ? 11.759  36.359  -31.021  1.00 46.67  ? 920  HOH   D O   1 
HETATM 14263 O  O   . HOH   BA 7 .   ? 28.517  16.288  -60.829  1.00 43.69  ? 921  HOH   D O   1 
HETATM 14264 O  O   . HOH   BA 7 .   ? 43.625  27.418  -47.147  1.00 64.55  ? 922  HOH   D O   1 
HETATM 14265 O  O   . HOH   BA 7 .   ? 20.447  20.574  -57.394  1.00 46.86  ? 923  HOH   D O   1 
HETATM 14266 O  O   . HOH   BA 7 .   ? 32.371  30.380  -36.912  1.00 48.20  ? 924  HOH   D O   1 
HETATM 14267 O  O   . HOH   BA 7 .   ? 36.936  22.664  -48.897  1.00 44.09  ? 925  HOH   D O   1 
HETATM 14268 O  O   . HOH   BA 7 .   ? 41.824  26.288  -49.011  1.00 58.36  ? 926  HOH   D O   1 
HETATM 14269 O  O   . HOH   BA 7 .   ? 16.055  24.523  -49.478  1.00 41.07  ? 927  HOH   D O   1 
HETATM 14270 O  O   . HOH   BA 7 .   ? 36.943  38.074  -36.366  1.00 42.51  ? 928  HOH   D O   1 
HETATM 14271 O  O   . HOH   BA 7 .   ? 32.595  20.406  -62.755  1.00 56.10  ? 929  HOH   D O   1 
HETATM 14272 O  O   . HOH   BA 7 .   ? 26.796  39.411  -50.464  1.00 48.66  ? 930  HOH   D O   1 
HETATM 14273 O  O   . HOH   BA 7 .   ? 18.579  41.765  -38.110  1.00 46.52  ? 931  HOH   D O   1 
HETATM 14274 O  O   . HOH   BA 7 .   ? 11.279  41.918  -35.719  1.00 33.37  ? 932  HOH   D O   1 
HETATM 14275 O  O   . HOH   BA 7 .   ? 20.103  20.264  -69.790  1.00 57.61  ? 933  HOH   D O   1 
HETATM 14276 O  O   . HOH   BA 7 .   ? 40.052  24.254  -62.967  1.00 42.52  ? 934  HOH   D O   1 
HETATM 14277 O  O   . HOH   BA 7 .   ? 31.800  46.304  -30.615  1.00 43.24  ? 935  HOH   D O   1 
HETATM 14278 O  O   . HOH   BA 7 .   ? 16.451  49.144  -44.953  1.00 43.56  ? 936  HOH   D O   1 
HETATM 14279 O  O   . HOH   BA 7 .   ? 22.021  39.695  -44.944  1.00 60.39  ? 937  HOH   D O   1 
HETATM 14280 O  O   . HOH   BA 7 .   ? 25.842  40.729  -43.901  1.00 48.78  ? 938  HOH   D O   1 
HETATM 14281 O  O   . HOH   BA 7 .   ? 37.695  33.039  -41.880  1.00 37.37  ? 939  HOH   D O   1 
HETATM 14282 O  O   . HOH   BA 7 .   ? 2.526   10.551  -38.623  1.00 54.76  ? 940  HOH   D O   1 
HETATM 14283 O  O   . HOH   BA 7 .   ? 17.907  39.570  -36.050  1.00 51.73  ? 941  HOH   D O   1 
HETATM 14284 O  O   . HOH   BA 7 .   ? 30.942  42.676  -44.123  1.00 64.36  ? 942  HOH   D O   1 
HETATM 14285 O  O   . HOH   BA 7 .   ? 47.741  46.783  -43.273  1.00 43.93  ? 943  HOH   D O   1 
HETATM 14286 O  O   . HOH   BA 7 .   ? 43.788  27.591  -38.456  1.00 58.05  ? 944  HOH   D O   1 
HETATM 14287 O  O   . HOH   BA 7 .   ? 9.570   45.864  -32.452  1.00 45.60  ? 945  HOH   D O   1 
HETATM 14288 O  O   . HOH   BA 7 .   ? 18.266  28.599  -45.836  1.00 50.43  ? 946  HOH   D O   1 
HETATM 14289 O  O   . HOH   BA 7 .   ? 28.001  44.869  -37.199  1.00 49.08  ? 947  HOH   D O   1 
HETATM 14290 O  O   . HOH   BA 7 .   ? 49.359  56.510  -73.525  1.00 57.46  ? 948  HOH   D O   1 
HETATM 14291 O  O   . HOH   BA 7 .   ? 31.542  23.252  -35.117  1.00 37.45  ? 949  HOH   D O   1 
HETATM 14292 O  O   . HOH   BA 7 .   ? 40.272  52.184  -37.609  1.00 56.51  ? 950  HOH   D O   1 
HETATM 14293 O  O   . HOH   BA 7 .   ? 20.390  27.763  -20.980  1.00 66.28  ? 951  HOH   D O   1 
HETATM 14294 O  O   . HOH   BA 7 .   ? 36.638  53.518  -47.924  1.00 58.49  ? 952  HOH   D O   1 
HETATM 14295 O  O   . HOH   BA 7 .   ? 29.859  30.837  -53.657  1.00 33.33  ? 953  HOH   D O   1 
HETATM 14296 O  O   . HOH   BA 7 .   ? 31.078  36.664  -52.052  1.00 32.89  ? 954  HOH   D O   1 
HETATM 14297 O  O   . HOH   BA 7 .   ? 38.241  47.917  -34.459  1.00 60.92  ? 955  HOH   D O   1 
HETATM 14298 O  O   . HOH   BA 7 .   ? 16.892  4.013   -28.450  1.00 51.17  ? 956  HOH   D O   1 
HETATM 14299 O  O   . HOH   BA 7 .   ? 10.622  36.507  -42.512  1.00 51.17  ? 957  HOH   D O   1 
HETATM 14300 O  O   . HOH   BA 7 .   ? 39.303  24.730  -59.646  1.00 49.99  ? 958  HOH   D O   1 
HETATM 14301 O  O   . HOH   BA 7 .   ? 40.781  43.563  -32.430  1.00 53.26  ? 959  HOH   D O   1 
HETATM 14302 O  O   . HOH   BA 7 .   ? 26.016  16.027  -62.120  1.00 51.55  ? 960  HOH   D O   1 
HETATM 14303 O  O   . HOH   BA 7 .   ? 6.259   35.590  -58.409  1.00 46.48  ? 961  HOH   D O   1 
HETATM 14304 O  O   . HOH   BA 7 .   ? 41.876  52.847  -39.428  1.00 55.34  ? 962  HOH   D O   1 
HETATM 14305 O  O   . HOH   BA 7 .   ? 18.474  28.134  -22.766  1.00 40.97  ? 963  HOH   D O   1 
HETATM 14306 O  O   . HOH   BA 7 .   ? 53.733  37.744  -43.605  1.00 54.55  ? 964  HOH   D O   1 
HETATM 14307 O  O   . HOH   BA 7 .   ? 7.199   41.158  -36.075  1.00 43.79  ? 965  HOH   D O   1 
HETATM 14308 O  O   . HOH   BA 7 .   ? 18.168  55.593  -34.867  1.00 66.59  ? 966  HOH   D O   1 
HETATM 14309 O  O   . HOH   BA 7 .   ? 39.882  46.780  -66.818  1.00 43.07  ? 967  HOH   D O   1 
HETATM 14310 O  O   . HOH   BA 7 .   ? 2.133   38.410  -43.588  1.00 64.15  ? 968  HOH   D O   1 
HETATM 14311 O  O   . HOH   BA 7 .   ? 14.597  32.869  -57.009  1.00 67.99  ? 969  HOH   D O   1 
HETATM 14312 O  O   . HOH   BA 7 .   ? 10.633  23.106  -40.756  1.00 47.07  ? 970  HOH   D O   1 
HETATM 14313 O  O   . HOH   BA 7 .   ? 28.095  57.815  -24.822  1.00 45.95  ? 971  HOH   D O   1 
HETATM 14314 O  O   . HOH   BA 7 .   ? 21.745  49.526  -22.091  1.00 44.03  ? 972  HOH   D O   1 
HETATM 14315 O  O   . HOH   BA 7 .   ? 9.611   32.871  -27.149  1.00 38.87  ? 973  HOH   D O   1 
HETATM 14316 O  O   . HOH   BA 7 .   ? 36.099  24.906  -26.371  1.00 48.79  ? 974  HOH   D O   1 
HETATM 14317 O  O   . HOH   BA 7 .   ? 37.091  18.835  -62.252  1.00 53.52  ? 975  HOH   D O   1 
HETATM 14318 O  O   . HOH   BA 7 .   ? 11.376  35.974  -23.245  1.00 52.18  ? 976  HOH   D O   1 
HETATM 14319 O  O   . HOH   BA 7 .   ? 31.094  54.178  -27.284  1.00 44.18  ? 977  HOH   D O   1 
HETATM 14320 O  O   . HOH   BA 7 .   ? 12.763  26.488  -24.011  1.00 44.96  ? 978  HOH   D O   1 
HETATM 14321 O  O   . HOH   BA 7 .   ? 39.851  33.033  -52.632  1.00 38.41  ? 979  HOH   D O   1 
HETATM 14322 O  O   . HOH   BA 7 .   ? 40.226  25.161  -45.279  1.00 49.06  ? 980  HOH   D O   1 
HETATM 14323 O  O   . HOH   BA 7 .   ? 55.046  46.923  -58.399  1.00 46.83  ? 981  HOH   D O   1 
HETATM 14324 O  O   . HOH   BA 7 .   ? 40.721  22.471  -57.470  1.00 48.46  ? 982  HOH   D O   1 
HETATM 14325 O  O   . HOH   BA 7 .   ? 10.661  20.328  -46.876  1.00 50.08  ? 983  HOH   D O   1 
HETATM 14326 O  O   . HOH   BA 7 .   ? 14.275  19.268  -24.123  1.00 50.19  ? 984  HOH   D O   1 
HETATM 14327 O  O   . HOH   BA 7 .   ? 21.554  10.126  -58.078  1.00 58.62  ? 985  HOH   D O   1 
HETATM 14328 O  O   . HOH   BA 7 .   ? 35.094  24.219  -46.069  1.00 44.40  ? 986  HOH   D O   1 
HETATM 14329 O  O   . HOH   BA 7 .   ? 2.389   33.797  -40.608  1.00 53.18  ? 987  HOH   D O   1 
HETATM 14330 O  O   . HOH   BA 7 .   ? 36.073  27.597  -26.099  1.00 48.19  ? 988  HOH   D O   1 
HETATM 14331 O  O   . HOH   BA 7 .   ? 25.968  18.914  -31.881  1.00 49.58  ? 989  HOH   D O   1 
HETATM 14332 O  O   . HOH   BA 7 .   ? 22.171  61.065  -27.991  1.00 50.92  ? 990  HOH   D O   1 
HETATM 14333 O  O   . HOH   BA 7 .   ? 15.487  17.970  -67.086  1.00 60.95  ? 991  HOH   D O   1 
HETATM 14334 O  O   . HOH   BA 7 .   ? 26.959  41.298  -46.998  1.00 55.13  ? 992  HOH   D O   1 
HETATM 14335 O  O   . HOH   BA 7 .   ? 40.666  35.048  -26.785  1.00 47.71  ? 993  HOH   D O   1 
HETATM 14336 O  O   . HOH   BA 7 .   ? 51.623  30.280  -45.212  1.00 61.22  ? 994  HOH   D O   1 
HETATM 14337 O  O   . HOH   BA 7 .   ? 9.028   34.952  -25.045  1.00 50.97  ? 995  HOH   D O   1 
HETATM 14338 O  O   . HOH   BA 7 .   ? 37.715  22.398  -40.200  1.00 59.59  ? 996  HOH   D O   1 
HETATM 14339 O  O   . HOH   BA 7 .   ? 10.556  30.509  -23.885  1.00 64.08  ? 997  HOH   D O   1 
HETATM 14340 O  O   . HOH   BA 7 .   ? 40.116  46.002  -32.393  1.00 64.19  ? 998  HOH   D O   1 
HETATM 14341 O  O   . HOH   BA 7 .   ? 9.733   39.687  -57.285  1.00 49.28  ? 999  HOH   D O   1 
HETATM 14342 O  O   . HOH   BA 7 .   ? 17.212  8.171   -52.354  1.00 59.31  ? 1000 HOH   D O   1 
HETATM 14343 O  O   . HOH   BA 7 .   ? 29.882  23.166  -25.472  1.00 47.44  ? 1001 HOH   D O   1 
HETATM 14344 O  O   . HOH   BA 7 .   ? 16.938  31.463  -50.070  1.00 58.92  ? 1002 HOH   D O   1 
HETATM 14345 O  O   . HOH   BA 7 .   ? 31.091  29.156  -21.451  1.00 46.32  ? 1003 HOH   D O   1 
HETATM 14346 O  O   . HOH   BA 7 .   ? 1.117   36.116  -43.205  1.00 72.80  ? 1004 HOH   D O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1     N N   . ARG A 3   ? 1.0320 1.1575 0.9959 0.1941  0.0143  -0.0615 304 ARG A N   
2     C CA  . ARG A 3   ? 1.1562 1.2428 1.1044 0.2034  0.0079  -0.0674 304 ARG A CA  
3     C C   . ARG A 3   ? 1.1947 1.2462 1.1369 0.1885  0.0065  -0.0650 304 ARG A C   
4     O O   . ARG A 3   ? 1.2764 1.2988 1.2128 0.1853  0.0032  -0.0622 304 ARG A O   
5     C CB  . ARG A 3   ? 1.2766 1.3622 1.2126 0.2220  0.0055  -0.0793 304 ARG A CB  
6     C CG  . ARG A 3   ? 1.3403 1.3836 1.2572 0.2338  -0.0012 -0.0861 304 ARG A CG  
7     C CD  . ARG A 3   ? 1.3943 1.4345 1.3093 0.2460  -0.0045 -0.0842 304 ARG A CD  
8     N NE  . ARG A 3   ? 1.4105 1.4369 1.3308 0.2319  -0.0047 -0.0741 304 ARG A NE  
9     C CZ  . ARG A 3   ? 1.4522 1.4689 1.3691 0.2395  -0.0081 -0.0712 304 ARG A CZ  
10    N NH1 . ARG A 3   ? 1.4913 1.5102 1.3994 0.2619  -0.0119 -0.0776 304 ARG A NH1 
11    N NH2 . ARG A 3   ? 1.4375 1.4427 1.3590 0.2259  -0.0079 -0.0621 304 ARG A NH2 
12    N N   . PHE A 4   ? 1.0511 1.1070 0.9944 0.1797  0.0090  -0.0662 305 PHE A N   
13    C CA  . PHE A 4   ? 1.0218 1.0540 0.9628 0.1640  0.0085  -0.0635 305 PHE A CA  
14    C C   . PHE A 4   ? 0.9375 0.9949 0.8891 0.1525  0.0136  -0.0586 305 PHE A C   
15    O O   . PHE A 4   ? 1.0125 1.1012 0.9703 0.1569  0.0173  -0.0583 305 PHE A O   
16    C CB  . PHE A 4   ? 1.1733 1.1742 1.0983 0.1672  0.0041  -0.0732 305 PHE A CB  
17    C CG  . PHE A 4   ? 1.4033 1.3715 1.3143 0.1776  -0.0011 -0.0773 305 PHE A CG  
18    C CD1 . PHE A 4   ? 1.5145 1.4839 1.4164 0.1976  -0.0037 -0.0854 305 PHE A CD1 
19    C CD2 . PHE A 4   ? 1.4241 1.3597 1.3295 0.1679  -0.0035 -0.0731 305 PHE A CD2 
20    C CE1 . PHE A 4   ? 1.5221 1.4582 1.4085 0.2087  -0.0089 -0.0890 305 PHE A CE1 
21    C CE2 . PHE A 4   ? 1.4451 1.3474 1.3351 0.1774  -0.0082 -0.0761 305 PHE A CE2 
22    C CZ  . PHE A 4   ? 1.4859 1.3871 1.3657 0.1982  -0.0111 -0.0840 305 PHE A CZ  
23    N N   . LEU A 5   ? 0.7337 0.7776 0.6865 0.1379  0.0138  -0.0547 306 LEU A N   
24    C CA  . LEU A 5   ? 0.6157 0.6786 0.5757 0.1278  0.0179  -0.0501 306 LEU A CA  
25    C C   . LEU A 5   ? 0.7612 0.8033 0.7168 0.1172  0.0158  -0.0516 306 LEU A C   
26    O O   . LEU A 5   ? 0.8666 0.8841 0.8193 0.1113  0.0132  -0.0504 306 LEU A O   
27    C CB  . LEU A 5   ? 0.5487 0.6288 0.5212 0.1194  0.0221  -0.0389 306 LEU A CB  
28    C CG  . LEU A 5   ? 0.6068 0.7192 0.5866 0.1247  0.0263  -0.0362 306 LEU A CG  
29    C CD1 . LEU A 5   ? 0.6179 0.7414 0.6085 0.1142  0.0297  -0.0257 306 LEU A CD1 
30    C CD2 . LEU A 5   ? 0.6822 0.8151 0.6605 0.1272  0.0294  -0.0389 306 LEU A CD2 
31    N N   . LYS A 6   ? 0.8159 0.8695 0.7706 0.1147  0.0171  -0.0541 307 LYS A N   
32    C CA  . LYS A 6   ? 0.7524 0.7913 0.7030 0.1055  0.0148  -0.0574 307 LYS A CA  
33    C C   . LYS A 6   ? 0.6823 0.7362 0.6411 0.0951  0.0180  -0.0492 307 LYS A C   
34    O O   . LYS A 6   ? 0.6228 0.7002 0.5861 0.0970  0.0220  -0.0444 307 LYS A O   
35    C CB  . LYS A 6   ? 0.7453 0.7830 0.6861 0.1119  0.0122  -0.0689 307 LYS A CB  
36    C CG  . LYS A 6   ? 0.8552 0.8655 0.7842 0.1190  0.0075  -0.0783 307 LYS A CG  
37    C CD  . LYS A 6   ? 1.0016 1.0057 0.9198 0.1223  0.0043  -0.0906 307 LYS A CD  
38    C CE  . LYS A 6   ? 1.1455 1.1266 1.0499 0.1347  0.0001  -0.1007 307 LYS A CE  
39    N NZ  . LYS A 6   ? 1.1630 1.1097 1.0614 0.1310  -0.0028 -0.0992 307 LYS A NZ  
40    N N   . VAL A 7   ? 0.6188 0.6584 0.5786 0.0843  0.0165  -0.0473 308 VAL A N   
41    C CA  . VAL A 7   ? 0.6389 0.6896 0.6041 0.0756  0.0184  -0.0416 308 VAL A CA  
42    C C   . VAL A 7   ? 0.6493 0.6932 0.6092 0.0709  0.0150  -0.0497 308 VAL A C   
43    O O   . VAL A 7   ? 0.6144 0.6371 0.5686 0.0683  0.0115  -0.0563 308 VAL A O   
44    C CB  . VAL A 7   ? 0.5115 0.5561 0.4837 0.0670  0.0198  -0.0322 308 VAL A CB  
45    C CG1 . VAL A 7   ? 0.4561 0.5094 0.4336 0.0706  0.0229  -0.0250 308 VAL A CG1 
46    C CG2 . VAL A 7   ? 0.4974 0.5172 0.4667 0.0612  0.0166  -0.0347 308 VAL A CG2 
47    N N   . LYS A 8   ? 0.6440 0.7057 0.6050 0.0697  0.0160  -0.0493 309 LYS A N   
48    C CA  . LYS A 8   ? 0.5617 0.6235 0.5184 0.0658  0.0127  -0.0576 309 LYS A CA  
49    C C   . LYS A 8   ? 0.5747 0.6451 0.5372 0.0574  0.0134  -0.0519 309 LYS A C   
50    O O   . LYS A 8   ? 0.6998 0.7827 0.6669 0.0586  0.0168  -0.0425 309 LYS A O   
51    C CB  . LYS A 8   ? 0.4782 0.5566 0.4293 0.0745  0.0126  -0.0638 309 LYS A CB  
52    C CG  . LYS A 8   ? 0.5798 0.6664 0.5276 0.0709  0.0095  -0.0712 309 LYS A CG  
53    C CD  . LYS A 8   ? 0.6677 0.7701 0.6084 0.0809  0.0092  -0.0779 309 LYS A CD  
54    C CE  . LYS A 8   ? 0.6640 0.7783 0.6016 0.0782  0.0060  -0.0849 309 LYS A CE  
55    N NZ  . LYS A 8   ? 0.8421 0.9706 0.7715 0.0886  0.0056  -0.0921 309 LYS A NZ  
56    N N   . ASN A 9   ? 0.5830 0.6465 0.5450 0.0489  0.0102  -0.0577 310 ASN A N   
57    C CA  . ASN A 9   ? 0.6869 0.7633 0.6537 0.0426  0.0101  -0.0548 310 ASN A CA  
58    C C   . ASN A 9   ? 0.6647 0.7600 0.6278 0.0462  0.0082  -0.0614 310 ASN A C   
59    O O   . ASN A 9   ? 0.7111 0.8024 0.6691 0.0444  0.0045  -0.0725 310 ASN A O   
60    C CB  . ASN A 9   ? 0.7165 0.7801 0.6857 0.0305  0.0081  -0.0574 310 ASN A CB  
61    C CG  . ASN A 9   ? 0.7287 0.8080 0.7043 0.0252  0.0086  -0.0532 310 ASN A CG  
62    O OD1 . ASN A 9   ? 0.6948 0.7916 0.6701 0.0252  0.0066  -0.0580 310 ASN A OD1 
63    N ND2 . ASN A 9   ? 0.8243 0.8985 0.8052 0.0218  0.0110  -0.0446 310 ASN A ND2 
64    N N   . TRP A 10  ? 0.6533 0.7677 0.6175 0.0516  0.0104  -0.0548 311 TRP A N   
65    C CA  . TRP A 10  ? 0.5893 0.7227 0.5484 0.0571  0.0087  -0.0602 311 TRP A CA  
66    C C   . TRP A 10  ? 0.6060 0.7502 0.5669 0.0509  0.0049  -0.0661 311 TRP A C   
67    O O   . TRP A 10  ? 0.6896 0.8507 0.6461 0.0551  0.0026  -0.0719 311 TRP A O   
68    C CB  . TRP A 10  ? 0.5041 0.6522 0.4611 0.0659  0.0127  -0.0503 311 TRP A CB  
69    C CG  . TRP A 10  ? 0.5807 0.7261 0.5347 0.0727  0.0160  -0.0480 311 TRP A CG  
70    C CD1 . TRP A 10  ? 0.5726 0.7087 0.5304 0.0725  0.0196  -0.0401 311 TRP A CD1 
71    C CD2 . TRP A 10  ? 0.5871 0.7416 0.5340 0.0808  0.0158  -0.0544 311 TRP A CD2 
72    N NE1 . TRP A 10  ? 0.6060 0.7468 0.5602 0.0798  0.0219  -0.0411 311 TRP A NE1 
73    C CE2 . TRP A 10  ? 0.6518 0.8036 0.5990 0.0853  0.0197  -0.0498 311 TRP A CE2 
74    C CE3 . TRP A 10  ? 0.7075 0.8738 0.6476 0.0848  0.0126  -0.0642 311 TRP A CE3 
75    C CZ2 . TRP A 10  ? 0.7381 0.8994 0.6793 0.0942  0.0209  -0.0543 311 TRP A CZ2 
76    C CZ3 . TRP A 10  ? 0.6898 0.8636 0.6230 0.0938  0.0136  -0.0687 311 TRP A CZ3 
77    C CH2 . TRP A 10  ? 0.6938 0.8655 0.6277 0.0986  0.0179  -0.0637 311 TRP A CH2 
78    N N   . GLU A 11  ? 0.6765 0.8132 0.6436 0.0410  0.0042  -0.0653 312 GLU A N   
79    C CA  . GLU A 11  ? 0.6260 0.7750 0.5962 0.0335  0.0007  -0.0717 312 GLU A CA  
80    C C   . GLU A 11  ? 0.6800 0.8163 0.6487 0.0228  -0.0029 -0.0838 312 GLU A C   
81    O O   . GLU A 11  ? 0.7507 0.9006 0.7194 0.0178  -0.0067 -0.0931 312 GLU A O   
82    C CB  . GLU A 11  ? 0.4688 0.6203 0.4466 0.0287  0.0026  -0.0634 312 GLU A CB  
83    C CG  . GLU A 11  ? 0.5427 0.7132 0.5252 0.0222  -0.0005 -0.0688 312 GLU A CG  
84    C CD  . GLU A 11  ? 0.8088 0.9774 0.7988 0.0154  0.0014  -0.0627 312 GLU A CD  
85    O OE1 . GLU A 11  ? 0.8895 1.0436 0.8804 0.0176  0.0050  -0.0530 312 GLU A OE1 
86    O OE2 . GLU A 11  ? 0.8558 1.0390 0.8508 0.0076  -0.0008 -0.0681 312 GLU A OE2 
87    N N   . THR A 12  ? 0.7244 0.8344 0.6909 0.0195  -0.0020 -0.0838 313 THR A N   
88    C CA  . THR A 12  ? 0.6032 0.6936 0.5658 0.0090  -0.0050 -0.0938 313 THR A CA  
89    C C   . THR A 12  ? 0.6850 0.7560 0.6377 0.0154  -0.0061 -0.0999 313 THR A C   
90    O O   . THR A 12  ? 0.7314 0.7808 0.6780 0.0078  -0.0087 -0.1082 313 THR A O   
91    C CB  . THR A 12  ? 0.6783 0.7503 0.6449 -0.0015 -0.0032 -0.0883 313 THR A CB  
92    O OG1 . THR A 12  ? 0.6931 0.7493 0.6588 0.0057  0.0000  -0.0793 313 THR A OG1 
93    C CG2 . THR A 12  ? 0.6890 0.7807 0.6650 -0.0070 -0.0019 -0.0827 313 THR A CG2 
94    N N   . GLU A 13  ? 0.7574 0.8347 0.7077 0.0290  -0.0040 -0.0958 314 GLU A N   
95    C CA  . GLU A 13  ? 0.7999 0.8632 0.7413 0.0378  -0.0047 -0.1012 314 GLU A CA  
96    C C   . GLU A 13  ? 0.8402 0.8733 0.7787 0.0363  -0.0041 -0.0992 314 GLU A C   
97    O O   . GLU A 13  ? 0.8439 0.8636 0.7742 0.0447  -0.0050 -0.1040 314 GLU A O   
98    C CB  . GLU A 13  ? 0.8268 0.8899 0.7596 0.0368  -0.0095 -0.1162 314 GLU A CB  
99    C CG  . GLU A 13  ? 0.7749 0.8674 0.7100 0.0362  -0.0113 -0.1201 314 GLU A CG  
100   C CD  . GLU A 13  ? 0.9796 1.0917 0.9100 0.0505  -0.0105 -0.1208 314 GLU A CD  
101   O OE1 . GLU A 13  ? 1.0418 1.1541 0.9719 0.0606  -0.0066 -0.1128 314 GLU A OE1 
102   O OE2 . GLU A 13  ? 1.0833 1.2124 1.0103 0.0512  -0.0138 -0.1294 314 GLU A OE2 
103   N N   . VAL A 14  ? 0.8227 0.8459 0.7669 0.0270  -0.0026 -0.0920 315 VAL A N   
104   C CA  . VAL A 14  ? 0.7922 0.7872 0.7329 0.0257  -0.0021 -0.0890 315 VAL A CA  
105   C C   . VAL A 14  ? 0.8688 0.8655 0.8103 0.0390  0.0008  -0.0819 315 VAL A C   
106   O O   . VAL A 14  ? 0.8983 0.9157 0.8473 0.0435  0.0041  -0.0735 315 VAL A O   
107   C CB  . VAL A 14  ? 0.7882 0.7773 0.7354 0.0133  -0.0006 -0.0818 315 VAL A CB  
108   C CG1 . VAL A 14  ? 0.6739 0.6370 0.6177 0.0140  0.0005  -0.0763 315 VAL A CG1 
109   C CG2 . VAL A 14  ? 0.8674 0.8529 0.8131 -0.0014 -0.0033 -0.0898 315 VAL A CG2 
110   N N   . VAL A 15  ? 0.8242 0.7987 0.7572 0.0453  -0.0005 -0.0853 316 VAL A N   
111   C CA  . VAL A 15  ? 0.7792 0.7577 0.7131 0.0584  0.0018  -0.0801 316 VAL A CA  
112   C C   . VAL A 15  ? 0.7948 0.7482 0.7256 0.0585  0.0016  -0.0759 316 VAL A C   
113   O O   . VAL A 15  ? 0.8570 0.7825 0.7776 0.0553  -0.0015 -0.0819 316 VAL A O   
114   C CB  . VAL A 15  ? 0.7252 0.7085 0.6510 0.0713  0.0004  -0.0890 316 VAL A CB  
115   C CG1 . VAL A 15  ? 0.6710 0.6657 0.5997 0.0842  0.0035  -0.0833 316 VAL A CG1 
116   C CG2 . VAL A 15  ? 0.7063 0.7132 0.6335 0.0708  0.0002  -0.0934 316 VAL A CG2 
117   N N   . LEU A 16  ? 0.8136 0.7763 0.7521 0.0624  0.0048  -0.0659 317 LEU A N   
118   C CA  . LEU A 16  ? 0.7198 0.6640 0.6572 0.0628  0.0048  -0.0603 317 LEU A CA  
119   C C   . LEU A 16  ? 0.7819 0.7348 0.7199 0.0771  0.0060  -0.0583 317 LEU A C   
120   O O   . LEU A 16  ? 0.8465 0.8254 0.7910 0.0827  0.0086  -0.0563 317 LEU A O   
121   C CB  . LEU A 16  ? 0.5259 0.4759 0.4732 0.0528  0.0075  -0.0500 317 LEU A CB  
122   C CG  . LEU A 16  ? 0.5351 0.4883 0.4854 0.0395  0.0073  -0.0510 317 LEU A CG  
123   C CD1 . LEU A 16  ? 0.3717 0.3363 0.3321 0.0329  0.0103  -0.0410 317 LEU A CD1 
124   C CD2 . LEU A 16  ? 0.5946 0.5200 0.5351 0.0309  0.0043  -0.0571 317 LEU A CD2 
125   N N   . THR A 17  ? 0.8278 0.7596 0.7588 0.0831  0.0040  -0.0585 318 THR A N   
126   C CA  . THR A 17  ? 0.8381 0.7783 0.7684 0.0983  0.0042  -0.0587 318 THR A CA  
127   C C   . THR A 17  ? 0.8042 0.7462 0.7410 0.0985  0.0056  -0.0492 318 THR A C   
128   O O   . THR A 17  ? 0.7516 0.6689 0.6817 0.0976  0.0034  -0.0476 318 THR A O   
129   C CB  . THR A 17  ? 0.8699 0.7862 0.7847 0.1095  0.0000  -0.0684 318 THR A CB  
130   O OG1 . THR A 17  ? 0.8632 0.7778 0.7716 0.1085  -0.0016 -0.0780 318 THR A OG1 
131   C CG2 . THR A 17  ? 0.8897 0.8209 0.8048 0.1269  0.0003  -0.0694 318 THR A CG2 
132   N N   . ASP A 18  ? 0.7940 0.7648 0.7427 0.0999  0.0093  -0.0432 319 ASP A N   
133   C CA  . ASP A 18  ? 0.7294 0.7063 0.6858 0.0981  0.0108  -0.0344 319 ASP A CA  
134   C C   . ASP A 18  ? 0.8042 0.7862 0.7587 0.1127  0.0096  -0.0362 319 ASP A C   
135   O O   . ASP A 18  ? 0.8306 0.8382 0.7901 0.1204  0.0116  -0.0376 319 ASP A O   
136   C CB  . ASP A 18  ? 0.7604 0.7637 0.7294 0.0909  0.0153  -0.0275 319 ASP A CB  
137   C CG  . ASP A 18  ? 0.8062 0.8152 0.7829 0.0874  0.0168  -0.0191 319 ASP A CG  
138   O OD1 . ASP A 18  ? 0.8164 0.8329 0.7943 0.0961  0.0163  -0.0190 319 ASP A OD1 
139   O OD2 . ASP A 18  ? 0.7830 0.7901 0.7644 0.0764  0.0183  -0.0132 319 ASP A OD2 
140   N N   . THR A 19  ? 0.6983 0.6571 0.6450 0.1167  0.0063  -0.0359 320 THR A N   
141   C CA  . THR A 19  ? 0.6574 0.6224 0.6030 0.1307  0.0047  -0.0362 320 THR A CA  
142   C C   . THR A 19  ? 0.7440 0.7200 0.6993 0.1263  0.0060  -0.0274 320 THR A C   
143   O O   . THR A 19  ? 0.7944 0.7872 0.7533 0.1364  0.0055  -0.0272 320 THR A O   
144   C CB  . THR A 19  ? 0.6224 0.5535 0.5509 0.1404  -0.0003 -0.0412 320 THR A CB  
145   O OG1 . THR A 19  ? 0.5743 0.4802 0.4986 0.1306  -0.0014 -0.0353 320 THR A OG1 
146   C CG2 . THR A 19  ? 0.5250 0.4385 0.4420 0.1421  -0.0021 -0.0503 320 THR A CG2 
147   N N   . LEU A 20  ? 0.6163 0.5843 0.5756 0.1117  0.0074  -0.0210 321 LEU A N   
148   C CA  . LEU A 20  ? 0.7131 0.6865 0.6793 0.1069  0.0081  -0.0133 321 LEU A CA  
149   C C   . LEU A 20  ? 0.6901 0.6981 0.6701 0.1065  0.0114  -0.0101 321 LEU A C   
150   O O   . LEU A 20  ? 0.6853 0.7026 0.6704 0.1076  0.0110  -0.0063 321 LEU A O   
151   C CB  . LEU A 20  ? 0.7477 0.7070 0.7148 0.0917  0.0093  -0.0081 321 LEU A CB  
152   C CG  . LEU A 20  ? 0.8174 0.7773 0.7892 0.0864  0.0096  -0.0007 321 LEU A CG  
153   C CD1 . LEU A 20  ? 0.8605 0.8018 0.8222 0.0955  0.0056  -0.0007 321 LEU A CD1 
154   C CD2 . LEU A 20  ? 0.7686 0.7194 0.7423 0.0718  0.0115  0.0039  321 LEU A CD2 
155   N N   . HIS A 21  ? 0.6339 0.6609 0.6194 0.1041  0.0147  -0.0116 322 HIS A N   
156   C CA  . HIS A 21  ? 0.5016 0.5599 0.4989 0.1013  0.0187  -0.0080 322 HIS A CA  
157   C C   . HIS A 21  ? 0.5303 0.6085 0.5309 0.1128  0.0178  -0.0103 322 HIS A C   
158   O O   . HIS A 21  ? 0.5783 0.6816 0.5891 0.1088  0.0207  -0.0067 322 HIS A O   
159   C CB  . HIS A 21  ? 0.6215 0.6942 0.6205 0.0991  0.0222  -0.0097 322 HIS A CB  
160   C CG  . HIS A 21  ? 0.5511 0.6308 0.5447 0.1122  0.0212  -0.0179 322 HIS A CG  
161   N ND1 . HIS A 21  ? 0.5815 0.6389 0.5638 0.1178  0.0178  -0.0248 322 HIS A ND1 
162   C CD2 . HIS A 21  ? 0.5473 0.6540 0.5446 0.1207  0.0232  -0.0207 322 HIS A CD2 
163   C CE1 . HIS A 21  ? 0.6133 0.6823 0.5919 0.1303  0.0175  -0.0318 322 HIS A CE1 
164   N NE2 . HIS A 21  ? 0.5779 0.6782 0.5659 0.1327  0.0208  -0.0294 322 HIS A NE2 
165   N N   . LEU A 22  ? 0.5828 0.6506 0.5744 0.1270  0.0139  -0.0166 323 LEU A N   
166   C CA  . LEU A 22  ? 0.6766 0.7645 0.6707 0.1402  0.0124  -0.0194 323 LEU A CA  
167   C C   . LEU A 22  ? 0.7878 0.8787 0.7870 0.1375  0.0109  -0.0142 323 LEU A C   
168   O O   . LEU A 22  ? 0.8469 0.9647 0.8533 0.1437  0.0108  -0.0149 323 LEU A O   
169   C CB  . LEU A 22  ? 0.7132 0.7838 0.6936 0.1576  0.0078  -0.0274 323 LEU A CB  
170   C CG  . LEU A 22  ? 0.7334 0.8035 0.7077 0.1630  0.0087  -0.0345 323 LEU A CG  
171   C CD1 . LEU A 22  ? 0.7372 0.7878 0.6963 0.1814  0.0036  -0.0430 323 LEU A CD1 
172   C CD2 . LEU A 22  ? 0.5927 0.7028 0.5782 0.1630  0.0136  -0.0353 323 LEU A CD2 
173   N N   . LYS A 23  ? 0.7776 0.8439 0.7735 0.1278  0.0098  -0.0092 324 LYS A N   
174   C CA  . LYS A 23  ? 0.5876 0.6514 0.5855 0.1256  0.0078  -0.0045 324 LYS A CA  
175   C C   . LYS A 23  ? 0.6324 0.7122 0.6424 0.1104  0.0114  0.0017  324 LYS A C   
176   O O   . LYS A 23  ? 0.6699 0.7405 0.6802 0.1045  0.0101  0.0061  324 LYS A O   
177   C CB  . LYS A 23  ? 0.6628 0.6888 0.6479 0.1248  0.0045  -0.0028 324 LYS A CB  
178   C CG  . LYS A 23  ? 0.8091 0.8166 0.7801 0.1416  -0.0004 -0.0076 324 LYS A CG  
179   C CD  . LYS A 23  ? 0.9230 0.8901 0.8796 0.1381  -0.0028 -0.0056 324 LYS A CD  
180   C CE  . LYS A 23  ? 1.0251 0.9671 0.9654 0.1504  -0.0060 -0.0121 324 LYS A CE  
181   N NZ  . LYS A 23  ? 0.9198 0.8611 0.8602 0.1461  -0.0037 -0.0172 324 LYS A NZ  
182   N N   . SER A 24  ? 0.7028 0.8045 0.7214 0.1038  0.0160  0.0022  325 SER A N   
183   C CA  . SER A 24  ? 0.8095 0.9241 0.8377 0.0896  0.0194  0.0080  325 SER A CA  
184   C C   . SER A 24  ? 0.9215 1.0712 0.9600 0.0909  0.0212  0.0071  325 SER A C   
185   O O   . SER A 24  ? 1.0303 1.1986 1.0699 0.1004  0.0218  0.0024  325 SER A O   
186   C CB  . SER A 24  ? 0.7550 0.8648 0.7835 0.0789  0.0236  0.0108  325 SER A CB  
187   O OG  . SER A 24  ? 0.7967 0.9326 0.8318 0.0764  0.0279  0.0110  325 SER A OG  
188   N N   . THR A 25  ? 0.9814 1.1413 1.0272 0.0814  0.0218  0.0110  326 THR A N   
189   C CA  . THR A 25  ? 1.0905 1.2857 1.1467 0.0803  0.0236  0.0099  326 THR A CA  
190   C C   . THR A 25  ? 1.0164 1.2207 1.0799 0.0626  0.0278  0.0153  326 THR A C   
191   O O   . THR A 25  ? 1.1048 1.3351 1.1771 0.0579  0.0287  0.0150  326 THR A O   
192   C CB  . THR A 25  ? 1.1181 1.3242 1.1763 0.0902  0.0185  0.0069  326 THR A CB  
193   O OG1 . THR A 25  ? 1.2163 1.3914 1.2650 0.0941  0.0140  0.0082  326 THR A OG1 
194   C CG2 . THR A 25  ? 0.8669 1.0950 0.9255 0.1071  0.0171  0.0002  326 THR A CG2 
195   N N   . LEU A 26  ? 0.9144 1.0982 0.9738 0.0527  0.0303  0.0198  327 LEU A N   
196   C CA  . LEU A 26  ? 0.9649 1.1503 1.0279 0.0367  0.0340  0.0251  327 LEU A CA  
197   C C   . LEU A 26  ? 0.9487 1.1372 1.0100 0.0312  0.0395  0.0278  327 LEU A C   
198   O O   . LEU A 26  ? 0.9726 1.1509 1.0280 0.0379  0.0397  0.0264  327 LEU A O   
199   C CB  . LEU A 26  ? 1.0587 1.2158 1.1166 0.0306  0.0320  0.0287  327 LEU A CB  
200   C CG  . LEU A 26  ? 1.0636 1.2031 1.1175 0.0360  0.0267  0.0278  327 LEU A CG  
201   C CD1 . LEU A 26  ? 0.9586 1.1024 1.0165 0.0278  0.0253  0.0294  327 LEU A CD1 
202   C CD2 . LEU A 26  ? 1.0881 1.2281 1.1390 0.0516  0.0224  0.0229  327 LEU A CD2 
203   N N   . GLU A 27  ? 0.8032 1.0051 0.8686 0.0186  0.0439  0.0316  328 GLU A N   
204   C CA  . GLU A 27  ? 0.6912 0.8964 0.7536 0.0130  0.0495  0.0352  328 GLU A CA  
205   C C   . GLU A 27  ? 0.6953 0.8711 0.7486 0.0110  0.0497  0.0390  328 GLU A C   
206   O O   . GLU A 27  ? 0.7988 0.9537 0.8494 0.0079  0.0471  0.0407  328 GLU A O   
207   C CB  . GLU A 27  ? 0.7174 0.9387 0.7843 -0.0019 0.0543  0.0394  328 GLU A CB  
208   C CG  . GLU A 27  ? 0.8594 1.1179 0.9359 -0.0015 0.0561  0.0360  328 GLU A CG  
209   C CD  . GLU A 27  ? 1.0521 1.3251 1.1324 -0.0193 0.0612  0.0404  328 GLU A CD  
210   O OE1 . GLU A 27  ? 1.1298 1.3812 1.2056 -0.0311 0.0616  0.0451  328 GLU A OE1 
211   O OE2 . GLU A 27  ? 1.0977 1.4033 1.1848 -0.0217 0.0649  0.0389  328 GLU A OE2 
212   N N   . THR A 28  ? 0.5519 0.7281 0.6002 0.0134  0.0527  0.0399  329 THR A N   
213   C CA  . THR A 28  ? 0.5117 0.6663 0.5516 0.0102  0.0539  0.0442  329 THR A CA  
214   C C   . THR A 28  ? 0.5189 0.6750 0.5554 -0.0014 0.0593  0.0512  329 THR A C   
215   O O   . THR A 28  ? 0.7143 0.8503 0.7431 -0.0051 0.0598  0.0557  329 THR A O   
216   C CB  . THR A 28  ? 0.7591 0.9120 0.7939 0.0201  0.0535  0.0410  329 THR A CB  
217   O OG1 . THR A 28  ? 0.8228 0.9984 0.8584 0.0211  0.0579  0.0410  329 THR A OG1 
218   C CG2 . THR A 28  ? 0.8495 0.9972 0.8853 0.0313  0.0483  0.0340  329 THR A CG2 
219   N N   . GLY A 29  ? 0.4881 0.6674 0.5292 -0.0069 0.0633  0.0523  330 GLY A N   
220   C CA  . GLY A 29  ? 0.6050 0.7860 0.6411 -0.0185 0.0692  0.0593  330 GLY A CA  
221   C C   . GLY A 29  ? 0.6992 0.8951 0.7314 -0.0148 0.0736  0.0603  330 GLY A C   
222   O O   . GLY A 29  ? 0.7887 0.9957 0.8187 -0.0245 0.0794  0.0655  330 GLY A O   
223   N N   . CYS A 30  ? 0.6034 0.7995 0.6340 -0.0017 0.0711  0.0554  331 CYS A N   
224   C CA  . CYS A 30  ? 0.5332 0.7449 0.5600 0.0035  0.0748  0.0551  331 CYS A CA  
225   C C   . CYS A 30  ? 0.5522 0.7973 0.5876 0.0058  0.0771  0.0509  331 CYS A C   
226   O O   . CYS A 30  ? 0.5890 0.8433 0.6330 0.0113  0.0733  0.0448  331 CYS A O   
227   C CB  . CYS A 30  ? 0.5153 0.7163 0.5374 0.0167  0.0707  0.0497  331 CYS A CB  
228   S SG  . CYS A 30  ? 0.5832 0.7513 0.5952 0.0159  0.0682  0.0537  331 CYS A SG  
229   N N   . THR A 31  ? 0.5560 0.8204 0.5887 0.0021  0.0833  0.0542  332 THR A N   
230   C CA  . THR A 31  ? 0.5600 0.8601 0.6005 0.0063  0.0859  0.0495  332 THR A CA  
231   C C   . THR A 31  ? 0.4617 0.7686 0.4970 0.0209  0.0855  0.0443  332 THR A C   
232   O O   . THR A 31  ? 0.6383 0.9233 0.6648 0.0260  0.0832  0.0445  332 THR A O   
233   C CB  . THR A 31  ? 0.6720 0.9937 0.7140 -0.0087 0.0937  0.0561  332 THR A CB  
234   O OG1 . THR A 31  ? 0.6646 0.9932 0.6972 -0.0084 0.0993  0.0602  332 THR A OG1 
235   C CG2 . THR A 31  ? 0.6459 0.9461 0.6853 -0.0256 0.0947  0.0639  332 THR A CG2 
236   N N   . GLU A 32  ? 0.4707 0.8095 0.5114 0.0282  0.0874  0.0387  333 GLU A N   
237   C CA  . GLU A 32  ? 0.5590 0.9051 0.5943 0.0430  0.0867  0.0325  333 GLU A CA  
238   C C   . GLU A 32  ? 0.6002 0.9447 0.6244 0.0391  0.0920  0.0386  333 GLU A C   
239   O O   . GLU A 32  ? 0.5509 0.8898 0.5676 0.0502  0.0900  0.0342  333 GLU A O   
240   C CB  . GLU A 32  ? 0.6977 1.0806 0.7406 0.0525  0.0880  0.0250  333 GLU A CB  
241   C CG  . GLU A 32  ? 0.8378 1.2262 0.8911 0.0576  0.0829  0.0191  333 GLU A CG  
242   C CD  . GLU A 32  ? 0.9413 1.3628 0.9999 0.0726  0.0825  0.0098  333 GLU A CD  
243   O OE1 . GLU A 32  ? 0.9092 1.3198 0.9656 0.0888  0.0761  0.0013  333 GLU A OE1 
244   O OE2 . GLU A 32  ? 0.9595 1.4173 1.0234 0.0682  0.0888  0.0110  333 GLU A OE2 
245   N N   . TYR A 33  ? 0.5514 0.8993 0.5731 0.0236  0.0984  0.0488  334 TYR A N   
246   C CA  . TYR A 33  ? 0.4666 0.8149 0.4762 0.0194  0.1043  0.0561  334 TYR A CA  
247   C C   . TYR A 33  ? 0.4634 0.7802 0.4633 0.0082  0.1051  0.0662  334 TYR A C   
248   O O   . TYR A 33  ? 0.6515 0.9661 0.6396 0.0038  0.1102  0.0739  334 TYR A O   
249   C CB  . TYR A 33  ? 0.5095 0.8928 0.5214 0.0110  0.1130  0.0601  334 TYR A CB  
250   C CG  . TYR A 33  ? 0.6051 1.0243 0.6239 0.0238  0.1136  0.0505  334 TYR A CG  
251   C CD1 . TYR A 33  ? 0.7090 1.1419 0.7195 0.0338  0.1162  0.0482  334 TYR A CD1 
252   C CD2 . TYR A 33  ? 0.7059 1.1459 0.7387 0.0271  0.1113  0.0434  334 TYR A CD2 
253   C CE1 . TYR A 33  ? 0.7458 1.2112 0.7615 0.0468  0.1167  0.0388  334 TYR A CE1 
254   C CE2 . TYR A 33  ? 0.8033 1.2762 0.8415 0.0407  0.1115  0.0342  334 TYR A CE2 
255   C CZ  . TYR A 33  ? 0.7993 1.2845 0.8288 0.0507  0.1143  0.0318  334 TYR A CZ  
256   O OH  . TYR A 33  ? 0.8118 1.3294 0.8454 0.0656  0.1145  0.0219  334 TYR A OH  
257   N N   . ILE A 34  ? 0.5982 0.8909 0.6015 0.0040  0.1004  0.0667  335 ILE A N   
258   C CA  . ILE A 34  ? 0.5586 0.8193 0.5515 -0.0031 0.1000  0.0749  335 ILE A CA  
259   C C   . ILE A 34  ? 0.4816 0.7185 0.4781 0.0027  0.0921  0.0699  335 ILE A C   
260   O O   . ILE A 34  ? 0.6911 0.9335 0.6989 0.0051  0.0883  0.0635  335 ILE A O   
261   C CB  . ILE A 34  ? 0.5919 0.8482 0.5822 -0.0213 0.1055  0.0847  335 ILE A CB  
262   C CG1 . ILE A 34  ? 0.6713 0.8922 0.6563 -0.0268 0.1020  0.0890  335 ILE A CG1 
263   C CG2 . ILE A 34  ? 0.6087 0.8927 0.6124 -0.0293 0.1081  0.0821  335 ILE A CG2 
264   C CD1 . ILE A 34  ? 0.8170 1.0191 0.7864 -0.0378 0.1072  0.1007  335 ILE A CD1 
265   N N   . CYS A 35  ? 0.5080 0.7201 0.4947 0.0057  0.0896  0.0726  336 CYS A N   
266   C CA  . CYS A 35  ? 0.4256 0.6162 0.4148 0.0107  0.0827  0.0682  336 CYS A CA  
267   C C   . CYS A 35  ? 0.6144 0.7799 0.5982 0.0015  0.0826  0.0756  336 CYS A C   
268   O O   . CYS A 35  ? 0.5411 0.6968 0.5130 -0.0029 0.0863  0.0837  336 CYS A O   
269   C CB  . CYS A 35  ? 0.4632 0.6475 0.4466 0.0225  0.0790  0.0635  336 CYS A CB  
270   S SG  . CYS A 35  ? 0.5885 0.7465 0.5735 0.0261  0.0715  0.0596  336 CYS A SG  
271   N N   . MET A 36  ? 0.6740 0.8278 0.6649 -0.0003 0.0783  0.0727  337 MET A N   
272   C CA  . MET A 36  ? 0.5989 0.7287 0.5849 -0.0080 0.0777  0.0784  337 MET A CA  
273   C C   . MET A 36  ? 0.5100 0.6210 0.4960 -0.0013 0.0717  0.0747  337 MET A C   
274   O O   . MET A 36  ? 0.6008 0.6949 0.5863 -0.0060 0.0699  0.0766  337 MET A O   
275   C CB  . MET A 36  ? 0.5603 0.6940 0.5537 -0.0194 0.0790  0.0795  337 MET A CB  
276   C CG  . MET A 36  ? 0.7317 0.8847 0.7246 -0.0287 0.0857  0.0841  337 MET A CG  
277   S SD  . MET A 36  ? 0.8321 0.9853 0.8299 -0.0461 0.0880  0.0872  337 MET A SD  
278   C CE  . MET A 36  ? 0.7953 0.9896 0.8026 -0.0504 0.0934  0.0854  337 MET A CE  
279   N N   . GLY A 37  ? 0.5102 0.6241 0.4958 0.0092  0.0687  0.0694  338 GLY A N   
280   C CA  . GLY A 37  ? 0.3879 0.4881 0.3748 0.0147  0.0633  0.0648  338 GLY A CA  
281   C C   . GLY A 37  ? 0.5138 0.5935 0.4924 0.0133  0.0624  0.0698  338 GLY A C   
282   O O   . GLY A 37  ? 0.6728 0.7427 0.6536 0.0164  0.0582  0.0662  338 GLY A O   
283   N N   . SER A 38  ? 0.4839 0.5567 0.4522 0.0091  0.0663  0.0778  339 SER A N   
284   C CA  . SER A 38  ? 0.5598 0.6112 0.5182 0.0092  0.0654  0.0827  339 SER A CA  
285   C C   . SER A 38  ? 0.6063 0.6430 0.5618 -0.0010 0.0674  0.0882  339 SER A C   
286   O O   . SER A 38  ? 0.6271 0.6438 0.5738 -0.0005 0.0663  0.0917  339 SER A O   
287   C CB  . SER A 38  ? 0.6281 0.6769 0.5726 0.0146  0.0673  0.0879  339 SER A CB  
288   O OG  . SER A 38  ? 0.6888 0.7405 0.6255 0.0087  0.0730  0.0950  339 SER A OG  
289   N N   . ILE A 39  ? 0.6682 0.7150 0.6305 -0.0099 0.0700  0.0885  340 ILE A N   
290   C CA  . ILE A 39  ? 0.7304 0.7652 0.6919 -0.0209 0.0712  0.0918  340 ILE A CA  
291   C C   . ILE A 39  ? 0.7427 0.7686 0.7111 -0.0192 0.0661  0.0867  340 ILE A C   
292   O O   . ILE A 39  ? 0.7318 0.7697 0.7113 -0.0144 0.0630  0.0801  340 ILE A O   
293   C CB  . ILE A 39  ? 0.6802 0.7339 0.6494 -0.0308 0.0749  0.0920  340 ILE A CB  
294   C CG1 . ILE A 39  ? 0.5657 0.6348 0.5303 -0.0306 0.0800  0.0955  340 ILE A CG1 
295   C CG2 . ILE A 39  ? 0.8476 0.8879 0.8131 -0.0443 0.0769  0.0963  340 ILE A CG2 
296   C CD1 . ILE A 39  ? 0.6576 0.7088 0.6046 -0.0340 0.0839  0.1049  340 ILE A CD1 
297   N N   . MET A 40  ? 0.7533 0.7571 0.7139 -0.0228 0.0654  0.0899  341 MET A N   
298   C CA  . MET A 40  ? 0.8487 0.8437 0.8140 -0.0200 0.0607  0.0854  341 MET A CA  
299   C C   . MET A 40  ? 0.8022 0.8066 0.7794 -0.0268 0.0594  0.0813  341 MET A C   
300   O O   . MET A 40  ? 0.8195 0.8291 0.8052 -0.0220 0.0557  0.0758  341 MET A O   
301   C CB  . MET A 40  ? 0.9761 0.9451 0.9285 -0.0203 0.0602  0.0892  341 MET A CB  
302   C CG  . MET A 40  ? 1.1335 1.0956 1.0900 -0.0161 0.0557  0.0844  341 MET A CG  
303   S SD  . MET A 40  ? 1.2372 1.1750 1.1785 -0.0083 0.0541  0.0870  341 MET A SD  
304   C CE  . MET A 40  ? 1.0895 1.0368 1.0266 0.0027  0.0545  0.0882  341 MET A CE  
305   N N   . HIS A 41  ? 0.8429 0.8494 0.8201 -0.0381 0.0623  0.0839  342 HIS A N   
306   C CA  . HIS A 41  ? 0.9198 0.9410 0.9088 -0.0445 0.0613  0.0798  342 HIS A CA  
307   C C   . HIS A 41  ? 0.9136 0.9559 0.9066 -0.0514 0.0658  0.0816  342 HIS A C   
308   O O   . HIS A 41  ? 1.0250 1.0614 1.0109 -0.0624 0.0699  0.0869  342 HIS A O   
309   C CB  . HIS A 41  ? 0.9704 0.9761 0.9567 -0.0533 0.0599  0.0800  342 HIS A CB  
310   C CG  . HIS A 41  ? 1.0306 1.0106 1.0070 -0.0483 0.0573  0.0808  342 HIS A CG  
311   N ND1 . HIS A 41  ? 1.0147 0.9930 0.9953 -0.0395 0.0530  0.0763  342 HIS A ND1 
312   C CD2 . HIS A 41  ? 1.0122 0.9673 0.9740 -0.0510 0.0585  0.0853  342 HIS A CD2 
313   C CE1 . HIS A 41  ? 0.9676 0.9243 0.9379 -0.0365 0.0518  0.0778  342 HIS A CE1 
314   N NE2 . HIS A 41  ? 0.9584 0.8999 0.9168 -0.0425 0.0548  0.0830  342 HIS A NE2 
315   N N   . PRO A 42  ? 0.8036 0.8702 0.8069 -0.0455 0.0654  0.0773  343 PRO A N   
316   C CA  . PRO A 42  ? 0.7588 0.8482 0.7655 -0.0514 0.0703  0.0788  343 PRO A CA  
317   C C   . PRO A 42  ? 0.6870 0.7916 0.7024 -0.0632 0.0711  0.0773  343 PRO A C   
318   O O   . PRO A 42  ? 0.7426 0.8644 0.7695 -0.0593 0.0678  0.0711  343 PRO A O   
319   C CB  . PRO A 42  ? 0.6862 0.7956 0.7003 -0.0389 0.0689  0.0735  343 PRO A CB  
320   C CG  . PRO A 42  ? 0.7336 0.8257 0.7444 -0.0281 0.0644  0.0711  343 PRO A CG  
321   C CD  . PRO A 42  ? 0.8146 0.8873 0.8240 -0.0327 0.0614  0.0715  343 PRO A CD  
322   N N   . ARG A 48  ? 1.3956 1.5153 1.4481 -0.1343 0.0388  0.0394  349 ARG A N   
323   C CA  . ARG A 48  ? 1.4793 1.6046 1.5340 -0.1464 0.0353  0.0337  349 ARG A CA  
324   C C   . ARG A 48  ? 1.5744 1.7010 1.6313 -0.1340 0.0282  0.0285  349 ARG A C   
325   O O   . ARG A 48  ? 1.5004 1.6345 1.5613 -0.1171 0.0261  0.0286  349 ARG A O   
326   C CB  . ARG A 48  ? 1.4103 1.5748 1.4782 -0.1588 0.0369  0.0304  349 ARG A CB  
327   C CG  . ARG A 48  ? 1.4062 1.5647 1.4699 -0.1826 0.0391  0.0295  349 ARG A CG  
328   C CD  . ARG A 48  ? 1.4372 1.6375 1.5159 -0.1930 0.0369  0.0222  349 ARG A CD  
329   N NE  . ARG A 48  ? 1.4658 1.6580 1.5417 -0.2025 0.0317  0.0158  349 ARG A NE  
330   C CZ  . ARG A 48  ? 1.5177 1.7398 1.6034 -0.2171 0.0297  0.0090  349 ARG A CZ  
331   N NH1 . ARG A 48  ? 1.5354 1.7994 1.6353 -0.2238 0.0328  0.0078  349 ARG A NH1 
332   N NH2 . ARG A 48  ? 1.5093 1.7214 1.5910 -0.2251 0.0245  0.0028  349 ARG A NH2 
333   N N   . PRO A 49  ? 1.6887 1.8061 1.7416 -0.1425 0.0244  0.0239  350 PRO A N   
334   C CA  . PRO A 49  ? 1.7460 1.8652 1.7998 -0.1312 0.0178  0.0191  350 PRO A CA  
335   C C   . PRO A 49  ? 1.8059 1.9645 1.8735 -0.1309 0.0135  0.0127  350 PRO A C   
336   O O   . PRO A 49  ? 1.8013 1.9679 1.8711 -0.1173 0.0083  0.0099  350 PRO A O   
337   C CB  . PRO A 49  ? 1.7248 1.8139 1.7660 -0.1403 0.0161  0.0172  350 PRO A CB  
338   C CG  . PRO A 49  ? 1.7146 1.8032 1.7545 -0.1614 0.0199  0.0172  350 PRO A CG  
339   C CD  . PRO A 49  ? 1.7045 1.8019 1.7482 -0.1617 0.0262  0.0236  350 PRO A CD  
340   N N   . GLU A 50  ? 1.8390 2.0230 1.9152 -0.1460 0.0156  0.0102  351 GLU A N   
341   C CA  . GLU A 50  ? 1.8149 2.0430 1.9059 -0.1441 0.0120  0.0043  351 GLU A CA  
342   C C   . GLU A 50  ? 1.7499 1.9990 1.8488 -0.1270 0.0131  0.0065  351 GLU A C   
343   O O   . GLU A 50  ? 1.7310 2.0126 1.8399 -0.1176 0.0089  0.0018  351 GLU A O   
344   C CB  . GLU A 50  ? 1.8336 2.0856 1.9323 -0.1665 0.0146  0.0009  351 GLU A CB  
345   C CG  . GLU A 50  ? 1.7626 2.0512 1.8724 -0.1715 0.0087  -0.0083 351 GLU A CG  
346   C CD  . GLU A 50  ? 1.6681 1.9403 1.7709 -0.1897 0.0062  -0.0131 351 GLU A CD  
347   O OE1 . GLU A 50  ? 1.6631 1.9165 1.7581 -0.1818 0.0008  -0.0157 351 GLU A OE1 
348   O OE2 . GLU A 50  ? 1.5844 1.8619 1.6886 -0.2122 0.0099  -0.0143 351 GLU A OE2 
349   N N   . ASP A 51  ? 1.7002 1.9307 1.7938 -0.1219 0.0182  0.0132  352 ASP A N   
350   C CA  . ASP A 51  ? 1.5865 1.8316 1.6853 -0.1060 0.0196  0.0153  352 ASP A CA  
351   C C   . ASP A 51  ? 1.4158 1.6542 1.5120 -0.0852 0.0141  0.0144  352 ASP A C   
352   O O   . ASP A 51  ? 1.4358 1.6651 1.5293 -0.0718 0.0154  0.0177  352 ASP A O   
353   C CB  . ASP A 51  ? 1.5460 1.7692 1.6377 -0.1069 0.0261  0.0225  352 ASP A CB  
354   C CG  . ASP A 51  ? 1.4306 1.6760 1.5286 -0.1198 0.0324  0.0241  352 ASP A CG  
355   O OD1 . ASP A 51  ? 1.4087 1.6667 1.5101 -0.1379 0.0337  0.0219  352 ASP A OD1 
356   O OD2 . ASP A 51  ? 1.3261 1.5758 1.4246 -0.1123 0.0363  0.0276  352 ASP A OD2 
357   N N   . VAL A 52  ? 1.1779 1.4198 1.2739 -0.0829 0.0079  0.0098  353 VAL A N   
358   C CA  . VAL A 52  ? 0.9250 1.1618 1.0175 -0.0640 0.0027  0.0092  353 VAL A CA  
359   C C   . VAL A 52  ? 0.7051 0.9780 0.8075 -0.0518 -0.0003 0.0054  353 VAL A C   
360   O O   . VAL A 52  ? 0.6821 0.9896 0.7953 -0.0590 -0.0009 0.0007  353 VAL A O   
361   C CB  . VAL A 52  ? 0.9878 1.2116 1.0739 -0.0657 -0.0024 0.0065  353 VAL A CB  
362   C CG1 . VAL A 52  ? 1.0600 1.2474 1.1352 -0.0752 0.0005  0.0099  353 VAL A CG1 
363   C CG2 . VAL A 52  ? 0.9646 1.2192 1.0593 -0.0758 -0.0061 -0.0006 353 VAL A CG2 
364   N N   . ALA A 53  ? 0.6024 0.8674 0.7004 -0.0330 -0.0023 0.0073  354 ALA A N   
365   C CA  . ALA A 53  ? 0.6238 0.9174 0.7287 -0.0188 -0.0041 0.0047  354 ALA A CA  
366   C C   . ALA A 53  ? 0.6009 0.9278 0.7129 -0.0151 -0.0102 -0.0018 354 ALA A C   
367   O O   . ALA A 53  ? 0.7873 1.1067 0.8944 -0.0144 -0.0151 -0.0033 354 ALA A O   
368   C CB  . ALA A 53  ? 0.6994 0.9708 0.7950 0.0001  -0.0054 0.0079  354 ALA A CB  
369   N N   . THR A 54  ? 0.5793 0.9451 0.7028 -0.0123 -0.0101 -0.0059 355 THR A N   
370   C CA  . THR A 54  ? 0.7287 1.1317 0.8596 -0.0048 -0.0163 -0.0126 355 THR A CA  
371   C C   . THR A 54  ? 0.8157 1.2125 0.9386 0.0209  -0.0219 -0.0123 355 THR A C   
372   O O   . THR A 54  ? 0.8001 1.1677 0.9134 0.0316  -0.0202 -0.0075 355 THR A O   
373   C CB  . THR A 54  ? 0.7526 1.2023 0.8990 -0.0100 -0.0138 -0.0172 355 THR A CB  
374   O OG1 . THR A 54  ? 0.7809 1.2384 0.9273 0.0081  -0.0127 -0.0166 355 THR A OG1 
375   C CG2 . THR A 54  ? 0.8005 1.2479 0.9515 -0.0346 -0.0062 -0.0150 355 THR A CG2 
376   N N   . LYS A 55  ? 0.8249 1.2496 0.9511 0.0307  -0.0288 -0.0177 356 LYS A N   
377   C CA  . LYS A 55  ? 0.7914 1.2110 0.9082 0.0562  -0.0346 -0.0175 356 LYS A CA  
378   C C   . LYS A 55  ? 0.8446 1.2675 0.9612 0.0711  -0.0321 -0.0167 356 LYS A C   
379   O O   . LYS A 55  ? 0.8897 1.2793 0.9933 0.0843  -0.0322 -0.0122 356 LYS A O   
380   C CB  . LYS A 55  ? 0.7417 1.1988 0.8636 0.0651  -0.0423 -0.0241 356 LYS A CB  
381   C CG  . LYS A 55  ? 0.6777 1.1302 0.7969 0.0547  -0.0464 -0.0256 356 LYS A CG  
382   C CD  . LYS A 55  ? 0.6805 1.1576 0.7976 0.0723  -0.0554 -0.0303 356 LYS A CD  
383   C CE  . LYS A 55  ? 0.8435 1.3474 0.9689 0.0574  -0.0592 -0.0367 356 LYS A CE  
384   N NZ  . LYS A 55  ? 0.8672 1.3788 0.9843 0.0734  -0.0683 -0.0392 356 LYS A NZ  
385   N N   . ASP A 56  ? 0.8539 1.3175 0.9846 0.0687  -0.0297 -0.0214 357 ASP A N   
386   C CA  . ASP A 56  ? 0.8788 1.3491 1.0094 0.0839  -0.0276 -0.0218 357 ASP A CA  
387   C C   . ASP A 56  ? 0.8048 1.2384 0.9288 0.0772  -0.0207 -0.0156 357 ASP A C   
388   O O   . ASP A 56  ? 0.8727 1.2914 0.9891 0.0929  -0.0203 -0.0144 357 ASP A O   
389   C CB  . ASP A 56  ? 0.8842 1.4092 1.0319 0.0809  -0.0257 -0.0282 357 ASP A CB  
390   C CG  . ASP A 56  ? 0.7908 1.3583 0.9462 0.0893  -0.0329 -0.0354 357 ASP A CG  
391   O OD1 . ASP A 56  ? 0.5682 1.1217 0.7131 0.1043  -0.0400 -0.0352 357 ASP A OD1 
392   O OD2 . ASP A 56  ? 0.8816 1.4977 1.0533 0.0806  -0.0313 -0.0411 357 ASP A OD2 
393   N N   . GLN A 57  ? 0.6181 1.0372 0.7445 0.0547  -0.0155 -0.0122 358 GLN A N   
394   C CA  . GLN A 57  ? 0.4779 0.8593 0.5964 0.0494  -0.0100 -0.0060 358 GLN A CA  
395   C C   . GLN A 57  ? 0.5617 0.9008 0.6642 0.0620  -0.0131 -0.0019 358 GLN A C   
396   O O   . GLN A 57  ? 0.5698 0.8859 0.6647 0.0695  -0.0108 0.0008  358 GLN A O   
397   C CB  . GLN A 57  ? 0.5999 0.9707 0.7213 0.0247  -0.0050 -0.0029 358 GLN A CB  
398   C CG  . GLN A 57  ? 0.7651 1.1693 0.8996 0.0091  0.0003  -0.0050 358 GLN A CG  
399   C CD  . GLN A 57  ? 0.8687 1.2508 1.0012 -0.0131 0.0062  -0.0002 358 GLN A CD  
400   O OE1 . GLN A 57  ? 0.8872 1.2600 1.0185 -0.0264 0.0049  -0.0002 358 GLN A OE1 
401   N NE2 . GLN A 57  ? 0.8800 1.2525 1.0107 -0.0163 0.0125  0.0038  358 GLN A NE2 
402   N N   . LEU A 58  ? 0.6424 0.9715 0.7392 0.0639  -0.0184 -0.0017 359 LEU A N   
403   C CA  . LEU A 58  ? 0.5890 0.8756 0.6703 0.0705  -0.0200 0.0033  359 LEU A CA  
404   C C   . LEU A 58  ? 0.6010 0.8773 0.6715 0.0936  -0.0241 0.0033  359 LEU A C   
405   O O   . LEU A 58  ? 0.5416 0.7821 0.6000 0.0982  -0.0229 0.0077  359 LEU A O   
406   C CB  . LEU A 58  ? 0.4727 0.7516 0.5503 0.0638  -0.0237 0.0038  359 LEU A CB  
407   C CG  . LEU A 58  ? 0.5684 0.8040 0.6321 0.0626  -0.0229 0.0098  359 LEU A CG  
408   C CD1 . LEU A 58  ? 0.6133 0.8280 0.6770 0.0514  -0.0161 0.0135  359 LEU A CD1 
409   C CD2 . LEU A 58  ? 0.4942 0.7245 0.5549 0.0542  -0.0257 0.0098  359 LEU A CD2 
410   N N   . PHE A 59  ? 0.6692 0.9758 0.7433 0.1083  -0.0288 -0.0017 360 PHE A N   
411   C CA  . PHE A 59  ? 0.7636 1.0578 0.8248 0.1320  -0.0334 -0.0018 360 PHE A CA  
412   C C   . PHE A 59  ? 0.7561 1.0255 0.8101 0.1381  -0.0297 0.0002  360 PHE A C   
413   O O   . PHE A 59  ? 0.8209 1.0524 0.8588 0.1460  -0.0311 0.0041  360 PHE A O   
414   C CB  . PHE A 59  ? 0.8789 1.2153 0.9467 0.1477  -0.0385 -0.0085 360 PHE A CB  
415   C CG  . PHE A 59  ? 1.0250 1.3813 1.0949 0.1487  -0.0446 -0.0107 360 PHE A CG  
416   C CD1 . PHE A 59  ? 1.0302 1.3585 1.0843 0.1573  -0.0494 -0.0069 360 PHE A CD1 
417   C CD2 . PHE A 59  ? 1.0893 1.4938 1.1763 0.1410  -0.0454 -0.0169 360 PHE A CD2 
418   C CE1 . PHE A 59  ? 1.0077 1.3558 1.0629 0.1590  -0.0553 -0.0093 360 PHE A CE1 
419   C CE2 . PHE A 59  ? 1.0041 1.4291 1.0932 0.1418  -0.0515 -0.0199 360 PHE A CE2 
420   C CZ  . PHE A 59  ? 0.9678 1.3646 1.0409 0.1514  -0.0566 -0.0162 360 PHE A CZ  
421   N N   . PRO A 60  ? 0.6774 0.9654 0.7413 0.1343  -0.0250 -0.0025 361 PRO A N   
422   C CA  . PRO A 60  ? 0.5270 0.7911 0.5825 0.1418  -0.0223 -0.0015 361 PRO A CA  
423   C C   . PRO A 60  ? 0.5187 0.7419 0.5662 0.1295  -0.0186 0.0046  361 PRO A C   
424   O O   . PRO A 60  ? 0.6233 0.8151 0.6577 0.1382  -0.0190 0.0063  361 PRO A O   
425   C CB  . PRO A 60  ? 0.6238 0.9222 0.6932 0.1378  -0.0177 -0.0055 361 PRO A CB  
426   C CG  . PRO A 60  ? 0.6250 0.9481 0.7085 0.1179  -0.0151 -0.0053 361 PRO A CG  
427   C CD  . PRO A 60  ? 0.6319 0.9597 0.7139 0.1204  -0.0211 -0.0058 361 PRO A CD  
428   N N   . LEU A 61  ? 0.4644 0.6868 0.5188 0.1098  -0.0151 0.0075  362 LEU A N   
429   C CA  . LEU A 61  ? 0.5066 0.6932 0.5539 0.0990  -0.0116 0.0128  362 LEU A CA  
430   C C   . LEU A 61  ? 0.7046 0.8587 0.7367 0.1062  -0.0154 0.0163  362 LEU A C   
431   O O   . LEU A 61  ? 0.6744 0.7979 0.6959 0.1086  -0.0142 0.0189  362 LEU A O   
432   C CB  . LEU A 61  ? 0.4199 0.6116 0.4758 0.0785  -0.0079 0.0150  362 LEU A CB  
433   C CG  . LEU A 61  ? 0.4817 0.7029 0.5512 0.0676  -0.0034 0.0128  362 LEU A CG  
434   C CD1 . LEU A 61  ? 0.4800 0.7019 0.5547 0.0485  -0.0012 0.0148  362 LEU A CD1 
435   C CD2 . LEU A 61  ? 0.4668 0.6790 0.5352 0.0672  0.0015  0.0139  362 LEU A CD2 
436   N N   . ALA A 62  ? 0.7150 0.8761 0.7455 0.1091  -0.0200 0.0162  363 ALA A N   
437   C CA  . ALA A 62  ? 0.5896 0.7217 0.6044 0.1169  -0.0236 0.0200  363 ALA A CA  
438   C C   . ALA A 62  ? 0.5819 0.6961 0.5835 0.1351  -0.0261 0.0196  363 ALA A C   
439   O O   . ALA A 62  ? 0.6691 0.7478 0.6566 0.1363  -0.0256 0.0237  363 ALA A O   
440   C CB  . ALA A 62  ? 0.6421 0.7904 0.6573 0.1198  -0.0287 0.0191  363 ALA A CB  
441   N N   . LYS A 63  ? 0.5651 0.7032 0.5704 0.1490  -0.0285 0.0145  364 LYS A N   
442   C CA  . LYS A 63  ? 0.6269 0.7459 0.6177 0.1680  -0.0314 0.0135  364 LYS A CA  
443   C C   . LYS A 63  ? 0.8018 0.8931 0.7872 0.1631  -0.0269 0.0147  364 LYS A C   
444   O O   . LYS A 63  ? 0.8810 0.9373 0.8494 0.1708  -0.0284 0.0168  364 LYS A O   
445   C CB  . LYS A 63  ? 0.5136 0.6665 0.5101 0.1848  -0.0347 0.0068  364 LYS A CB  
446   C CG  . LYS A 63  ? 0.6481 0.7797 0.6254 0.2091  -0.0400 0.0058  364 LYS A CG  
447   C CD  . LYS A 63  ? 0.8012 0.9483 0.7806 0.2233  -0.0398 -0.0008 364 LYS A CD  
448   C CE  . LYS A 63  ? 0.8998 1.0235 0.8580 0.2490  -0.0457 -0.0024 364 LYS A CE  
449   N NZ  . LYS A 63  ? 0.9059 0.9753 0.8437 0.2490  -0.0449 0.0017  364 LYS A NZ  
450   N N   . GLU A 64  ? 0.7715 0.8772 0.7703 0.1500  -0.0216 0.0133  365 GLU A N   
451   C CA  . GLU A 64  ? 0.7502 0.8323 0.7441 0.1458  -0.0177 0.0138  365 GLU A CA  
452   C C   . GLU A 64  ? 0.6906 0.7361 0.6740 0.1359  -0.0164 0.0196  365 GLU A C   
453   O O   . GLU A 64  ? 0.6964 0.7115 0.6669 0.1395  -0.0165 0.0204  365 GLU A O   
454   C CB  . GLU A 64  ? 0.8155 0.9205 0.8248 0.1335  -0.0121 0.0121  365 GLU A CB  
455   C CG  . GLU A 64  ? 0.9084 1.0165 0.9165 0.1422  -0.0107 0.0075  365 GLU A CG  
456   C CD  . GLU A 64  ? 1.0736 1.1681 1.0830 0.1295  -0.0054 0.0090  365 GLU A CD  
457   O OE1 . GLU A 64  ? 1.1572 1.2293 1.1564 0.1354  -0.0056 0.0072  365 GLU A OE1 
458   O OE2 . GLU A 64  ? 1.0842 1.1899 1.1040 0.1140  -0.0014 0.0117  365 GLU A OE2 
459   N N   . PHE A 65  ? 0.6634 0.7119 0.6518 0.1235  -0.0155 0.0234  366 PHE A N   
460   C CA  . PHE A 65  ? 0.6627 0.6811 0.6425 0.1136  -0.0138 0.0286  366 PHE A CA  
461   C C   . PHE A 65  ? 0.7347 0.7251 0.6961 0.1240  -0.0177 0.0316  366 PHE A C   
462   O O   . PHE A 65  ? 0.8323 0.7921 0.7823 0.1208  -0.0163 0.0344  366 PHE A O   
463   C CB  . PHE A 65  ? 0.5596 0.5889 0.5482 0.0996  -0.0121 0.0312  366 PHE A CB  
464   C CG  . PHE A 65  ? 0.5743 0.5769 0.5538 0.0914  -0.0108 0.0363  366 PHE A CG  
465   C CD1 . PHE A 65  ? 0.5569 0.5423 0.5350 0.0823  -0.0066 0.0379  366 PHE A CD1 
466   C CD2 . PHE A 65  ? 0.6281 0.6247 0.6003 0.0932  -0.0137 0.0393  366 PHE A CD2 
467   C CE1 . PHE A 65  ? 0.6132 0.5773 0.5835 0.0747  -0.0051 0.0422  366 PHE A CE1 
468   C CE2 . PHE A 65  ? 0.6055 0.5796 0.5692 0.0857  -0.0120 0.0441  366 PHE A CE2 
469   C CZ  . PHE A 65  ? 0.6093 0.5678 0.5725 0.0761  -0.0075 0.0455  366 PHE A CZ  
470   N N   . ILE A 66  ? 0.6691 0.6694 0.6266 0.1360  -0.0227 0.0312  367 ILE A N   
471   C CA  . ILE A 66  ? 0.7106 0.6822 0.6483 0.1463  -0.0265 0.0350  367 ILE A CA  
472   C C   . ILE A 66  ? 0.7814 0.7281 0.7053 0.1578  -0.0275 0.0334  367 ILE A C   
473   O O   . ILE A 66  ? 0.7664 0.6767 0.6733 0.1571  -0.0273 0.0375  367 ILE A O   
474   C CB  . ILE A 66  ? 0.6629 0.6526 0.5987 0.1589  -0.0323 0.0346  367 ILE A CB  
475   C CG1 . ILE A 66  ? 0.5636 0.5771 0.5125 0.1464  -0.0316 0.0352  367 ILE A CG1 
476   C CG2 . ILE A 66  ? 0.5818 0.5390 0.4945 0.1701  -0.0361 0.0396  367 ILE A CG2 
477   C CD1 . ILE A 66  ? 0.5630 0.5533 0.5047 0.1337  -0.0291 0.0413  367 ILE A CD1 
478   N N   . ASP A 67  ? 0.7688 0.7344 0.6991 0.1679  -0.0284 0.0273  368 ASP A N   
479   C CA  . ASP A 67  ? 0.7386 0.6810 0.6562 0.1787  -0.0292 0.0244  368 ASP A CA  
480   C C   . ASP A 67  ? 0.7664 0.6839 0.6817 0.1637  -0.0244 0.0259  368 ASP A C   
481   O O   . ASP A 67  ? 0.8256 0.7065 0.7233 0.1657  -0.0250 0.0275  368 ASP A O   
482   C CB  . ASP A 67  ? 0.6148 0.5874 0.5426 0.1901  -0.0300 0.0168  368 ASP A CB  
483   C CG  . ASP A 67  ? 0.7544 0.7558 0.6850 0.2067  -0.0351 0.0141  368 ASP A CG  
484   O OD1 . ASP A 67  ? 0.7788 0.7684 0.6970 0.2160  -0.0397 0.0174  368 ASP A OD1 
485   O OD2 . ASP A 67  ? 0.8300 0.8679 0.7751 0.2108  -0.0346 0.0084  368 ASP A OD2 
486   N N   . GLN A 68  ? 0.6969 0.6342 0.6293 0.1483  -0.0197 0.0253  369 GLN A N   
487   C CA  . GLN A 68  ? 0.7026 0.6219 0.6348 0.1339  -0.0152 0.0264  369 GLN A CA  
488   C C   . GLN A 68  ? 0.7688 0.6559 0.6875 0.1259  -0.0148 0.0326  369 GLN A C   
489   O O   . GLN A 68  ? 0.8179 0.6768 0.7259 0.1216  -0.0135 0.0329  369 GLN A O   
490   C CB  . GLN A 68  ? 0.6579 0.6046 0.6096 0.1197  -0.0107 0.0261  369 GLN A CB  
491   C CG  . GLN A 68  ? 0.7081 0.6429 0.6617 0.1057  -0.0062 0.0267  369 GLN A CG  
492   C CD  . GLN A 68  ? 0.8659 0.8253 0.8361 0.0931  -0.0023 0.0275  369 GLN A CD  
493   O OE1 . GLN A 68  ? 0.8905 0.8777 0.8718 0.0952  -0.0023 0.0258  369 GLN A OE1 
494   N NE2 . GLN A 68  ? 0.9160 0.8651 0.8872 0.0800  0.0011  0.0302  369 GLN A NE2 
495   N N   . TYR A 69  ? 0.7574 0.6489 0.6760 0.1239  -0.0159 0.0372  370 TYR A N   
496   C CA  . TYR A 69  ? 0.6843 0.5488 0.5907 0.1157  -0.0149 0.0435  370 TYR A CA  
497   C C   . TYR A 69  ? 0.6908 0.5207 0.5741 0.1267  -0.0182 0.0456  370 TYR A C   
498   O O   . TYR A 69  ? 0.6159 0.4155 0.4867 0.1185  -0.0161 0.0488  370 TYR A O   
499   C CB  . TYR A 69  ? 0.6668 0.5465 0.5784 0.1116  -0.0153 0.0473  370 TYR A CB  
500   C CG  . TYR A 69  ? 0.7789 0.6324 0.6759 0.1057  -0.0146 0.0540  370 TYR A CG  
501   C CD1 . TYR A 69  ? 0.8349 0.6796 0.7339 0.0895  -0.0097 0.0567  370 TYR A CD1 
502   C CD2 . TYR A 69  ? 0.7197 0.5582 0.6002 0.1169  -0.0187 0.0579  370 TYR A CD2 
503   C CE1 . TYR A 69  ? 0.9123 0.7355 0.7980 0.0835  -0.0085 0.0629  370 TYR A CE1 
504   C CE2 . TYR A 69  ? 0.7671 0.5814 0.6329 0.1110  -0.0174 0.0646  370 TYR A CE2 
505   C CZ  . TYR A 69  ? 0.8670 0.6744 0.7358 0.0938  -0.0121 0.0671  370 TYR A CZ  
506   O OH  . TYR A 69  ? 0.9564 0.7422 0.8107 0.0872  -0.0103 0.0740  370 TYR A OH  
507   N N   . TYR A 70  ? 0.6078 0.4411 0.4841 0.1451  -0.0233 0.0439  371 TYR A N   
508   C CA  . TYR A 70  ? 0.7534 0.5500 0.6050 0.1568  -0.0267 0.0464  371 TYR A CA  
509   C C   . TYR A 70  ? 0.8537 0.6268 0.6969 0.1583  -0.0259 0.0421  371 TYR A C   
510   O O   . TYR A 70  ? 0.9057 0.6390 0.7276 0.1588  -0.0265 0.0450  371 TYR A O   
511   C CB  . TYR A 70  ? 0.7867 0.5933 0.6317 0.1782  -0.0329 0.0457  371 TYR A CB  
512   C CG  . TYR A 70  ? 0.7591 0.5681 0.6002 0.1762  -0.0341 0.0522  371 TYR A CG  
513   C CD1 . TYR A 70  ? 0.7064 0.5535 0.5665 0.1717  -0.0341 0.0511  371 TYR A CD1 
514   C CD2 . TYR A 70  ? 0.6596 0.4316 0.4778 0.1765  -0.0348 0.0595  371 TYR A CD2 
515   C CE1 . TYR A 70  ? 0.7681 0.6180 0.6247 0.1693  -0.0353 0.0562  371 TYR A CE1 
516   C CE2 . TYR A 70  ? 0.7944 0.5700 0.6088 0.1742  -0.0356 0.0655  371 TYR A CE2 
517   C CZ  . TYR A 70  ? 0.7566 0.5718 0.5907 0.1711  -0.0360 0.0634  371 TYR A CZ  
518   O OH  . TYR A 70  ? 0.8339 0.6545 0.6647 0.1691  -0.0371 0.0683  371 TYR A OH  
519   N N   . SER A 71  ? 0.9612 0.7572 0.8198 0.1579  -0.0244 0.0352  372 SER A N   
520   C CA  . SER A 71  ? 0.9436 0.7191 0.7955 0.1568  -0.0233 0.0305  372 SER A CA  
521   C C   . SER A 71  ? 0.8533 0.6064 0.7020 0.1364  -0.0189 0.0339  372 SER A C   
522   O O   . SER A 71  ? 0.9334 0.6490 0.7633 0.1346  -0.0192 0.0347  372 SER A O   
523   C CB  . SER A 71  ? 0.9079 0.7164 0.7780 0.1592  -0.0221 0.0231  372 SER A CB  
524   O OG  . SER A 71  ? 1.0961 0.8919 0.9660 0.1494  -0.0191 0.0195  372 SER A OG  
525   N N   . SER A 72  ? 0.7237 0.4991 0.5896 0.1207  -0.0147 0.0362  373 SER A N   
526   C CA  . SER A 72  ? 0.7085 0.4700 0.5742 0.1016  -0.0103 0.0386  373 SER A CA  
527   C C   . SER A 72  ? 0.8643 0.5882 0.7088 0.0971  -0.0104 0.0448  373 SER A C   
528   O O   . SER A 72  ? 0.9038 0.6068 0.7418 0.0843  -0.0077 0.0450  373 SER A O   
529   C CB  . SER A 72  ? 0.7608 0.5509 0.6452 0.0891  -0.0067 0.0412  373 SER A CB  
530   O OG  . SER A 72  ? 0.9747 0.7627 0.8542 0.0891  -0.0075 0.0476  373 SER A OG  
531   N N   . ILE A 73  ? 0.8832 0.5991 0.7166 0.1069  -0.0134 0.0499  374 ILE A N   
532   C CA  . ILE A 73  ? 0.8454 0.5282 0.6588 0.1015  -0.0129 0.0574  374 ILE A CA  
533   C C   . ILE A 73  ? 0.9416 0.5872 0.7290 0.1166  -0.0173 0.0581  374 ILE A C   
534   O O   . ILE A 73  ? 0.9341 0.5535 0.7023 0.1177  -0.0181 0.0654  374 ILE A O   
535   C CB  . ILE A 73  ? 0.8210 0.5191 0.6381 0.0997  -0.0125 0.0640  374 ILE A CB  
536   C CG1 . ILE A 73  ? 0.9176 0.6300 0.7337 0.1200  -0.0181 0.0633  374 ILE A CG1 
537   C CG2 . ILE A 73  ? 0.7986 0.5303 0.6394 0.0860  -0.0084 0.0627  374 ILE A CG2 
538   C CD1 . ILE A 73  ? 0.9196 0.6284 0.7256 0.1237  -0.0198 0.0707  374 ILE A CD1 
539   N N   . LYS A 74  ? 0.9584 0.6006 0.7437 0.1291  -0.0203 0.0508  375 LYS A N   
540   C CA  . LYS A 74  ? 1.1957 0.7980 0.9544 0.1437  -0.0245 0.0503  375 LYS A CA  
541   C C   . LYS A 74  ? 1.1926 0.7924 0.9388 0.1643  -0.0298 0.0543  375 LYS A C   
542   O O   . LYS A 74  ? 1.2503 0.8103 0.9695 0.1745  -0.0329 0.0575  375 LYS A O   
543   C CB  . LYS A 74  ? 1.3711 0.9275 1.1084 0.1289  -0.0219 0.0549  375 LYS A CB  
544   C CG  . LYS A 74  ? 1.4746 1.0107 1.2072 0.1222  -0.0210 0.0477  375 LYS A CG  
545   C CD  . LYS A 74  ? 1.5009 0.9972 1.2067 0.1405  -0.0262 0.0448  375 LYS A CD  
546   C CE  . LYS A 74  ? 1.5049 0.9870 1.2088 0.1354  -0.0258 0.0356  375 LYS A CE  
547   N NZ  . LYS A 74  ? 1.4471 0.9757 1.1815 0.1284  -0.0231 0.0289  375 LYS A NZ  
548   N N   . ARG A 75  ? 1.1268 0.7682 0.8914 0.1707  -0.0310 0.0540  376 ARG A N   
549   C CA  . ARG A 75  ? 1.1044 0.7490 0.8591 0.1896  -0.0363 0.0574  376 ARG A CA  
550   C C   . ARG A 75  ? 1.0951 0.7781 0.8644 0.2082  -0.0404 0.0500  376 ARG A C   
551   O O   . ARG A 75  ? 1.0927 0.7955 0.8632 0.2206  -0.0442 0.0517  376 ARG A O   
552   C CB  . ARG A 75  ? 1.0195 0.6771 0.7792 0.1795  -0.0344 0.0651  376 ARG A CB  
553   C CG  . ARG A 75  ? 1.0379 0.6579 0.7795 0.1644  -0.0308 0.0736  376 ARG A CG  
554   C CD  . ARG A 75  ? 1.1020 0.6733 0.8109 0.1769  -0.0343 0.0771  376 ARG A CD  
555   N NE  . ARG A 75  ? 1.2208 0.7575 0.9098 0.1640  -0.0311 0.0870  376 ARG A NE  
556   C CZ  . ARG A 75  ? 1.3129 0.8212 0.9941 0.1449  -0.0262 0.0889  376 ARG A CZ  
557   N NH1 . ARG A 75  ? 1.2586 0.7436 0.9246 0.1319  -0.0228 0.0973  376 ARG A NH1 
558   N NH2 . ARG A 75  ? 1.3941 0.9042 1.0858 0.1368  -0.0242 0.0811  376 ARG A NH2 
559   N N   . PHE A 76  ? 0.9851 0.6806 0.7651 0.2103  -0.0397 0.0417  377 PHE A N   
560   C CA  . PHE A 76  ? 0.8908 0.6274 0.6867 0.2256  -0.0425 0.0345  377 PHE A CA  
561   C C   . PHE A 76  ? 0.9891 0.7149 0.7660 0.2531  -0.0495 0.0332  377 PHE A C   
562   O O   . PHE A 76  ? 1.1751 0.8570 0.9261 0.2626  -0.0519 0.0339  377 PHE A O   
563   C CB  . PHE A 76  ? 0.9208 0.6703 0.7296 0.2218  -0.0398 0.0262  377 PHE A CB  
564   C CG  . PHE A 76  ? 0.9634 0.7586 0.7900 0.2351  -0.0416 0.0190  377 PHE A CG  
565   C CD1 . PHE A 76  ? 0.8251 0.6644 0.6781 0.2235  -0.0383 0.0182  377 PHE A CD1 
566   C CD2 . PHE A 76  ? 1.0769 0.8707 0.8928 0.2594  -0.0465 0.0129  377 PHE A CD2 
567   C CE1 . PHE A 76  ? 0.8312 0.7130 0.7002 0.2338  -0.0394 0.0120  377 PHE A CE1 
568   C CE2 . PHE A 76  ? 0.9700 0.8095 0.8028 0.2712  -0.0477 0.0061  377 PHE A CE2 
569   C CZ  . PHE A 76  ? 0.8931 0.7770 0.7528 0.2574  -0.0439 0.0059  377 PHE A CZ  
570   N N   . GLY A 77  ? 1.0162 0.7820 0.8052 0.2663  -0.0529 0.0309  378 GLY A N   
571   C CA  . GLY A 77  ? 1.0834 0.8453 0.8557 0.2938  -0.0601 0.0298  378 GLY A CA  
572   C C   . GLY A 77  ? 1.1339 0.8632 0.8824 0.2978  -0.0629 0.0385  378 GLY A C   
573   O O   . GLY A 77  ? 1.0542 0.7853 0.7909 0.3138  -0.0673 0.0367  378 GLY A O   
574   N N   . SER A 78  ? 1.1498 0.8550 0.8931 0.2788  -0.0591 0.0470  379 SER A N   
575   C CA  . SER A 78  ? 1.1146 0.7893 0.8355 0.2783  -0.0603 0.0553  379 SER A CA  
576   C C   . SER A 78  ? 1.0986 0.8066 0.8259 0.2877  -0.0642 0.0575  379 SER A C   
577   O O   . SER A 78  ? 0.9695 0.7232 0.7194 0.2920  -0.0658 0.0534  379 SER A O   
578   C CB  . SER A 78  ? 1.1055 0.7499 0.8204 0.2552  -0.0547 0.0638  379 SER A CB  
579   O OG  . SER A 78  ? 1.0433 0.7245 0.7817 0.2398  -0.0515 0.0654  379 SER A OG  
580   N N   . LYS A 79  ? 1.1825 0.8674 0.8893 0.2898  -0.0656 0.0638  380 LYS A N   
581   C CA  . LYS A 79  ? 1.2395 0.9522 0.9494 0.2981  -0.0694 0.0661  380 LYS A CA  
582   C C   . LYS A 79  ? 1.1643 0.9043 0.8940 0.2846  -0.0674 0.0697  380 LYS A C   
583   O O   . LYS A 79  ? 1.0657 0.8505 0.8135 0.2911  -0.0707 0.0660  380 LYS A O   
584   C CB  . LYS A 79  ? 1.3441 1.0219 1.0266 0.3006  -0.0703 0.0733  380 LYS A CB  
585   C CG  . LYS A 79  ? 1.4491 1.1488 1.1262 0.3203  -0.0764 0.0715  380 LYS A CG  
586   C CD  . LYS A 79  ? 1.5384 1.1990 1.1860 0.3230  -0.0768 0.0790  380 LYS A CD  
587   C CE  . LYS A 79  ? 1.5141 1.1918 1.1526 0.3455  -0.0831 0.0762  380 LYS A CE  
588   N NZ  . LYS A 79  ? 1.3937 1.1114 1.0460 0.3467  -0.0857 0.0772  380 LYS A NZ  
589   N N   . ALA A 80  ? 1.1344 0.8506 0.8622 0.2634  -0.0615 0.0759  381 ALA A N   
590   C CA  . ALA A 80  ? 1.0689 0.8159 0.8199 0.2425  -0.0570 0.0763  381 ALA A CA  
591   C C   . ALA A 80  ? 1.0195 0.8087 0.8017 0.2350  -0.0549 0.0671  381 ALA A C   
592   O O   . ALA A 80  ? 0.9508 0.7762 0.7537 0.2253  -0.0538 0.0652  381 ALA A O   
593   C CB  . ALA A 80  ? 1.0180 0.7337 0.7616 0.2200  -0.0503 0.0834  381 ALA A CB  
594   N N   . HIS A 81  ? 0.9308 0.7148 0.7156 0.2390  -0.0541 0.0613  382 HIS A N   
595   C CA  . HIS A 81  ? 0.8883 0.7132 0.7008 0.2344  -0.0523 0.0528  382 HIS A CA  
596   C C   . HIS A 81  ? 0.8225 0.6906 0.6464 0.2506  -0.0578 0.0475  382 HIS A C   
597   O O   . HIS A 81  ? 0.8112 0.7195 0.6583 0.2408  -0.0565 0.0443  382 HIS A O   
598   C CB  . HIS A 81  ? 0.8965 0.7051 0.7064 0.2372  -0.0507 0.0477  382 HIS A CB  
599   C CG  . HIS A 81  ? 0.8386 0.6868 0.6744 0.2330  -0.0484 0.0395  382 HIS A CG  
600   N ND1 . HIS A 81  ? 0.8512 0.6959 0.6869 0.2401  -0.0481 0.0331  382 HIS A ND1 
601   C CD2 . HIS A 81  ? 0.8095 0.7001 0.6707 0.2218  -0.0461 0.0369  382 HIS A CD2 
602   C CE1 . HIS A 81  ? 0.7702 0.6548 0.6302 0.2338  -0.0455 0.0274  382 HIS A CE1 
603   N NE2 . HIS A 81  ? 0.7925 0.7044 0.6680 0.2222  -0.0441 0.0297  382 HIS A NE2 
604   N N   . MET A 82  ? 0.7779 0.6383 0.5850 0.2754  -0.0642 0.0464  383 MET A N   
605   C CA  . MET A 82  ? 0.8793 0.7838 0.6971 0.2927  -0.0699 0.0404  383 MET A CA  
606   C C   . MET A 82  ? 0.9467 0.8769 0.7714 0.2886  -0.0722 0.0431  383 MET A C   
607   O O   . MET A 82  ? 0.9554 0.9337 0.8007 0.2900  -0.0742 0.0370  383 MET A O   
608   C CB  . MET A 82  ? 0.9139 0.8011 0.7091 0.3219  -0.0766 0.0389  383 MET A CB  
609   C CG  . MET A 82  ? 1.0684 0.9378 0.8586 0.3269  -0.0747 0.0332  383 MET A CG  
610   S SD  . MET A 82  ? 1.1387 1.0599 0.9613 0.3236  -0.0719 0.0229  383 MET A SD  
611   C CE  . MET A 82  ? 1.0711 0.9607 0.8778 0.3354  -0.0715 0.0172  383 MET A CE  
612   N N   . GLU A 83  ? 0.9003 0.8000 0.7078 0.2833  -0.0720 0.0518  384 GLU A N   
613   C CA  . GLU A 83  ? 0.9004 0.8237 0.7135 0.2793  -0.0742 0.0539  384 GLU A CA  
614   C C   . GLU A 83  ? 0.8741 0.8234 0.7128 0.2539  -0.0685 0.0518  384 GLU A C   
615   O O   . GLU A 83  ? 0.8058 0.7950 0.6610 0.2511  -0.0706 0.0477  384 GLU A O   
616   C CB  . GLU A 83  ? 1.0339 0.9173 0.8199 0.2813  -0.0752 0.0641  384 GLU A CB  
617   C CG  . GLU A 83  ? 1.1943 1.0613 0.9553 0.3076  -0.0822 0.0661  384 GLU A CG  
618   C CD  . GLU A 83  ? 1.2412 1.0626 0.9751 0.3034  -0.0803 0.0757  384 GLU A CD  
619   O OE1 . GLU A 83  ? 1.1752 0.9796 0.9072 0.2864  -0.0760 0.0829  384 GLU A OE1 
620   O OE2 . GLU A 83  ? 1.2625 1.0664 0.9769 0.3169  -0.0829 0.0759  384 GLU A OE2 
621   N N   . ARG A 84  ? 0.8707 0.7970 0.7119 0.2353  -0.0615 0.0543  385 ARG A N   
622   C CA  . ARG A 84  ? 0.7922 0.7400 0.6561 0.2126  -0.0561 0.0522  385 ARG A CA  
623   C C   . ARG A 84  ? 0.8226 0.8149 0.7108 0.2126  -0.0564 0.0434  385 ARG A C   
624   O O   . ARG A 84  ? 0.7632 0.7855 0.6696 0.1999  -0.0552 0.0406  385 ARG A O   
625   C CB  . ARG A 84  ? 0.7828 0.6995 0.6444 0.1964  -0.0491 0.0555  385 ARG A CB  
626   C CG  . ARG A 84  ? 0.7631 0.6984 0.6462 0.1746  -0.0433 0.0534  385 ARG A CG  
627   C CD  . ARG A 84  ? 0.6487 0.5972 0.5359 0.1657  -0.0436 0.0556  385 ARG A CD  
628   N NE  . ARG A 84  ? 0.7483 0.7131 0.6545 0.1465  -0.0385 0.0533  385 ARG A NE  
629   C CZ  . ARG A 84  ? 0.7459 0.7276 0.6598 0.1373  -0.0385 0.0529  385 ARG A CZ  
630   N NH1 . ARG A 84  ? 0.8436 0.8303 0.7487 0.1454  -0.0434 0.0545  385 ARG A NH1 
631   N NH2 . ARG A 84  ? 0.6332 0.6260 0.5622 0.1208  -0.0340 0.0508  385 ARG A NH2 
632   N N   . LEU A 85  ? 0.8716 0.8682 0.7593 0.2270  -0.0582 0.0388  386 LEU A N   
633   C CA  . LEU A 85  ? 0.8019 0.8416 0.7118 0.2273  -0.0580 0.0305  386 LEU A CA  
634   C C   . LEU A 85  ? 0.8985 0.9803 0.8189 0.2332  -0.0631 0.0266  386 LEU A C   
635   O O   . LEU A 85  ? 0.8993 1.0142 0.8403 0.2186  -0.0610 0.0229  386 LEU A O   
636   C CB  . LEU A 85  ? 0.8091 0.8447 0.7132 0.2450  -0.0596 0.0262  386 LEU A CB  
637   C CG  . LEU A 85  ? 0.7251 0.7768 0.6464 0.2356  -0.0543 0.0209  386 LEU A CG  
638   C CD1 . LEU A 85  ? 0.7847 0.8836 0.7319 0.2220  -0.0522 0.0167  386 LEU A CD1 
639   C CD2 . LEU A 85  ? 0.7246 0.7399 0.6410 0.2195  -0.0483 0.0253  386 LEU A CD2 
640   N N   . GLU A 86  ? 0.9664 1.0466 0.8715 0.2545  -0.0701 0.0273  387 GLU A N   
641   C CA  . GLU A 86  ? 0.9611 1.0833 0.8751 0.2617  -0.0759 0.0230  387 GLU A CA  
642   C C   . GLU A 86  ? 0.8450 0.9714 0.7635 0.2446  -0.0751 0.0260  387 GLU A C   
643   O O   . GLU A 86  ? 0.8062 0.9732 0.7408 0.2397  -0.0774 0.0207  387 GLU A O   
644   C CB  . GLU A 86  ? 1.1441 1.2605 1.0380 0.2905  -0.0840 0.0236  387 GLU A CB  
645   C CG  . GLU A 86  ? 1.2315 1.3403 1.1109 0.2955  -0.0889 0.0287  387 GLU A CG  
646   C CD  . GLU A 86  ? 1.3024 1.4337 1.1731 0.3233  -0.0981 0.0255  387 GLU A CD  
647   O OE1 . GLU A 86  ? 1.3408 1.5243 1.2315 0.3261  -0.1011 0.0170  387 GLU A OE1 
648   O OE2 . GLU A 86  ? 1.3012 1.3967 1.1457 0.3371  -0.1001 0.0301  387 GLU A OE2 
649   N N   . GLU A 87  ? 0.7332 0.8192 0.6382 0.2344  -0.0716 0.0338  388 GLU A N   
650   C CA  . GLU A 87  ? 0.6370 0.7259 0.5459 0.2180  -0.0702 0.0362  388 GLU A CA  
651   C C   . GLU A 87  ? 0.7574 0.8716 0.6909 0.1960  -0.0652 0.0314  388 GLU A C   
652   O O   . GLU A 87  ? 0.7895 0.9242 0.7321 0.1855  -0.0661 0.0292  388 GLU A O   
653   C CB  . GLU A 87  ? 0.6020 0.6437 0.4916 0.2115  -0.0667 0.0454  388 GLU A CB  
654   C CG  . GLU A 87  ? 0.5537 0.5953 0.4410 0.2005  -0.0666 0.0486  388 GLU A CG  
655   C CD  . GLU A 87  ? 0.7250 0.7277 0.6009 0.1873  -0.0605 0.0563  388 GLU A CD  
656   O OE1 . GLU A 87  ? 0.8174 0.8001 0.6943 0.1805  -0.0553 0.0576  388 GLU A OE1 
657   O OE2 . GLU A 87  ? 0.8061 0.8001 0.6723 0.1833  -0.0609 0.0607  388 GLU A OE2 
658   N N   . VAL A 88  ? 0.6249 0.7362 0.5680 0.1888  -0.0599 0.0297  389 VAL A N   
659   C CA  . VAL A 88  ? 0.5411 0.6741 0.5055 0.1686  -0.0549 0.0258  389 VAL A CA  
660   C C   . VAL A 88  ? 0.6678 0.8492 0.6498 0.1710  -0.0580 0.0178  389 VAL A C   
661   O O   . VAL A 88  ? 0.5668 0.7717 0.5634 0.1554  -0.0568 0.0145  389 VAL A O   
662   C CB  . VAL A 88  ? 0.4437 0.5591 0.4119 0.1604  -0.0483 0.0268  389 VAL A CB  
663   C CG1 . VAL A 88  ? 0.4896 0.6293 0.4785 0.1418  -0.0436 0.0230  389 VAL A CG1 
664   C CG2 . VAL A 88  ? 0.4581 0.5297 0.4116 0.1541  -0.0445 0.0340  389 VAL A CG2 
665   N N   . ASN A 89  ? 0.8397 1.0364 0.8197 0.1906  -0.0622 0.0144  390 ASN A N   
666   C CA  . ASN A 89  ? 0.8444 1.0914 0.8415 0.1941  -0.0652 0.0063  390 ASN A CA  
667   C C   . ASN A 89  ? 0.8111 1.0833 0.8116 0.1925  -0.0706 0.0038  390 ASN A C   
668   O O   . ASN A 89  ? 0.8668 1.1772 0.8857 0.1805  -0.0705 -0.0023 390 ASN A O   
669   C CB  . ASN A 89  ? 0.9505 1.2073 0.9419 0.2188  -0.0692 0.0032  390 ASN A CB  
670   C CG  . ASN A 89  ? 0.9787 1.2367 0.9779 0.2171  -0.0638 0.0010  390 ASN A CG  
671   O OD1 . ASN A 89  ? 1.0803 1.3746 1.0904 0.2260  -0.0649 -0.0055 390 ASN A OD1 
672   N ND2 . ASN A 89  ? 0.8283 1.0489 0.8221 0.2055  -0.0577 0.0060  390 ASN A ND2 
673   N N   . LYS A 90  ? 0.7894 1.0401 0.7714 0.2036  -0.0753 0.0083  391 LYS A N   
674   C CA  . LYS A 90  ? 0.7527 1.0259 0.7362 0.2023  -0.0808 0.0058  391 LYS A CA  
675   C C   . LYS A 90  ? 0.6437 0.9192 0.6388 0.1761  -0.0764 0.0050  391 LYS A C   
676   O O   . LYS A 90  ? 0.7494 1.0601 0.7578 0.1674  -0.0790 -0.0013 391 LYS A O   
677   C CB  . LYS A 90  ? 0.7705 1.0150 0.7293 0.2184  -0.0858 0.0122  391 LYS A CB  
678   C CG  . LYS A 90  ? 0.8426 1.0958 0.7896 0.2473  -0.0930 0.0111  391 LYS A CG  
679   C CD  . LYS A 90  ? 0.9794 1.1898 0.8973 0.2626  -0.0960 0.0199  391 LYS A CD  
680   C CE  . LYS A 90  ? 1.1354 1.3504 1.0393 0.2930  -0.1032 0.0190  391 LYS A CE  
681   N NZ  . LYS A 90  ? 1.2322 1.4052 1.1051 0.3086  -0.1067 0.0282  391 LYS A NZ  
682   N N   . GLU A 91  ? 0.5669 0.8055 0.5569 0.1633  -0.0699 0.0109  392 GLU A N   
683   C CA  . GLU A 91  ? 0.6363 0.8729 0.6350 0.1402  -0.0657 0.0104  392 GLU A CA  
684   C C   . GLU A 91  ? 0.7326 0.9998 0.7531 0.1249  -0.0622 0.0041  392 GLU A C   
685   O O   . GLU A 91  ? 0.8266 1.1147 0.8575 0.1106  -0.0629 -0.0006 392 GLU A O   
686   C CB  . GLU A 91  ? 0.6391 0.8311 0.6268 0.1323  -0.0597 0.0180  392 GLU A CB  
687   C CG  . GLU A 91  ? 0.6958 0.8696 0.6728 0.1262  -0.0603 0.0215  392 GLU A CG  
688   C CD  . GLU A 91  ? 0.7354 0.8675 0.7004 0.1213  -0.0547 0.0291  392 GLU A CD  
689   O OE1 . GLU A 91  ? 0.7448 0.8664 0.7106 0.1070  -0.0513 0.0302  392 GLU A OE1 
690   O OE2 . GLU A 91  ? 0.7351 0.8454 0.6894 0.1319  -0.0538 0.0337  392 GLU A OE2 
691   N N   . ILE A 92  ? 0.6699 0.9392 0.6967 0.1269  -0.0584 0.0038  393 ILE A N   
692   C CA  . ILE A 92  ? 0.6846 0.9832 0.7310 0.1121  -0.0545 -0.0014 393 ILE A CA  
693   C C   . ILE A 92  ? 0.8228 1.1707 0.8815 0.1154  -0.0599 -0.0094 393 ILE A C   
694   O O   . ILE A 92  ? 0.8993 1.2728 0.9726 0.0979  -0.0584 -0.0143 393 ILE A O   
695   C CB  . ILE A 92  ? 0.5816 0.8739 0.6311 0.1149  -0.0493 -0.0001 393 ILE A CB  
696   C CG1 . ILE A 92  ? 0.5494 0.7946 0.5858 0.1136  -0.0448 0.0073  393 ILE A CG1 
697   C CG2 . ILE A 92  ? 0.5724 0.8897 0.6399 0.0969  -0.0441 -0.0038 393 ILE A CG2 
698   C CD1 . ILE A 92  ? 0.4703 0.7083 0.5076 0.1189  -0.0407 0.0080  393 ILE A CD1 
699   N N   . ASP A 93  ? 0.8774 1.2392 0.9298 0.1377  -0.0665 -0.0111 394 ASP A N   
700   C CA  . ASP A 93  ? 0.8267 1.2381 0.8903 0.1428  -0.0725 -0.0192 394 ASP A CA  
701   C C   . ASP A 93  ? 0.8294 1.2502 0.8950 0.1296  -0.0759 -0.0220 394 ASP A C   
702   O O   . ASP A 93  ? 0.8333 1.2895 0.9152 0.1144  -0.0759 -0.0289 394 ASP A O   
703   C CB  . ASP A 93  ? 0.9190 1.3378 0.9714 0.1720  -0.0797 -0.0197 394 ASP A CB  
704   C CG  . ASP A 93  ? 1.0243 1.4806 1.0882 0.1835  -0.0801 -0.0255 394 ASP A CG  
705   O OD1 . ASP A 93  ? 1.0454 1.5153 1.1018 0.2083  -0.0867 -0.0275 394 ASP A OD1 
706   O OD2 . ASP A 93  ? 1.0733 1.5450 1.1526 0.1687  -0.0739 -0.0279 394 ASP A OD2 
707   N N   . THR A 94  ? 0.7370 1.1261 0.7855 0.1347  -0.0785 -0.0169 395 THR A N   
708   C CA  . THR A 94  ? 0.8092 1.2055 0.8577 0.1235  -0.0819 -0.0199 395 THR A CA  
709   C C   . THR A 94  ? 0.9143 1.2933 0.9689 0.0974  -0.0753 -0.0193 395 THR A C   
710   O O   . THR A 94  ? 0.9907 1.3965 1.0605 0.0800  -0.0743 -0.0257 395 THR A O   
711   C CB  . THR A 94  ? 0.7716 1.1417 0.7988 0.1385  -0.0869 -0.0146 395 THR A CB  
712   O OG1 . THR A 94  ? 0.7418 1.0628 0.7548 0.1384  -0.0814 -0.0054 395 THR A OG1 
713   C CG2 . THR A 94  ? 0.8016 1.1890 0.8213 0.1652  -0.0940 -0.0154 395 THR A CG2 
714   N N   . THR A 95  ? 0.9267 1.2608 0.9688 0.0942  -0.0707 -0.0117 396 THR A N   
715   C CA  . THR A 95  ? 0.7839 1.0991 0.8282 0.0725  -0.0656 -0.0110 396 THR A CA  
716   C C   . THR A 95  ? 0.7653 1.0849 0.8234 0.0567  -0.0586 -0.0121 396 THR A C   
717   O O   . THR A 95  ? 0.8472 1.1538 0.9074 0.0384  -0.0547 -0.0123 396 THR A O   
718   C CB  . THR A 95  ? 0.7037 0.9730 0.7309 0.0750  -0.0627 -0.0028 396 THR A CB  
719   O OG1 . THR A 95  ? 0.7106 0.9574 0.7345 0.0805  -0.0575 0.0032  396 THR A OG1 
720   C CG2 . THR A 95  ? 0.5108 0.7737 0.5219 0.0914  -0.0690 -0.0005 396 THR A CG2 
721   N N   . SER A 96  ? 0.7225 1.0592 0.7885 0.0639  -0.0571 -0.0126 397 SER A N   
722   C CA  . SER A 96  ? 0.6487 0.9894 0.7262 0.0509  -0.0501 -0.0126 397 SER A CA  
723   C C   . SER A 96  ? 0.6280 0.9264 0.6972 0.0465  -0.0435 -0.0053 397 SER A C   
724   O O   . SER A 96  ? 0.5480 0.8439 0.6244 0.0334  -0.0375 -0.0045 397 SER A O   
725   C CB  . SER A 96  ? 0.6415 1.0055 0.7322 0.0287  -0.0487 -0.0185 397 SER A CB  
726   O OG  . SER A 96  ? 0.7263 1.1380 0.8300 0.0310  -0.0525 -0.0258 397 SER A OG  
727   N N   . THR A 97  ? 0.6739 0.9403 0.7278 0.0569  -0.0446 0.0003  398 THR A N   
728   C CA  . THR A 97  ? 0.6171 0.8452 0.6624 0.0549  -0.0390 0.0070  398 THR A CA  
729   C C   . THR A 97  ? 0.6331 0.8381 0.6623 0.0720  -0.0420 0.0119  398 THR A C   
730   O O   . THR A 97  ? 0.6973 0.9161 0.7223 0.0864  -0.0480 0.0103  398 THR A O   
731   C CB  . THR A 97  ? 0.6242 0.8337 0.6683 0.0373  -0.0355 0.0081  398 THR A CB  
732   O OG1 . THR A 97  ? 0.5564 0.7326 0.5930 0.0363  -0.0303 0.0142  398 THR A OG1 
733   C CG2 . THR A 97  ? 0.5990 0.8054 0.6350 0.0377  -0.0404 0.0067  398 THR A CG2 
734   N N   . TYR A 98  ? 0.5748 0.7450 0.5943 0.0707  -0.0378 0.0180  399 TYR A N   
735   C CA  . TYR A 98  ? 0.4802 0.6254 0.4828 0.0840  -0.0400 0.0233  399 TYR A CA  
736   C C   . TYR A 98  ? 0.6059 0.7181 0.6001 0.0752  -0.0352 0.0287  399 TYR A C   
737   O O   . TYR A 98  ? 0.7171 0.8259 0.7182 0.0610  -0.0307 0.0281  399 TYR A O   
738   C CB  . TYR A 98  ? 0.4610 0.6030 0.4592 0.0999  -0.0409 0.0245  399 TYR A CB  
739   C CG  . TYR A 98  ? 0.5143 0.6405 0.5148 0.0961  -0.0350 0.0266  399 TYR A CG  
740   C CD1 . TYR A 98  ? 0.4612 0.5539 0.4481 0.1012  -0.0331 0.0321  399 TYR A CD1 
741   C CD2 . TYR A 98  ? 0.5913 0.7363 0.6068 0.0867  -0.0314 0.0230  399 TYR A CD2 
742   C CE1 . TYR A 98  ? 0.5771 0.6568 0.5659 0.0976  -0.0282 0.0331  399 TYR A CE1 
743   C CE2 . TYR A 98  ? 0.4850 0.6164 0.5018 0.0839  -0.0263 0.0248  399 TYR A CE2 
744   C CZ  . TYR A 98  ? 0.5504 0.6499 0.5542 0.0897  -0.0250 0.0294  399 TYR A CZ  
745   O OH  . TYR A 98  ? 0.6071 0.6940 0.6118 0.0871  -0.0204 0.0304  399 TYR A OH  
746   N N   . GLN A 99  ? 0.5533 0.6415 0.5317 0.0840  -0.0361 0.0340  400 GLN A N   
747   C CA  . GLN A 99  ? 0.6213 0.6819 0.5907 0.0765  -0.0321 0.0391  400 GLN A CA  
748   C C   . GLN A 99  ? 0.7313 0.7652 0.6903 0.0825  -0.0294 0.0445  400 GLN A C   
749   O O   . GLN A 99  ? 0.7445 0.7707 0.6926 0.0960  -0.0327 0.0468  400 GLN A O   
750   C CB  . GLN A 99  ? 0.6690 0.7257 0.6275 0.0784  -0.0353 0.0406  400 GLN A CB  
751   C CG  . GLN A 99  ? 0.5787 0.6563 0.5456 0.0695  -0.0374 0.0349  400 GLN A CG  
752   C CD  . GLN A 99  ? 0.6267 0.6985 0.6013 0.0538  -0.0321 0.0336  400 GLN A CD  
753   O OE1 . GLN A 99  ? 0.6637 0.7133 0.6322 0.0497  -0.0277 0.0379  400 GLN A OE1 
754   N NE2 . GLN A 99  ? 0.6042 0.6962 0.5917 0.0447  -0.0326 0.0277  400 GLN A NE2 
755   N N   . LEU A 100 ? 0.7221 0.7412 0.6836 0.0726  -0.0237 0.0464  401 LEU A N   
756   C CA  . LEU A 100 ? 0.6691 0.6634 0.6213 0.0760  -0.0210 0.0507  401 LEU A CA  
757   C C   . LEU A 100 ? 0.5806 0.5519 0.5158 0.0780  -0.0210 0.0567  401 LEU A C   
758   O O   . LEU A 100 ? 0.6205 0.5905 0.5539 0.0708  -0.0197 0.0579  401 LEU A O   
759   C CB  . LEU A 100 ? 0.5761 0.5642 0.5361 0.0646  -0.0151 0.0505  401 LEU A CB  
760   C CG  . LEU A 100 ? 0.4420 0.4484 0.4167 0.0619  -0.0139 0.0460  401 LEU A CG  
761   C CD1 . LEU A 100 ? 0.4836 0.4822 0.4632 0.0503  -0.0084 0.0467  401 LEU A CD1 
762   C CD2 . LEU A 100 ? 0.4731 0.4780 0.4454 0.0732  -0.0154 0.0451  401 LEU A CD2 
763   N N   . LYS A 101 ? 0.5408 0.4928 0.4625 0.0878  -0.0222 0.0604  402 LYS A N   
764   C CA  . LYS A 101 ? 0.4931 0.4184 0.3976 0.0867  -0.0205 0.0671  402 LYS A CA  
765   C C   . LYS A 101 ? 0.6228 0.5375 0.5308 0.0723  -0.0140 0.0687  402 LYS A C   
766   O O   . LYS A 101 ? 0.7973 0.7202 0.7184 0.0657  -0.0113 0.0651  402 LYS A O   
767   C CB  . LYS A 101 ? 0.5064 0.4088 0.3949 0.0984  -0.0224 0.0707  402 LYS A CB  
768   C CG  . LYS A 101 ? 0.7631 0.6766 0.6468 0.1158  -0.0294 0.0690  402 LYS A CG  
769   C CD  . LYS A 101 ? 0.9182 0.8094 0.7784 0.1259  -0.0324 0.0758  402 LYS A CD  
770   C CE  . LYS A 101 ? 1.0192 0.9290 0.8782 0.1299  -0.0365 0.0757  402 LYS A CE  
771   N NZ  . LYS A 101 ? 1.0887 1.0301 0.9591 0.1406  -0.0424 0.0688  402 LYS A NZ  
772   N N   . ASP A 102 ? 0.7877 0.6853 0.6833 0.0677  -0.0115 0.0741  403 ASP A N   
773   C CA  . ASP A 102 ? 0.7590 0.6502 0.6580 0.0546  -0.0055 0.0753  403 ASP A CA  
774   C C   . ASP A 102 ? 0.7118 0.5894 0.6116 0.0518  -0.0028 0.0751  403 ASP A C   
775   O O   . ASP A 102 ? 0.8305 0.7136 0.7410 0.0430  0.0009  0.0726  403 ASP A O   
776   C CB  . ASP A 102 ? 0.9355 0.8132 0.8203 0.0505  -0.0032 0.0813  403 ASP A CB  
777   C CG  . ASP A 102 ? 1.0347 0.9279 0.9208 0.0502  -0.0047 0.0802  403 ASP A CG  
778   O OD1 . ASP A 102 ? 1.0320 0.9447 0.9288 0.0534  -0.0082 0.0749  403 ASP A OD1 
779   O OD2 . ASP A 102 ? 1.0811 0.9673 0.9571 0.0462  -0.0022 0.0845  403 ASP A OD2 
780   N N   . THR A 103 ? 0.6343 0.4932 0.5216 0.0598  -0.0048 0.0775  404 THR A N   
781   C CA  . THR A 103 ? 0.6393 0.4831 0.5254 0.0574  -0.0027 0.0767  404 THR A CA  
782   C C   . THR A 103 ? 0.6462 0.5081 0.5487 0.0594  -0.0034 0.0701  404 THR A C   
783   O O   . THR A 103 ? 0.6104 0.4710 0.5196 0.0523  -0.0001 0.0678  404 THR A O   
784   C CB  . THR A 103 ? 0.5738 0.3914 0.4408 0.0672  -0.0054 0.0802  404 THR A CB  
785   O OG1 . THR A 103 ? 0.6640 0.4917 0.5291 0.0822  -0.0112 0.0790  404 THR A OG1 
786   C CG2 . THR A 103 ? 0.5971 0.3909 0.4460 0.0614  -0.0029 0.0878  404 THR A CG2 
787   N N   . GLU A 104 ? 0.7393 0.6194 0.6479 0.0691  -0.0076 0.0669  405 GLU A N   
788   C CA  . GLU A 104 ? 0.6594 0.5598 0.5836 0.0704  -0.0079 0.0610  405 GLU A CA  
789   C C   . GLU A 104 ? 0.6623 0.5769 0.6007 0.0577  -0.0039 0.0591  405 GLU A C   
790   O O   . GLU A 104 ? 0.7263 0.6459 0.6735 0.0541  -0.0015 0.0561  405 GLU A O   
791   C CB  . GLU A 104 ? 0.5705 0.4917 0.4988 0.0816  -0.0131 0.0580  405 GLU A CB  
792   C CG  . GLU A 104 ? 0.5146 0.4228 0.4278 0.0974  -0.0178 0.0596  405 GLU A CG  
793   C CD  . GLU A 104 ? 0.5975 0.5281 0.5132 0.1087  -0.0234 0.0573  405 GLU A CD  
794   O OE1 . GLU A 104 ? 0.6926 0.6161 0.5969 0.1241  -0.0278 0.0576  405 GLU A OE1 
795   O OE2 . GLU A 104 ? 0.6024 0.5569 0.5302 0.1027  -0.0236 0.0549  405 GLU A OE2 
796   N N   . LEU A 105 ? 0.6324 0.5522 0.5716 0.0517  -0.0031 0.0607  406 LEU A N   
797   C CA  . LEU A 105 ? 0.6356 0.5673 0.5864 0.0414  0.0003  0.0588  406 LEU A CA  
798   C C   . LEU A 105 ? 0.6464 0.5667 0.5971 0.0334  0.0049  0.0598  406 LEU A C   
799   O O   . LEU A 105 ? 0.5948 0.5239 0.5555 0.0284  0.0073  0.0572  406 LEU A O   
800   C CB  . LEU A 105 ? 0.4392 0.3762 0.3884 0.0379  -0.0001 0.0599  406 LEU A CB  
801   C CG  . LEU A 105 ? 0.4668 0.4141 0.4253 0.0289  0.0026  0.0576  406 LEU A CG  
802   C CD1 . LEU A 105 ? 0.4149 0.3813 0.3845 0.0288  0.0004  0.0531  406 LEU A CD1 
803   C CD2 . LEU A 105 ? 0.4976 0.4412 0.4494 0.0253  0.0034  0.0596  406 LEU A CD2 
804   N N   . ILE A 106 ? 0.6444 0.5458 0.5833 0.0319  0.0063  0.0637  407 ILE A N   
805   C CA  . ILE A 106 ? 0.5576 0.4501 0.4962 0.0235  0.0105  0.0642  407 ILE A CA  
806   C C   . ILE A 106 ? 0.6052 0.4951 0.5475 0.0255  0.0105  0.0610  407 ILE A C   
807   O O   . ILE A 106 ? 0.4785 0.3738 0.4284 0.0195  0.0133  0.0587  407 ILE A O   
808   C CB  . ILE A 106 ? 0.5521 0.4252 0.4762 0.0200  0.0121  0.0692  407 ILE A CB  
809   C CG1 . ILE A 106 ? 0.5472 0.4266 0.4701 0.0150  0.0140  0.0717  407 ILE A CG1 
810   C CG2 . ILE A 106 ? 0.5591 0.4203 0.4811 0.0127  0.0153  0.0690  407 ILE A CG2 
811   C CD1 . ILE A 106 ? 0.6032 0.4656 0.5097 0.0143  0.0146  0.0776  407 ILE A CD1 
812   N N   . TYR A 107 ? 0.5763 0.4579 0.5122 0.0349  0.0071  0.0605  408 TYR A N   
813   C CA  . TYR A 107 ? 0.6314 0.5115 0.5700 0.0388  0.0066  0.0566  408 TYR A CA  
814   C C   . TYR A 107 ? 0.6615 0.5654 0.6156 0.0386  0.0071  0.0526  408 TYR A C   
815   O O   . TYR A 107 ? 0.6758 0.5832 0.6357 0.0357  0.0091  0.0497  408 TYR A O   
816   C CB  . TYR A 107 ? 0.6431 0.5118 0.5712 0.0515  0.0024  0.0565  408 TYR A CB  
817   C CG  . TYR A 107 ? 0.6033 0.4762 0.5354 0.0584  0.0012  0.0513  408 TYR A CG  
818   C CD1 . TYR A 107 ? 0.6756 0.5283 0.5992 0.0584  0.0016  0.0498  408 TYR A CD1 
819   C CD2 . TYR A 107 ? 0.5287 0.4259 0.4724 0.0647  -0.0004 0.0477  408 TYR A CD2 
820   C CE1 . TYR A 107 ? 0.6371 0.4937 0.5634 0.0655  0.0005  0.0444  408 TYR A CE1 
821   C CE2 . TYR A 107 ? 0.6216 0.5248 0.5688 0.0714  -0.0011 0.0429  408 TYR A CE2 
822   C CZ  . TYR A 107 ? 0.6599 0.5426 0.5982 0.0724  -0.0007 0.0411  408 TYR A CZ  
823   O OH  . TYR A 107 ? 0.6593 0.5478 0.6001 0.0798  -0.0015 0.0357  408 TYR A OH  
824   N N   . GLY A 108 ? 0.6369 0.5572 0.5969 0.0415  0.0053  0.0523  409 GLY A N   
825   C CA  . GLY A 108 ? 0.5839 0.5258 0.5574 0.0396  0.0061  0.0492  409 GLY A CA  
826   C C   . GLY A 108 ? 0.5862 0.5308 0.5659 0.0296  0.0101  0.0493  409 GLY A C   
827   O O   . GLY A 108 ? 0.7793 0.7298 0.7649 0.0281  0.0120  0.0470  409 GLY A O   
828   N N   . ALA A 109 ? 0.5501 0.4904 0.5272 0.0236  0.0116  0.0518  410 ALA A N   
829   C CA  . ALA A 109 ? 0.5286 0.4727 0.5107 0.0159  0.0150  0.0516  410 ALA A CA  
830   C C   . ALA A 109 ? 0.5418 0.4788 0.5230 0.0132  0.0173  0.0509  410 ALA A C   
831   O O   . ALA A 109 ? 0.4979 0.4418 0.4849 0.0097  0.0196  0.0495  410 ALA A O   
832   C CB  . ALA A 109 ? 0.4358 0.3772 0.4142 0.0117  0.0159  0.0538  410 ALA A CB  
833   N N   . LYS A 110 ? 0.5430 0.4655 0.5159 0.0145  0.0167  0.0516  411 LYS A N   
834   C CA  . LYS A 110 ? 0.5193 0.4350 0.4909 0.0107  0.0185  0.0501  411 LYS A CA  
835   C C   . LYS A 110 ? 0.7321 0.6535 0.7085 0.0152  0.0178  0.0462  411 LYS A C   
836   O O   . LYS A 110 ? 0.7001 0.6250 0.6800 0.0118  0.0196  0.0439  411 LYS A O   
837   C CB  . LYS A 110 ? 0.4652 0.3607 0.4247 0.0095  0.0181  0.0520  411 LYS A CB  
838   C CG  . LYS A 110 ? 0.4413 0.3326 0.3964 0.0016  0.0206  0.0554  411 LYS A CG  
839   C CD  . LYS A 110 ? 0.4486 0.3187 0.3896 0.0010  0.0200  0.0588  411 LYS A CD  
840   C CE  . LYS A 110 ? 0.5396 0.4057 0.4761 -0.0096 0.0237  0.0615  411 LYS A CE  
841   N NZ  . LYS A 110 ? 0.6355 0.4772 0.5561 -0.0116 0.0235  0.0653  411 LYS A NZ  
842   N N   . HIS A 111 ? 0.6982 0.6228 0.6747 0.0233  0.0152  0.0452  412 HIS A N   
843   C CA  . HIS A 111 ? 0.6228 0.5546 0.6035 0.0281  0.0148  0.0413  412 HIS A CA  
844   C C   . HIS A 111 ? 0.6130 0.5644 0.6046 0.0258  0.0167  0.0406  412 HIS A C   
845   O O   . HIS A 111 ? 0.5944 0.5519 0.5895 0.0260  0.0180  0.0380  412 HIS A O   
846   C CB  . HIS A 111 ? 0.5518 0.4809 0.5279 0.0387  0.0113  0.0400  412 HIS A CB  
847   C CG  . HIS A 111 ? 0.5758 0.4820 0.5395 0.0420  0.0098  0.0392  412 HIS A CG  
848   N ND1 . HIS A 111 ? 0.5929 0.4798 0.5466 0.0373  0.0100  0.0427  412 HIS A ND1 
849   C CD2 . HIS A 111 ? 0.6078 0.5058 0.5662 0.0489  0.0083  0.0352  412 HIS A CD2 
850   C CE1 . HIS A 111 ? 0.6576 0.5236 0.5999 0.0402  0.0087  0.0412  412 HIS A CE1 
851   N NE2 . HIS A 111 ? 0.5765 0.4481 0.5212 0.0478  0.0074  0.0364  412 HIS A NE2 
852   N N   . ALA A 112 ? 0.4387 0.3986 0.4344 0.0231  0.0170  0.0428  413 ALA A N   
853   C CA  . ALA A 112 ? 0.4462 0.4202 0.4498 0.0195  0.0191  0.0427  413 ALA A CA  
854   C C   . ALA A 112 ? 0.5430 0.5147 0.5470 0.0147  0.0219  0.0427  413 ALA A C   
855   O O   . ALA A 112 ? 0.7030 0.6832 0.7109 0.0144  0.0236  0.0417  413 ALA A O   
856   C CB  . ALA A 112 ? 0.4996 0.4790 0.5055 0.0163  0.0188  0.0446  413 ALA A CB  
857   N N   . TRP A 113 ? 0.5840 0.5459 0.5837 0.0111  0.0224  0.0438  414 TRP A N   
858   C CA  . TRP A 113 ? 0.5619 0.5242 0.5621 0.0073  0.0246  0.0430  414 TRP A CA  
859   C C   . TRP A 113 ? 0.6131 0.5742 0.6125 0.0094  0.0243  0.0396  414 TRP A C   
860   O O   . TRP A 113 ? 0.7092 0.6782 0.7118 0.0093  0.0256  0.0381  414 TRP A O   
861   C CB  . TRP A 113 ? 0.4333 0.3880 0.4292 0.0027  0.0253  0.0443  414 TRP A CB  
862   C CG  . TRP A 113 ? 0.4937 0.4529 0.4911 -0.0011 0.0273  0.0432  414 TRP A CG  
863   C CD1 . TRP A 113 ? 0.4698 0.4381 0.4710 0.0000  0.0283  0.0416  414 TRP A CD1 
864   C CD2 . TRP A 113 ? 0.6863 0.6433 0.6811 -0.0063 0.0286  0.0434  414 TRP A CD2 
865   N NE1 . TRP A 113 ? 0.4642 0.4367 0.4655 -0.0033 0.0296  0.0404  414 TRP A NE1 
866   C CE2 . TRP A 113 ? 0.6423 0.6092 0.6404 -0.0076 0.0299  0.0413  414 TRP A CE2 
867   C CE3 . TRP A 113 ? 0.6403 0.5892 0.6299 -0.0100 0.0289  0.0453  414 TRP A CE3 
868   C CZ2 . TRP A 113 ? 0.5855 0.5571 0.5834 -0.0127 0.0315  0.0403  414 TRP A CZ2 
869   C CZ3 . TRP A 113 ? 0.4454 0.3978 0.4342 -0.0161 0.0310  0.0449  414 TRP A CZ3 
870   C CH2 . TRP A 113 ? 0.5079 0.4728 0.5016 -0.0174 0.0322  0.0421  414 TRP A CH2 
871   N N   . ARG A 114 ? 0.5121 0.4622 0.5062 0.0119  0.0224  0.0383  415 ARG A N   
872   C CA  . ARG A 114 ? 0.4119 0.3579 0.4035 0.0144  0.0217  0.0342  415 ARG A CA  
873   C C   . ARG A 114 ? 0.5382 0.4979 0.5350 0.0197  0.0219  0.0321  415 ARG A C   
874   O O   . ARG A 114 ? 0.6628 0.6263 0.6602 0.0202  0.0225  0.0288  415 ARG A O   
875   C CB  . ARG A 114 ? 0.4509 0.3800 0.4337 0.0183  0.0192  0.0336  415 ARG A CB  
876   C CG  . ARG A 114 ? 0.5219 0.4400 0.4987 0.0201  0.0180  0.0288  415 ARG A CG  
877   C CD  . ARG A 114 ? 0.4737 0.3718 0.4395 0.0257  0.0152  0.0288  415 ARG A CD  
878   N NE  . ARG A 114 ? 0.5704 0.4518 0.5275 0.0251  0.0142  0.0243  415 ARG A NE  
879   C CZ  . ARG A 114 ? 0.6407 0.4998 0.5853 0.0303  0.0116  0.0234  415 ARG A CZ  
880   N NH1 . ARG A 114 ? 0.5295 0.3711 0.4652 0.0288  0.0106  0.0187  415 ARG A NH1 
881   N NH2 . ARG A 114 ? 0.6427 0.4959 0.5824 0.0374  0.0097  0.0270  415 ARG A NH2 
882   N N   . ASN A 115 ? 0.5142 0.4831 0.5149 0.0230  0.0217  0.0339  416 ASN A N   
883   C CA  . ASN A 115 ? 0.3914 0.3750 0.3970 0.0272  0.0224  0.0324  416 ASN A CA  
884   C C   . ASN A 115 ? 0.4872 0.4823 0.4979 0.0226  0.0253  0.0346  416 ASN A C   
885   O O   . ASN A 115 ? 0.6085 0.6161 0.6224 0.0246  0.0267  0.0339  416 ASN A O   
886   C CB  . ASN A 115 ? 0.4121 0.4026 0.4197 0.0322  0.0207  0.0328  416 ASN A CB  
887   C CG  . ASN A 115 ? 0.5095 0.4889 0.5103 0.0400  0.0174  0.0304  416 ASN A CG  
888   O OD1 . ASN A 115 ? 0.6279 0.5953 0.6226 0.0423  0.0166  0.0275  416 ASN A OD1 
889   N ND2 . ASN A 115 ? 0.4941 0.4771 0.4951 0.0444  0.0152  0.0314  416 ASN A ND2 
890   N N   . ALA A 116 ? 0.3081 0.2990 0.3184 0.0170  0.0264  0.0373  417 ALA A N   
891   C CA  . ALA A 116 ? 0.4821 0.4803 0.4946 0.0139  0.0289  0.0397  417 ALA A CA  
892   C C   . ALA A 116 ? 0.5706 0.5737 0.5824 0.0154  0.0301  0.0376  417 ALA A C   
893   O O   . ALA A 116 ? 0.5252 0.5245 0.5349 0.0140  0.0299  0.0361  417 ALA A O   
894   C CB  . ALA A 116 ? 0.2506 0.2425 0.2614 0.0097  0.0293  0.0422  417 ALA A CB  
895   N N   . SER A 117 ? 0.5455 0.5590 0.5590 0.0177  0.0315  0.0375  418 SER A N   
896   C CA  A SER A 117 ? 0.5568 0.5756 0.5687 0.0204  0.0322  0.0348  418 SER A CA  
897   C CA  B SER A 117 ? 0.5474 0.5667 0.5594 0.0204  0.0323  0.0349  418 SER A CA  
898   C C   . SER A 117 ? 0.5542 0.5741 0.5640 0.0184  0.0337  0.0370  418 SER A C   
899   O O   . SER A 117 ? 0.6487 0.6718 0.6566 0.0202  0.0334  0.0342  418 SER A O   
900   C CB  A SER A 117 ? 0.5203 0.5516 0.5339 0.0240  0.0336  0.0341  418 SER A CB  
901   C CB  B SER A 117 ? 0.5225 0.5546 0.5364 0.0235  0.0339  0.0348  418 SER A CB  
902   O OG  A SER A 117 ? 0.4885 0.5264 0.5038 0.0205  0.0362  0.0390  418 SER A OG  
903   O OG  B SER A 117 ? 0.4945 0.5287 0.5102 0.0275  0.0323  0.0320  418 SER A OG  
904   N N   . ARG A 118 ? 0.5620 0.5791 0.5712 0.0153  0.0349  0.0416  419 ARG A N   
905   C CA  . ARG A 118 ? 0.5491 0.5659 0.5546 0.0154  0.0360  0.0439  419 ARG A CA  
906   C C   . ARG A 118 ? 0.5642 0.5766 0.5690 0.0147  0.0346  0.0423  419 ARG A C   
907   O O   . ARG A 118 ? 0.6669 0.6810 0.6686 0.0163  0.0351  0.0435  419 ARG A O   
908   C CB  . ARG A 118 ? 0.4599 0.4730 0.4628 0.0131  0.0380  0.0493  419 ARG A CB  
909   C CG  . ARG A 118 ? 0.3889 0.4086 0.3922 0.0120  0.0402  0.0515  419 ARG A CG  
910   C CD  . ARG A 118 ? 0.4306 0.4442 0.4297 0.0079  0.0424  0.0569  419 ARG A CD  
911   N NE  . ARG A 118 ? 0.6007 0.6225 0.5989 0.0061  0.0454  0.0594  419 ARG A NE  
912   C CZ  . ARG A 118 ? 0.5927 0.6110 0.5876 0.0003  0.0479  0.0640  419 ARG A CZ  
913   N NH1 . ARG A 118 ? 0.4352 0.4404 0.4270 -0.0037 0.0474  0.0661  419 ARG A NH1 
914   N NH2 . ARG A 118 ? 0.4869 0.5150 0.4811 -0.0021 0.0512  0.0663  419 ARG A NH2 
915   N N   . CYS A 119 ? 0.4903 0.4977 0.4971 0.0125  0.0330  0.0399  420 CYS A N   
916   C CA  . CYS A 119 ? 0.4875 0.4922 0.4938 0.0102  0.0323  0.0390  420 CYS A CA  
917   C C   . CYS A 119 ? 0.4622 0.4709 0.4689 0.0094  0.0313  0.0341  420 CYS A C   
918   O O   . CYS A 119 ? 0.4191 0.4236 0.4259 0.0085  0.0301  0.0311  420 CYS A O   
919   C CB  . CYS A 119 ? 0.4889 0.4850 0.4957 0.0072  0.0316  0.0400  420 CYS A CB  
920   S SG  . CYS A 119 ? 0.5042 0.4990 0.5101 0.0034  0.0315  0.0390  420 CYS A SG  
921   N N   . VAL A 120 ? 0.4657 0.4824 0.4720 0.0100  0.0314  0.0330  421 VAL A N   
922   C CA  . VAL A 120 ? 0.5431 0.5663 0.5503 0.0079  0.0303  0.0276  421 VAL A CA  
923   C C   . VAL A 120 ? 0.5673 0.5867 0.5755 0.0012  0.0299  0.0257  421 VAL A C   
924   O O   . VAL A 120 ? 0.5780 0.6011 0.5866 -0.0030 0.0290  0.0209  421 VAL A O   
925   C CB  . VAL A 120 ? 0.6577 0.6944 0.6641 0.0119  0.0304  0.0270  421 VAL A CB  
926   C CG1 . VAL A 120 ? 0.5278 0.5689 0.5348 0.0112  0.0308  0.0280  421 VAL A CG1 
927   C CG2 . VAL A 120 ? 0.7254 0.7719 0.7324 0.0112  0.0288  0.0208  421 VAL A CG2 
928   N N   . GLY A 121 ? 0.5964 0.6083 0.6042 -0.0007 0.0306  0.0292  422 GLY A N   
929   C CA  . GLY A 121 ? 0.4070 0.4162 0.4147 -0.0072 0.0310  0.0285  422 GLY A CA  
930   C C   . GLY A 121 ? 0.4671 0.4609 0.4717 -0.0112 0.0303  0.0287  422 GLY A C   
931   O O   . GLY A 121 ? 0.5548 0.5437 0.5577 -0.0167 0.0311  0.0297  422 GLY A O   
932   N N   . ARG A 122 ? 0.4177 0.4038 0.4208 -0.0079 0.0291  0.0278  423 ARG A N   
933   C CA  . ARG A 122 ? 0.4115 0.3820 0.4104 -0.0085 0.0280  0.0287  423 ARG A CA  
934   C C   . ARG A 122 ? 0.4714 0.4308 0.4654 -0.0153 0.0275  0.0258  423 ARG A C   
935   O O   . ARG A 122 ? 0.5280 0.4713 0.5160 -0.0154 0.0265  0.0271  423 ARG A O   
936   C CB  . ARG A 122 ? 0.4151 0.3834 0.4138 -0.0016 0.0267  0.0278  423 ARG A CB  
937   C CG  . ARG A 122 ? 0.3856 0.3618 0.3880 0.0031  0.0275  0.0315  423 ARG A CG  
938   C CD  . ARG A 122 ? 0.4838 0.4618 0.4866 0.0090  0.0267  0.0301  423 ARG A CD  
939   N NE  . ARG A 122 ? 0.4441 0.4334 0.4488 0.0114  0.0276  0.0282  423 ARG A NE  
940   C CZ  . ARG A 122 ? 0.5258 0.5194 0.5306 0.0164  0.0273  0.0261  423 ARG A CZ  
941   N NH1 . ARG A 122 ? 0.4868 0.4749 0.4904 0.0200  0.0259  0.0254  423 ARG A NH1 
942   N NH2 . ARG A 122 ? 0.4788 0.4831 0.4844 0.0186  0.0283  0.0248  423 ARG A NH2 
943   N N   . ILE A 123 ? 0.4272 0.3941 0.4225 -0.0211 0.0279  0.0219  424 ILE A N   
944   C CA  . ILE A 123 ? 0.5477 0.5016 0.5372 -0.0297 0.0276  0.0192  424 ILE A CA  
945   C C   . ILE A 123 ? 0.6261 0.5715 0.6119 -0.0353 0.0292  0.0240  424 ILE A C   
946   O O   . ILE A 123 ? 0.6673 0.5940 0.6449 -0.0406 0.0290  0.0244  424 ILE A O   
947   C CB  . ILE A 123 ? 0.5221 0.4885 0.5145 -0.0367 0.0277  0.0134  424 ILE A CB  
948   C CG1 . ILE A 123 ? 0.5412 0.4915 0.5264 -0.0477 0.0276  0.0106  424 ILE A CG1 
949   C CG2 . ILE A 123 ? 0.5765 0.5642 0.5757 -0.0386 0.0296  0.0146  424 ILE A CG2 
950   C CD1 . ILE A 123 ? 0.4734 0.4328 0.4601 -0.0551 0.0268  0.0032  424 ILE A CD1 
951   N N   . GLN A 124 ? 0.6277 0.5848 0.6179 -0.0338 0.0309  0.0277  425 GLN A N   
952   C CA  . GLN A 124 ? 0.7571 0.7091 0.7440 -0.0376 0.0325  0.0324  425 GLN A CA  
953   C C   . GLN A 124 ? 0.7260 0.6642 0.7083 -0.0311 0.0313  0.0368  425 GLN A C   
954   O O   . GLN A 124 ? 0.7429 0.6784 0.7224 -0.0326 0.0324  0.0408  425 GLN A O   
955   C CB  . GLN A 124 ? 0.7532 0.7246 0.7462 -0.0371 0.0345  0.0336  425 GLN A CB  
956   C CG  . GLN A 124 ? 0.7361 0.7252 0.7336 -0.0434 0.0360  0.0297  425 GLN A CG  
957   C CD  . GLN A 124 ? 0.8938 0.8808 0.8878 -0.0552 0.0383  0.0302  425 GLN A CD  
958   O OE1 . GLN A 124 ? 1.0635 1.0303 1.0496 -0.0604 0.0383  0.0321  425 GLN A OE1 
959   N NE2 . GLN A 124 ? 0.8943 0.9022 0.8932 -0.0594 0.0405  0.0286  425 GLN A NE2 
960   N N   . TRP A 125 ? 0.6636 0.5951 0.6452 -0.0238 0.0289  0.0357  426 TRP A N   
961   C CA  . TRP A 125 ? 0.6294 0.5568 0.6101 -0.0163 0.0275  0.0391  426 TRP A CA  
962   C C   . TRP A 125 ? 0.7121 0.6234 0.6838 -0.0178 0.0272  0.0429  426 TRP A C   
963   O O   . TRP A 125 ? 0.6843 0.5971 0.6558 -0.0147 0.0269  0.0464  426 TRP A O   
964   C CB  . TRP A 125 ? 0.6408 0.5666 0.6223 -0.0085 0.0253  0.0366  426 TRP A CB  
965   C CG  . TRP A 125 ? 0.6260 0.5336 0.5989 -0.0069 0.0233  0.0346  426 TRP A CG  
966   C CD1 . TRP A 125 ? 0.6939 0.5960 0.6641 -0.0088 0.0227  0.0297  426 TRP A CD1 
967   C CD2 . TRP A 125 ? 0.6390 0.5308 0.6036 -0.0019 0.0213  0.0370  426 TRP A CD2 
968   N NE1 . TRP A 125 ? 0.6823 0.5636 0.6422 -0.0055 0.0205  0.0288  426 TRP A NE1 
969   C CE2 . TRP A 125 ? 0.6622 0.5369 0.6182 -0.0006 0.0196  0.0336  426 TRP A CE2 
970   C CE3 . TRP A 125 ? 0.6751 0.5653 0.6378 0.0022  0.0204  0.0414  426 TRP A CE3 
971   C CZ2 . TRP A 125 ? 0.6309 0.4856 0.5756 0.0058  0.0170  0.0349  426 TRP A CZ2 
972   C CZ3 . TRP A 125 ? 0.6438 0.5170 0.5963 0.0082  0.0178  0.0427  426 TRP A CZ3 
973   C CH2 . TRP A 125 ? 0.6414 0.4963 0.5846 0.0104  0.0162  0.0397  426 TRP A CH2 
974   N N   . SER A 126 ? 0.5805 0.4753 0.5436 -0.0226 0.0270  0.0424  427 SER A N   
975   C CA  . SER A 126 ? 0.6212 0.4970 0.5730 -0.0226 0.0264  0.0466  427 SER A CA  
976   C C   . SER A 126 ? 0.7653 0.6417 0.7139 -0.0315 0.0294  0.0505  427 SER A C   
977   O O   . SER A 126 ? 0.7848 0.6443 0.7222 -0.0331 0.0295  0.0547  427 SER A O   
978   C CB  . SER A 126 ? 0.6710 0.5239 0.6119 -0.0232 0.0247  0.0447  427 SER A CB  
979   O OG  . SER A 126 ? 0.8794 0.7297 0.8190 -0.0348 0.0268  0.0420  427 SER A OG  
980   N N   . LYS A 127 ? 0.7212 0.6167 0.6783 -0.0369 0.0320  0.0493  428 LYS A N   
981   C CA  . LYS A 127 ? 0.5925 0.4945 0.5484 -0.0430 0.0351  0.0527  428 LYS A CA  
982   C C   . LYS A 127 ? 0.6955 0.6141 0.6590 -0.0362 0.0349  0.0533  428 LYS A C   
983   O O   . LYS A 127 ? 0.8347 0.7711 0.8057 -0.0375 0.0366  0.0513  428 LYS A O   
984   C CB  . LYS A 127 ? 0.6040 0.5160 0.5625 -0.0546 0.0383  0.0503  428 LYS A CB  
985   C CG  . LYS A 127 ? 0.8039 0.6968 0.7528 -0.0647 0.0390  0.0499  428 LYS A CG  
986   C CD  . LYS A 127 ? 1.0122 0.9169 0.9624 -0.0788 0.0431  0.0492  428 LYS A CD  
987   C CE  . LYS A 127 ? 1.1308 1.0348 1.0745 -0.0836 0.0464  0.0553  428 LYS A CE  
988   N NZ  . LYS A 127 ? 1.0966 1.0297 1.0500 -0.0840 0.0492  0.0546  428 LYS A NZ  
989   N N   . LEU A 128 ? 0.6668 0.5793 0.6279 -0.0284 0.0325  0.0556  429 LEU A N   
990   C CA  . LEU A 128 ? 0.4670 0.3912 0.4331 -0.0229 0.0320  0.0561  429 LEU A CA  
991   C C   . LEU A 128 ? 0.5684 0.4867 0.5266 -0.0228 0.0321  0.0603  429 LEU A C   
992   O O   . LEU A 128 ? 0.5893 0.4920 0.5380 -0.0229 0.0312  0.0633  429 LEU A O   
993   C CB  . LEU A 128 ? 0.3914 0.3168 0.3620 -0.0148 0.0290  0.0545  429 LEU A CB  
994   C CG  . LEU A 128 ? 0.4691 0.4038 0.4438 -0.0104 0.0281  0.0548  429 LEU A CG  
995   C CD1 . LEU A 128 ? 0.4832 0.4307 0.4642 -0.0115 0.0300  0.0528  429 LEU A CD1 
996   C CD2 . LEU A 128 ? 0.3297 0.2642 0.3070 -0.0043 0.0252  0.0540  429 LEU A CD2 
997   N N   . GLN A 129 ? 0.6354 0.5649 0.5959 -0.0219 0.0332  0.0606  430 GLN A N   
998   C CA  . GLN A 129 ? 0.5871 0.5137 0.5400 -0.0219 0.0336  0.0641  430 GLN A CA  
999   C C   . GLN A 129 ? 0.5583 0.4878 0.5130 -0.0143 0.0305  0.0634  430 GLN A C   
1000  O O   . GLN A 129 ? 0.5185 0.4586 0.4793 -0.0124 0.0305  0.0607  430 GLN A O   
1001  C CB  . GLN A 129 ? 0.6052 0.5436 0.5582 -0.0271 0.0376  0.0642  430 GLN A CB  
1002  C CG  . GLN A 129 ? 0.7000 0.6359 0.6437 -0.0281 0.0388  0.0680  430 GLN A CG  
1003  C CD  . GLN A 129 ? 0.7244 0.6417 0.6567 -0.0307 0.0384  0.0729  430 GLN A CD  
1004  O OE1 . GLN A 129 ? 0.7466 0.6546 0.6728 -0.0247 0.0353  0.0751  430 GLN A OE1 
1005  N NE2 . GLN A 129 ? 0.5956 0.5071 0.5242 -0.0397 0.0414  0.0744  430 GLN A NE2 
1006  N N   . VAL A 130 ? 0.5641 0.4841 0.5130 -0.0101 0.0274  0.0655  431 VAL A N   
1007  C CA  . VAL A 130 ? 0.5586 0.4832 0.5104 -0.0038 0.0239  0.0640  431 VAL A CA  
1008  C C   . VAL A 130 ? 0.6346 0.5607 0.5797 -0.0028 0.0235  0.0657  431 VAL A C   
1009  O O   . VAL A 130 ? 0.7304 0.6483 0.6654 -0.0035 0.0240  0.0696  431 VAL A O   
1010  C CB  . VAL A 130 ? 0.5387 0.4566 0.4892 0.0018  0.0203  0.0642  431 VAL A CB  
1011  C CG1 . VAL A 130 ? 0.4044 0.3319 0.3599 0.0068  0.0168  0.0618  431 VAL A CG1 
1012  C CG2 . VAL A 130 ? 0.5432 0.4592 0.4989 0.0011  0.0209  0.0622  431 VAL A CG2 
1013  N N   . PHE A 131 ? 0.5671 0.5025 0.5166 -0.0013 0.0226  0.0627  432 PHE A N   
1014  C CA  . PHE A 131 ? 0.5061 0.4443 0.4498 0.0003  0.0217  0.0629  432 PHE A CA  
1015  C C   . PHE A 131 ? 0.4795 0.4202 0.4247 0.0048  0.0170  0.0608  432 PHE A C   
1016  O O   . PHE A 131 ? 0.6673 0.6137 0.6201 0.0046  0.0158  0.0571  432 PHE A O   
1017  C CB  . PHE A 131 ? 0.5576 0.5036 0.5035 -0.0014 0.0242  0.0600  432 PHE A CB  
1018  C CG  . PHE A 131 ? 0.4792 0.4278 0.4237 -0.0055 0.0288  0.0616  432 PHE A CG  
1019  C CD1 . PHE A 131 ? 0.5001 0.4469 0.4356 -0.0079 0.0310  0.0653  432 PHE A CD1 
1020  C CD2 . PHE A 131 ? 0.4274 0.3816 0.3789 -0.0073 0.0311  0.0594  432 PHE A CD2 
1021  C CE1 . PHE A 131 ? 0.4183 0.3703 0.3531 -0.0132 0.0356  0.0665  432 PHE A CE1 
1022  C CE2 . PHE A 131 ? 0.4284 0.3887 0.3794 -0.0115 0.0352  0.0602  432 PHE A CE2 
1023  C CZ  . PHE A 131 ? 0.4552 0.4152 0.3985 -0.0151 0.0376  0.0635  432 PHE A CZ  
1024  N N   . ASP A 132 ? 0.4827 0.4196 0.4204 0.0086  0.0142  0.0633  433 ASP A N   
1025  C CA  . ASP A 132 ? 0.4866 0.4294 0.4255 0.0132  0.0092  0.0610  433 ASP A CA  
1026  C C   . ASP A 132 ? 0.5787 0.5286 0.5167 0.0124  0.0081  0.0575  433 ASP A C   
1027  O O   . ASP A 132 ? 0.5460 0.4946 0.4748 0.0135  0.0082  0.0592  433 ASP A O   
1028  C CB  . ASP A 132 ? 0.4982 0.4349 0.4273 0.0191  0.0064  0.0648  433 ASP A CB  
1029  C CG  . ASP A 132 ? 0.5890 0.5349 0.5215 0.0250  0.0009  0.0619  433 ASP A CG  
1030  O OD1 . ASP A 132 ? 0.6418 0.5832 0.5676 0.0319  -0.0019 0.0646  433 ASP A OD1 
1031  O OD2 . ASP A 132 ? 0.4800 0.4377 0.4212 0.0228  -0.0006 0.0570  433 ASP A OD2 
1032  N N   . ALA A 133 ? 0.5798 0.5362 0.5260 0.0102  0.0070  0.0528  434 ALA A N   
1033  C CA  . ALA A 133 ? 0.5795 0.5402 0.5238 0.0091  0.0052  0.0486  434 ALA A CA  
1034  C C   . ALA A 133 ? 0.5176 0.4870 0.4653 0.0100  0.0001  0.0449  434 ALA A C   
1035  O O   . ALA A 133 ? 0.4090 0.3820 0.3581 0.0068  -0.0016 0.0400  434 ALA A O   
1036  C CB  . ALA A 133 ? 0.6263 0.5850 0.5746 0.0052  0.0080  0.0456  434 ALA A CB  
1037  N N   . ARG A 134 ? 0.4502 0.4234 0.3986 0.0143  -0.0025 0.0468  435 ARG A N   
1038  C CA  . ARG A 134 ? 0.4821 0.4681 0.4355 0.0152  -0.0074 0.0428  435 ARG A CA  
1039  C C   . ARG A 134 ? 0.5045 0.4966 0.4515 0.0164  -0.0114 0.0396  435 ARG A C   
1040  O O   . ARG A 134 ? 0.6305 0.6352 0.5828 0.0146  -0.0154 0.0346  435 ARG A O   
1041  C CB  . ARG A 134 ? 0.4184 0.4080 0.3732 0.0217  -0.0094 0.0454  435 ARG A CB  
1042  C CG  . ARG A 134 ? 0.4274 0.4174 0.3919 0.0194  -0.0068 0.0454  435 ARG A CG  
1043  C CD  . ARG A 134 ? 0.3670 0.3593 0.3315 0.0273  -0.0088 0.0473  435 ARG A CD  
1044  N NE  . ARG A 134 ? 0.3914 0.3683 0.3439 0.0324  -0.0080 0.0527  435 ARG A NE  
1045  C CZ  . ARG A 134 ? 0.4886 0.4618 0.4354 0.0413  -0.0105 0.0552  435 ARG A CZ  
1046  N NH1 . ARG A 134 ? 0.4385 0.4260 0.3920 0.0468  -0.0140 0.0520  435 ARG A NH1 
1047  N NH2 . ARG A 134 ? 0.4715 0.4272 0.4053 0.0446  -0.0094 0.0606  435 ARG A NH2 
1048  N N   . ASP A 135 ? 0.6423 0.6274 0.5785 0.0185  -0.0103 0.0418  436 ASP A N   
1049  C CA  . ASP A 135 ? 0.6697 0.6609 0.5988 0.0201  -0.0143 0.0383  436 ASP A CA  
1050  C C   . ASP A 135 ? 0.6588 0.6492 0.5888 0.0139  -0.0138 0.0322  436 ASP A C   
1051  O O   . ASP A 135 ? 0.6567 0.6515 0.5805 0.0146  -0.0171 0.0280  436 ASP A O   
1052  C CB  . ASP A 135 ? 0.6713 0.6561 0.5866 0.0258  -0.0133 0.0436  436 ASP A CB  
1053  C CG  . ASP A 135 ? 0.6747 0.6484 0.5862 0.0229  -0.0070 0.0472  436 ASP A CG  
1054  O OD1 . ASP A 135 ? 0.5387 0.5086 0.4388 0.0254  -0.0053 0.0509  436 ASP A OD1 
1055  O OD2 . ASP A 135 ? 0.6810 0.6511 0.6006 0.0183  -0.0036 0.0464  436 ASP A OD2 
1056  N N   . CYS A 136 ? 0.6280 0.6119 0.5643 0.0085  -0.0102 0.0313  437 CYS A N   
1057  C CA  . CYS A 136 ? 0.5182 0.4964 0.4528 0.0038  -0.0094 0.0260  437 CYS A CA  
1058  C C   . CYS A 136 ? 0.6462 0.6314 0.5849 -0.0018 -0.0140 0.0191  437 CYS A C   
1059  O O   . CYS A 136 ? 0.6847 0.6797 0.6323 -0.0041 -0.0159 0.0188  437 CYS A O   
1060  C CB  . CYS A 136 ? 0.4169 0.3855 0.3557 0.0011  -0.0043 0.0280  437 CYS A CB  
1061  S SG  . CYS A 136 ? 0.5724 0.5289 0.5061 -0.0015 -0.0023 0.0232  437 CYS A SG  
1062  N N   . THR A 137 ? 0.6000 0.5812 0.5319 -0.0041 -0.0158 0.0132  438 THR A N   
1063  C CA  . THR A 137 ? 0.5549 0.5415 0.4894 -0.0113 -0.0203 0.0057  438 THR A CA  
1064  C C   . THR A 137 ? 0.4986 0.4699 0.4292 -0.0177 -0.0191 0.0006  438 THR A C   
1065  O O   . THR A 137 ? 0.5549 0.5273 0.4888 -0.0266 -0.0216 -0.0047 438 THR A O   
1066  C CB  . THR A 137 ? 0.6215 0.6199 0.5500 -0.0083 -0.0260 0.0014  438 THR A CB  
1067  O OG1 . THR A 137 ? 0.4683 0.4581 0.3843 -0.0049 -0.0259 -0.0014 438 THR A OG1 
1068  C CG2 . THR A 137 ? 0.5495 0.5604 0.4787 0.0000  -0.0276 0.0070  438 THR A CG2 
1069  N N   . THR A 138 ? 0.4821 0.4391 0.4052 -0.0137 -0.0153 0.0020  439 THR A N   
1070  C CA  . THR A 138 ? 0.5598 0.4998 0.4759 -0.0173 -0.0148 -0.0033 439 THR A CA  
1071  C C   . THR A 138 ? 0.5572 0.4843 0.4732 -0.0147 -0.0094 0.0011  439 THR A C   
1072  O O   . THR A 138 ? 0.5803 0.5123 0.5000 -0.0094 -0.0059 0.0074  439 THR A O   
1073  C CB  . THR A 138 ? 0.5997 0.5355 0.5029 -0.0124 -0.0168 -0.0087 439 THR A CB  
1074  O OG1 . THR A 138 ? 0.6910 0.6317 0.5909 -0.0031 -0.0137 -0.0034 439 THR A OG1 
1075  C CG2 . THR A 138 ? 0.6351 0.5826 0.5370 -0.0155 -0.0229 -0.0146 439 THR A CG2 
1076  N N   . ALA A 139 ? 0.5870 0.4968 0.4973 -0.0184 -0.0089 -0.0027 440 ALA A N   
1077  C CA  . ALA A 139 ? 0.6322 0.5294 0.5399 -0.0139 -0.0044 0.0006  440 ALA A CA  
1078  C C   . ALA A 139 ? 0.7058 0.6058 0.6076 -0.0032 -0.0020 0.0020  440 ALA A C   
1079  O O   . ALA A 139 ? 0.7531 0.6559 0.6585 0.0013  0.0020  0.0073  440 ALA A O   
1080  C CB  . ALA A 139 ? 0.6186 0.4933 0.5169 -0.0177 -0.0049 -0.0041 440 ALA A CB  
1081  N N   . HIS A 140 ? 0.7429 0.6438 0.6355 0.0004  -0.0044 -0.0030 441 HIS A N   
1082  C CA  . HIS A 140 ? 0.6001 0.5062 0.4867 0.0100  -0.0018 -0.0019 441 HIS A CA  
1083  C C   . HIS A 140 ? 0.5831 0.5053 0.4781 0.0116  0.0010  0.0059  441 HIS A C   
1084  O O   . HIS A 140 ? 0.6377 0.5635 0.5329 0.0166  0.0053  0.0096  441 HIS A O   
1085  C CB  . HIS A 140 ? 0.6401 0.5468 0.5155 0.0132  -0.0051 -0.0086 441 HIS A CB  
1086  C CG  . HIS A 140 ? 0.5619 0.4509 0.4249 0.0168  -0.0059 -0.0160 441 HIS A CG  
1087  N ND1 . HIS A 140 ? 0.5775 0.4496 0.4357 0.0100  -0.0096 -0.0223 441 HIS A ND1 
1088  C CD2 . HIS A 140 ? 0.5677 0.4521 0.4212 0.0266  -0.0035 -0.0182 441 HIS A CD2 
1089  C CE1 . HIS A 140 ? 0.6299 0.4847 0.4748 0.0161  -0.0097 -0.0280 441 HIS A CE1 
1090  N NE2 . HIS A 140 ? 0.5736 0.4366 0.4158 0.0271  -0.0060 -0.0258 441 HIS A NE2 
1091  N N   . GLY A 141 ? 0.6284 0.5601 0.5297 0.0073  -0.0014 0.0082  442 GLY A N   
1092  C CA  . GLY A 141 ? 0.6690 0.6115 0.5763 0.0088  0.0009  0.0156  442 GLY A CA  
1093  C C   . GLY A 141 ? 0.7160 0.6563 0.6320 0.0073  0.0046  0.0204  442 GLY A C   
1094  O O   . GLY A 141 ? 0.6183 0.5633 0.5360 0.0098  0.0083  0.0255  442 GLY A O   
1095  N N   . MET A 142 ? 0.7455 0.6787 0.6664 0.0026  0.0038  0.0188  443 MET A N   
1096  C CA  . MET A 142 ? 0.6219 0.5530 0.5499 0.0017  0.0072  0.0229  443 MET A CA  
1097  C C   . MET A 142 ? 0.6333 0.5607 0.5570 0.0074  0.0111  0.0235  443 MET A C   
1098  O O   . MET A 142 ? 0.5374 0.4711 0.4654 0.0092  0.0144  0.0279  443 MET A O   
1099  C CB  . MET A 142 ? 0.6533 0.5767 0.5850 -0.0046 0.0060  0.0210  443 MET A CB  
1100  C CG  . MET A 142 ? 0.5064 0.4393 0.4472 -0.0102 0.0037  0.0222  443 MET A CG  
1101  S SD  . MET A 142 ? 0.5747 0.5001 0.5172 -0.0201 0.0019  0.0182  443 MET A SD  
1102  C CE  . MET A 142 ? 0.3981 0.3190 0.3465 -0.0208 0.0065  0.0236  443 MET A CE  
1103  N N   . PHE A 143 ? 0.5319 0.4497 0.4464 0.0106  0.0105  0.0185  444 PHE A N   
1104  C CA  . PHE A 143 ? 0.4962 0.4132 0.4059 0.0180  0.0138  0.0182  444 PHE A CA  
1105  C C   . PHE A 143 ? 0.6428 0.5750 0.5535 0.0213  0.0167  0.0214  444 PHE A C   
1106  O O   . PHE A 143 ? 0.7748 0.7134 0.6882 0.0243  0.0203  0.0238  444 PHE A O   
1107  C CB  . PHE A 143 ? 0.5117 0.4161 0.4089 0.0226  0.0120  0.0114  444 PHE A CB  
1108  C CG  . PHE A 143 ? 0.6195 0.5268 0.5106 0.0324  0.0149  0.0100  444 PHE A CG  
1109  C CD1 . PHE A 143 ? 0.7842 0.7000 0.6684 0.0379  0.0153  0.0072  444 PHE A CD1 
1110  C CD2 . PHE A 143 ? 0.4577 0.3613 0.3497 0.0368  0.0172  0.0114  444 PHE A CD2 
1111  C CE1 . PHE A 143 ? 0.7884 0.7107 0.6676 0.0475  0.0182  0.0054  444 PHE A CE1 
1112  C CE2 . PHE A 143 ? 0.5881 0.4979 0.4750 0.0469  0.0196  0.0097  444 PHE A CE2 
1113  C CZ  . PHE A 143 ? 0.7246 0.6446 0.6056 0.0521  0.0202  0.0065  444 PHE A CZ  
1114  N N   . ASN A 144 ? 0.6293 0.5680 0.5375 0.0202  0.0153  0.0216  445 ASN A N   
1115  C CA  . ASN A 144 ? 0.5133 0.4647 0.4207 0.0219  0.0185  0.0256  445 ASN A CA  
1116  C C   . ASN A 144 ? 0.4962 0.4525 0.4128 0.0177  0.0209  0.0321  445 ASN A C   
1117  O O   . ASN A 144 ? 0.6526 0.6162 0.5714 0.0185  0.0250  0.0346  445 ASN A O   
1118  C CB  . ASN A 144 ? 0.5647 0.5197 0.4653 0.0219  0.0161  0.0250  445 ASN A CB  
1119  C CG  . ASN A 144 ? 0.6779 0.6443 0.5745 0.0235  0.0198  0.0292  445 ASN A CG  
1120  O OD1 . ASN A 144 ? 0.7571 0.7267 0.6541 0.0206  0.0200  0.0345  445 ASN A OD1 
1121  N ND2 . ASN A 144 ? 0.6790 0.6515 0.5707 0.0283  0.0230  0.0268  445 ASN A ND2 
1122  N N   . TYR A 145 ? 0.5591 0.5126 0.4810 0.0134  0.0183  0.0343  446 TYR A N   
1123  C CA  . TYR A 145 ? 0.6522 0.6075 0.5819 0.0101  0.0199  0.0395  446 TYR A CA  
1124  C C   . TYR A 145 ? 0.6020 0.5573 0.5375 0.0101  0.0228  0.0398  446 TYR A C   
1125  O O   . TYR A 145 ? 0.3786 0.3386 0.3181 0.0085  0.0257  0.0433  446 TYR A O   
1126  C CB  . TYR A 145 ? 0.6750 0.6275 0.6098 0.0072  0.0161  0.0399  446 TYR A CB  
1127  C CG  . TYR A 145 ? 0.5555 0.5108 0.4870 0.0075  0.0138  0.0426  446 TYR A CG  
1128  C CD1 . TYR A 145 ? 0.3964 0.3531 0.3244 0.0082  0.0093  0.0393  446 TYR A CD1 
1129  C CD2 . TYR A 145 ? 0.4425 0.3984 0.3735 0.0072  0.0158  0.0482  446 TYR A CD2 
1130  C CE1 . TYR A 145 ? 0.3767 0.3367 0.3008 0.0101  0.0068  0.0419  446 TYR A CE1 
1131  C CE2 . TYR A 145 ? 0.5261 0.4819 0.4518 0.0089  0.0136  0.0512  446 TYR A CE2 
1132  C CZ  . TYR A 145 ? 0.5590 0.5176 0.4813 0.0111  0.0090  0.0482  446 TYR A CZ  
1133  O OH  . TYR A 145 ? 0.6284 0.5876 0.5445 0.0143  0.0064  0.0513  446 TYR A OH  
1134  N N   . ILE A 146 ? 0.6265 0.5754 0.5615 0.0119  0.0219  0.0360  447 ILE A N   
1135  C CA  . ILE A 146 ? 0.6128 0.5613 0.5523 0.0130  0.0241  0.0365  447 ILE A CA  
1136  C C   . ILE A 146 ? 0.6506 0.6081 0.5876 0.0175  0.0276  0.0361  447 ILE A C   
1137  O O   . ILE A 146 ? 0.5351 0.4996 0.4776 0.0170  0.0302  0.0382  447 ILE A O   
1138  C CB  . ILE A 146 ? 0.5562 0.4926 0.4936 0.0137  0.0222  0.0334  447 ILE A CB  
1139  C CG1 . ILE A 146 ? 0.5486 0.4812 0.4916 0.0075  0.0198  0.0346  447 ILE A CG1 
1140  C CG2 . ILE A 146 ? 0.5062 0.4413 0.4438 0.0179  0.0244  0.0335  447 ILE A CG2 
1141  C CD1 . ILE A 146 ? 0.6031 0.5238 0.5443 0.0055  0.0186  0.0326  447 ILE A CD1 
1142  N N   . CYS A 147 ? 0.6682 0.6280 0.5973 0.0219  0.0278  0.0331  448 CYS A N   
1143  C CA  . CYS A 147 ? 0.6364 0.6091 0.5636 0.0264  0.0314  0.0323  448 CYS A CA  
1144  C C   . CYS A 147 ? 0.6433 0.6286 0.5753 0.0208  0.0347  0.0370  448 CYS A C   
1145  O O   . CYS A 147 ? 0.6079 0.6051 0.5440 0.0208  0.0379  0.0377  448 CYS A O   
1146  C CB  . CYS A 147 ? 0.5742 0.5479 0.4912 0.0323  0.0309  0.0279  448 CYS A CB  
1147  S SG  . CYS A 147 ? 0.6301 0.5888 0.5382 0.0410  0.0281  0.0212  448 CYS A SG  
1148  N N   . ASN A 148 ? 0.5297 0.5123 0.4601 0.0160  0.0338  0.0402  449 ASN A N   
1149  C CA  . ASN A 148 ? 0.5070 0.4967 0.4392 0.0101  0.0369  0.0452  449 ASN A CA  
1150  C C   . ASN A 148 ? 0.5430 0.5311 0.4839 0.0057  0.0375  0.0475  449 ASN A C   
1151  O O   . ASN A 148 ? 0.5412 0.5375 0.4849 0.0011  0.0408  0.0498  449 ASN A O   
1152  C CB  . ASN A 148 ? 0.5194 0.5035 0.4456 0.0076  0.0353  0.0484  449 ASN A CB  
1153  C CG  . ASN A 148 ? 0.6448 0.6325 0.5613 0.0119  0.0349  0.0459  449 ASN A CG  
1154  O OD1 . ASN A 148 ? 0.5776 0.5748 0.4914 0.0159  0.0374  0.0427  449 ASN A OD1 
1155  N ND2 . ASN A 148 ? 0.5907 0.5721 0.5016 0.0119  0.0317  0.0470  449 ASN A ND2 
1156  N N   . HIS A 149 ? 0.5468 0.5254 0.4920 0.0065  0.0343  0.0465  450 HIS A N   
1157  C CA  . HIS A 149 ? 0.5039 0.4818 0.4568 0.0038  0.0347  0.0478  450 HIS A CA  
1158  C C   . HIS A 149 ? 0.5503 0.5388 0.5065 0.0061  0.0373  0.0457  450 HIS A C   
1159  O O   . HIS A 149 ? 0.5410 0.5380 0.5014 0.0021  0.0398  0.0470  450 HIS A O   
1160  C CB  . HIS A 149 ? 0.4565 0.4241 0.4123 0.0046  0.0312  0.0469  450 HIS A CB  
1161  C CG  . HIS A 149 ? 0.5308 0.4978 0.4938 0.0025  0.0315  0.0481  450 HIS A CG  
1162  N ND1 . HIS A 149 ? 0.4924 0.4531 0.4589 0.0009  0.0291  0.0490  450 HIS A ND1 
1163  C CD2 . HIS A 149 ? 0.5739 0.5477 0.5414 0.0020  0.0337  0.0480  450 HIS A CD2 
1164  C CE1 . HIS A 149 ? 0.5847 0.5471 0.5566 -0.0002 0.0300  0.0495  450 HIS A CE1 
1165  N NE2 . HIS A 149 ? 0.4749 0.4449 0.4475 0.0002  0.0326  0.0489  450 HIS A NE2 
1166  N N   . VAL A 150 ? 0.4077 0.3955 0.3612 0.0130  0.0365  0.0421  451 VAL A N   
1167  C CA  . VAL A 150 ? 0.4092 0.4078 0.3642 0.0180  0.0384  0.0397  451 VAL A CA  
1168  C C   . VAL A 150 ? 0.5084 0.5255 0.4646 0.0157  0.0422  0.0398  451 VAL A C   
1169  O O   . VAL A 150 ? 0.6591 0.6888 0.6213 0.0139  0.0441  0.0397  451 VAL A O   
1170  C CB  . VAL A 150 ? 0.3777 0.3699 0.3255 0.0272  0.0367  0.0357  451 VAL A CB  
1171  C CG1 . VAL A 150 ? 0.3262 0.3318 0.2740 0.0347  0.0385  0.0330  451 VAL A CG1 
1172  C CG2 . VAL A 150 ? 0.3591 0.3341 0.3063 0.0274  0.0337  0.0359  451 VAL A CG2 
1173  N N   . LYS A 151 ? 0.6302 0.6507 0.5808 0.0153  0.0434  0.0400  452 LYS A N   
1174  C CA  . LYS A 151 ? 0.5678 0.6076 0.5185 0.0126  0.0476  0.0403  452 LYS A CA  
1175  C C   . LYS A 151 ? 0.4636 0.5069 0.4195 0.0015  0.0499  0.0443  452 LYS A C   
1176  O O   . LYS A 151 ? 0.5028 0.5635 0.4633 -0.0023 0.0532  0.0437  452 LYS A O   
1177  C CB  . LYS A 151 ? 0.5138 0.5549 0.4559 0.0140  0.0485  0.0403  452 LYS A CB  
1178  C CG  . LYS A 151 ? 0.5107 0.5742 0.4518 0.0117  0.0536  0.0403  452 LYS A CG  
1179  C CD  . LYS A 151 ? 0.4659 0.5319 0.3972 0.0180  0.0538  0.0382  452 LYS A CD  
1180  C CE  . LYS A 151 ? 0.5136 0.6047 0.4433 0.0170  0.0592  0.0377  452 LYS A CE  
1181  N NZ  . LYS A 151 ? 0.6201 0.7160 0.5410 0.0278  0.0588  0.0328  452 LYS A NZ  
1182  N N   . TYR A 152 ? 0.4885 0.5153 0.4433 -0.0038 0.0480  0.0481  453 TYR A N   
1183  C CA  . TYR A 152 ? 0.5584 0.5833 0.5157 -0.0137 0.0497  0.0518  453 TYR A CA  
1184  C C   . TYR A 152 ? 0.5764 0.6048 0.5421 -0.0151 0.0493  0.0499  453 TYR A C   
1185  O O   . TYR A 152 ? 0.5496 0.5891 0.5190 -0.0222 0.0521  0.0499  453 TYR A O   
1186  C CB  . TYR A 152 ? 0.6170 0.6224 0.5694 -0.0161 0.0471  0.0557  453 TYR A CB  
1187  C CG  . TYR A 152 ? 0.6455 0.6431 0.5989 -0.0244 0.0479  0.0590  453 TYR A CG  
1188  C CD1 . TYR A 152 ? 0.6317 0.6290 0.5792 -0.0328 0.0512  0.0630  453 TYR A CD1 
1189  C CD2 . TYR A 152 ? 0.5074 0.4966 0.4662 -0.0240 0.0453  0.0582  453 TYR A CD2 
1190  C CE1 . TYR A 152 ? 0.7102 0.6965 0.6563 -0.0405 0.0517  0.0657  453 TYR A CE1 
1191  C CE2 . TYR A 152 ? 0.5846 0.5648 0.5428 -0.0308 0.0457  0.0604  453 TYR A CE2 
1192  C CZ  . TYR A 152 ? 0.6349 0.6125 0.5864 -0.0391 0.0487  0.0641  453 TYR A CZ  
1193  O OH  . TYR A 152 ? 0.7506 0.7155 0.6993 -0.0463 0.0491  0.0662  453 TYR A OH  
1194  N N   . ALA A 153 ? 0.5561 0.5757 0.5246 -0.0092 0.0459  0.0483  454 ALA A N   
1195  C CA  . ALA A 153 ? 0.5366 0.5589 0.5121 -0.0094 0.0452  0.0466  454 ALA A CA  
1196  C C   . ALA A 153 ? 0.5147 0.5578 0.4942 -0.0070 0.0473  0.0431  454 ALA A C   
1197  O O   . ALA A 153 ? 0.4885 0.5410 0.4735 -0.0121 0.0484  0.0421  454 ALA A O   
1198  C CB  . ALA A 153 ? 0.3488 0.3589 0.3248 -0.0030 0.0417  0.0459  454 ALA A CB  
1199  N N   . THR A 154 ? 0.5436 0.5951 0.5202 0.0012  0.0477  0.0407  455 THR A N   
1200  C CA  . THR A 154 ? 0.5010 0.5745 0.4809 0.0059  0.0493  0.0368  455 THR A CA  
1201  C C   . THR A 154 ? 0.6857 0.7795 0.6692 -0.0035 0.0534  0.0368  455 THR A C   
1202  O O   . THR A 154 ? 0.8560 0.9683 0.8460 -0.0054 0.0545  0.0341  455 THR A O   
1203  C CB  . THR A 154 ? 0.3922 0.4681 0.3661 0.0180  0.0487  0.0340  455 THR A CB  
1204  O OG1 . THR A 154 ? 0.3984 0.4538 0.3682 0.0248  0.0451  0.0341  455 THR A OG1 
1205  C CG2 . THR A 154 ? 0.3716 0.4717 0.3485 0.0251  0.0499  0.0297  455 THR A CG2 
1206  N N   . ASN A 155 ? 0.5741 0.6653 0.5529 -0.0100 0.0557  0.0397  456 ASN A N   
1207  C CA  . ASN A 155 ? 0.3639 0.4706 0.3441 -0.0216 0.0603  0.0410  456 ASN A CA  
1208  C C   . ASN A 155 ? 0.5027 0.6412 0.4895 -0.0203 0.0628  0.0363  456 ASN A C   
1209  O O   . ASN A 155 ? 0.4821 0.6345 0.4744 -0.0313 0.0654  0.0357  456 ASN A O   
1210  C CB  . ASN A 155 ? 0.3403 0.4333 0.3219 -0.0340 0.0602  0.0442  456 ASN A CB  
1211  C CG  . ASN A 155 ? 0.4392 0.5428 0.4201 -0.0482 0.0650  0.0462  456 ASN A CG  
1212  O OD1 . ASN A 155 ? 0.5903 0.7061 0.5674 -0.0502 0.0686  0.0473  456 ASN A OD1 
1213  N ND2 . ASN A 155 ? 0.4318 0.5302 0.4155 -0.0588 0.0651  0.0466  456 ASN A ND2 
1214  N N   . LYS A 156 ? 0.5740 0.7242 0.5598 -0.0067 0.0620  0.0324  457 LYS A N   
1215  C CA  . LYS A 156 ? 0.5174 0.7008 0.5084 -0.0021 0.0642  0.0273  457 LYS A CA  
1216  C C   . LYS A 156 ? 0.5523 0.7476 0.5521 -0.0025 0.0626  0.0241  457 LYS A C   
1217  O O   . LYS A 156 ? 0.4278 0.6539 0.4344 -0.0054 0.0650  0.0205  457 LYS A O   
1218  C CB  . LYS A 156 ? 0.5930 0.7996 0.5851 -0.0130 0.0699  0.0279  457 LYS A CB  
1219  C CG  . LYS A 156 ? 0.6064 0.8122 0.5899 -0.0090 0.0720  0.0293  457 LYS A CG  
1220  C CD  . LYS A 156 ? 0.7529 0.9816 0.7375 -0.0223 0.0783  0.0309  457 LYS A CD  
1221  C CE  . LYS A 156 ? 0.8030 1.0273 0.7774 -0.0208 0.0807  0.0337  457 LYS A CE  
1222  N NZ  . LYS A 156 ? 0.8091 1.0683 0.7843 -0.0137 0.0844  0.0289  457 LYS A NZ  
1223  N N   . GLY A 157 ? 0.5829 0.7564 0.5824 0.0007  0.0586  0.0252  458 GLY A N   
1224  C CA  . GLY A 157 ? 0.6122 0.7948 0.6184 0.0018  0.0566  0.0224  458 GLY A CA  
1225  C C   . GLY A 157 ? 0.6329 0.8046 0.6430 -0.0124 0.0564  0.0244  458 GLY A C   
1226  O O   . GLY A 157 ? 0.5799 0.7483 0.5932 -0.0103 0.0536  0.0230  458 GLY A O   
1227  N N   . ASN A 158 ? 0.5416 0.7065 0.5502 -0.0262 0.0593  0.0277  459 ASN A N   
1228  C CA  . ASN A 158 ? 0.5477 0.6987 0.5577 -0.0392 0.0590  0.0295  459 ASN A CA  
1229  C C   . ASN A 158 ? 0.6056 0.7228 0.6093 -0.0368 0.0562  0.0339  459 ASN A C   
1230  O O   . ASN A 158 ? 0.7042 0.8048 0.7021 -0.0437 0.0573  0.0382  459 ASN A O   
1231  C CB  . ASN A 158 ? 0.4427 0.6017 0.4523 -0.0555 0.0635  0.0310  459 ASN A CB  
1232  C CG  . ASN A 158 ? 0.6052 0.7455 0.6136 -0.0688 0.0631  0.0326  459 ASN A CG  
1233  O OD1 . ASN A 158 ? 0.7685 0.9006 0.7798 -0.0665 0.0597  0.0305  459 ASN A OD1 
1234  N ND2 . ASN A 158 ? 0.6044 0.7364 0.6072 -0.0823 0.0665  0.0365  459 ASN A ND2 
1235  N N   . LEU A 159 ? 0.5679 0.6759 0.5724 -0.0269 0.0524  0.0329  460 LEU A N   
1236  C CA  . LEU A 159 ? 0.5570 0.6385 0.5563 -0.0220 0.0498  0.0364  460 LEU A CA  
1237  C C   . LEU A 159 ? 0.5656 0.6269 0.5625 -0.0312 0.0493  0.0396  460 LEU A C   
1238  O O   . LEU A 159 ? 0.4684 0.5305 0.4681 -0.0391 0.0495  0.0383  460 LEU A O   
1239  C CB  . LEU A 159 ? 0.4700 0.5467 0.4706 -0.0118 0.0465  0.0350  460 LEU A CB  
1240  C CG  . LEU A 159 ? 0.6177 0.7094 0.6188 -0.0001 0.0459  0.0319  460 LEU A CG  
1241  C CD1 . LEU A 159 ? 0.6972 0.7722 0.6951 0.0088  0.0429  0.0331  460 LEU A CD1 
1242  C CD2 . LEU A 159 ? 0.4418 0.5426 0.4392 0.0049  0.0476  0.0312  460 LEU A CD2 
1243  N N   . ARG A 160 ? 0.5707 0.6134 0.5616 -0.0292 0.0483  0.0433  461 ARG A N   
1244  C CA  . ARG A 160 ? 0.5638 0.5856 0.5510 -0.0340 0.0469  0.0465  461 ARG A CA  
1245  C C   . ARG A 160 ? 0.5790 0.5869 0.5656 -0.0258 0.0434  0.0472  461 ARG A C   
1246  O O   . ARG A 160 ? 0.5784 0.5878 0.5645 -0.0182 0.0424  0.0468  461 ARG A O   
1247  C CB  . ARG A 160 ? 0.5271 0.5411 0.5067 -0.0395 0.0489  0.0506  461 ARG A CB  
1248  C CG  . ARG A 160 ? 0.5221 0.5508 0.5016 -0.0492 0.0531  0.0503  461 ARG A CG  
1249  C CD  . ARG A 160 ? 0.7020 0.7229 0.6724 -0.0544 0.0555  0.0552  461 ARG A CD  
1250  N NE  . ARG A 160 ? 0.7105 0.7424 0.6792 -0.0476 0.0565  0.0552  461 ARG A NE  
1251  C CZ  . ARG A 160 ? 0.5909 0.6254 0.5526 -0.0517 0.0597  0.0584  461 ARG A CZ  
1252  N NH1 . ARG A 160 ? 0.5522 0.5774 0.5077 -0.0631 0.0622  0.0626  461 ARG A NH1 
1253  N NH2 . ARG A 160 ? 0.6544 0.6991 0.6141 -0.0445 0.0603  0.0574  461 ARG A NH2 
1254  N N   . SER A 161 ? 0.6046 0.5993 0.5909 -0.0276 0.0415  0.0480  462 SER A N   
1255  C CA  . SER A 161 ? 0.6246 0.6095 0.6112 -0.0209 0.0386  0.0485  462 SER A CA  
1256  C C   . SER A 161 ? 0.4945 0.4672 0.4751 -0.0200 0.0375  0.0518  462 SER A C   
1257  O O   . SER A 161 ? 0.4125 0.3787 0.3877 -0.0250 0.0385  0.0543  462 SER A O   
1258  C CB  . SER A 161 ? 0.6866 0.6662 0.6761 -0.0211 0.0370  0.0471  462 SER A CB  
1259  O OG  . SER A 161 ? 0.8943 0.8649 0.8804 -0.0276 0.0372  0.0476  462 SER A OG  
1260  N N   . ALA A 162 ? 0.3702 0.3398 0.3512 -0.0141 0.0353  0.0519  463 ALA A N   
1261  C CA  . ALA A 162 ? 0.4983 0.4610 0.4740 -0.0124 0.0339  0.0541  463 ALA A CA  
1262  C C   . ALA A 162 ? 0.5577 0.5178 0.5357 -0.0076 0.0312  0.0531  463 ALA A C   
1263  O O   . ALA A 162 ? 0.5633 0.5275 0.5450 -0.0053 0.0313  0.0513  463 ALA A O   
1264  C CB  . ALA A 162 ? 0.4171 0.3863 0.3890 -0.0125 0.0359  0.0543  463 ALA A CB  
1265  N N   . ILE A 163 ? 0.5948 0.5486 0.5698 -0.0063 0.0289  0.0545  464 ILE A N   
1266  C CA  . ILE A 163 ? 0.5125 0.4657 0.4894 -0.0034 0.0262  0.0534  464 ILE A CA  
1267  C C   . ILE A 163 ? 0.5564 0.5075 0.5277 -0.0023 0.0244  0.0541  464 ILE A C   
1268  O O   . ILE A 163 ? 0.5365 0.4838 0.5022 -0.0027 0.0243  0.0566  464 ILE A O   
1269  C CB  . ILE A 163 ? 0.3462 0.2980 0.3272 -0.0022 0.0244  0.0534  464 ILE A CB  
1270  C CG1 . ILE A 163 ? 0.3137 0.2689 0.2983 -0.0009 0.0224  0.0519  464 ILE A CG1 
1271  C CG2 . ILE A 163 ? 0.3478 0.2927 0.3240 -0.0012 0.0230  0.0554  464 ILE A CG2 
1272  C CD1 . ILE A 163 ? 0.3366 0.2944 0.3257 0.0008  0.0209  0.0514  464 ILE A CD1 
1273  N N   . THR A 164 ? 0.5013 0.4541 0.4730 -0.0012 0.0229  0.0520  465 THR A N   
1274  C CA  . THR A 164 ? 0.5532 0.5054 0.5201 -0.0001 0.0203  0.0515  465 THR A CA  
1275  C C   . THR A 164 ? 0.5313 0.4858 0.5024 0.0000  0.0171  0.0496  465 THR A C   
1276  O O   . THR A 164 ? 0.4499 0.4049 0.4245 -0.0018 0.0172  0.0475  465 THR A O   
1277  C CB  . THR A 164 ? 0.6054 0.5579 0.5677 0.0005  0.0213  0.0494  465 THR A CB  
1278  O OG1 . THR A 164 ? 0.7078 0.6621 0.6660 0.0003  0.0242  0.0513  465 THR A OG1 
1279  C CG2 . THR A 164 ? 0.4708 0.4230 0.4286 0.0013  0.0180  0.0474  465 THR A CG2 
1280  N N   . ILE A 165 ? 0.5920 0.5481 0.5617 0.0020  0.0142  0.0503  466 ILE A N   
1281  C CA  . ILE A 165 ? 0.5447 0.5075 0.5197 0.0023  0.0110  0.0484  466 ILE A CA  
1282  C C   . ILE A 165 ? 0.6578 0.6245 0.6294 0.0023  0.0076  0.0459  466 ILE A C   
1283  O O   . ILE A 165 ? 0.5918 0.5583 0.5572 0.0058  0.0056  0.0471  466 ILE A O   
1284  C CB  . ILE A 165 ? 0.5532 0.5171 0.5292 0.0065  0.0097  0.0503  466 ILE A CB  
1285  C CG1 . ILE A 165 ? 0.5330 0.4914 0.5106 0.0061  0.0128  0.0522  466 ILE A CG1 
1286  C CG2 . ILE A 165 ? 0.5866 0.5616 0.5693 0.0075  0.0068  0.0479  466 ILE A CG2 
1287  C CD1 . ILE A 165 ? 0.5203 0.4774 0.4976 0.0109  0.0112  0.0532  466 ILE A CD1 
1288  N N   . PHE A 166 ? 0.5830 0.5529 0.5581 -0.0020 0.0067  0.0423  467 PHE A N   
1289  C CA  . PHE A 166 ? 0.3934 0.3673 0.3659 -0.0038 0.0033  0.0385  467 PHE A CA  
1290  C C   . PHE A 166 ? 0.4812 0.4687 0.4599 -0.0038 -0.0005 0.0366  467 PHE A C   
1291  O O   . PHE A 166 ? 0.6207 0.6133 0.6049 -0.0015 0.0000  0.0384  467 PHE A O   
1292  C CB  . PHE A 166 ? 0.3287 0.2961 0.3003 -0.0093 0.0044  0.0353  467 PHE A CB  
1293  C CG  . PHE A 166 ? 0.4345 0.3916 0.3988 -0.0072 0.0071  0.0359  467 PHE A CG  
1294  C CD1 . PHE A 166 ? 0.4784 0.4345 0.4349 -0.0040 0.0061  0.0351  467 PHE A CD1 
1295  C CD2 . PHE A 166 ? 0.5954 0.5456 0.5605 -0.0077 0.0107  0.0371  467 PHE A CD2 
1296  C CE1 . PHE A 166 ? 0.6148 0.5646 0.5650 -0.0015 0.0088  0.0352  467 PHE A CE1 
1297  C CE2 . PHE A 166 ? 0.6498 0.5936 0.6086 -0.0045 0.0130  0.0371  467 PHE A CE2 
1298  C CZ  . PHE A 166 ? 0.6138 0.5582 0.5655 -0.0015 0.0122  0.0360  467 PHE A CZ  
1299  N N   . PRO A 167 ? 0.6459 0.6412 0.6236 -0.0054 -0.0045 0.0326  468 PRO A N   
1300  C CA  . PRO A 167 ? 0.5957 0.6078 0.5790 -0.0033 -0.0084 0.0309  468 PRO A CA  
1301  C C   . PRO A 167 ? 0.4633 0.4847 0.4572 -0.0081 -0.0071 0.0299  468 PRO A C   
1302  O O   . PRO A 167 ? 0.3978 0.4154 0.3941 -0.0165 -0.0049 0.0282  468 PRO A O   
1303  C CB  . PRO A 167 ? 0.5151 0.5344 0.4955 -0.0062 -0.0128 0.0257  468 PRO A CB  
1304  C CG  . PRO A 167 ? 0.4585 0.4634 0.4290 -0.0060 -0.0115 0.0259  468 PRO A CG  
1305  C CD  . PRO A 167 ? 0.5847 0.5758 0.5557 -0.0084 -0.0062 0.0287  468 PRO A CD  
1306  N N   . GLN A 168 ? 0.4765 0.5099 0.4754 -0.0023 -0.0085 0.0309  469 GLN A N   
1307  C CA  . GLN A 168 ? 0.4463 0.4923 0.4554 -0.0057 -0.0071 0.0298  469 GLN A CA  
1308  C C   . GLN A 168 ? 0.5020 0.5617 0.5173 -0.0160 -0.0085 0.0249  469 GLN A C   
1309  O O   . GLN A 168 ? 0.5424 0.6021 0.5541 -0.0200 -0.0112 0.0215  469 GLN A O   
1310  C CB  . GLN A 168 ? 0.4681 0.5273 0.4804 0.0041  -0.0094 0.0303  469 GLN A CB  
1311  C CG  . GLN A 168 ? 0.5404 0.6187 0.5542 0.0078  -0.0151 0.0266  469 GLN A CG  
1312  C CD  . GLN A 168 ? 0.5723 0.6514 0.5807 0.0220  -0.0181 0.0288  469 GLN A CD  
1313  O OE1 . GLN A 168 ? 0.6522 0.7113 0.6511 0.0273  -0.0168 0.0334  469 GLN A OE1 
1314  N NE2 . GLN A 168 ? 0.5144 0.6164 0.5280 0.0282  -0.0223 0.0256  469 GLN A NE2 
1315  N N   . ARG A 169 ? 0.6579 0.7299 0.6821 -0.0209 -0.0065 0.0241  470 ARG A N   
1316  C CA  . ARG A 169 ? 0.6446 0.7308 0.6749 -0.0326 -0.0073 0.0196  470 ARG A CA  
1317  C C   . ARG A 169 ? 0.5455 0.6574 0.5809 -0.0291 -0.0128 0.0151  470 ARG A C   
1318  O O   . ARG A 169 ? 0.5851 0.7043 0.6200 -0.0165 -0.0154 0.0162  470 ARG A O   
1319  C CB  . ARG A 169 ? 0.6514 0.7441 0.6891 -0.0393 -0.0027 0.0210  470 ARG A CB  
1320  C CG  . ARG A 169 ? 0.7649 0.8663 0.8068 -0.0547 -0.0020 0.0175  470 ARG A CG  
1321  C CD  . ARG A 169 ? 0.7499 0.8561 0.7972 -0.0608 0.0032  0.0201  470 ARG A CD  
1322  N NE  . ARG A 169 ? 0.7698 0.8485 0.8088 -0.0636 0.0076  0.0246  470 ARG A NE  
1323  C CZ  . ARG A 169 ? 0.9523 1.0279 0.9919 -0.0724 0.0123  0.0270  470 ARG A CZ  
1324  N NH1 . ARG A 169 ? 1.1425 1.2419 1.1912 -0.0803 0.0135  0.0254  470 ARG A NH1 
1325  N NH2 . ARG A 169 ? 0.9260 0.9761 0.9567 -0.0731 0.0157  0.0311  470 ARG A NH2 
1326  N N   . THR A 170 ? 0.5765 0.7011 0.6157 -0.0403 -0.0149 0.0097  471 THR A N   
1327  C CA  . THR A 170 ? 0.6090 0.7633 0.6548 -0.0380 -0.0204 0.0044  471 THR A CA  
1328  C C   . THR A 170 ? 0.6284 0.8080 0.6862 -0.0506 -0.0193 0.0004  471 THR A C   
1329  O O   . THR A 170 ? 0.6812 0.8806 0.7477 -0.0465 -0.0179 0.0011  471 THR A O   
1330  C CB  . THR A 170 ? 0.5888 0.7412 0.6278 -0.0390 -0.0256 0.0001  471 THR A CB  
1331  O OG1 . THR A 170 ? 0.6068 0.7479 0.6434 -0.0547 -0.0243 -0.0032 471 THR A OG1 
1332  C CG2 . THR A 170 ? 0.4994 0.6293 0.5261 -0.0271 -0.0263 0.0043  471 THR A CG2 
1333  N N   . ASP A 171 ? 0.6007 0.7797 0.6585 -0.0663 -0.0197 -0.0040 472 ASP A N   
1334  C CA  . ASP A 171 ? 0.5606 0.7619 0.6287 -0.0819 -0.0181 -0.0078 472 ASP A CA  
1335  C C   . ASP A 171 ? 0.7023 0.8805 0.7667 -0.0960 -0.0116 -0.0044 472 ASP A C   
1336  O O   . ASP A 171 ? 0.8015 0.9895 0.8704 -0.1131 -0.0100 -0.0074 472 ASP A O   
1337  C CB  . ASP A 171 ? 0.6994 0.9181 0.7698 -0.0916 -0.0236 -0.0160 472 ASP A CB  
1338  C CG  . ASP A 171 ? 0.8432 1.0313 0.9009 -0.0990 -0.0245 -0.0177 472 ASP A CG  
1339  O OD1 . ASP A 171 ? 0.8748 1.0324 0.9219 -0.0909 -0.0226 -0.0127 472 ASP A OD1 
1340  O OD2 . ASP A 171 ? 0.8432 1.0384 0.9014 -0.1128 -0.0274 -0.0246 472 ASP A OD2 
1341  N N   . GLY A 172 ? 0.6349 0.7827 0.6903 -0.0895 -0.0080 0.0019  473 GLY A N   
1342  C CA  . GLY A 172 ? 0.6032 0.7253 0.6520 -0.1002 -0.0025 0.0056  473 GLY A CA  
1343  C C   . GLY A 172 ? 0.7355 0.8359 0.7745 -0.1123 -0.0036 0.0022  473 GLY A C   
1344  O O   . GLY A 172 ? 0.7748 0.8483 0.8050 -0.1191 0.0006  0.0055  473 GLY A O   
1345  N N   . LYS A 173 ? 0.7245 0.8345 0.7634 -0.1144 -0.0093 -0.0045 474 LYS A N   
1346  C CA  . LYS A 173 ? 0.6030 0.6928 0.6317 -0.1256 -0.0111 -0.0091 474 LYS A CA  
1347  C C   . LYS A 173 ? 0.6634 0.7299 0.6800 -0.1138 -0.0137 -0.0092 474 LYS A C   
1348  O O   . LYS A 173 ? 0.6740 0.7210 0.6803 -0.1206 -0.0154 -0.0134 474 LYS A O   
1349  C CB  . LYS A 173 ? 0.4313 0.5481 0.4673 -0.1376 -0.0158 -0.0177 474 LYS A CB  
1350  C CG  . LYS A 173 ? 0.5736 0.7050 0.6177 -0.1563 -0.0122 -0.0186 474 LYS A CG  
1351  C CD  . LYS A 173 ? 0.6938 0.8695 0.7525 -0.1628 -0.0163 -0.0258 474 LYS A CD  
1352  C CE  . LYS A 173 ? 0.7685 0.9607 0.8354 -0.1835 -0.0119 -0.0265 474 LYS A CE  
1353  N NZ  . LYS A 173 ? 0.6965 0.9349 0.7780 -0.1913 -0.0162 -0.0348 474 LYS A NZ  
1354  N N   . HIS A 174 ? 0.7105 0.7777 0.7272 -0.0969 -0.0138 -0.0048 475 HIS A N   
1355  C CA  . HIS A 174 ? 0.6894 0.7382 0.6951 -0.0860 -0.0157 -0.0044 475 HIS A CA  
1356  C C   . HIS A 174 ? 0.6894 0.7240 0.6923 -0.0741 -0.0116 0.0033  475 HIS A C   
1357  O O   . HIS A 174 ? 0.6427 0.6789 0.6438 -0.0614 -0.0129 0.0056  475 HIS A O   
1358  C CB  . HIS A 174 ? 0.6294 0.6985 0.6370 -0.0780 -0.0219 -0.0084 475 HIS A CB  
1359  C CG  . HIS A 174 ? 0.7498 0.8368 0.7610 -0.0895 -0.0266 -0.0168 475 HIS A CG  
1360  N ND1 . HIS A 174 ? 0.8043 0.9223 0.8288 -0.0958 -0.0279 -0.0195 475 HIS A ND1 
1361  C CD2 . HIS A 174 ? 0.8192 0.8985 0.8227 -0.0965 -0.0303 -0.0237 475 HIS A CD2 
1362  C CE1 . HIS A 174 ? 0.8484 0.9784 0.8738 -0.1070 -0.0323 -0.0278 475 HIS A CE1 
1363  N NE2 . HIS A 174 ? 0.8765 0.9822 0.8889 -0.1077 -0.0340 -0.0306 475 HIS A NE2 
1364  N N   . ASP A 175 ? 0.7385 0.7592 0.7406 -0.0788 -0.0064 0.0074  476 ASP A N   
1365  C CA  . ASP A 175 ? 0.6692 0.6780 0.6692 -0.0688 -0.0025 0.0140  476 ASP A CA  
1366  C C   . ASP A 175 ? 0.6536 0.6394 0.6414 -0.0620 -0.0024 0.0145  476 ASP A C   
1367  O O   . ASP A 175 ? 0.5542 0.5231 0.5329 -0.0675 -0.0030 0.0113  476 ASP A O   
1368  C CB  . ASP A 175 ? 0.7216 0.7224 0.7226 -0.0755 0.0027  0.0179  476 ASP A CB  
1369  C CG  . ASP A 175 ? 0.7454 0.7709 0.7589 -0.0796 0.0039  0.0186  476 ASP A CG  
1370  O OD1 . ASP A 175 ? 0.7487 0.7933 0.7697 -0.0706 0.0023  0.0191  476 ASP A OD1 
1371  O OD2 . ASP A 175 ? 0.7525 0.7779 0.7671 -0.0919 0.0066  0.0187  476 ASP A OD2 
1372  N N   . PHE A 176 ? 0.5584 0.5439 0.5457 -0.0502 -0.0017 0.0183  477 PHE A N   
1373  C CA  . PHE A 176 ? 0.5006 0.4666 0.4783 -0.0438 0.0004  0.0204  477 PHE A CA  
1374  C C   . PHE A 176 ? 0.6855 0.6404 0.6630 -0.0442 0.0052  0.0249  477 PHE A C   
1375  O O   . PHE A 176 ? 0.6480 0.6127 0.6334 -0.0431 0.0072  0.0283  477 PHE A O   
1376  C CB  . PHE A 176 ? 0.5371 0.5084 0.5142 -0.0330 -0.0004 0.0229  477 PHE A CB  
1377  C CG  . PHE A 176 ? 0.6853 0.6636 0.6587 -0.0306 -0.0049 0.0192  477 PHE A CG  
1378  C CD1 . PHE A 176 ? 0.7314 0.7283 0.7110 -0.0326 -0.0089 0.0164  477 PHE A CD1 
1379  C CD2 . PHE A 176 ? 0.7173 0.6858 0.6809 -0.0256 -0.0052 0.0184  477 PHE A CD2 
1380  C CE1 . PHE A 176 ? 0.6833 0.6874 0.6587 -0.0295 -0.0134 0.0131  477 PHE A CE1 
1381  C CE2 . PHE A 176 ? 0.6250 0.6003 0.5841 -0.0229 -0.0093 0.0153  477 PHE A CE2 
1382  C CZ  . PHE A 176 ? 0.6106 0.6032 0.5754 -0.0248 -0.0136 0.0127  477 PHE A CZ  
1383  N N   . ARG A 177 ? 0.6548 0.5895 0.6226 -0.0447 0.0068  0.0246  478 ARG A N   
1384  C CA  . ARG A 177 ? 0.4686 0.3925 0.4345 -0.0437 0.0110  0.0289  478 ARG A CA  
1385  C C   . ARG A 177 ? 0.6155 0.5230 0.5711 -0.0359 0.0121  0.0292  478 ARG A C   
1386  O O   . ARG A 177 ? 0.6370 0.5325 0.5832 -0.0360 0.0103  0.0252  478 ARG A O   
1387  C CB  . ARG A 177 ? 0.5586 0.4736 0.5221 -0.0546 0.0123  0.0287  478 ARG A CB  
1388  C CG  . ARG A 177 ? 0.6714 0.6060 0.6464 -0.0627 0.0124  0.0290  478 ARG A CG  
1389  C CD  . ARG A 177 ? 0.6317 0.5796 0.6155 -0.0566 0.0150  0.0337  478 ARG A CD  
1390  N NE  . ARG A 177 ? 0.6218 0.5566 0.6008 -0.0548 0.0190  0.0382  478 ARG A NE  
1391  C CZ  . ARG A 177 ? 0.6635 0.5995 0.6442 -0.0615 0.0221  0.0411  478 ARG A CZ  
1392  N NH1 . ARG A 177 ? 0.6251 0.5760 0.6130 -0.0713 0.0220  0.0396  478 ARG A NH1 
1393  N NH2 . ARG A 177 ? 0.5228 0.4468 0.4978 -0.0581 0.0254  0.0453  478 ARG A NH2 
1394  N N   . VAL A 178 ? 0.6103 0.5187 0.5674 -0.0289 0.0150  0.0333  479 VAL A N   
1395  C CA  . VAL A 178 ? 0.5848 0.4788 0.5325 -0.0221 0.0167  0.0338  479 VAL A CA  
1396  C C   . VAL A 178 ? 0.6208 0.5004 0.5632 -0.0257 0.0188  0.0359  479 VAL A C   
1397  O O   . VAL A 178 ? 0.7810 0.6664 0.7291 -0.0266 0.0211  0.0399  479 VAL A O   
1398  C CB  . VAL A 178 ? 0.5703 0.4733 0.5218 -0.0137 0.0187  0.0367  479 VAL A CB  
1399  C CG1 . VAL A 178 ? 0.5842 0.4765 0.5260 -0.0058 0.0199  0.0359  479 VAL A CG1 
1400  C CG2 . VAL A 178 ? 0.4897 0.4069 0.4468 -0.0119 0.0173  0.0363  479 VAL A CG2 
1401  N N   . TRP A 179 ? 0.5596 0.4193 0.4899 -0.0277 0.0179  0.0333  480 TRP A N   
1402  C CA  . TRP A 179 ? 0.6738 0.5160 0.5964 -0.0320 0.0199  0.0360  480 TRP A CA  
1403  C C   . TRP A 179 ? 0.7057 0.5425 0.6239 -0.0220 0.0226  0.0401  480 TRP A C   
1404  O O   . TRP A 179 ? 0.7443 0.5750 0.6604 -0.0247 0.0250  0.0443  480 TRP A O   
1405  C CB  . TRP A 179 ? 0.6543 0.4724 0.5626 -0.0366 0.0181  0.0320  480 TRP A CB  
1406  C CG  . TRP A 179 ? 0.5997 0.4224 0.5123 -0.0501 0.0160  0.0286  480 TRP A CG  
1407  C CD1 . TRP A 179 ? 0.5462 0.3933 0.4722 -0.0539 0.0142  0.0267  480 TRP A CD1 
1408  C CD2 . TRP A 179 ? 0.5437 0.3468 0.4466 -0.0622 0.0155  0.0265  480 TRP A CD2 
1409  N NE1 . TRP A 179 ? 0.5883 0.4355 0.5150 -0.0672 0.0123  0.0231  480 TRP A NE1 
1410  C CE2 . TRP A 179 ? 0.5691 0.3893 0.4819 -0.0736 0.0132  0.0228  480 TRP A CE2 
1411  C CE3 . TRP A 179 ? 0.5722 0.3440 0.4580 -0.0645 0.0167  0.0275  480 TRP A CE3 
1412  C CZ2 . TRP A 179 ? 0.6283 0.4377 0.5360 -0.0888 0.0123  0.0196  480 TRP A CZ2 
1413  C CZ3 . TRP A 179 ? 0.5297 0.2866 0.4087 -0.0798 0.0159  0.0248  480 TRP A CZ3 
1414  C CH2 . TRP A 179 ? 0.6415 0.4183 0.5321 -0.0926 0.0138  0.0207  480 TRP A CH2 
1415  N N   . ASN A 180 ? 0.7419 0.5820 0.6582 -0.0107 0.0223  0.0388  481 ASN A N   
1416  C CA  . ASN A 180 ? 0.6399 0.4819 0.5548 -0.0011 0.0245  0.0420  481 ASN A CA  
1417  C C   . ASN A 180 ? 0.7091 0.5689 0.6367 -0.0037 0.0264  0.0460  481 ASN A C   
1418  O O   . ASN A 180 ? 0.6251 0.5014 0.5642 -0.0078 0.0258  0.0455  481 ASN A O   
1419  C CB  . ASN A 180 ? 0.5530 0.4039 0.4677 0.0095  0.0240  0.0395  481 ASN A CB  
1420  C CG  . ASN A 180 ? 0.5898 0.4276 0.4933 0.0131  0.0219  0.0345  481 ASN A CG  
1421  O OD1 . ASN A 180 ? 0.7131 0.5519 0.6179 0.0073  0.0199  0.0312  481 ASN A OD1 
1422  N ND2 . ASN A 180 ? 0.4953 0.3216 0.3870 0.0238  0.0221  0.0334  481 ASN A ND2 
1423  N N   . SER A 181 ? 0.5598 0.4155 0.4841 -0.0002 0.0285  0.0499  482 SER A N   
1424  C CA  . SER A 181 ? 0.4644 0.3367 0.3993 -0.0011 0.0303  0.0531  482 SER A CA  
1425  C C   . SER A 181 ? 0.5770 0.4667 0.5196 0.0059  0.0302  0.0517  482 SER A C   
1426  O O   . SER A 181 ? 0.6582 0.5634 0.6118 0.0030  0.0304  0.0519  482 SER A O   
1427  C CB  . SER A 181 ? 0.5320 0.3953 0.4597 0.0010  0.0325  0.0575  482 SER A CB  
1428  O OG  . SER A 181 ? 0.6013 0.4510 0.5162 0.0113  0.0323  0.0576  482 SER A OG  
1429  N N   . GLN A 182 ? 0.6212 0.5083 0.5574 0.0150  0.0299  0.0501  483 GLN A N   
1430  C CA  . GLN A 182 ? 0.6844 0.5881 0.6271 0.0197  0.0299  0.0481  483 GLN A CA  
1431  C C   . GLN A 182 ? 0.6073 0.5071 0.5443 0.0231  0.0286  0.0445  483 GLN A C   
1432  O O   . GLN A 182 ? 0.7227 0.6053 0.6487 0.0250  0.0276  0.0430  483 GLN A O   
1433  C CB  . GLN A 182 ? 0.7387 0.6505 0.6808 0.0280  0.0311  0.0489  483 GLN A CB  
1434  C CG  . GLN A 182 ? 0.7698 0.6889 0.7178 0.0258  0.0323  0.0519  483 GLN A CG  
1435  C CD  . GLN A 182 ? 0.7255 0.6500 0.6698 0.0351  0.0328  0.0523  483 GLN A CD  
1436  O OE1 . GLN A 182 ? 0.5131 0.4512 0.4602 0.0404  0.0328  0.0496  483 GLN A OE1 
1437  N NE2 . GLN A 182 ? 0.6535 0.5683 0.5908 0.0372  0.0334  0.0556  483 GLN A NE2 
1438  N N   . LEU A 183 ? 0.5064 0.4212 0.4497 0.0238  0.0288  0.0429  484 LEU A N   
1439  C CA  . LEU A 183 ? 0.6444 0.5579 0.5821 0.0272  0.0280  0.0394  484 LEU A CA  
1440  C C   . LEU A 183 ? 0.6843 0.5951 0.6129 0.0383  0.0283  0.0373  484 LEU A C   
1441  O O   . LEU A 183 ? 0.5789 0.4763 0.4967 0.0427  0.0270  0.0344  484 LEU A O   
1442  C CB  . LEU A 183 ? 0.4131 0.3431 0.3586 0.0245  0.0286  0.0391  484 LEU A CB  
1443  C CG  . LEU A 183 ? 0.4142 0.3474 0.3674 0.0159  0.0278  0.0410  484 LEU A CG  
1444  C CD1 . LEU A 183 ? 0.3352 0.2812 0.2928 0.0144  0.0287  0.0415  484 LEU A CD1 
1445  C CD2 . LEU A 183 ? 0.3717 0.2941 0.3212 0.0118  0.0254  0.0395  484 LEU A CD2 
1446  N N   . ILE A 184 ? 0.6862 0.6093 0.6181 0.0437  0.0298  0.0383  485 ILE A N   
1447  C CA  . ILE A 184 ? 0.6716 0.5949 0.5950 0.0559  0.0299  0.0363  485 ILE A CA  
1448  C C   . ILE A 184 ? 0.6445 0.5572 0.5629 0.0595  0.0297  0.0392  485 ILE A C   
1449  O O   . ILE A 184 ? 0.7082 0.6310 0.6347 0.0561  0.0306  0.0418  485 ILE A O   
1450  C CB  . ILE A 184 ? 0.5515 0.5007 0.4820 0.0600  0.0315  0.0344  485 ILE A CB  
1451  C CG1 . ILE A 184 ? 0.6932 0.6516 0.6282 0.0542  0.0322  0.0329  485 ILE A CG1 
1452  C CG2 . ILE A 184 ? 0.5152 0.4674 0.4368 0.0742  0.0312  0.0314  485 ILE A CG2 
1453  C CD1 . ILE A 184 ? 0.8198 0.8030 0.7648 0.0512  0.0345  0.0329  485 ILE A CD1 
1454  N N   . ARG A 185 ? 0.5254 0.4161 0.4291 0.0662  0.0285  0.0388  486 ARG A N   
1455  C CA  . ARG A 185 ? 0.6727 0.5480 0.5668 0.0711  0.0283  0.0421  486 ARG A CA  
1456  C C   . ARG A 185 ? 0.7439 0.6006 0.6201 0.0842  0.0268  0.0396  486 ARG A C   
1457  O O   . ARG A 185 ? 0.6263 0.4743 0.4965 0.0854  0.0257  0.0357  486 ARG A O   
1458  C CB  . ARG A 185 ? 0.7632 0.6194 0.6552 0.0598  0.0285  0.0461  486 ARG A CB  
1459  C CG  . ARG A 185 ? 0.9391 0.8099 0.8457 0.0491  0.0299  0.0492  486 ARG A CG  
1460  C CD  . ARG A 185 ? 1.0701 0.9537 0.9800 0.0544  0.0310  0.0517  486 ARG A CD  
1461  N NE  . ARG A 185 ? 1.0835 0.9488 0.9803 0.0589  0.0313  0.0557  486 ARG A NE  
1462  C CZ  . ARG A 185 ? 1.0587 0.9127 0.9537 0.0503  0.0325  0.0601  486 ARG A CZ  
1463  N NH1 . ARG A 185 ? 0.9935 0.8541 0.8998 0.0377  0.0332  0.0603  486 ARG A NH1 
1464  N NH2 . ARG A 185 ? 1.0682 0.9046 0.9493 0.0548  0.0331  0.0643  486 ARG A NH2 
1465  N N   . TYR A 186 ? 0.6704 0.5204 0.5368 0.0949  0.0265  0.0418  487 TYR A N   
1466  C CA  . TYR A 186 ? 0.5828 0.4118 0.4295 0.1095  0.0248  0.0399  487 TYR A CA  
1467  C C   . TYR A 186 ? 0.6530 0.4434 0.4833 0.1045  0.0242  0.0432  487 TYR A C   
1468  O O   . TYR A 186 ? 0.7236 0.5072 0.5579 0.0916  0.0255  0.0479  487 TYR A O   
1469  C CB  . TYR A 186 ? 0.6183 0.4595 0.4609 0.1253  0.0244  0.0405  487 TYR A CB  
1470  C CG  . TYR A 186 ? 0.5965 0.4763 0.4540 0.1300  0.0250  0.0364  487 TYR A CG  
1471  C CD1 . TYR A 186 ? 0.6579 0.5638 0.5300 0.1259  0.0262  0.0382  487 TYR A CD1 
1472  C CD2 . TYR A 186 ? 0.6597 0.5503 0.5162 0.1379  0.0245  0.0305  487 TYR A CD2 
1473  C CE1 . TYR A 186 ? 0.6792 0.6201 0.5646 0.1280  0.0269  0.0342  487 TYR A CE1 
1474  C CE2 . TYR A 186 ? 0.7102 0.6382 0.5805 0.1404  0.0257  0.0269  487 TYR A CE2 
1475  C CZ  . TYR A 186 ? 0.6815 0.6341 0.5664 0.1347  0.0269  0.0289  487 TYR A CZ  
1476  O OH  . TYR A 186 ? 0.5841 0.5732 0.4825 0.1349  0.0283  0.0254  487 TYR A OH  
1477  N N   . ALA A 187 ? 0.6958 0.4612 0.5072 0.1144  0.0223  0.0403  488 ALA A N   
1478  C CA  . ALA A 187 ? 0.7627 0.4879 0.5557 0.1095  0.0216  0.0428  488 ALA A CA  
1479  C C   . ALA A 187 ? 1.0093 0.7162 0.7865 0.1192  0.0218  0.0485  488 ALA A C   
1480  O O   . ALA A 187 ? 1.0484 0.7725 0.8262 0.1336  0.0215  0.0490  488 ALA A O   
1481  C CB  . ALA A 187 ? 0.8013 0.5039 0.5786 0.1160  0.0192  0.0364  488 ALA A CB  
1482  N N   . GLY A 188 ? 1.1215 0.7936 0.8839 0.1106  0.0222  0.0530  489 GLY A N   
1483  C CA  . GLY A 188 ? 1.0916 0.7384 0.8342 0.1187  0.0225  0.0594  489 GLY A CA  
1484  C C   . GLY A 188 ? 1.2209 0.8191 0.9381 0.1156  0.0216  0.0601  489 GLY A C   
1485  O O   . GLY A 188 ? 1.3641 0.9497 1.0836 0.0968  0.0224  0.0598  489 GLY A O   
1486  N N   . TYR A 189 ? 1.1673 0.7376 0.8593 0.1339  0.0196  0.0605  490 TYR A N   
1487  C CA  . TYR A 189 ? 1.0856 0.6047 0.7495 0.1329  0.0183  0.0606  490 TYR A CA  
1488  C C   . TYR A 189 ? 1.1118 0.6006 0.7527 0.1397  0.0192  0.0697  490 TYR A C   
1489  O O   . TYR A 189 ? 1.0790 0.5746 0.7121 0.1609  0.0179  0.0713  490 TYR A O   
1490  C CB  . TYR A 189 ? 1.0112 0.5181 0.6611 0.1510  0.0145  0.0519  490 TYR A CB  
1491  C CG  . TYR A 189 ? 1.0835 0.6294 0.7559 0.1520  0.0136  0.0433  490 TYR A CG  
1492  C CD1 . TYR A 189 ? 1.0614 0.6497 0.7496 0.1659  0.0136  0.0412  490 TYR A CD1 
1493  C CD2 . TYR A 189 ? 1.1189 0.6592 0.7954 0.1390  0.0128  0.0370  490 TYR A CD2 
1494  C CE1 . TYR A 189 ? 1.0502 0.6727 0.7571 0.1661  0.0133  0.0341  490 TYR A CE1 
1495  C CE2 . TYR A 189 ? 1.0250 0.6002 0.7201 0.1404  0.0122  0.0298  490 TYR A CE2 
1496  C CZ  . TYR A 189 ? 0.9818 0.5969 0.6916 0.1538  0.0127  0.0288  490 TYR A CZ  
1497  O OH  . TYR A 189 ? 0.9737 0.6225 0.7005 0.1543  0.0127  0.0225  490 TYR A OH  
1498  N N   . LYS A 190 ? 1.0458 0.5031 0.6756 0.1215  0.0215  0.0757  491 LYS A N   
1499  C CA  . LYS A 190 ? 1.1178 0.5549 0.7303 0.1231  0.0223  0.0820  491 LYS A CA  
1500  C C   . LYS A 190 ? 1.1131 0.5189 0.7008 0.1362  0.0187  0.0769  491 LYS A C   
1501  O O   . LYS A 190 ? 1.1539 0.5380 0.7343 0.1289  0.0171  0.0709  491 LYS A O   
1502  C CB  . LYS A 190 ? 1.2716 0.6949 0.8852 0.0967  0.0261  0.0884  491 LYS A CB  
1503  C CG  . LYS A 190 ? 1.3670 0.7838 0.9708 0.0968  0.0286  0.0978  491 LYS A CG  
1504  C CD  . LYS A 190 ? 1.3180 0.7694 0.9409 0.0941  0.0319  0.1042  491 LYS A CD  
1505  C CE  . LYS A 190 ? 1.3363 0.7796 0.9500 0.0886  0.0350  0.1137  491 LYS A CE  
1506  N NZ  . LYS A 190 ? 1.3236 0.7486 0.9353 0.0623  0.0385  0.1174  491 LYS A NZ  
1507  N N   . GLN A 191 ? 1.1144 0.5184 0.6884 0.1560  0.0174  0.0791  492 GLN A N   
1508  C CA  . GLN A 191 ? 1.1592 0.5331 0.7070 0.1705  0.0141  0.0752  492 GLN A CA  
1509  C C   . GLN A 191 ? 1.1776 0.5122 0.7057 0.1563  0.0158  0.0812  492 GLN A C   
1510  O O   . GLN A 191 ? 1.2636 0.6005 0.7978 0.1407  0.0196  0.0895  492 GLN A O   
1511  C CB  . GLN A 191 ? 1.1580 0.5496 0.6998 0.1981  0.0119  0.0747  492 GLN A CB  
1512  C CG  . GLN A 191 ? 1.1381 0.5707 0.6984 0.2137  0.0101  0.0681  492 GLN A CG  
1513  C CD  . GLN A 191 ? 1.2198 0.6472 0.7803 0.2152  0.0077  0.0584  492 GLN A CD  
1514  O OE1 . GLN A 191 ? 1.1467 0.5910 0.7264 0.2045  0.0088  0.0558  492 GLN A OE1 
1515  N NE2 . GLN A 191 ? 1.3233 0.7270 0.8614 0.2288  0.0045  0.0530  492 GLN A NE2 
1516  N N   . PRO A 192 ? 1.1192 0.4176 0.6231 0.1610  0.0133  0.0773  493 PRO A N   
1517  C CA  . PRO A 192 ? 1.2056 0.4653 0.6897 0.1469  0.0151  0.0833  493 PRO A CA  
1518  C C   . PRO A 192 ? 1.2997 0.5589 0.7751 0.1535  0.0171  0.0927  493 PRO A C   
1519  O O   . PRO A 192 ? 1.3147 0.5557 0.7840 0.1363  0.0205  0.1004  493 PRO A O   
1520  C CB  . PRO A 192 ? 1.2228 0.4463 0.6806 0.1575  0.0111  0.0764  493 PRO A CB  
1521  C CG  . PRO A 192 ? 1.0887 0.3330 0.5565 0.1710  0.0077  0.0663  493 PRO A CG  
1522  C CD  . PRO A 192 ? 1.1295 0.4206 0.6215 0.1801  0.0087  0.0676  493 PRO A CD  
1523  N N   . ASP A 193 ? 1.3556 0.6365 0.8307 0.1781  0.0152  0.0922  494 ASP A N   
1524  C CA  . ASP A 193 ? 1.3185 0.5982 0.7818 0.1890  0.0162  0.0999  494 ASP A CA  
1525  C C   . ASP A 193 ? 1.2189 0.5290 0.7032 0.1784  0.0201  0.1076  494 ASP A C   
1526  O O   . ASP A 193 ? 1.4305 0.7456 0.9079 0.1878  0.0210  0.1139  494 ASP A O   
1527  C CB  . ASP A 193 ? 1.3338 0.6266 0.7878 0.2204  0.0122  0.0949  494 ASP A CB  
1528  C CG  . ASP A 193 ? 1.3017 0.6458 0.7822 0.2308  0.0116  0.0916  494 ASP A CG  
1529  O OD1 . ASP A 193 ? 1.3273 0.6917 0.8048 0.2527  0.0097  0.0910  494 ASP A OD1 
1530  O OD2 . ASP A 193 ? 1.2647 0.6292 0.7686 0.2169  0.0130  0.0897  494 ASP A OD2 
1531  N N   . GLY A 194 ? 1.1087 0.4388 0.6174 0.1595  0.0224  0.1072  495 GLY A N   
1532  C CA  . GLY A 194 ? 1.1413 0.5012 0.6703 0.1490  0.0261  0.1137  495 GLY A CA  
1533  C C   . GLY A 194 ? 1.0903 0.4944 0.6423 0.1606  0.0249  0.1100  495 GLY A C   
1534  O O   . GLY A 194 ? 1.0277 0.4570 0.6011 0.1474  0.0277  0.1128  495 GLY A O   
1535  N N   . SER A 195 ? 1.1483 0.5634 0.6963 0.1847  0.0209  0.1036  496 SER A N   
1536  C CA  . SER A 195 ? 1.1707 0.6296 0.7400 0.1968  0.0196  0.0997  496 SER A CA  
1537  C C   . SER A 195 ? 1.1823 0.6548 0.7721 0.1842  0.0202  0.0948  496 SER A C   
1538  O O   . SER A 195 ? 1.2949 0.7431 0.8810 0.1689  0.0207  0.0927  496 SER A O   
1539  C CB  . SER A 195 ? 1.2040 0.6726 0.7637 0.2249  0.0153  0.0932  496 SER A CB  
1540  O OG  . SER A 195 ? 1.3503 0.7970 0.8983 0.2293  0.0127  0.0857  496 SER A OG  
1541  N N   . THR A 196 ? 1.1145 0.6268 0.7258 0.1904  0.0200  0.0929  497 THR A N   
1542  C CA  . THR A 196 ? 1.0885 0.6172 0.7203 0.1789  0.0209  0.0894  497 THR A CA  
1543  C C   . THR A 196 ? 1.1821 0.7452 0.8268 0.1971  0.0180  0.0816  497 THR A C   
1544  O O   . THR A 196 ? 1.2355 0.8295 0.8876 0.2111  0.0171  0.0818  497 THR A O   
1545  C CB  . THR A 196 ? 1.0719 0.6220 0.7237 0.1598  0.0249  0.0954  497 THR A CB  
1546  O OG1 . THR A 196 ? 1.1990 0.7184 0.8378 0.1435  0.0280  0.1031  497 THR A OG1 
1547  C CG2 . THR A 196 ? 1.0105 0.5891 0.6908 0.1430  0.0257  0.0884  497 THR A CG2 
1548  N N   . LEU A 197 ? 1.1094 0.6734 0.7599 0.1945  0.0167  0.0733  498 LEU A N   
1549  C CA  . LEU A 197 ? 0.9222 0.5219 0.5864 0.2086  0.0145  0.0642  498 LEU A CA  
1550  C C   . LEU A 197 ? 0.8436 0.4803 0.5395 0.1899  0.0164  0.0600  498 LEU A C   
1551  O O   . LEU A 197 ? 0.9562 0.5792 0.6565 0.1706  0.0178  0.0599  498 LEU A O   
1552  C CB  . LEU A 197 ? 0.9134 0.4855 0.5568 0.2233  0.0113  0.0576  498 LEU A CB  
1553  C CG  . LEU A 197 ? 0.9768 0.5880 0.6355 0.2355  0.0097  0.0479  498 LEU A CG  
1554  C CD1 . LEU A 197 ? 0.7897 0.4404 0.4574 0.2529  0.0089  0.0479  498 LEU A CD1 
1555  C CD2 . LEU A 197 ? 1.0463 0.6296 0.6834 0.2505  0.0066  0.0406  498 LEU A CD2 
1556  N N   . GLY A 198 ? 0.8117 0.4950 0.5289 0.1955  0.0165  0.0566  499 GLY A N   
1557  C CA  . GLY A 198 ? 0.8817 0.5995 0.6280 0.1777  0.0186  0.0545  499 GLY A CA  
1558  C C   . GLY A 198 ? 0.9429 0.6688 0.7006 0.1623  0.0213  0.0614  499 GLY A C   
1559  O O   . GLY A 198 ? 1.1588 0.8796 0.9077 0.1686  0.0216  0.0672  499 GLY A O   
1560  N N   . ASP A 199 ? 0.9219 0.6608 0.6988 0.1427  0.0233  0.0606  500 ASP A N   
1561  C CA  . ASP A 199 ? 0.8681 0.6236 0.6606 0.1286  0.0258  0.0653  500 ASP A CA  
1562  C C   . ASP A 199 ? 0.8562 0.5799 0.6384 0.1144  0.0277  0.0715  500 ASP A C   
1563  O O   . ASP A 199 ? 0.8671 0.5791 0.6517 0.1008  0.0281  0.0697  500 ASP A O   
1564  C CB  . ASP A 199 ? 0.8785 0.6656 0.6963 0.1166  0.0267  0.0608  500 ASP A CB  
1565  C CG  . ASP A 199 ? 0.8999 0.7080 0.7343 0.1052  0.0288  0.0641  500 ASP A CG  
1566  O OD1 . ASP A 199 ? 0.8265 0.6200 0.6593 0.0928  0.0306  0.0689  500 ASP A OD1 
1567  O OD2 . ASP A 199 ? 0.9137 0.7536 0.7628 0.1083  0.0286  0.0614  500 ASP A OD2 
1568  N N   . PRO A 200 ? 0.9210 0.6316 0.6915 0.1162  0.0290  0.0787  501 PRO A N   
1569  C CA  . PRO A 200 ? 0.8918 0.5698 0.6495 0.1023  0.0313  0.0851  501 PRO A CA  
1570  C C   . PRO A 200 ? 0.8951 0.5867 0.6720 0.0802  0.0338  0.0853  501 PRO A C   
1571  O O   . PRO A 200 ? 0.8469 0.5148 0.6156 0.0662  0.0358  0.0891  501 PRO A O   
1572  C CB  . PRO A 200 ? 0.7881 0.4583 0.5321 0.1104  0.0324  0.0930  501 PRO A CB  
1573  C CG  . PRO A 200 ? 0.7747 0.4603 0.5155 0.1333  0.0293  0.0897  501 PRO A CG  
1574  C CD  . PRO A 200 ? 0.7418 0.4645 0.5071 0.1324  0.0282  0.0814  501 PRO A CD  
1575  N N   . ALA A 201 ? 0.9129 0.6416 0.7143 0.0765  0.0339  0.0813  502 ALA A N   
1576  C CA  . ALA A 201 ? 0.8364 0.5786 0.6553 0.0578  0.0359  0.0813  502 ALA A CA  
1577  C C   . ALA A 201 ? 0.9237 0.6517 0.7421 0.0474  0.0350  0.0773  502 ALA A C   
1578  O O   . ALA A 201 ? 1.0255 0.7457 0.8458 0.0315  0.0367  0.0792  502 ALA A O   
1579  C CB  . ALA A 201 ? 0.7452 0.5264 0.5875 0.0578  0.0357  0.0776  502 ALA A CB  
1580  N N   . ASN A 202 ? 0.9315 0.6574 0.7471 0.0566  0.0323  0.0714  503 ASN A N   
1581  C CA  . ASN A 202 ? 0.8391 0.5594 0.6575 0.0486  0.0308  0.0659  503 ASN A CA  
1582  C C   . ASN A 202 ? 0.8879 0.5679 0.6833 0.0482  0.0297  0.0655  503 ASN A C   
1583  O O   . ASN A 202 ? 1.0115 0.6839 0.8051 0.0459  0.0276  0.0596  503 ASN A O   
1584  C CB  . ASN A 202 ? 0.8719 0.6154 0.7007 0.0584  0.0288  0.0594  503 ASN A CB  
1585  C CG  . ASN A 202 ? 0.8799 0.6599 0.7293 0.0585  0.0299  0.0597  503 ASN A CG  
1586  O OD1 . ASN A 202 ? 0.9189 0.7120 0.7819 0.0462  0.0314  0.0614  503 ASN A OD1 
1587  N ND2 . ASN A 202 ? 0.8083 0.6053 0.6597 0.0724  0.0291  0.0574  503 ASN A ND2 
1588  N N   . VAL A 203 ? 0.8758 0.5284 0.6523 0.0498  0.0310  0.0717  504 VAL A N   
1589  C CA  . VAL A 203 ? 0.8456 0.4549 0.5964 0.0510  0.0297  0.0716  504 VAL A CA  
1590  C C   . VAL A 203 ? 1.0062 0.6013 0.7577 0.0301  0.0301  0.0698  504 VAL A C   
1591  O O   . VAL A 203 ? 1.1036 0.6737 0.8419 0.0298  0.0278  0.0647  504 VAL A O   
1592  C CB  . VAL A 203 ? 0.8779 0.4603 0.6070 0.0574  0.0313  0.0799  504 VAL A CB  
1593  C CG1 . VAL A 203 ? 0.9632 0.4954 0.6637 0.0556  0.0304  0.0805  504 VAL A CG1 
1594  C CG2 . VAL A 203 ? 0.9779 0.5737 0.7041 0.0805  0.0298  0.0801  504 VAL A CG2 
1595  N N   . GLN A 204 ? 0.9710 0.5824 0.7374 0.0128  0.0330  0.0732  505 GLN A N   
1596  C CA  . GLN A 204 ? 1.0203 0.6232 0.7890 -0.0071 0.0331  0.0705  505 GLN A CA  
1597  C C   . GLN A 204 ? 1.0680 0.6911 0.8517 -0.0079 0.0299  0.0616  505 GLN A C   
1598  O O   . GLN A 204 ? 1.0889 0.6955 0.8663 -0.0169 0.0280  0.0565  505 GLN A O   
1599  C CB  . GLN A 204 ? 1.0077 0.6272 0.7894 -0.0246 0.0369  0.0758  505 GLN A CB  
1600  C CG  . GLN A 204 ? 1.1494 0.7468 0.9230 -0.0456 0.0380  0.0759  505 GLN A CG  
1601  C CD  . GLN A 204 ? 1.2155 0.8449 1.0125 -0.0630 0.0389  0.0733  505 GLN A CD  
1602  O OE1 . GLN A 204 ? 1.0518 0.7096 0.8646 -0.0661 0.0416  0.0770  505 GLN A OE1 
1603  N NE2 . GLN A 204 ? 1.3207 0.9461 1.1194 -0.0735 0.0362  0.0663  505 GLN A NE2 
1604  N N   . PHE A 205 ? 0.9527 0.6105 0.7549 0.0009  0.0294  0.0596  506 PHE A N   
1605  C CA  . PHE A 205 ? 0.8315 0.5077 0.6460 0.0013  0.0267  0.0521  506 PHE A CA  
1606  C C   . PHE A 205 ? 0.9574 0.6145 0.7562 0.0148  0.0237  0.0464  506 PHE A C   
1607  O O   . PHE A 205 ? 1.0262 0.6816 0.8254 0.0112  0.0212  0.0398  506 PHE A O   
1608  C CB  . PHE A 205 ? 0.6505 0.3653 0.4864 0.0067  0.0273  0.0522  506 PHE A CB  
1609  C CG  . PHE A 205 ? 0.7774 0.5117 0.6259 0.0051  0.0251  0.0460  506 PHE A CG  
1610  C CD1 . PHE A 205 ? 0.8272 0.5766 0.6896 -0.0090 0.0249  0.0448  506 PHE A CD1 
1611  C CD2 . PHE A 205 ? 0.7833 0.5225 0.6295 0.0184  0.0233  0.0413  506 PHE A CD2 
1612  C CE1 . PHE A 205 ? 0.8444 0.6112 0.7169 -0.0096 0.0227  0.0396  506 PHE A CE1 
1613  C CE2 . PHE A 205 ? 0.8113 0.5684 0.6680 0.0166  0.0216  0.0363  506 PHE A CE2 
1614  C CZ  . PHE A 205 ? 0.8243 0.5939 0.6935 0.0029  0.0212  0.0357  506 PHE A CZ  
1615  N N   . THR A 206 ? 0.9242 0.5685 0.7090 0.0314  0.0236  0.0485  507 THR A N   
1616  C CA  . THR A 206 ? 0.8133 0.4368 0.5804 0.0458  0.0208  0.0430  507 THR A CA  
1617  C C   . THR A 206 ? 1.0224 0.6063 0.7700 0.0365  0.0192  0.0402  507 THR A C   
1618  O O   . THR A 206 ? 1.1050 0.6797 0.8458 0.0397  0.0163  0.0326  507 THR A O   
1619  C CB  . THR A 206 ? 0.6789 0.2949 0.4328 0.0655  0.0210  0.0463  507 THR A CB  
1620  O OG1 . THR A 206 ? 0.6902 0.3451 0.4635 0.0717  0.0223  0.0480  507 THR A OG1 
1621  C CG2 . THR A 206 ? 0.7016 0.3007 0.4382 0.0831  0.0179  0.0399  507 THR A CG2 
1622  N N   . GLU A 207 ? 1.0915 0.6524 0.8299 0.0237  0.0212  0.0461  508 GLU A N   
1623  C CA  . GLU A 207 ? 1.1011 0.6241 0.8213 0.0114  0.0200  0.0435  508 GLU A CA  
1624  C C   . GLU A 207 ? 0.9659 0.5049 0.7006 -0.0035 0.0181  0.0363  508 GLU A C   
1625  O O   . GLU A 207 ? 0.9606 0.4785 0.6830 -0.0044 0.0149  0.0290  508 GLU A O   
1626  C CB  . GLU A 207 ? 1.1488 0.6490 0.8589 -0.0026 0.0233  0.0520  508 GLU A CB  
1627  C CG  . GLU A 207 ? 1.2538 0.7187 0.9374 0.0114  0.0240  0.0579  508 GLU A CG  
1628  C CD  . GLU A 207 ? 1.4362 0.9006 1.1193 0.0036  0.0285  0.0688  508 GLU A CD  
1629  O OE1 . GLU A 207 ? 1.4103 0.9009 1.1135 -0.0137 0.0313  0.0712  508 GLU A OE1 
1630  O OE2 . GLU A 207 ? 1.4711 0.9096 1.1330 0.0158  0.0292  0.0749  508 GLU A OE2 
1631  N N   . ILE A 208 ? 0.8772 0.4535 0.6374 -0.0142 0.0197  0.0379  509 ILE A N   
1632  C CA  . ILE A 208 ? 0.9002 0.4936 0.6740 -0.0277 0.0177  0.0316  509 ILE A CA  
1633  C C   . ILE A 208 ? 0.9203 0.5213 0.6942 -0.0150 0.0142  0.0234  509 ILE A C   
1634  O O   . ILE A 208 ? 1.0512 0.6381 0.8172 -0.0203 0.0110  0.0160  509 ILE A O   
1635  C CB  . ILE A 208 ? 0.9023 0.5358 0.7026 -0.0373 0.0198  0.0349  509 ILE A CB  
1636  C CG1 . ILE A 208 ? 0.9868 0.6155 0.7871 -0.0495 0.0238  0.0428  509 ILE A CG1 
1637  C CG2 . ILE A 208 ? 0.6992 0.3493 0.5116 -0.0498 0.0173  0.0283  509 ILE A CG2 
1638  C CD1 . ILE A 208 ? 0.9546 0.6227 0.7798 -0.0567 0.0259  0.0458  509 ILE A CD1 
1639  N N   . CYS A 209 ? 0.8472 0.4712 0.6297 0.0013  0.0147  0.0244  510 CYS A N   
1640  C CA  . CYS A 209 ? 0.8368 0.4702 0.6186 0.0148  0.0122  0.0174  510 CYS A CA  
1641  C C   . CYS A 209 ? 0.8961 0.4926 0.6530 0.0214  0.0093  0.0112  510 CYS A C   
1642  O O   . CYS A 209 ? 0.9646 0.5587 0.7189 0.0186  0.0063  0.0034  510 CYS A O   
1643  C CB  . CYS A 209 ? 0.7956 0.4509 0.5841 0.0321  0.0138  0.0203  510 CYS A CB  
1644  S SG  . CYS A 209 ? 0.8349 0.5369 0.6528 0.0271  0.0161  0.0242  510 CYS A SG  
1645  N N   . ILE A 210 ? 0.8977 0.4641 0.6347 0.0311  0.0098  0.0143  511 ILE A N   
1646  C CA  . ILE A 210 ? 0.9207 0.4479 0.6311 0.0395  0.0069  0.0083  511 ILE A CA  
1647  C C   . ILE A 210 ? 0.9910 0.4947 0.6937 0.0205  0.0047  0.0033  511 ILE A C   
1648  O O   . ILE A 210 ? 1.1591 0.6478 0.8500 0.0237  0.0012  -0.0056 511 ILE A O   
1649  C CB  . ILE A 210 ? 0.9157 0.4111 0.6045 0.0512  0.0079  0.0141  511 ILE A CB  
1650  C CG1 . ILE A 210 ? 0.8222 0.3450 0.5193 0.0711  0.0094  0.0174  511 ILE A CG1 
1651  C CG2 . ILE A 210 ? 0.8625 0.3121 0.5211 0.0597  0.0046  0.0079  511 ILE A CG2 
1652  C CD1 . ILE A 210 ? 0.9039 0.4014 0.5823 0.0829  0.0104  0.0242  511 ILE A CD1 
1653  N N   . GLN A 211 ? 0.9145 0.4173 0.6244 0.0000  0.0068  0.0084  512 GLN A N   
1654  C CA  . GLN A 211 ? 1.0631 0.5449 0.7660 -0.0202 0.0049  0.0037  512 GLN A CA  
1655  C C   . GLN A 211 ? 1.1616 0.6709 0.8800 -0.0264 0.0019  -0.0048 512 GLN A C   
1656  O O   . GLN A 211 ? 1.1951 0.6859 0.9037 -0.0366 -0.0013 -0.0126 512 GLN A O   
1657  C CB  . GLN A 211 ? 1.0547 0.5359 0.7640 -0.0410 0.0084  0.0113  512 GLN A CB  
1658  C CG  . GLN A 211 ? 1.1800 0.6251 0.8726 -0.0607 0.0074  0.0084  512 GLN A CG  
1659  C CD  . GLN A 211 ? 1.3127 0.7826 1.0251 -0.0852 0.0091  0.0097  512 GLN A CD  
1660  O OE1 . GLN A 211 ? 1.3156 0.8159 1.0469 -0.0883 0.0126  0.0169  512 GLN A OE1 
1661  N NE2 . GLN A 211 ? 1.4126 0.8716 1.1208 -0.1025 0.0063  0.0020  512 GLN A NE2 
1662  N N   . GLN A 212 ? 1.0257 0.5781 0.7671 -0.0205 0.0028  -0.0035 513 GLN A N   
1663  C CA  . GLN A 212 ? 0.9721 0.5515 0.7266 -0.0227 0.0000  -0.0105 513 GLN A CA  
1664  C C   . GLN A 212 ? 1.0141 0.5901 0.7581 -0.0041 -0.0026 -0.0177 513 GLN A C   
1665  O O   . GLN A 212 ? 0.9469 0.5444 0.6995 -0.0040 -0.0049 -0.0235 513 GLN A O   
1666  C CB  . GLN A 212 ? 1.0287 0.6531 0.8104 -0.0243 0.0021  -0.0055 513 GLN A CB  
1667  C CG  . GLN A 212 ? 1.0852 0.7191 0.8794 -0.0403 0.0050  0.0015  513 GLN A CG  
1668  C CD  . GLN A 212 ? 1.1544 0.7801 0.9477 -0.0611 0.0031  -0.0026 513 GLN A CD  
1669  O OE1 . GLN A 212 ? 1.2893 0.9195 1.0828 -0.0649 -0.0008 -0.0108 513 GLN A OE1 
1670  N NE2 . GLN A 212 ? 1.1731 0.7883 0.9653 -0.0751 0.0058  0.0028  513 GLN A NE2 
1671  N N   . GLY A 213 ? 1.0071 0.5587 0.7327 0.0125  -0.0022 -0.0172 514 GLY A N   
1672  C CA  . GLY A 213 ? 1.0650 0.6102 0.7775 0.0299  -0.0049 -0.0253 514 GLY A CA  
1673  C C   . GLY A 213 ? 1.0284 0.5863 0.7403 0.0526  -0.0030 -0.0228 514 GLY A C   
1674  O O   . GLY A 213 ? 1.1140 0.6562 0.8084 0.0695  -0.0048 -0.0287 514 GLY A O   
1675  N N   . TRP A 214 ? 0.9429 0.5300 0.6734 0.0533  0.0005  -0.0146 515 TRP A N   
1676  C CA  . TRP A 214 ? 0.8776 0.4836 0.6112 0.0726  0.0025  -0.0121 515 TRP A CA  
1677  C C   . TRP A 214 ? 1.0106 0.5842 0.7189 0.0906  0.0014  -0.0139 515 TRP A C   
1678  O O   . TRP A 214 ? 0.9760 0.5150 0.6688 0.0872  0.0013  -0.0104 515 TRP A O   
1679  C CB  . TRP A 214 ? 0.9444 0.5736 0.6963 0.0676  0.0062  -0.0025 515 TRP A CB  
1680  C CG  . TRP A 214 ? 1.0359 0.6934 0.7965 0.0835  0.0082  -0.0002 515 TRP A CG  
1681  C CD1 . TRP A 214 ? 0.9739 0.6628 0.7452 0.0910  0.0087  -0.0037 515 TRP A CD1 
1682  C CD2 . TRP A 214 ? 0.9444 0.6035 0.7040 0.0928  0.0103  0.0061  515 TRP A CD2 
1683  N NE1 . TRP A 214 ? 0.9454 0.6556 0.7230 0.1034  0.0109  -0.0004 515 TRP A NE1 
1684  C CE2 . TRP A 214 ? 0.8680 0.5612 0.6388 0.1053  0.0117  0.0053  515 TRP A CE2 
1685  C CE3 . TRP A 214 ? 0.9244 0.5598 0.6740 0.0915  0.0112  0.0124  515 TRP A CE3 
1686  C CZ2 . TRP A 214 ? 0.7914 0.4970 0.5646 0.1166  0.0134  0.0097  515 TRP A CZ2 
1687  C CZ3 . TRP A 214 ? 1.0144 0.6615 0.7656 0.1037  0.0128  0.0173  515 TRP A CZ3 
1688  C CH2 . TRP A 214 ? 0.9054 0.5880 0.6687 0.1162  0.0137  0.0155  515 TRP A CH2 
1689  N N   . LYS A 215 ? 1.0952 0.6799 0.7984 0.1099  0.0006  -0.0194 516 LYS A N   
1690  C CA  . LYS A 215 ? 0.9802 0.5412 0.6608 0.1314  -0.0006 -0.0215 516 LYS A CA  
1691  C C   . LYS A 215 ? 0.9277 0.5144 0.6188 0.1429  0.0023  -0.0147 516 LYS A C   
1692  O O   . LYS A 215 ? 0.9945 0.6216 0.7022 0.1495  0.0040  -0.0156 516 LYS A O   
1693  C CB  . LYS A 215 ? 1.0752 0.6390 0.7456 0.1473  -0.0029 -0.0319 516 LYS A CB  
1694  C CG  . LYS A 215 ? 1.2274 0.7742 0.8906 0.1358  -0.0060 -0.0399 516 LYS A CG  
1695  C CD  . LYS A 215 ? 1.2521 0.7456 0.8839 0.1414  -0.0097 -0.0456 516 LYS A CD  
1696  C CE  . LYS A 215 ? 1.2193 0.6889 0.8474 0.1185  -0.0120 -0.0488 516 LYS A CE  
1697  N NZ  . LYS A 215 ? 1.1557 0.6289 0.7988 0.0970  -0.0094 -0.0392 516 LYS A NZ  
1698  N N   . PRO A 216 ? 1.0197 0.5856 0.7015 0.1449  0.0031  -0.0078 517 PRO A N   
1699  C CA  . PRO A 216 ? 0.9523 0.5459 0.6465 0.1531  0.0057  -0.0010 517 PRO A CA  
1700  C C   . PRO A 216 ? 0.9734 0.5701 0.6545 0.1802  0.0045  -0.0044 517 PRO A C   
1701  O O   . PRO A 216 ? 1.0788 0.6392 0.7336 0.1936  0.0017  -0.0084 517 PRO A O   
1702  C CB  . PRO A 216 ? 0.9507 0.5173 0.6378 0.1428  0.0067  0.0077  517 PRO A CB  
1703  C CG  . PRO A 216 ? 1.0112 0.5259 0.6705 0.1413  0.0041  0.0045  517 PRO A CG  
1704  C CD  . PRO A 216 ? 1.0549 0.5718 0.7157 0.1364  0.0018  -0.0051 517 PRO A CD  
1705  N N   . PRO A 217 ? 0.9269 0.5668 0.6253 0.1892  0.0064  -0.0034 518 PRO A N   
1706  C CA  . PRO A 217 ? 0.9036 0.5515 0.5912 0.2155  0.0054  -0.0062 518 PRO A CA  
1707  C C   . PRO A 217 ? 1.0122 0.6308 0.6809 0.2264  0.0043  -0.0004 518 PRO A C   
1708  O O   . PRO A 217 ? 0.9093 0.5182 0.5594 0.2502  0.0021  -0.0038 518 PRO A O   
1709  C CB  . PRO A 217 ? 0.8181 0.5220 0.5325 0.2162  0.0083  -0.0053 518 PRO A CB  
1710  C CG  . PRO A 217 ? 0.8150 0.5363 0.5499 0.1936  0.0102  -0.0049 518 PRO A CG  
1711  C CD  . PRO A 217 ? 0.8705 0.5548 0.5985 0.1759  0.0094  -0.0010 518 PRO A CD  
1712  N N   . ARG A 218 ? 1.1400 0.7445 0.8118 0.2103  0.0058  0.0081  519 ARG A N   
1713  C CA  . ARG A 218 ? 1.1510 0.7331 0.8075 0.2184  0.0056  0.0155  519 ARG A CA  
1714  C C   . ARG A 218 ? 1.1760 0.7920 0.8376 0.2400  0.0054  0.0155  519 ARG A C   
1715  O O   . ARG A 218 ? 1.1937 0.7939 0.8340 0.2632  0.0029  0.0141  519 ARG A O   
1716  C CB  . ARG A 218 ? 1.1664 0.6897 0.7884 0.2259  0.0028  0.0149  519 ARG A CB  
1717  C CG  . ARG A 218 ? 1.1873 0.6785 0.8053 0.2014  0.0031  0.0154  519 ARG A CG  
1718  C CD  . ARG A 218 ? 1.1934 0.6295 0.7818 0.1990  0.0018  0.0189  519 ARG A CD  
1719  N NE  . ARG A 218 ? 1.3568 0.7743 0.9493 0.1716  0.0041  0.0246  519 ARG A NE  
1720  C CZ  . ARG A 218 ? 1.4602 0.8738 1.0546 0.1608  0.0068  0.0345  519 ARG A CZ  
1721  N NH1 . ARG A 218 ? 1.3850 0.7867 0.9848 0.1352  0.0091  0.0388  519 ARG A NH1 
1722  N NH2 . ARG A 218 ? 1.4867 0.9104 1.0773 0.1757  0.0072  0.0397  519 ARG A NH2 
1723  N N   . GLY A 219 ? 1.1331 0.7971 0.8233 0.2319  0.0079  0.0166  520 GLY A N   
1724  C CA  . GLY A 219 ? 1.0822 0.7829 0.7819 0.2462  0.0083  0.0176  520 GLY A CA  
1725  C C   . GLY A 219 ? 1.1062 0.8221 0.8224 0.2312  0.0107  0.0257  520 GLY A C   
1726  O O   . GLY A 219 ? 1.1306 0.8227 0.8460 0.2131  0.0120  0.0312  520 GLY A O   
1727  N N   . ARG A 220 ? 1.0860 0.8429 0.8175 0.2380  0.0114  0.0259  521 ARG A N   
1728  C CA  . ARG A 220 ? 1.0353 0.8068 0.7809 0.2257  0.0133  0.0327  521 ARG A CA  
1729  C C   . ARG A 220 ? 0.9229 0.7264 0.6969 0.2049  0.0161  0.0321  521 ARG A C   
1730  O O   . ARG A 220 ? 0.9007 0.7076 0.6851 0.1905  0.0179  0.0377  521 ARG A O   
1731  C CB  . ARG A 220 ? 1.1343 0.9317 0.8801 0.2438  0.0121  0.0333  521 ARG A CB  
1732  C CG  . ARG A 220 ? 1.2117 1.0149 0.9642 0.2356  0.0133  0.0408  521 ARG A CG  
1733  C CD  . ARG A 220 ? 1.2741 1.0683 1.0070 0.2576  0.0107  0.0437  521 ARG A CD  
1734  N NE  . ARG A 220 ? 1.3016 1.1063 1.0406 0.2523  0.0116  0.0501  521 ARG A NE  
1735  C CZ  . ARG A 220 ? 1.3314 1.1775 1.0840 0.2592  0.0109  0.0482  521 ARG A CZ  
1736  N NH1 . ARG A 220 ? 1.2218 1.1041 0.9842 0.2709  0.0096  0.0403  521 ARG A NH1 
1737  N NH2 . ARG A 220 ? 1.3802 1.2327 1.1364 0.2542  0.0116  0.0539  521 ARG A NH2 
1738  N N   . PHE A 221 ? 0.9486 0.7752 0.7341 0.2035  0.0167  0.0257  522 PHE A N   
1739  C CA  . PHE A 221 ? 0.9206 0.7796 0.7317 0.1861  0.0193  0.0252  522 PHE A CA  
1740  C C   . PHE A 221 ? 0.8151 0.6709 0.6294 0.1773  0.0199  0.0209  522 PHE A C   
1741  O O   . PHE A 221 ? 0.7786 0.6653 0.6075 0.1742  0.0214  0.0171  522 PHE A O   
1742  C CB  . PHE A 221 ? 0.8871 0.7917 0.7133 0.1931  0.0201  0.0225  522 PHE A CB  
1743  C CG  . PHE A 221 ? 0.8509 0.7638 0.6782 0.1976  0.0196  0.0268  522 PHE A CG  
1744  C CD1 . PHE A 221 ? 0.8783 0.8130 0.7022 0.2166  0.0179  0.0241  522 PHE A CD1 
1745  C CD2 . PHE A 221 ? 0.8881 0.7889 0.7197 0.1833  0.0206  0.0333  522 PHE A CD2 
1746  C CE1 . PHE A 221 ? 0.8813 0.8246 0.7055 0.2213  0.0171  0.0278  522 PHE A CE1 
1747  C CE2 . PHE A 221 ? 0.9128 0.8215 0.7443 0.1877  0.0201  0.0371  522 PHE A CE2 
1748  C CZ  . PHE A 221 ? 0.8590 0.7884 0.6866 0.2066  0.0182  0.0344  522 PHE A CZ  
1749  N N   . ASP A 222 ? 0.7216 0.5393 0.5216 0.1726  0.0187  0.0215  523 ASP A N   
1750  C CA  . ASP A 222 ? 0.7384 0.5500 0.5409 0.1619  0.0188  0.0178  523 ASP A CA  
1751  C C   . ASP A 222 ? 0.8599 0.6853 0.6825 0.1404  0.0209  0.0214  523 ASP A C   
1752  O O   . ASP A 222 ? 1.0530 0.8668 0.8776 0.1303  0.0214  0.0271  523 ASP A O   
1753  C CB  . ASP A 222 ? 0.6137 0.3795 0.3940 0.1625  0.0165  0.0170  523 ASP A CB  
1754  C CG  . ASP A 222 ? 0.8677 0.6125 0.6244 0.1849  0.0141  0.0146  523 ASP A CG  
1755  O OD1 . ASP A 222 ? 0.8971 0.6661 0.6555 0.2013  0.0140  0.0132  523 ASP A OD1 
1756  O OD2 . ASP A 222 ? 0.9831 0.6864 0.7188 0.1860  0.0121  0.0141  523 ASP A OD2 
1757  N N   . VAL A 223 ? 0.8125 0.6630 0.6490 0.1342  0.0221  0.0183  524 VAL A N   
1758  C CA  . VAL A 223 ? 0.6761 0.5359 0.5289 0.1152  0.0236  0.0213  524 VAL A CA  
1759  C C   . VAL A 223 ? 0.6996 0.5306 0.5447 0.1050  0.0220  0.0210  524 VAL A C   
1760  O O   . VAL A 223 ? 0.7976 0.6132 0.6303 0.1101  0.0203  0.0160  524 VAL A O   
1761  C CB  . VAL A 223 ? 0.5878 0.4803 0.4549 0.1122  0.0254  0.0186  524 VAL A CB  
1762  C CG1 . VAL A 223 ? 0.5815 0.4835 0.4643 0.0949  0.0267  0.0223  524 VAL A CG1 
1763  C CG2 . VAL A 223 ? 0.5081 0.4297 0.3806 0.1233  0.0268  0.0173  524 VAL A CG2 
1764  N N   . LEU A 224 ? 0.5418 0.3663 0.3939 0.0907  0.0226  0.0256  525 LEU A N   
1765  C CA  . LEU A 224 ? 0.6247 0.4225 0.4687 0.0808  0.0209  0.0249  525 LEU A CA  
1766  C C   . LEU A 224 ? 0.7184 0.5270 0.5703 0.0725  0.0203  0.0211  525 LEU A C   
1767  O O   . LEU A 224 ? 0.8390 0.6745 0.7057 0.0692  0.0217  0.0218  525 LEU A O   
1768  C CB  . LEU A 224 ? 0.5523 0.3406 0.4002 0.0682  0.0218  0.0308  525 LEU A CB  
1769  C CG  . LEU A 224 ? 0.6761 0.4396 0.5088 0.0737  0.0219  0.0346  525 LEU A CG  
1770  C CD1 . LEU A 224 ? 0.6832 0.4508 0.5251 0.0624  0.0239  0.0410  525 LEU A CD1 
1771  C CD2 . LEU A 224 ? 0.6455 0.3721 0.4581 0.0729  0.0199  0.0321  525 LEU A CD2 
1772  N N   . PRO A 225 ? 0.6030 0.3902 0.4442 0.0688  0.0180  0.0172  526 PRO A N   
1773  C CA  . PRO A 225 ? 0.6535 0.4510 0.5016 0.0606  0.0170  0.0138  526 PRO A CA  
1774  C C   . PRO A 225 ? 0.6780 0.4856 0.5410 0.0454  0.0176  0.0180  526 PRO A C   
1775  O O   . PRO A 225 ? 0.7628 0.5604 0.6266 0.0387  0.0182  0.0221  526 PRO A O   
1776  C CB  . PRO A 225 ? 0.6644 0.4327 0.4954 0.0600  0.0139  0.0082  526 PRO A CB  
1777  C CG  . PRO A 225 ? 0.6414 0.3821 0.4615 0.0585  0.0139  0.0116  526 PRO A CG  
1778  C CD  . PRO A 225 ? 0.5859 0.3369 0.4072 0.0710  0.0161  0.0155  526 PRO A CD  
1779  N N   . LEU A 226 ? 0.5778 0.4057 0.4518 0.0406  0.0175  0.0171  527 LEU A N   
1780  C CA  . LEU A 226 ? 0.5282 0.3641 0.4142 0.0274  0.0172  0.0199  527 LEU A CA  
1781  C C   . LEU A 226 ? 0.6934 0.5107 0.5727 0.0181  0.0144  0.0167  527 LEU A C   
1782  O O   . LEU A 226 ? 0.8893 0.6936 0.7569 0.0209  0.0121  0.0110  527 LEU A O   
1783  C CB  . LEU A 226 ? 0.6489 0.5084 0.5454 0.0262  0.0175  0.0198  527 LEU A CB  
1784  C CG  . LEU A 226 ? 0.6664 0.5453 0.5722 0.0306  0.0206  0.0238  527 LEU A CG  
1785  C CD1 . LEU A 226 ? 0.6026 0.5013 0.5156 0.0295  0.0213  0.0242  527 LEU A CD1 
1786  C CD2 . LEU A 226 ? 0.5930 0.4732 0.5075 0.0243  0.0216  0.0287  527 LEU A CD2 
1787  N N   . LEU A 227 ? 0.7792 0.5959 0.6654 0.0068  0.0145  0.0199  528 LEU A N   
1788  C CA  . LEU A 227 ? 0.7190 0.5229 0.6018 -0.0052 0.0122  0.0172  528 LEU A CA  
1789  C C   . LEU A 227 ? 0.7439 0.5702 0.6423 -0.0143 0.0115  0.0183  528 LEU A C   
1790  O O   . LEU A 227 ? 0.6962 0.5318 0.6045 -0.0194 0.0133  0.0230  528 LEU A O   
1791  C CB  . LEU A 227 ? 0.7114 0.4942 0.5869 -0.0109 0.0135  0.0201  528 LEU A CB  
1792  C CG  . LEU A 227 ? 0.7780 0.5319 0.6378 -0.0174 0.0113  0.0157  528 LEU A CG  
1793  C CD1 . LEU A 227 ? 0.7602 0.5060 0.6213 -0.0315 0.0128  0.0195  528 LEU A CD1 
1794  C CD2 . LEU A 227 ? 0.8585 0.6159 0.7176 -0.0216 0.0076  0.0084  528 LEU A CD2 
1795  N N   . LEU A 228 ? 0.7638 0.5990 0.6636 -0.0154 0.0087  0.0139  529 LEU A N   
1796  C CA  . LEU A 228 ? 0.7344 0.5925 0.6476 -0.0199 0.0077  0.0152  529 LEU A CA  
1797  C C   . LEU A 228 ? 0.7955 0.6545 0.7099 -0.0310 0.0042  0.0108  529 LEU A C   
1798  O O   . LEU A 228 ? 0.7122 0.5576 0.6161 -0.0334 0.0015  0.0049  529 LEU A O   
1799  C CB  . LEU A 228 ? 0.6224 0.4942 0.5369 -0.0115 0.0074  0.0147  529 LEU A CB  
1800  C CG  . LEU A 228 ? 0.5802 0.4520 0.4926 -0.0014 0.0108  0.0177  529 LEU A CG  
1801  C CD1 . LEU A 228 ? 0.5559 0.4394 0.4671 0.0055  0.0110  0.0167  529 LEU A CD1 
1802  C CD2 . LEU A 228 ? 0.6049 0.4865 0.5281 -0.0025 0.0136  0.0237  529 LEU A CD2 
1803  N N   . GLN A 229 ? 0.7955 0.6716 0.7225 -0.0376 0.0040  0.0132  530 GLN A N   
1804  C CA  . GLN A 229 ? 0.7545 0.6385 0.6856 -0.0484 0.0008  0.0092  530 GLN A CA  
1805  C C   . GLN A 229 ? 0.6757 0.5851 0.6178 -0.0458 -0.0012 0.0099  530 GLN A C   
1806  O O   . GLN A 229 ? 0.6057 0.5267 0.5564 -0.0416 0.0009  0.0152  530 GLN A O   
1807  C CB  . GLN A 229 ? 0.6999 0.5807 0.6349 -0.0596 0.0026  0.0113  530 GLN A CB  
1808  C CG  . GLN A 229 ? 0.4905 0.3931 0.4376 -0.0696 0.0008  0.0098  530 GLN A CG  
1809  C CD  . GLN A 229 ? 0.6786 0.5768 0.6276 -0.0818 0.0034  0.0117  530 GLN A CD  
1810  O OE1 . GLN A 229 ? 0.8010 0.6990 0.7532 -0.0800 0.0074  0.0177  530 GLN A OE1 
1811  N NE2 . GLN A 229 ? 0.6997 0.5942 0.6458 -0.0950 0.0013  0.0066  530 GLN A NE2 
1812  N N   . ALA A 230 ? 0.7240 0.6409 0.6646 -0.0477 -0.0056 0.0045  531 ALA A N   
1813  C CA  . ALA A 230 ? 0.6758 0.6157 0.6246 -0.0448 -0.0083 0.0047  531 ALA A CA  
1814  C C   . ALA A 230 ? 0.6956 0.6487 0.6496 -0.0550 -0.0124 -0.0006 531 ALA A C   
1815  O O   . ALA A 230 ? 0.6830 0.6260 0.6306 -0.0633 -0.0145 -0.0066 531 ALA A O   
1816  C CB  . ALA A 230 ? 0.5944 0.5349 0.5357 -0.0353 -0.0100 0.0036  531 ALA A CB  
1817  N N   . ASN A 231 ? 0.7348 0.7106 0.7000 -0.0543 -0.0137 0.0011  532 ASN A N   
1818  C CA  . ASN A 231 ? 0.7151 0.7112 0.6874 -0.0622 -0.0180 -0.0042 532 ASN A CA  
1819  C C   . ASN A 231 ? 0.7281 0.7178 0.7007 -0.0778 -0.0175 -0.0083 532 ASN A C   
1820  O O   . ASN A 231 ? 0.7741 0.7709 0.7463 -0.0866 -0.0216 -0.0154 532 ASN A O   
1821  C CB  . ASN A 231 ? 0.6163 0.6201 0.5832 -0.0581 -0.0235 -0.0094 532 ASN A CB  
1822  C CG  . ASN A 231 ? 0.7377 0.7690 0.7129 -0.0522 -0.0272 -0.0091 532 ASN A CG  
1823  O OD1 . ASN A 231 ? 0.7776 0.8145 0.7569 -0.0432 -0.0254 -0.0029 532 ASN A OD1 
1824  N ND2 . ASN A 231 ? 0.8144 0.8627 0.7914 -0.0570 -0.0327 -0.0161 532 ASN A ND2 
1825  N N   . GLY A 232 ? 0.6854 0.6617 0.6581 -0.0819 -0.0125 -0.0038 533 GLY A N   
1826  C CA  . GLY A 232 ? 0.5496 0.5171 0.5212 -0.0975 -0.0111 -0.0060 533 GLY A CA  
1827  C C   . GLY A 232 ? 0.6125 0.5543 0.5696 -0.1040 -0.0127 -0.0117 533 GLY A C   
1828  O O   . GLY A 232 ? 0.6978 0.6320 0.6524 -0.1190 -0.0125 -0.0149 533 GLY A O   
1829  N N   . ASN A 233 ? 0.6716 0.5996 0.6182 -0.0934 -0.0142 -0.0132 534 ASN A N   
1830  C CA  . ASN A 233 ? 0.6570 0.5582 0.5880 -0.0974 -0.0158 -0.0190 534 ASN A CA  
1831  C C   . ASN A 233 ? 0.6219 0.4928 0.5421 -0.0954 -0.0111 -0.0146 534 ASN A C   
1832  O O   . ASN A 233 ? 0.5962 0.4680 0.5207 -0.0886 -0.0070 -0.0071 534 ASN A O   
1833  C CB  . ASN A 233 ? 0.7439 0.6453 0.6676 -0.0863 -0.0194 -0.0232 534 ASN A CB  
1834  C CG  . ASN A 233 ? 0.8541 0.7810 0.7842 -0.0894 -0.0250 -0.0291 534 ASN A CG  
1835  O OD1 . ASN A 233 ? 0.9424 0.8769 0.8763 -0.1033 -0.0276 -0.0346 534 ASN A OD1 
1836  N ND2 . ASN A 233 ? 0.7829 0.7245 0.7145 -0.0768 -0.0268 -0.0279 534 ASN A ND2 
1837  N N   . ASP A 234 ? 0.6394 0.4822 0.5442 -0.1011 -0.0122 -0.0197 535 ASP A N   
1838  C CA  . ASP A 234 ? 0.7181 0.5290 0.6095 -0.0977 -0.0085 -0.0160 535 ASP A CA  
1839  C C   . ASP A 234 ? 0.7264 0.5384 0.6169 -0.0791 -0.0064 -0.0113 535 ASP A C   
1840  O O   . ASP A 234 ? 0.7843 0.6115 0.6779 -0.0700 -0.0086 -0.0134 535 ASP A O   
1841  C CB  . ASP A 234 ? 0.7910 0.5691 0.6629 -0.1028 -0.0109 -0.0232 535 ASP A CB  
1842  C CG  . ASP A 234 ? 0.8087 0.5809 0.6796 -0.1242 -0.0122 -0.0274 535 ASP A CG  
1843  O OD1 . ASP A 234 ? 0.8239 0.5686 0.6785 -0.1308 -0.0147 -0.0343 535 ASP A OD1 
1844  O OD2 . ASP A 234 ? 0.8148 0.6100 0.7007 -0.1345 -0.0106 -0.0241 535 ASP A OD2 
1845  N N   . PRO A 235 ? 0.7493 0.5482 0.6363 -0.0733 -0.0022 -0.0049 536 PRO A N   
1846  C CA  . PRO A 235 ? 0.7441 0.5472 0.6312 -0.0566 -0.0002 -0.0011 536 PRO A CA  
1847  C C   . PRO A 235 ? 0.7191 0.5029 0.5900 -0.0464 -0.0018 -0.0062 536 PRO A C   
1848  O O   . PRO A 235 ? 0.6582 0.4167 0.5145 -0.0506 -0.0037 -0.0114 536 PRO A O   
1849  C CB  . PRO A 235 ? 0.7314 0.5268 0.6192 -0.0551 0.0044  0.0066  536 PRO A CB  
1850  C CG  . PRO A 235 ? 0.7957 0.5677 0.6738 -0.0682 0.0048  0.0058  536 PRO A CG  
1851  C CD  . PRO A 235 ? 0.8720 0.6558 0.7562 -0.0823 0.0013  -0.0001 536 PRO A CD  
1852  N N   . GLU A 236 ? 0.6638 0.4599 0.5369 -0.0327 -0.0009 -0.0048 537 GLU A N   
1853  C CA  . GLU A 236 ? 0.7078 0.4922 0.5673 -0.0211 -0.0021 -0.0097 537 GLU A CA  
1854  C C   . GLU A 236 ? 0.7573 0.5418 0.6151 -0.0072 0.0016  -0.0050 537 GLU A C   
1855  O O   . GLU A 236 ? 0.7320 0.5342 0.6022 -0.0054 0.0045  0.0014  537 GLU A O   
1856  C CB  . GLU A 236 ? 0.6744 0.4779 0.5371 -0.0185 -0.0050 -0.0142 537 GLU A CB  
1857  C CG  . GLU A 236 ? 0.6128 0.4170 0.4756 -0.0312 -0.0095 -0.0204 537 GLU A CG  
1858  C CD  . GLU A 236 ? 0.7953 0.6211 0.6621 -0.0285 -0.0126 -0.0237 537 GLU A CD  
1859  O OE1 . GLU A 236 ? 0.8868 0.7105 0.7441 -0.0184 -0.0132 -0.0274 537 GLU A OE1 
1860  O OE2 . GLU A 236 ? 0.8588 0.7045 0.7377 -0.0358 -0.0142 -0.0226 537 GLU A OE2 
1861  N N   . LEU A 237 ? 0.7462 0.5114 0.5881 0.0030  0.0012  -0.0089 538 LEU A N   
1862  C CA  . LEU A 237 ? 0.7842 0.5498 0.6228 0.0173  0.0042  -0.0058 538 LEU A CA  
1863  C C   . LEU A 237 ? 0.8497 0.6387 0.6926 0.0274  0.0050  -0.0070 538 LEU A C   
1864  O O   . LEU A 237 ? 0.8715 0.6658 0.7116 0.0275  0.0027  -0.0123 538 LEU A O   
1865  C CB  . LEU A 237 ? 0.7570 0.4907 0.5749 0.0251  0.0033  -0.0096 538 LEU A CB  
1866  C CG  . LEU A 237 ? 0.7759 0.4837 0.5870 0.0168  0.0038  -0.0062 538 LEU A CG  
1867  C CD1 . LEU A 237 ? 0.7342 0.4066 0.5219 0.0262  0.0027  -0.0096 538 LEU A CD1 
1868  C CD2 . LEU A 237 ? 0.8436 0.5662 0.6675 0.0167  0.0076  0.0027  538 LEU A CD2 
1869  N N   . PHE A 238 ? 0.9109 0.7147 0.7606 0.0354  0.0085  -0.0021 539 PHE A N   
1870  C CA  . PHE A 238 ? 0.7875 0.6128 0.6400 0.0450  0.0102  -0.0028 539 PHE A CA  
1871  C C   . PHE A 238 ? 0.8429 0.6730 0.6951 0.0561  0.0133  0.0001  539 PHE A C   
1872  O O   . PHE A 238 ? 0.8828 0.7093 0.7395 0.0539  0.0146  0.0050  539 PHE A O   
1873  C CB  . PHE A 238 ? 0.6277 0.4782 0.4955 0.0380  0.0112  0.0013  539 PHE A CB  
1874  C CG  . PHE A 238 ? 0.6503 0.5001 0.5195 0.0283  0.0078  -0.0012 539 PHE A CG  
1875  C CD1 . PHE A 238 ? 0.6335 0.4813 0.5107 0.0169  0.0067  0.0014  539 PHE A CD1 
1876  C CD2 . PHE A 238 ? 0.7358 0.5884 0.5976 0.0311  0.0057  -0.0068 539 PHE A CD2 
1877  C CE1 . PHE A 238 ? 0.7396 0.5901 0.6188 0.0082  0.0032  -0.0015 539 PHE A CE1 
1878  C CE2 . PHE A 238 ? 0.7313 0.5849 0.5941 0.0227  0.0020  -0.0097 539 PHE A CE2 
1879  C CZ  . PHE A 238 ? 0.7770 0.6304 0.6490 0.0112  0.0007  -0.0071 539 PHE A CZ  
1880  N N   . GLN A 239 ? 0.7478 0.5878 0.5945 0.0683  0.0143  -0.0033 540 GLN A N   
1881  C CA  . GLN A 239 ? 0.7731 0.6243 0.6207 0.0797  0.0171  -0.0016 540 GLN A CA  
1882  C C   . GLN A 239 ? 0.7844 0.6681 0.6468 0.0776  0.0205  0.0020  540 GLN A C   
1883  O O   . GLN A 239 ? 0.8431 0.7413 0.7049 0.0797  0.0212  -0.0006 540 GLN A O   
1884  C CB  . GLN A 239 ? 0.8027 0.6454 0.6342 0.0956  0.0162  -0.0083 540 GLN A CB  
1885  C CG  . GLN A 239 ? 0.9099 0.7668 0.7414 0.1096  0.0187  -0.0075 540 GLN A CG  
1886  C CD  . GLN A 239 ? 1.0031 0.8775 0.8288 0.1232  0.0197  -0.0134 540 GLN A CD  
1887  O OE1 . GLN A 239 ? 1.1988 1.0970 1.0325 0.1192  0.0217  -0.0136 540 GLN A OE1 
1888  N NE2 . GLN A 239 ? 0.7887 0.6512 0.5995 0.1396  0.0184  -0.0182 540 GLN A NE2 
1889  N N   . ILE A 240 ? 0.6533 0.5475 0.5278 0.0726  0.0225  0.0080  541 ILE A N   
1890  C CA  . ILE A 240 ? 0.5937 0.5162 0.4807 0.0706  0.0259  0.0113  541 ILE A CA  
1891  C C   . ILE A 240 ? 0.7057 0.6442 0.5880 0.0831  0.0278  0.0074  541 ILE A C   
1892  O O   . ILE A 240 ? 0.7595 0.6923 0.6346 0.0944  0.0274  0.0051  541 ILE A O   
1893  C CB  . ILE A 240 ? 0.5760 0.5052 0.4740 0.0663  0.0275  0.0167  541 ILE A CB  
1894  C CG1 . ILE A 240 ? 0.5972 0.5101 0.4985 0.0561  0.0256  0.0200  541 ILE A CG1 
1895  C CG2 . ILE A 240 ? 0.4648 0.4197 0.3747 0.0613  0.0306  0.0197  541 ILE A CG2 
1896  C CD1 . ILE A 240 ? 0.6157 0.5319 0.5247 0.0540  0.0269  0.0244  541 ILE A CD1 
1897  N N   . PRO A 241 ? 0.7307 0.6894 0.6158 0.0822  0.0301  0.0067  542 PRO A N   
1898  C CA  . PRO A 241 ? 0.7146 0.6906 0.5946 0.0944  0.0321  0.0023  542 PRO A CA  
1899  C C   . PRO A 241 ? 0.6168 0.6105 0.5039 0.0995  0.0345  0.0038  542 PRO A C   
1900  O O   . PRO A 241 ? 0.5628 0.5699 0.4625 0.0902  0.0365  0.0087  542 PRO A O   
1901  C CB  . PRO A 241 ? 0.5155 0.5112 0.3991 0.0885  0.0348  0.0032  542 PRO A CB  
1902  C CG  . PRO A 241 ? 0.4874 0.4682 0.3726 0.0766  0.0325  0.0062  542 PRO A CG  
1903  C CD  . PRO A 241 ? 0.5769 0.5450 0.4691 0.0707  0.0311  0.0102  542 PRO A CD  
1904  N N   . PRO A 242 ? 0.5101 0.5037 0.3887 0.1148  0.0338  -0.0008 543 PRO A N   
1905  C CA  . PRO A 242 ? 0.6307 0.6394 0.5151 0.1208  0.0350  0.0003  543 PRO A CA  
1906  C C   . PRO A 242 ? 0.7396 0.7842 0.6386 0.1141  0.0392  0.0025  543 PRO A C   
1907  O O   . PRO A 242 ? 0.8265 0.8830 0.7346 0.1121  0.0401  0.0049  543 PRO A O   
1908  C CB  . PRO A 242 ? 0.6535 0.6600 0.5241 0.1408  0.0335  -0.0061 543 PRO A CB  
1909  C CG  . PRO A 242 ? 0.6878 0.6668 0.5437 0.1434  0.0307  -0.0100 543 PRO A CG  
1910  C CD  . PRO A 242 ? 0.5956 0.5788 0.4584 0.1283  0.0319  -0.0077 543 PRO A CD  
1911  N N   . GLU A 243 ? 0.5883 0.6499 0.4891 0.1097  0.0421  0.0016  544 GLU A N   
1912  C CA  . GLU A 243 ? 0.5693 0.6633 0.4826 0.1013  0.0466  0.0040  544 GLU A CA  
1913  C C   . GLU A 243 ? 0.5847 0.6740 0.5089 0.0843  0.0472  0.0106  544 GLU A C   
1914  O O   . GLU A 243 ? 0.5061 0.6181 0.4403 0.0757  0.0507  0.0128  544 GLU A O   
1915  C CB  . GLU A 243 ? 0.5403 0.6515 0.4505 0.1004  0.0499  0.0021  544 GLU A CB  
1916  C CG  . GLU A 243 ? 0.5393 0.6333 0.4460 0.0898  0.0493  0.0053  544 GLU A CG  
1917  C CD  . GLU A 243 ? 0.6578 0.7327 0.5503 0.0991  0.0461  0.0004  544 GLU A CD  
1918  O OE1 . GLU A 243 ? 0.6821 0.7462 0.5662 0.1127  0.0434  -0.0047 544 GLU A OE1 
1919  O OE2 . GLU A 243 ? 0.8332 0.9032 0.7216 0.0931  0.0462  0.0014  544 GLU A OE2 
1920  N N   . LEU A 244 ? 0.5745 0.6352 0.4965 0.0792  0.0439  0.0134  545 LEU A N   
1921  C CA  . LEU A 244 ? 0.5024 0.5571 0.4336 0.0652  0.0440  0.0191  545 LEU A CA  
1922  C C   . LEU A 244 ? 0.4794 0.5265 0.4152 0.0658  0.0423  0.0206  545 LEU A C   
1923  O O   . LEU A 244 ? 0.4744 0.5194 0.4181 0.0553  0.0425  0.0246  545 LEU A O   
1924  C CB  . LEU A 244 ? 0.4759 0.5079 0.4029 0.0584  0.0417  0.0213  545 LEU A CB  
1925  C CG  . LEU A 244 ? 0.4965 0.5314 0.4196 0.0538  0.0428  0.0219  545 LEU A CG  
1926  C CD1 . LEU A 244 ? 0.4504 0.4634 0.3719 0.0472  0.0395  0.0243  545 LEU A CD1 
1927  C CD2 . LEU A 244 ? 0.6035 0.6593 0.5335 0.0448  0.0472  0.0256  545 LEU A CD2 
1928  N N   . VAL A 245 ? 0.3957 0.4368 0.3252 0.0783  0.0403  0.0176  546 VAL A N   
1929  C CA  . VAL A 245 ? 0.4698 0.5031 0.4013 0.0804  0.0386  0.0193  546 VAL A CA  
1930  C C   . VAL A 245 ? 0.5235 0.5855 0.4619 0.0852  0.0405  0.0176  546 VAL A C   
1931  O O   . VAL A 245 ? 0.4539 0.5252 0.3864 0.0993  0.0401  0.0135  546 VAL A O   
1932  C CB  . VAL A 245 ? 0.5738 0.5814 0.4922 0.0912  0.0354  0.0177  546 VAL A CB  
1933  C CG1 . VAL A 245 ? 0.6102 0.6089 0.5296 0.0924  0.0341  0.0206  546 VAL A CG1 
1934  C CG2 . VAL A 245 ? 0.5279 0.5105 0.4395 0.0857  0.0335  0.0180  546 VAL A CG2 
1935  N N   . LEU A 246 ? 0.3927 0.4692 0.3428 0.0742  0.0423  0.0200  547 LEU A N   
1936  C CA  . LEU A 246 ? 0.4563 0.5616 0.4137 0.0774  0.0437  0.0177  547 LEU A CA  
1937  C C   . LEU A 246 ? 0.6026 0.7005 0.5570 0.0869  0.0408  0.0176  547 LEU A C   
1938  O O   . LEU A 246 ? 0.6966 0.7716 0.6494 0.0833  0.0390  0.0212  547 LEU A O   
1939  C CB  . LEU A 246 ? 0.4889 0.6097 0.4585 0.0616  0.0462  0.0198  547 LEU A CB  
1940  C CG  . LEU A 246 ? 0.4422 0.5938 0.4211 0.0606  0.0476  0.0172  547 LEU A CG  
1941  C CD1 . LEU A 246 ? 0.4825 0.6612 0.4601 0.0715  0.0491  0.0122  547 LEU A CD1 
1942  C CD2 . LEU A 246 ? 0.4298 0.5912 0.4179 0.0428  0.0505  0.0192  547 LEU A CD2 
1943  N N   . GLU A 247 ? 0.5428 0.6613 0.4961 0.0998  0.0405  0.0137  548 GLU A N   
1944  C CA  . GLU A 247 ? 0.5293 0.6418 0.4772 0.1117  0.0377  0.0136  548 GLU A CA  
1945  C C   . GLU A 247 ? 0.6011 0.7502 0.5576 0.1160  0.0382  0.0100  548 GLU A C   
1946  O O   . GLU A 247 ? 0.6512 0.8305 0.6143 0.1152  0.0407  0.0062  548 GLU A O   
1947  C CB  . GLU A 247 ? 0.5133 0.6053 0.4444 0.1291  0.0353  0.0119  548 GLU A CB  
1948  C CG  . GLU A 247 ? 0.3581 0.4103 0.2788 0.1256  0.0337  0.0151  548 GLU A CG  
1949  C CD  . GLU A 247 ? 0.6030 0.6326 0.5051 0.1428  0.0311  0.0130  548 GLU A CD  
1950  O OE1 . GLU A 247 ? 0.5689 0.6115 0.4657 0.1554  0.0313  0.0078  548 GLU A OE1 
1951  O OE2 . GLU A 247 ? 0.6658 0.6640 0.5577 0.1440  0.0291  0.0163  548 GLU A OE2 
1952  N N   . VAL A 248 ? 0.6168 0.7651 0.5733 0.1205  0.0360  0.0111  549 VAL A N   
1953  C CA  . VAL A 248 ? 0.4677 0.6512 0.4327 0.1241  0.0358  0.0074  549 VAL A CA  
1954  C C   . VAL A 248 ? 0.5013 0.6826 0.4549 0.1452  0.0323  0.0061  549 VAL A C   
1955  O O   . VAL A 248 ? 0.4936 0.6481 0.4387 0.1486  0.0301  0.0102  549 VAL A O   
1956  C CB  . VAL A 248 ? 0.4442 0.6333 0.4207 0.1086  0.0361  0.0092  549 VAL A CB  
1957  C CG1 . VAL A 248 ? 0.4686 0.6957 0.4539 0.1117  0.0356  0.0044  549 VAL A CG1 
1958  C CG2 . VAL A 248 ? 0.4296 0.6154 0.4145 0.0889  0.0392  0.0111  549 VAL A CG2 
1959  N N   . PRO A 249 ? 0.4346 0.6436 0.3868 0.1602  0.0318  0.0006  550 PRO A N   
1960  C CA  . PRO A 249 ? 0.4988 0.7071 0.4392 0.1820  0.0281  -0.0006 550 PRO A CA  
1961  C C   . PRO A 249 ? 0.6368 0.8657 0.5856 0.1799  0.0265  -0.0008 550 PRO A C   
1962  O O   . PRO A 249 ? 0.6576 0.9216 0.6225 0.1687  0.0282  -0.0044 550 PRO A O   
1963  C CB  . PRO A 249 ? 0.4822 0.7204 0.4210 0.1976  0.0284  -0.0073 550 PRO A CB  
1964  C CG  . PRO A 249 ? 0.4503 0.7223 0.4072 0.1800  0.0326  -0.0103 550 PRO A CG  
1965  C CD  . PRO A 249 ? 0.3750 0.6195 0.3362 0.1579  0.0348  -0.0046 550 PRO A CD  
1966  N N   . ILE A 250 ? 0.5924 0.7989 0.5295 0.1897  0.0234  0.0030  551 ILE A N   
1967  C CA  . ILE A 250 ? 0.5565 0.7768 0.4999 0.1867  0.0218  0.0036  551 ILE A CA  
1968  C C   . ILE A 250 ? 0.4935 0.7471 0.4348 0.2065  0.0187  -0.0016 551 ILE A C   
1969  O O   . ILE A 250 ? 0.4639 0.7030 0.3880 0.2278  0.0158  -0.0005 551 ILE A O   
1970  C CB  . ILE A 250 ? 0.5000 0.6808 0.4324 0.1853  0.0205  0.0110  551 ILE A CB  
1971  C CG1 . ILE A 250 ? 0.5010 0.6527 0.4362 0.1665  0.0233  0.0154  551 ILE A CG1 
1972  C CG2 . ILE A 250 ? 0.4744 0.6713 0.4138 0.1811  0.0191  0.0111  551 ILE A CG2 
1973  C CD1 . ILE A 250 ? 0.4481 0.6215 0.4022 0.1466  0.0262  0.0127  551 ILE A CD1 
1974  N N   . ARG A 251 ? 0.4282 0.7268 0.3866 0.1994  0.0193  -0.0075 552 ARG A N   
1975  C CA  . ARG A 251 ? 0.5783 0.9154 0.5380 0.2157  0.0161  -0.0132 552 ARG A CA  
1976  C C   . ARG A 251 ? 0.5879 0.9448 0.5589 0.2048  0.0147  -0.0145 552 ARG A C   
1977  O O   . ARG A 251 ? 0.6012 0.9472 0.5813 0.1833  0.0169  -0.0122 552 ARG A O   
1978  C CB  . ARG A 251 ? 0.4638 0.8442 0.4332 0.2194  0.0177  -0.0210 552 ARG A CB  
1979  C CG  . ARG A 251 ? 0.5932 1.0008 0.5833 0.1940  0.0220  -0.0243 552 ARG A CG  
1980  C CD  . ARG A 251 ? 0.5832 0.9647 0.5726 0.1811  0.0263  -0.0207 552 ARG A CD  
1981  N NE  . ARG A 251 ? 0.5364 0.9462 0.5428 0.1599  0.0307  -0.0239 552 ARG A NE  
1982  C CZ  . ARG A 251 ? 0.6618 1.0525 0.6703 0.1437  0.0347  -0.0205 552 ARG A CZ  
1983  N NH1 . ARG A 251 ? 0.6838 1.0999 0.7058 0.1249  0.0388  -0.0229 552 ARG A NH1 
1984  N NH2 . ARG A 251 ? 0.5704 0.9163 0.5665 0.1461  0.0345  -0.0146 552 ARG A NH2 
1985  N N   . HIS A 252 ? 0.5851 0.9709 0.5545 0.2209  0.0107  -0.0185 553 HIS A N   
1986  C CA  . HIS A 252 ? 0.6087 1.0138 0.5868 0.2131  0.0086  -0.0205 553 HIS A CA  
1987  C C   . HIS A 252 ? 0.6309 1.0954 0.6263 0.2101  0.0081  -0.0304 553 HIS A C   
1988  O O   . HIS A 252 ? 0.7001 1.1932 0.6946 0.2262  0.0071  -0.0354 553 HIS A O   
1989  C CB  . HIS A 252 ? 0.5265 0.9158 0.4874 0.2331  0.0040  -0.0165 553 HIS A CB  
1990  C CG  . HIS A 252 ? 0.5076 0.9075 0.4746 0.2245  0.0020  -0.0172 553 HIS A CG  
1991  N ND1 . HIS A 252 ? 0.4528 0.9008 0.4302 0.2275  -0.0011 -0.0252 553 HIS A ND1 
1992  C CD2 . HIS A 252 ? 0.5059 0.8756 0.4695 0.2137  0.0025  -0.0113 553 HIS A CD2 
1993  C CE1 . HIS A 252 ? 0.3825 0.8280 0.3624 0.2184  -0.0025 -0.0245 553 HIS A CE1 
1994  N NE2 . HIS A 252 ? 0.4478 0.8463 0.4194 0.2103  -0.0002 -0.0160 553 HIS A NE2 
1995  N N   . PRO A 253 ? 0.5817 1.0662 0.5926 0.1896  0.0086  -0.0340 554 PRO A N   
1996  C CA  . PRO A 253 ? 0.4666 1.0078 0.4952 0.1822  0.0088  -0.0439 554 PRO A CA  
1997  C C   . PRO A 253 ? 0.6055 1.1860 0.6332 0.2018  0.0033  -0.0501 554 PRO A C   
1998  O O   . PRO A 253 ? 0.6809 1.3002 0.7161 0.1953  0.0018  -0.0579 554 PRO A O   
1999  C CB  . PRO A 253 ? 0.3817 0.9219 0.4235 0.1537  0.0107  -0.0451 554 PRO A CB  
2000  C CG  . PRO A 253 ? 0.4592 0.9552 0.4892 0.1552  0.0090  -0.0377 554 PRO A CG  
2001  C CD  . PRO A 253 ? 0.4789 0.9344 0.4916 0.1712  0.0095  -0.0296 554 PRO A CD  
2002  N N   . LYS A 254 ? 0.6757 1.2345 0.6874 0.2203  -0.0010 -0.0456 555 LYS A N   
2003  C CA  . LYS A 254 ? 0.7193 1.2984 0.7204 0.2356  -0.0075 -0.0496 555 LYS A CA  
2004  C C   . LYS A 254 ? 0.6808 1.2363 0.6568 0.2631  -0.0106 -0.0453 555 LYS A C   
2005  O O   . LYS A 254 ? 0.7543 1.3323 0.7208 0.2762  -0.0148 -0.0503 555 LYS A O   
2006  C CB  . LYS A 254 ? 0.8187 1.3965 0.8204 0.2333  -0.0103 -0.0489 555 LYS A CB  
2007  C CG  . LYS A 254 ? 0.9028 1.5167 0.9254 0.2095  -0.0101 -0.0572 555 LYS A CG  
2008  C CD  . LYS A 254 ? 1.1145 1.7606 1.1322 0.2167  -0.0160 -0.0646 555 LYS A CD  
2009  C CE  . LYS A 254 ? 1.1904 1.8671 1.2037 0.2252  -0.0178 -0.0712 555 LYS A CE  
2010  N NZ  . LYS A 254 ? 1.1903 1.8983 1.2234 0.2020  -0.0145 -0.0783 555 LYS A NZ  
2011  N N   . PHE A 255 ? 0.6303 1.1403 0.5940 0.2720  -0.0085 -0.0365 556 PHE A N   
2012  C CA  . PHE A 255 ? 0.6963 1.1757 0.6328 0.2971  -0.0114 -0.0317 556 PHE A CA  
2013  C C   . PHE A 255 ? 0.6847 1.1583 0.6171 0.3024  -0.0094 -0.0328 556 PHE A C   
2014  O O   . PHE A 255 ? 0.6762 1.1215 0.6101 0.2974  -0.0052 -0.0282 556 PHE A O   
2015  C CB  . PHE A 255 ? 0.7426 1.1725 0.6650 0.3033  -0.0110 -0.0211 556 PHE A CB  
2016  C CG  . PHE A 255 ? 0.7621 1.1966 0.6841 0.3019  -0.0137 -0.0196 556 PHE A CG  
2017  C CD1 . PHE A 255 ? 0.6916 1.0864 0.6057 0.2988  -0.0127 -0.0103 556 PHE A CD1 
2018  C CD2 . PHE A 255 ? 0.8041 1.2807 0.7319 0.3012  -0.0171 -0.0276 556 PHE A CD2 
2019  C CE1 . PHE A 255 ? 0.7150 1.1142 0.6279 0.2969  -0.0151 -0.0090 556 PHE A CE1 
2020  C CE2 . PHE A 255 ? 0.7605 1.2417 0.6875 0.2999  -0.0196 -0.0269 556 PHE A CE2 
2021  C CZ  . PHE A 255 ? 0.7541 1.1986 0.6744 0.2995  -0.0188 -0.0174 556 PHE A CZ  
2022  N N   . GLU A 256 ? 0.7461 1.2482 0.6727 0.3130  -0.0125 -0.0395 557 GLU A N   
2023  C CA  . GLU A 256 ? 0.7391 1.2372 0.6584 0.3215  -0.0116 -0.0412 557 GLU A CA  
2024  C C   . GLU A 256 ? 0.7232 1.1652 0.6205 0.3358  -0.0109 -0.0331 557 GLU A C   
2025  O O   . GLU A 256 ? 0.8466 1.2735 0.7430 0.3351  -0.0081 -0.0325 557 GLU A O   
2026  C CB  . GLU A 256 ? 0.8979 1.4286 0.8072 0.3370  -0.0163 -0.0484 557 GLU A CB  
2027  C CG  . GLU A 256 ? 1.0498 1.6358 0.9800 0.3226  -0.0161 -0.0575 557 GLU A CG  
2028  C CD  . GLU A 256 ? 1.3250 1.9192 1.2565 0.3238  -0.0142 -0.0603 557 GLU A CD  
2029  O OE1 . GLU A 256 ? 1.4009 1.9746 1.3402 0.3128  -0.0093 -0.0566 557 GLU A OE1 
2030  O OE2 . GLU A 256 ? 1.4116 2.0326 1.3351 0.3368  -0.0177 -0.0663 557 GLU A OE2 
2031  N N   . TRP A 257 ? 0.8047 1.2143 0.6827 0.3481  -0.0132 -0.0271 558 TRP A N   
2032  C CA  . TRP A 257 ? 0.7706 1.1242 0.6236 0.3616  -0.0130 -0.0197 558 TRP A CA  
2033  C C   . TRP A 257 ? 0.7095 1.0274 0.5692 0.3482  -0.0086 -0.0127 558 TRP A C   
2034  O O   . TRP A 257 ? 0.7033 0.9743 0.5438 0.3560  -0.0080 -0.0072 558 TRP A O   
2035  C CB  . TRP A 257 ? 0.8463 1.1757 0.6757 0.3769  -0.0161 -0.0149 558 TRP A CB  
2036  C CG  . TRP A 257 ? 0.8139 1.1491 0.6532 0.3666  -0.0162 -0.0115 558 TRP A CG  
2037  C CD1 . TRP A 257 ? 0.9343 1.3115 0.7837 0.3643  -0.0186 -0.0169 558 TRP A CD1 
2038  C CD2 . TRP A 257 ? 0.8953 1.1935 0.7341 0.3574  -0.0141 -0.0021 558 TRP A CD2 
2039  N NE1 . TRP A 257 ? 1.0436 1.4121 0.8990 0.3546  -0.0182 -0.0118 558 TRP A NE1 
2040  C CE2 . TRP A 257 ? 0.9669 1.2879 0.8161 0.3505  -0.0154 -0.0024 558 TRP A CE2 
2041  C CE3 . TRP A 257 ? 0.8629 1.1114 0.6930 0.3539  -0.0114 0.0062  558 TRP A CE3 
2042  C CZ2 . TRP A 257 ? 0.8459 1.1424 0.6967 0.3411  -0.0143 0.0057  558 TRP A CZ2 
2043  C CZ3 . TRP A 257 ? 0.8697 1.0943 0.7017 0.3436  -0.0102 0.0146  558 TRP A CZ3 
2044  C CH2 . TRP A 257 ? 0.8600 1.1089 0.7020 0.3379  -0.0117 0.0144  558 TRP A CH2 
2045  N N   . PHE A 258 ? 0.6835 1.0213 0.5686 0.3280  -0.0055 -0.0131 559 PHE A N   
2046  C CA  . PHE A 258 ? 0.6690 0.9674 0.5562 0.3122  -0.0017 -0.0056 559 PHE A CA  
2047  C C   . PHE A 258 ? 0.6860 0.9603 0.5703 0.3073  0.0016  -0.0051 559 PHE A C   
2048  O O   . PHE A 258 ? 0.6711 0.8953 0.5407 0.3046  0.0027  0.0019  559 PHE A O   
2049  C CB  . PHE A 258 ? 0.6350 0.9536 0.5451 0.2847  0.0008  -0.0068 559 PHE A CB  
2050  C CG  . PHE A 258 ? 0.6683 0.9434 0.5749 0.2673  0.0030  0.0016  559 PHE A CG  
2051  C CD1 . PHE A 258 ? 0.6958 0.9661 0.6005 0.2641  0.0014  0.0052  559 PHE A CD1 
2052  C CD2 . PHE A 258 ? 0.6696 0.9108 0.5748 0.2543  0.0066  0.0055  559 PHE A CD2 
2053  C CE1 . PHE A 258 ? 0.6400 0.8735 0.5419 0.2486  0.0037  0.0125  559 PHE A CE1 
2054  C CE2 . PHE A 258 ? 0.6061 0.8115 0.5090 0.2388  0.0086  0.0126  559 PHE A CE2 
2055  C CZ  . PHE A 258 ? 0.6335 0.8352 0.5348 0.2361  0.0073  0.0161  559 PHE A CZ  
2056  N N   . LYS A 259 ? 0.5872 0.8980 0.4852 0.3057  0.0034  -0.0128 560 LYS A N   
2057  C CA  . LYS A 259 ? 0.6457 0.9391 0.5412 0.3024  0.0065  -0.0134 560 LYS A CA  
2058  C C   . LYS A 259 ? 0.7308 0.9820 0.5988 0.3251  0.0041  -0.0104 560 LYS A C   
2059  O O   . LYS A 259 ? 0.7261 0.9441 0.5868 0.3199  0.0062  -0.0084 560 LYS A O   
2060  C CB  . LYS A 259 ? 0.6540 0.9994 0.5658 0.3024  0.0084  -0.0226 560 LYS A CB  
2061  C CG  . LYS A 259 ? 0.6717 1.0473 0.5754 0.3194  0.0030  -0.0282 560 LYS A CG  
2062  C CD  . LYS A 259 ? 0.7613 1.1757 0.6743 0.3166  0.0039  -0.0358 560 LYS A CD  
2063  C CE  . LYS A 259 ? 0.7227 1.1654 0.6251 0.3335  -0.0021 -0.0415 560 LYS A CE  
2064  N NZ  . LYS A 259 ? 0.6765 1.1544 0.5891 0.3285  -0.0048 -0.0442 560 LYS A NZ  
2065  N N   . ASP A 260 ? 0.7075 0.9545 0.5570 0.3450  -0.0008 -0.0101 561 ASP A N   
2066  C CA  . ASP A 260 ? 0.8417 1.0423 0.6606 0.3620  -0.0034 -0.0071 561 ASP A CA  
2067  C C   . ASP A 260 ? 0.8434 0.9877 0.6479 0.3586  -0.0027 0.0029  561 ASP A C   
2068  O O   . ASP A 260 ? 0.8199 0.9191 0.5983 0.3687  -0.0041 0.0060  561 ASP A O   
2069  C CB  . ASP A 260 ? 0.9217 1.1344 0.7232 0.3807  -0.0083 -0.0099 561 ASP A CB  
2070  C CG  . ASP A 260 ? 1.0636 1.3354 0.8795 0.3828  -0.0097 -0.0194 561 ASP A CG  
2071  O OD1 . ASP A 260 ? 1.1496 1.4421 0.9800 0.3749  -0.0072 -0.0240 561 ASP A OD1 
2072  O OD2 . ASP A 260 ? 1.0543 1.3521 0.8666 0.3916  -0.0131 -0.0223 561 ASP A OD2 
2073  N N   . LEU A 261 ? 0.7520 0.8961 0.5713 0.3408  -0.0005 0.0078  562 LEU A N   
2074  C CA  . LEU A 261 ? 0.7509 0.8409 0.5569 0.3295  0.0008  0.0170  562 LEU A CA  
2075  C C   . LEU A 261 ? 0.9193 0.9802 0.7241 0.3172  0.0038  0.0171  562 LEU A C   
2076  O O   . LEU A 261 ? 1.0607 1.0723 0.8483 0.3140  0.0041  0.0235  562 LEU A O   
2077  C CB  . LEU A 261 ? 0.5278 0.6259 0.3489 0.3086  0.0025  0.0212  562 LEU A CB  
2078  C CG  . LEU A 261 ? 0.7065 0.8275 0.5250 0.3217  -0.0010 0.0216  562 LEU A CG  
2079  C CD1 . LEU A 261 ? 0.7349 0.8796 0.5745 0.3006  0.0007  0.0218  562 LEU A CD1 
2080  C CD2 . LEU A 261 ? 0.7678 0.8444 0.5570 0.3371  -0.0033 0.0301  562 LEU A CD2 
2081  N N   . GLY A 262 ? 0.8573 0.9482 0.6789 0.3105  0.0058  0.0102  563 GLY A N   
2082  C CA  . GLY A 262 ? 0.6771 0.7449 0.4969 0.3013  0.0082  0.0093  563 GLY A CA  
2083  C C   . GLY A 262 ? 0.8049 0.8600 0.6388 0.2724  0.0119  0.0134  563 GLY A C   
2084  O O   . GLY A 262 ? 0.8318 0.8585 0.6607 0.2641  0.0133  0.0143  563 GLY A O   
2085  N N   . LEU A 263 ? 0.7958 0.8713 0.6466 0.2574  0.0131  0.0154  564 LEU A N   
2086  C CA  . LEU A 263 ? 0.7458 0.8047 0.6067 0.2327  0.0159  0.0200  564 LEU A CA  
2087  C C   . LEU A 263 ? 0.7709 0.8575 0.6530 0.2159  0.0190  0.0158  564 LEU A C   
2088  O O   . LEU A 263 ? 0.6801 0.8080 0.5748 0.2183  0.0195  0.0099  564 LEU A O   
2089  C CB  . LEU A 263 ? 0.6500 0.7114 0.5156 0.2255  0.0156  0.0247  564 LEU A CB  
2090  C CG  . LEU A 263 ? 0.7223 0.7650 0.5677 0.2434  0.0125  0.0291  564 LEU A CG  
2091  C CD1 . LEU A 263 ? 0.6923 0.7541 0.5472 0.2373  0.0122  0.0311  564 LEU A CD1 
2092  C CD2 . LEU A 263 ? 0.7137 0.7029 0.5378 0.2435  0.0127  0.0362  564 LEU A CD2 
2093  N N   . LYS A 264 ? 0.8428 0.9059 0.7279 0.1985  0.0213  0.0189  565 LYS A N   
2094  C CA  . LYS A 264 ? 0.7079 0.7885 0.6110 0.1798  0.0243  0.0170  565 LYS A CA  
2095  C C   . LYS A 264 ? 0.7033 0.7572 0.6093 0.1615  0.0256  0.0228  565 LYS A C   
2096  O O   . LYS A 264 ? 0.7757 0.7970 0.6691 0.1632  0.0245  0.0276  565 LYS A O   
2097  C CB  . LYS A 264 ? 0.7301 0.8127 0.6308 0.1830  0.0255  0.0128  565 LYS A CB  
2098  C CG  . LYS A 264 ? 0.7263 0.7665 0.6080 0.1892  0.0242  0.0145  565 LYS A CG  
2099  C CD  . LYS A 264 ? 0.6276 0.6715 0.5081 0.1904  0.0254  0.0098  565 LYS A CD  
2100  C CE  . LYS A 264 ? 0.7687 0.7772 0.6268 0.2049  0.0230  0.0087  565 LYS A CE  
2101  N NZ  . LYS A 264 ? 0.8864 0.8786 0.7426 0.1955  0.0241  0.0072  565 LYS A NZ  
2102  N N   . TRP A 265 ? 0.6180 0.6864 0.5402 0.1440  0.0280  0.0223  566 TRP A N   
2103  C CA  . TRP A 265 ? 0.6606 0.7057 0.5857 0.1279  0.0291  0.0269  566 TRP A CA  
2104  C C   . TRP A 265 ? 0.6920 0.7435 0.6261 0.1156  0.0313  0.0252  566 TRP A C   
2105  O O   . TRP A 265 ? 0.7200 0.7983 0.6613 0.1161  0.0327  0.0211  566 TRP A O   
2106  C CB  . TRP A 265 ? 0.4255 0.4770 0.3595 0.1187  0.0292  0.0296  566 TRP A CB  
2107  C CG  . TRP A 265 ? 0.4560 0.4786 0.3867 0.1091  0.0295  0.0350  566 TRP A CG  
2108  C CD1 . TRP A 265 ? 0.4891 0.5105 0.4305 0.0933  0.0309  0.0367  566 TRP A CD1 
2109  C CD2 . TRP A 265 ? 0.4707 0.4618 0.3861 0.1144  0.0285  0.0393  566 TRP A CD2 
2110  N NE1 . TRP A 265 ? 0.4012 0.3957 0.3361 0.0888  0.0308  0.0414  566 TRP A NE1 
2111  C CE2 . TRP A 265 ? 0.4480 0.4233 0.3671 0.1004  0.0296  0.0432  566 TRP A CE2 
2112  C CE3 . TRP A 265 ? 0.5699 0.5436 0.4677 0.1298  0.0268  0.0402  566 TRP A CE3 
2113  C CZ2 . TRP A 265 ? 0.4768 0.4225 0.3840 0.0995  0.0295  0.0480  566 TRP A CZ2 
2114  C CZ3 . TRP A 265 ? 0.6701 0.6100 0.5543 0.1288  0.0266  0.0453  566 TRP A CZ3 
2115  C CH2 . TRP A 265 ? 0.7017 0.6290 0.5913 0.1128  0.0282  0.0492  566 TRP A CH2 
2116  N N   . TYR A 266 ? 0.5611 0.5887 0.4943 0.1047  0.0317  0.0286  567 TYR A N   
2117  C CA  . TYR A 266 ? 0.5096 0.5428 0.4514 0.0923  0.0336  0.0279  567 TYR A CA  
2118  C C   . TYR A 266 ? 0.5465 0.5981 0.5028 0.0796  0.0351  0.0285  567 TYR A C   
2119  O O   . TYR A 266 ? 0.6404 0.6944 0.6000 0.0782  0.0344  0.0300  567 TYR A O   
2120  C CB  . TYR A 266 ? 0.4218 0.4261 0.3581 0.0853  0.0331  0.0307  567 TYR A CB  
2121  C CG  . TYR A 266 ? 0.5573 0.5409 0.4907 0.0814  0.0321  0.0351  567 TYR A CG  
2122  C CD1 . TYR A 266 ? 0.6420 0.6258 0.5851 0.0685  0.0328  0.0378  567 TYR A CD1 
2123  C CD2 . TYR A 266 ? 0.6247 0.5879 0.5446 0.0907  0.0306  0.0367  567 TYR A CD2 
2124  C CE1 . TYR A 266 ? 0.6773 0.6451 0.6180 0.0649  0.0323  0.0416  567 TYR A CE1 
2125  C CE2 . TYR A 266 ? 0.6360 0.5811 0.5527 0.0859  0.0304  0.0412  567 TYR A CE2 
2126  C CZ  . TYR A 266 ? 0.7413 0.6906 0.6691 0.0729  0.0313  0.0434  567 TYR A CZ  
2127  O OH  . TYR A 266 ? 0.8255 0.7598 0.7505 0.0682  0.0315  0.0477  567 TYR A OH  
2128  N N   . GLY A 267 ? 0.5374 0.6008 0.5009 0.0703  0.0371  0.0274  568 GLY A N   
2129  C CA  . GLY A 267 ? 0.4423 0.5228 0.4177 0.0585  0.0387  0.0274  568 GLY A CA  
2130  C C   . GLY A 267 ? 0.4600 0.5242 0.4390 0.0459  0.0388  0.0310  568 GLY A C   
2131  O O   . GLY A 267 ? 0.5261 0.5992 0.5130 0.0366  0.0396  0.0310  568 GLY A O   
2132  N N   . LEU A 268 ? 0.4538 0.4948 0.4268 0.0455  0.0378  0.0335  569 LEU A N   
2133  C CA  . LEU A 268 ? 0.5386 0.5673 0.5147 0.0346  0.0379  0.0363  569 LEU A CA  
2134  C C   . LEU A 268 ? 0.5745 0.5833 0.5472 0.0351  0.0361  0.0390  569 LEU A C   
2135  O O   . LEU A 268 ? 0.5367 0.5299 0.5015 0.0393  0.0350  0.0395  569 LEU A O   
2136  C CB  . LEU A 268 ? 0.4975 0.5218 0.4705 0.0319  0.0386  0.0364  569 LEU A CB  
2137  C CG  . LEU A 268 ? 0.4910 0.5031 0.4659 0.0224  0.0381  0.0393  569 LEU A CG  
2138  C CD1 . LEU A 268 ? 0.4643 0.4866 0.4454 0.0133  0.0399  0.0401  569 LEU A CD1 
2139  C CD2 . LEU A 268 ? 0.3222 0.3242 0.2906 0.0232  0.0375  0.0393  569 LEU A CD2 
2140  N N   . PRO A 269 ? 0.5798 0.5886 0.5577 0.0306  0.0358  0.0404  570 PRO A N   
2141  C CA  . PRO A 269 ? 0.4923 0.4846 0.4678 0.0294  0.0347  0.0431  570 PRO A CA  
2142  C C   . PRO A 269 ? 0.5176 0.5009 0.4950 0.0218  0.0344  0.0445  570 PRO A C   
2143  O O   . PRO A 269 ? 0.4927 0.4817 0.4757 0.0157  0.0348  0.0444  570 PRO A O   
2144  C CB  . PRO A 269 ? 0.2692 0.2691 0.2498 0.0279  0.0348  0.0434  570 PRO A CB  
2145  C CG  . PRO A 269 ? 0.3466 0.3630 0.3342 0.0232  0.0357  0.0408  570 PRO A CG  
2146  C CD  . PRO A 269 ? 0.4908 0.5157 0.4763 0.0264  0.0366  0.0389  570 PRO A CD  
2147  N N   . ALA A 270 ? 0.5346 0.5036 0.5067 0.0221  0.0334  0.0455  571 ALA A N   
2148  C CA  . ALA A 270 ? 0.5621 0.5249 0.5356 0.0160  0.0325  0.0461  571 ALA A CA  
2149  C C   . ALA A 270 ? 0.5693 0.5194 0.5403 0.0140  0.0314  0.0476  571 ALA A C   
2150  O O   . ALA A 270 ? 0.6320 0.5711 0.5954 0.0164  0.0308  0.0471  571 ALA A O   
2151  C CB  . ALA A 270 ? 0.5102 0.4732 0.4798 0.0170  0.0324  0.0445  571 ALA A CB  
2152  N N   . VAL A 271 ? 0.4958 0.4474 0.4724 0.0095  0.0313  0.0490  572 VAL A N   
2153  C CA  . VAL A 271 ? 0.5028 0.4464 0.4781 0.0063  0.0309  0.0505  572 VAL A CA  
2154  C C   . VAL A 271 ? 0.4905 0.4310 0.4667 0.0016  0.0292  0.0496  572 VAL A C   
2155  O O   . VAL A 271 ? 0.5388 0.4857 0.5196 -0.0001 0.0283  0.0492  572 VAL A O   
2156  C CB  . VAL A 271 ? 0.5621 0.5120 0.5431 0.0046  0.0318  0.0520  572 VAL A CB  
2157  C CG1 . VAL A 271 ? 0.4903 0.4387 0.4739 -0.0010 0.0313  0.0530  572 VAL A CG1 
2158  C CG2 . VAL A 271 ? 0.5553 0.5035 0.5320 0.0089  0.0331  0.0534  572 VAL A CG2 
2159  N N   . SER A 272 ? 0.4028 0.3326 0.3734 -0.0007 0.0285  0.0493  573 SER A N   
2160  C CA  . SER A 272 ? 0.4829 0.4102 0.4530 -0.0051 0.0264  0.0475  573 SER A CA  
2161  C C   . SER A 272 ? 0.6836 0.6071 0.6542 -0.0123 0.0259  0.0478  573 SER A C   
2162  O O   . SER A 272 ? 0.7923 0.7138 0.7619 -0.0166 0.0239  0.0455  573 SER A O   
2163  C CB  . SER A 272 ? 0.5169 0.4351 0.4783 -0.0019 0.0254  0.0450  573 SER A CB  
2164  O OG  . SER A 272 ? 0.4450 0.3504 0.3975 0.0014  0.0263  0.0452  573 SER A OG  
2165  N N   . ASN A 273 ? 0.6338 0.5575 0.6058 -0.0142 0.0279  0.0504  574 ASN A N   
2166  C CA  . ASN A 273 ? 0.4325 0.3530 0.4041 -0.0225 0.0282  0.0510  574 ASN A CA  
2167  C C   . ASN A 273 ? 0.5044 0.4410 0.4862 -0.0260 0.0289  0.0520  574 ASN A C   
2168  O O   . ASN A 273 ? 0.5730 0.5108 0.5555 -0.0333 0.0301  0.0530  574 ASN A O   
2169  C CB  . ASN A 273 ? 0.4135 0.3180 0.3750 -0.0229 0.0304  0.0537  574 ASN A CB  
2170  C CG  . ASN A 273 ? 0.6087 0.5179 0.5712 -0.0176 0.0328  0.0570  574 ASN A CG  
2171  O OD1 . ASN A 273 ? 0.6604 0.5843 0.6315 -0.0143 0.0328  0.0567  574 ASN A OD1 
2172  N ND2 . ASN A 273 ? 0.5610 0.4564 0.5135 -0.0166 0.0346  0.0601  574 ASN A ND2 
2173  N N   . MET A 274 ? 0.4471 0.3959 0.4359 -0.0213 0.0282  0.0515  575 MET A N   
2174  C CA  . MET A 274 ? 0.4738 0.4377 0.4713 -0.0221 0.0285  0.0516  575 MET A CA  
2175  C C   . MET A 274 ? 0.6072 0.5809 0.6100 -0.0225 0.0254  0.0490  575 MET A C   
2176  O O   . MET A 274 ? 0.8065 0.7755 0.8062 -0.0216 0.0232  0.0474  575 MET A O   
2177  C CB  . MET A 274 ? 0.4496 0.4179 0.4495 -0.0157 0.0296  0.0526  575 MET A CB  
2178  C CG  . MET A 274 ? 0.5704 0.5339 0.5661 -0.0149 0.0325  0.0553  575 MET A CG  
2179  S SD  . MET A 274 ? 0.6010 0.5718 0.5996 -0.0081 0.0333  0.0551  575 MET A SD  
2180  C CE  . MET A 274 ? 0.5589 0.5446 0.5656 -0.0092 0.0334  0.0542  575 MET A CE  
2181  N N   . LEU A 275 ? 0.5532 0.5415 0.5634 -0.0227 0.0251  0.0485  576 LEU A N   
2182  C CA  . LEU A 275 ? 0.4795 0.4795 0.4945 -0.0223 0.0220  0.0459  576 LEU A CA  
2183  C C   . LEU A 275 ? 0.5395 0.5454 0.5573 -0.0141 0.0209  0.0457  576 LEU A C   
2184  O O   . LEU A 275 ? 0.5357 0.5473 0.5566 -0.0117 0.0226  0.0463  576 LEU A O   
2185  C CB  . LEU A 275 ? 0.4724 0.4868 0.4933 -0.0294 0.0223  0.0447  576 LEU A CB  
2186  C CG  . LEU A 275 ? 0.4597 0.4896 0.4859 -0.0298 0.0185  0.0412  576 LEU A CG  
2187  C CD1 . LEU A 275 ? 0.4334 0.4707 0.4620 -0.0412 0.0186  0.0394  576 LEU A CD1 
2188  C CD2 . LEU A 275 ? 0.3493 0.3965 0.3822 -0.0227 0.0176  0.0403  576 LEU A CD2 
2189  N N   . LEU A 276 ? 0.6125 0.6160 0.6280 -0.0097 0.0180  0.0449  577 LEU A N   
2190  C CA  . LEU A 276 ? 0.4920 0.4969 0.5076 -0.0020 0.0166  0.0449  577 LEU A CA  
2191  C C   . LEU A 276 ? 0.6012 0.6216 0.6216 0.0012  0.0137  0.0427  577 LEU A C   
2192  O O   . LEU A 276 ? 0.5791 0.6062 0.6004 -0.0008 0.0112  0.0411  577 LEU A O   
2193  C CB  . LEU A 276 ? 0.4697 0.4625 0.4784 0.0011  0.0154  0.0460  577 LEU A CB  
2194  C CG  . LEU A 276 ? 0.4769 0.4677 0.4830 0.0084  0.0134  0.0463  577 LEU A CG  
2195  C CD1 . LEU A 276 ? 0.3661 0.3529 0.3726 0.0104  0.0155  0.0466  577 LEU A CD1 
2196  C CD2 . LEU A 276 ? 0.2973 0.2769 0.2953 0.0099  0.0122  0.0480  577 LEU A CD2 
2197  N N   . GLU A 277 ? 0.6360 0.6639 0.6595 0.0067  0.0139  0.0420  578 GLU A N   
2198  C CA  . GLU A 277 ? 0.5509 0.5967 0.5794 0.0114  0.0113  0.0394  578 GLU A CA  
2199  C C   . GLU A 277 ? 0.5317 0.5725 0.5557 0.0228  0.0089  0.0390  578 GLU A C   
2200  O O   . GLU A 277 ? 0.5615 0.5973 0.5843 0.0264  0.0105  0.0390  578 GLU A O   
2201  C CB  . GLU A 277 ? 0.5161 0.5793 0.5525 0.0078  0.0139  0.0382  578 GLU A CB  
2202  C CG  . GLU A 277 ? 0.5377 0.6242 0.5805 0.0126  0.0114  0.0348  578 GLU A CG  
2203  C CD  . GLU A 277 ? 0.7328 0.8257 0.7765 0.0224  0.0117  0.0334  578 GLU A CD  
2204  O OE1 . GLU A 277 ? 0.7034 0.7985 0.7446 0.0336  0.0080  0.0315  578 GLU A OE1 
2205  O OE2 . GLU A 277 ? 0.8338 0.9287 0.8797 0.0195  0.0155  0.0340  578 GLU A OE2 
2206  N N   . ILE A 278 ? 0.5822 0.6234 0.6025 0.0285  0.0049  0.0385  579 ILE A N   
2207  C CA  . ILE A 278 ? 0.4723 0.5053 0.4853 0.0400  0.0020  0.0387  579 ILE A CA  
2208  C C   . ILE A 278 ? 0.5314 0.5839 0.5474 0.0481  -0.0022 0.0358  579 ILE A C   
2209  O O   . ILE A 278 ? 0.5866 0.6502 0.6053 0.0449  -0.0044 0.0349  579 ILE A O   
2210  C CB  . ILE A 278 ? 0.4936 0.5046 0.4956 0.0404  0.0012  0.0420  579 ILE A CB  
2211  C CG1 . ILE A 278 ? 0.6036 0.5999 0.6039 0.0322  0.0053  0.0443  579 ILE A CG1 
2212  C CG2 . ILE A 278 ? 0.5319 0.5305 0.5241 0.0515  -0.0015 0.0428  579 ILE A CG2 
2213  C CD1 . ILE A 278 ? 0.6838 0.6642 0.6753 0.0299  0.0053  0.0474  579 ILE A CD1 
2214  N N   . GLY A 279 ? 0.4788 0.5364 0.4940 0.0590  -0.0037 0.0337  580 GLY A N   
2215  C CA  . GLY A 279 ? 0.4104 0.4881 0.4278 0.0695  -0.0080 0.0305  580 GLY A CA  
2216  C C   . GLY A 279 ? 0.5250 0.6334 0.5551 0.0629  -0.0083 0.0274  580 GLY A C   
2217  O O   . GLY A 279 ? 0.5750 0.7004 0.6066 0.0687  -0.0127 0.0250  580 GLY A O   
2218  N N   . GLY A 280 ? 0.5772 0.6936 0.6159 0.0507  -0.0037 0.0272  581 GLY A N   
2219  C CA  . GLY A 280 ? 0.5444 0.6867 0.5941 0.0411  -0.0032 0.0247  581 GLY A CA  
2220  C C   . GLY A 280 ? 0.5699 0.7060 0.6184 0.0305  -0.0041 0.0256  581 GLY A C   
2221  O O   . GLY A 280 ? 0.6171 0.7712 0.6736 0.0202  -0.0036 0.0233  581 GLY A O   
2222  N N   . LEU A 281 ? 0.5320 0.6435 0.5704 0.0325  -0.0053 0.0286  582 LEU A N   
2223  C CA  . LEU A 281 ? 0.5720 0.6751 0.6079 0.0231  -0.0056 0.0293  582 LEU A CA  
2224  C C   . LEU A 281 ? 0.5520 0.6395 0.5875 0.0121  -0.0005 0.0318  582 LEU A C   
2225  O O   . LEU A 281 ? 0.5604 0.6352 0.5934 0.0142  0.0026  0.0343  582 LEU A O   
2226  C CB  . LEU A 281 ? 0.5185 0.6042 0.5429 0.0307  -0.0089 0.0316  582 LEU A CB  
2227  C CG  . LEU A 281 ? 0.4988 0.5967 0.5208 0.0444  -0.0142 0.0299  582 LEU A CG  
2228  C CD1 . LEU A 281 ? 0.5287 0.6058 0.5368 0.0523  -0.0168 0.0334  582 LEU A CD1 
2229  C CD2 . LEU A 281 ? 0.5395 0.6657 0.5697 0.0414  -0.0178 0.0251  582 LEU A CD2 
2230  N N   . GLU A 282 ? 0.4827 0.5707 0.5197 0.0008  0.0002  0.0309  583 GLU A N   
2231  C CA  . GLU A 282 ? 0.4861 0.5589 0.5213 -0.0087 0.0047  0.0331  583 GLU A CA  
2232  C C   . GLU A 282 ? 0.4921 0.5466 0.5190 -0.0114 0.0038  0.0339  583 GLU A C   
2233  O O   . GLU A 282 ? 0.4457 0.5047 0.4722 -0.0164 0.0013  0.0311  583 GLU A O   
2234  C CB  . GLU A 282 ? 0.4443 0.5307 0.4866 -0.0204 0.0069  0.0313  583 GLU A CB  
2235  C CG  . GLU A 282 ? 0.3998 0.5093 0.4511 -0.0193 0.0083  0.0301  583 GLU A CG  
2236  C CD  . GLU A 282 ? 0.4930 0.6158 0.5503 -0.0334 0.0108  0.0288  583 GLU A CD  
2237  O OE1 . GLU A 282 ? 0.5307 0.6564 0.5883 -0.0422 0.0088  0.0262  583 GLU A OE1 
2238  O OE2 . GLU A 282 ? 0.6073 0.7366 0.6682 -0.0366 0.0150  0.0304  583 GLU A OE2 
2239  N N   . PHE A 283 ? 0.3740 0.4093 0.3943 -0.0084 0.0060  0.0371  584 PHE A N   
2240  C CA  . PHE A 283 ? 0.3264 0.3453 0.3387 -0.0103 0.0061  0.0379  584 PHE A CA  
2241  C C   . PHE A 283 ? 0.3675 0.3761 0.3785 -0.0179 0.0097  0.0386  584 PHE A C   
2242  O O   . PHE A 283 ? 0.5042 0.5027 0.5129 -0.0162 0.0128  0.0412  584 PHE A O   
2243  C CB  . PHE A 283 ? 0.4378 0.4445 0.4437 -0.0028 0.0065  0.0409  584 PHE A CB  
2244  C CG  . PHE A 283 ? 0.4472 0.4588 0.4509 0.0054  0.0028  0.0410  584 PHE A CG  
2245  C CD1 . PHE A 283 ? 0.3994 0.4158 0.4055 0.0120  0.0024  0.0416  584 PHE A CD1 
2246  C CD2 . PHE A 283 ? 0.4032 0.4141 0.4011 0.0073  -0.0004 0.0405  584 PHE A CD2 
2247  C CE1 . PHE A 283 ? 0.4094 0.4279 0.4113 0.0210  -0.0012 0.0419  584 PHE A CE1 
2248  C CE2 . PHE A 283 ? 0.4108 0.4253 0.4049 0.0160  -0.0040 0.0411  584 PHE A CE2 
2249  C CZ  . PHE A 283 ? 0.4103 0.4276 0.4059 0.0231  -0.0045 0.0420  584 PHE A CZ  
2250  N N   . SER A 284 ? 0.3155 0.3259 0.3269 -0.0262 0.0091  0.0361  585 SER A N   
2251  C CA  . SER A 284 ? 0.4601 0.4587 0.4683 -0.0336 0.0123  0.0369  585 SER A CA  
2252  C C   . SER A 284 ? 0.4679 0.4469 0.4669 -0.0309 0.0135  0.0382  585 SER A C   
2253  O O   . SER A 284 ? 0.5500 0.5167 0.5443 -0.0348 0.0160  0.0392  585 SER A O   
2254  C CB  . SER A 284 ? 0.4579 0.4605 0.4668 -0.0441 0.0109  0.0334  585 SER A CB  
2255  O OG  . SER A 284 ? 0.5199 0.5221 0.5251 -0.0434 0.0068  0.0299  585 SER A OG  
2256  N N   . ALA A 285 ? 0.5224 0.4983 0.5176 -0.0243 0.0121  0.0383  586 ALA A N   
2257  C CA  . ALA A 285 ? 0.5238 0.4851 0.5108 -0.0214 0.0134  0.0390  586 ALA A CA  
2258  C C   . ALA A 285 ? 0.5431 0.5058 0.5297 -0.0142 0.0138  0.0413  586 ALA A C   
2259  O O   . ALA A 285 ? 0.7426 0.7093 0.7278 -0.0114 0.0114  0.0408  586 ALA A O   
2260  C CB  . ALA A 285 ? 0.6078 0.5628 0.5880 -0.0236 0.0110  0.0353  586 ALA A CB  
2261  N N   . CYS A 286 ? 0.4778 0.4368 0.4648 -0.0118 0.0169  0.0437  587 CYS A N   
2262  C CA  . CYS A 286 ? 0.5064 0.4671 0.4941 -0.0072 0.0177  0.0459  587 CYS A CA  
2263  C C   . CYS A 286 ? 0.6257 0.5815 0.6113 -0.0055 0.0208  0.0472  587 CYS A C   
2264  O O   . CYS A 286 ? 0.6550 0.6132 0.6439 -0.0043 0.0223  0.0486  587 CYS A O   
2265  C CB  . CYS A 286 ? 0.5083 0.4770 0.5025 -0.0062 0.0173  0.0467  587 CYS A CB  
2266  S SG  . CYS A 286 ? 0.5444 0.5161 0.5438 -0.0091 0.0199  0.0471  587 CYS A SG  
2267  N N   . PRO A 287 ? 0.5921 0.5420 0.5720 -0.0048 0.0217  0.0463  588 PRO A N   
2268  C CA  . PRO A 287 ? 0.3474 0.2957 0.3260 -0.0023 0.0244  0.0470  588 PRO A CA  
2269  C C   . PRO A 287 ? 0.4605 0.4142 0.4416 -0.0011 0.0257  0.0485  588 PRO A C   
2270  O O   . PRO A 287 ? 0.5694 0.5241 0.5490 -0.0013 0.0251  0.0491  588 PRO A O   
2271  C CB  . PRO A 287 ? 0.4070 0.3501 0.3781 0.0001  0.0244  0.0451  588 PRO A CB  
2272  C CG  . PRO A 287 ? 0.5847 0.5273 0.5534 -0.0014 0.0219  0.0437  588 PRO A CG  
2273  C CD  . PRO A 287 ? 0.5876 0.5334 0.5617 -0.0051 0.0199  0.0440  588 PRO A CD  
2274  N N   . PHE A 288 ? 0.5075 0.4638 0.4914 -0.0002 0.0275  0.0490  589 PHE A N   
2275  C CA  . PHE A 288 ? 0.4065 0.3675 0.3927 -0.0005 0.0289  0.0495  589 PHE A CA  
2276  C C   . PHE A 288 ? 0.4411 0.4068 0.4272 0.0017  0.0309  0.0487  589 PHE A C   
2277  O O   . PHE A 288 ? 0.4821 0.4461 0.4666 0.0044  0.0311  0.0484  589 PHE A O   
2278  C CB  . PHE A 288 ? 0.4795 0.4415 0.4701 -0.0015 0.0282  0.0500  589 PHE A CB  
2279  C CG  . PHE A 288 ? 0.6290 0.5926 0.6228 -0.0009 0.0284  0.0499  589 PHE A CG  
2280  C CD1 . PHE A 288 ? 0.5329 0.5001 0.5282 0.0004  0.0299  0.0496  589 PHE A CD1 
2281  C CD2 . PHE A 288 ? 0.5655 0.5285 0.5607 -0.0020 0.0271  0.0500  589 PHE A CD2 
2282  C CE1 . PHE A 288 ? 0.4225 0.3909 0.4193 0.0009  0.0304  0.0501  589 PHE A CE1 
2283  C CE2 . PHE A 288 ? 0.4980 0.4631 0.4954 -0.0027 0.0279  0.0505  589 PHE A CE2 
2284  C CZ  . PHE A 288 ? 0.4704 0.4374 0.4681 -0.0010 0.0297  0.0508  589 PHE A CZ  
2285  N N   . SER A 289 ? 0.4123 0.3841 0.3995 0.0003  0.0322  0.0484  590 SER A N   
2286  C CA  . SER A 289 ? 0.4634 0.4441 0.4508 0.0025  0.0340  0.0469  590 SER A CA  
2287  C C   . SER A 289 ? 0.5504 0.5385 0.5415 -0.0016 0.0351  0.0461  590 SER A C   
2288  O O   . SER A 289 ? 0.3886 0.3724 0.3794 -0.0063 0.0351  0.0471  590 SER A O   
2289  C CB  . SER A 289 ? 0.5169 0.5006 0.4999 0.0046  0.0348  0.0461  590 SER A CB  
2290  O OG  . SER A 289 ? 0.5540 0.5395 0.5364 -0.0002 0.0357  0.0470  590 SER A OG  
2291  N N   . GLY A 290 ? 0.5442 0.5424 0.5377 0.0002  0.0359  0.0442  591 GLY A N   
2292  C CA  . GLY A 290 ? 0.4808 0.4881 0.4777 -0.0047 0.0370  0.0424  591 GLY A CA  
2293  C C   . GLY A 290 ? 0.5563 0.5805 0.5547 -0.0021 0.0383  0.0398  591 GLY A C   
2294  O O   . GLY A 290 ? 0.7447 0.7748 0.7410 -0.0010 0.0396  0.0396  591 GLY A O   
2295  N N   . TRP A 291 ? 0.4410 0.4747 0.4427 -0.0004 0.0379  0.0375  592 TRP A N   
2296  C CA  . TRP A 291 ? 0.4515 0.5029 0.4542 0.0051  0.0383  0.0348  592 TRP A CA  
2297  C C   . TRP A 291 ? 0.5533 0.6062 0.5560 0.0114  0.0367  0.0341  592 TRP A C   
2298  O O   . TRP A 291 ? 0.5346 0.5784 0.5380 0.0095  0.0358  0.0351  592 TRP A O   
2299  C CB  . TRP A 291 ? 0.3950 0.4653 0.4025 -0.0018 0.0400  0.0315  592 TRP A CB  
2300  C CG  . TRP A 291 ? 0.5270 0.5952 0.5378 -0.0107 0.0396  0.0300  592 TRP A CG  
2301  C CD1 . TRP A 291 ? 0.5558 0.6314 0.5697 -0.0104 0.0382  0.0269  592 TRP A CD1 
2302  C CD2 . TRP A 291 ? 0.5350 0.5907 0.5445 -0.0206 0.0404  0.0315  592 TRP A CD2 
2303  N NE1 . TRP A 291 ? 0.5909 0.6589 0.6057 -0.0198 0.0380  0.0257  592 TRP A NE1 
2304  C CE2 . TRP A 291 ? 0.6047 0.6593 0.6164 -0.0260 0.0394  0.0288  592 TRP A CE2 
2305  C CE3 . TRP A 291 ? 0.5125 0.5566 0.5179 -0.0248 0.0416  0.0349  592 TRP A CE3 
2306  C CZ2 . TRP A 291 ? 0.6584 0.6985 0.6673 -0.0351 0.0395  0.0293  592 TRP A CZ2 
2307  C CZ3 . TRP A 291 ? 0.5665 0.5973 0.5693 -0.0335 0.0419  0.0361  592 TRP A CZ3 
2308  C CH2 . TRP A 291 ? 0.7021 0.7299 0.7063 -0.0385 0.0408  0.0333  592 TRP A CH2 
2309  N N   . TYR A 292 ? 0.5676 0.6333 0.5690 0.0198  0.0365  0.0324  593 TYR A N   
2310  C CA  . TYR A 292 ? 0.4867 0.5530 0.4852 0.0280  0.0350  0.0326  593 TYR A CA  
2311  C C   . TYR A 292 ? 0.4211 0.5025 0.4250 0.0253  0.0342  0.0291  593 TYR A C   
2312  O O   . TYR A 292 ? 0.5585 0.6582 0.5679 0.0204  0.0346  0.0251  593 TYR A O   
2313  C CB  . TYR A 292 ? 0.4867 0.5598 0.4796 0.0399  0.0346  0.0320  593 TYR A CB  
2314  C CG  . TYR A 292 ? 0.6440 0.6958 0.6275 0.0464  0.0342  0.0358  593 TYR A CG  
2315  C CD1 . TYR A 292 ? 0.7382 0.7882 0.7163 0.0526  0.0345  0.0352  593 TYR A CD1 
2316  C CD2 . TYR A 292 ? 0.6389 0.6730 0.6184 0.0461  0.0337  0.0395  593 TYR A CD2 
2317  C CE1 . TYR A 292 ? 0.6766 0.7049 0.6447 0.0579  0.0339  0.0380  593 TYR A CE1 
2318  C CE2 . TYR A 292 ? 0.6843 0.6983 0.6547 0.0501  0.0335  0.0427  593 TYR A CE2 
2319  C CZ  . TYR A 292 ? 0.7097 0.7197 0.6741 0.0558  0.0334  0.0418  593 TYR A CZ  
2320  O OH  . TYR A 292 ? 0.8365 0.8243 0.7907 0.0589  0.0330  0.0444  593 TYR A OH  
2321  N N   . MET A 293 ? 0.3912 0.4657 0.3931 0.0279  0.0331  0.0304  594 MET A N   
2322  C CA  . MET A 293 ? 0.3258 0.4155 0.3293 0.0309  0.0317  0.0272  594 MET A CA  
2323  C C   . MET A 293 ? 0.4276 0.5244 0.4248 0.0441  0.0307  0.0280  594 MET A C   
2324  O O   . MET A 293 ? 0.5192 0.6001 0.5085 0.0508  0.0310  0.0323  594 MET A O   
2325  C CB  . MET A 293 ? 0.4416 0.5215 0.4444 0.0289  0.0311  0.0284  594 MET A CB  
2326  C CG  . MET A 293 ? 0.5318 0.6272 0.5361 0.0310  0.0295  0.0244  594 MET A CG  
2327  S SD  . MET A 293 ? 0.5441 0.6271 0.5480 0.0270  0.0293  0.0250  594 MET A SD  
2328  C CE  . MET A 293 ? 0.4734 0.5419 0.4684 0.0360  0.0303  0.0324  594 MET A CE  
2329  N N   . GLY A 294 ? 0.3866 0.5068 0.3865 0.0481  0.0294  0.0235  595 GLY A N   
2330  C CA  . GLY A 294 ? 0.4712 0.6008 0.4647 0.0623  0.0282  0.0235  595 GLY A CA  
2331  C C   . GLY A 294 ? 0.6122 0.7237 0.5941 0.0725  0.0274  0.0289  595 GLY A C   
2332  O O   . GLY A 294 ? 0.6351 0.7379 0.6075 0.0833  0.0272  0.0316  595 GLY A O   
2333  N N   . THR A 295 ? 0.5714 0.6760 0.5528 0.0691  0.0273  0.0306  596 THR A N   
2334  C CA  . THR A 295 ? 0.5419 0.6324 0.5117 0.0779  0.0270  0.0359  596 THR A CA  
2335  C C   . THR A 295 ? 0.5156 0.5784 0.4768 0.0786  0.0286  0.0421  596 THR A C   
2336  O O   . THR A 295 ? 0.5590 0.6081 0.5076 0.0875  0.0285  0.0469  596 THR A O   
2337  C CB  . THR A 295 ? 0.5463 0.6362 0.5179 0.0729  0.0271  0.0362  596 THR A CB  
2338  O OG1 . THR A 295 ? 0.5982 0.6801 0.5778 0.0601  0.0285  0.0355  596 THR A OG1 
2339  C CG2 . THR A 295 ? 0.4213 0.5370 0.3969 0.0757  0.0247  0.0304  596 THR A CG2 
2340  N N   . GLU A 296 ? 0.5254 0.5785 0.4921 0.0689  0.0301  0.0422  597 GLU A N   
2341  C CA  . GLU A 296 ? 0.4305 0.4588 0.3897 0.0682  0.0313  0.0471  597 GLU A CA  
2342  C C   . GLU A 296 ? 0.5570 0.5783 0.5052 0.0798  0.0306  0.0482  597 GLU A C   
2343  O O   . GLU A 296 ? 0.5920 0.5913 0.5279 0.0839  0.0309  0.0529  597 GLU A O   
2344  C CB  . GLU A 296 ? 0.5428 0.5661 0.5100 0.0572  0.0324  0.0461  597 GLU A CB  
2345  C CG  . GLU A 296 ? 0.5240 0.5514 0.5007 0.0468  0.0329  0.0448  597 GLU A CG  
2346  C CD  . GLU A 296 ? 0.6208 0.6423 0.6033 0.0379  0.0335  0.0441  597 GLU A CD  
2347  O OE1 . GLU A 296 ? 0.5952 0.6008 0.5743 0.0356  0.0341  0.0473  597 GLU A OE1 
2348  O OE2 . GLU A 296 ? 0.5432 0.5760 0.5329 0.0328  0.0334  0.0405  597 GLU A OE2 
2349  N N   . ILE A 297 ? 0.5840 0.6236 0.5358 0.0850  0.0295  0.0435  598 ILE A N   
2350  C CA  . ILE A 297 ? 0.6297 0.6657 0.5706 0.0986  0.0284  0.0434  598 ILE A CA  
2351  C C   . ILE A 297 ? 0.6705 0.7133 0.6025 0.1123  0.0266  0.0442  598 ILE A C   
2352  O O   . ILE A 297 ? 0.6778 0.7026 0.5942 0.1239  0.0258  0.0477  598 ILE A O   
2353  C CB  . ILE A 297 ? 0.6097 0.6662 0.5583 0.0993  0.0284  0.0377  598 ILE A CB  
2354  C CG1 . ILE A 297 ? 0.5139 0.5676 0.4721 0.0848  0.0303  0.0370  598 ILE A CG1 
2355  C CG2 . ILE A 297 ? 0.4640 0.5139 0.4007 0.1135  0.0275  0.0372  598 ILE A CG2 
2356  C CD1 . ILE A 297 ? 0.5201 0.6009 0.4899 0.0800  0.0310  0.0316  598 ILE A CD1 
2357  N N   . GLY A 298 ? 0.7273 0.7952 0.6680 0.1112  0.0256  0.0408  599 GLY A N   
2358  C CA  . GLY A 298 ? 0.8148 0.8968 0.7487 0.1252  0.0232  0.0400  599 GLY A CA  
2359  C C   . GLY A 298 ? 0.8451 0.9080 0.7661 0.1297  0.0231  0.0465  599 GLY A C   
2360  O O   . GLY A 298 ? 0.7376 0.7922 0.6433 0.1446  0.0216  0.0496  599 GLY A O   
2361  N N   . VAL A 299 ? 0.8377 0.8932 0.7637 0.1174  0.0249  0.0488  600 VAL A N   
2362  C CA  . VAL A 299 ? 0.7296 0.7689 0.6442 0.1196  0.0257  0.0553  600 VAL A CA  
2363  C C   . VAL A 299 ? 0.8004 0.8056 0.7036 0.1166  0.0280  0.0622  600 VAL A C   
2364  O O   . VAL A 299 ? 0.6265 0.6125 0.5120 0.1260  0.0279  0.0680  600 VAL A O   
2365  C CB  . VAL A 299 ? 0.7012 0.7520 0.6266 0.1087  0.0265  0.0536  600 VAL A CB  
2366  C CG1 . VAL A 299 ? 0.5920 0.6291 0.5057 0.1108  0.0278  0.0603  600 VAL A CG1 
2367  C CG2 . VAL A 299 ? 0.7340 0.8171 0.6697 0.1104  0.0240  0.0461  600 VAL A CG2 
2368  N N   . ARG A 300 ? 0.7953 0.7921 0.7072 0.1036  0.0298  0.0616  601 ARG A N   
2369  C CA  . ARG A 300 ? 0.8253 0.7929 0.7289 0.0974  0.0320  0.0674  601 ARG A CA  
2370  C C   . ARG A 300 ? 0.7917 0.7394 0.6834 0.1043  0.0313  0.0683  601 ARG A C   
2371  O O   . ARG A 300 ? 0.7079 0.6302 0.5824 0.1090  0.0318  0.0739  601 ARG A O   
2372  C CB  . ARG A 300 ? 0.8087 0.7773 0.7262 0.0816  0.0337  0.0660  601 ARG A CB  
2373  C CG  . ARG A 300 ? 0.7158 0.7025 0.6450 0.0748  0.0342  0.0639  601 ARG A CG  
2374  C CD  . ARG A 300 ? 0.6834 0.6672 0.6041 0.0775  0.0354  0.0687  601 ARG A CD  
2375  N NE  . ARG A 300 ? 0.6416 0.5997 0.5488 0.0759  0.0377  0.0760  601 ARG A NE  
2376  C CZ  . ARG A 300 ? 0.5080 0.4564 0.4180 0.0644  0.0402  0.0787  601 ARG A CZ  
2377  N NH1 . ARG A 300 ? 0.3935 0.3548 0.3185 0.0553  0.0406  0.0748  601 ARG A NH1 
2378  N NH2 . ARG A 300 ? 0.4867 0.4122 0.3835 0.0621  0.0424  0.0852  601 ARG A NH2 
2379  N N   . ASP A 301 ? 0.8669 0.8246 0.7665 0.1046  0.0303  0.0628  602 ASP A N   
2380  C CA  . ASP A 301 ? 0.8431 0.7824 0.7322 0.1106  0.0296  0.0626  602 ASP A CA  
2381  C C   . ASP A 301 ? 0.8970 0.8288 0.7686 0.1289  0.0276  0.0639  602 ASP A C   
2382  O O   . ASP A 301 ? 0.9406 0.8428 0.7949 0.1340  0.0275  0.0675  602 ASP A O   
2383  C CB  . ASP A 301 ? 0.7503 0.7063 0.6518 0.1078  0.0292  0.0562  602 ASP A CB  
2384  C CG  . ASP A 301 ? 0.6926 0.6470 0.6062 0.0915  0.0308  0.0558  602 ASP A CG  
2385  O OD1 . ASP A 301 ? 0.6766 0.6088 0.5847 0.0845  0.0319  0.0599  602 ASP A OD1 
2386  O OD2 . ASP A 301 ? 0.6357 0.6111 0.5636 0.0856  0.0310  0.0516  602 ASP A OD2 
2387  N N   . TYR A 302 ? 0.8638 0.8217 0.7389 0.1392  0.0258  0.0609  603 TYR A N   
2388  C CA  . TYR A 302 ? 0.9076 0.8629 0.7666 0.1592  0.0233  0.0613  603 TYR A CA  
2389  C C   . TYR A 302 ? 0.8293 0.7689 0.6719 0.1663  0.0231  0.0683  603 TYR A C   
2390  O O   . TYR A 302 ? 0.6940 0.6171 0.5168 0.1826  0.0213  0.0709  603 TYR A O   
2391  C CB  . TYR A 302 ? 0.8870 0.8814 0.7572 0.1679  0.0211  0.0542  603 TYR A CB  
2392  C CG  . TYR A 302 ? 0.8247 0.8331 0.7052 0.1659  0.0212  0.0479  603 TYR A CG  
2393  C CD1 . TYR A 302 ? 0.7622 0.8091 0.6566 0.1682  0.0202  0.0409  603 TYR A CD1 
2394  C CD2 . TYR A 302 ? 0.7777 0.7618 0.6535 0.1610  0.0225  0.0487  603 TYR A CD2 
2395  C CE1 . TYR A 302 ? 0.7446 0.8055 0.6477 0.1659  0.0209  0.0356  603 TYR A CE1 
2396  C CE2 . TYR A 302 ? 0.7688 0.7665 0.6531 0.1596  0.0228  0.0431  603 TYR A CE2 
2397  C CZ  . TYR A 302 ? 0.7559 0.7922 0.6537 0.1621  0.0223  0.0369  603 TYR A CZ  
2398  O OH  . TYR A 302 ? 0.8104 0.8619 0.7161 0.1603  0.0231  0.0317  603 TYR A OH  
2399  N N   . CYS A 303 ? 0.8431 0.7869 0.6921 0.1554  0.0249  0.0714  604 CYS A N   
2400  C CA  . CYS A 303 ? 0.9255 0.8656 0.7615 0.1636  0.0245  0.0769  604 CYS A CA  
2401  C C   . CYS A 303 ? 0.8411 0.7529 0.6666 0.1538  0.0278  0.0855  604 CYS A C   
2402  O O   . CYS A 303 ? 0.7872 0.6840 0.5940 0.1631  0.0278  0.0919  604 CYS A O   
2403  C CB  . CYS A 303 ? 0.8209 0.7987 0.6718 0.1637  0.0231  0.0721  604 CYS A CB  
2404  S SG  . CYS A 303 ? 0.7840 0.7971 0.6419 0.1787  0.0190  0.0631  604 CYS A SG  
2405  N N   . ASP A 304 ? 0.8322 0.7370 0.6683 0.1358  0.0307  0.0860  605 ASP A N   
2406  C CA  . ASP A 304 ? 0.7734 0.6505 0.5983 0.1262  0.0341  0.0940  605 ASP A CA  
2407  C C   . ASP A 304 ? 0.8511 0.6914 0.6502 0.1353  0.0339  0.0999  605 ASP A C   
2408  O O   . ASP A 304 ? 0.8916 0.7223 0.6855 0.1431  0.0318  0.0966  605 ASP A O   
2409  C CB  . ASP A 304 ? 0.7892 0.6635 0.6283 0.1073  0.0366  0.0925  605 ASP A CB  
2410  C CG  . ASP A 304 ? 0.8356 0.7385 0.6954 0.0975  0.0375  0.0889  605 ASP A CG  
2411  O OD1 . ASP A 304 ? 0.9274 0.8540 0.7927 0.1044  0.0358  0.0859  605 ASP A OD1 
2412  O OD2 . ASP A 304 ? 0.7276 0.6288 0.5975 0.0832  0.0396  0.0886  605 ASP A OD2 
2413  N N   . ASN A 305 ? 0.8748 0.6939 0.6562 0.1350  0.0362  0.1086  606 ASN A N   
2414  C CA  . ASN A 305 ? 0.9713 0.7514 0.7249 0.1440  0.0360  0.1149  606 ASN A CA  
2415  C C   . ASN A 305 ? 1.0608 0.8125 0.8109 0.1325  0.0373  0.1147  606 ASN A C   
2416  O O   . ASN A 305 ? 1.0875 0.8106 0.8186 0.1421  0.0355  0.1154  606 ASN A O   
2417  C CB  . ASN A 305 ? 1.1616 0.9243 0.8963 0.1440  0.0388  0.1252  606 ASN A CB  
2418  C CG  . ASN A 305 ? 1.2521 1.0366 0.9826 0.1611  0.0363  0.1258  606 ASN A CG  
2419  O OD1 . ASN A 305 ? 1.2722 1.0483 0.9857 0.1809  0.0329  0.1264  606 ASN A OD1 
2420  N ND2 . ASN A 305 ? 1.1819 0.9950 0.9274 0.1542  0.0378  0.1249  606 ASN A ND2 
2421  N N   . SER A 306 ? 1.1243 0.8838 0.8918 0.1129  0.0399  0.1130  607 SER A N   
2422  C CA  . SER A 306 ? 1.2551 0.9929 1.0222 0.1007  0.0407  0.1115  607 SER A CA  
2423  C C   . SER A 306 ? 1.2082 0.9598 0.9886 0.1044  0.0376  0.1022  607 SER A C   
2424  O O   . SER A 306 ? 1.2171 0.9529 0.9973 0.0957  0.0376  0.0999  607 SER A O   
2425  C CB  . SER A 306 ? 1.3456 1.0892 1.1260 0.0790  0.0446  0.1133  607 SER A CB  
2426  O OG  . SER A 306 ? 1.4078 1.1452 1.1785 0.0746  0.0481  0.1216  607 SER A OG  
2427  N N   . ARG A 307 ? 1.1866 0.9681 0.9782 0.1162  0.0350  0.0968  608 ARG A N   
2428  C CA  . ARG A 307 ? 1.0227 0.8212 0.8271 0.1197  0.0326  0.0883  608 ARG A CA  
2429  C C   . ARG A 307 ? 0.9992 0.7939 0.7893 0.1413  0.0292  0.0861  608 ARG A C   
2430  O O   . ARG A 307 ? 1.0173 0.7792 0.7834 0.1499  0.0287  0.0907  608 ARG A O   
2431  C CB  . ARG A 307 ? 0.8779 0.7151 0.7080 0.1127  0.0329  0.0837  608 ARG A CB  
2432  C CG  . ARG A 307 ? 0.8753 0.7157 0.7179 0.0936  0.0359  0.0858  608 ARG A CG  
2433  C CD  . ARG A 307 ? 0.9274 0.7563 0.7754 0.0809  0.0365  0.0834  608 ARG A CD  
2434  N NE  . ARG A 307 ? 0.8547 0.6917 0.7083 0.0864  0.0341  0.0767  608 ARG A NE  
2435  C CZ  . ARG A 307 ? 0.7266 0.5923 0.5983 0.0851  0.0333  0.0712  608 ARG A CZ  
2436  N NH1 . ARG A 307 ? 0.5711 0.4591 0.4573 0.0790  0.0343  0.0709  608 ARG A NH1 
2437  N NH2 . ARG A 307 ? 0.8005 0.6718 0.6748 0.0900  0.0317  0.0659  608 ARG A NH2 
2438  N N   . TYR A 308 ? 0.8592 0.6854 0.6622 0.1503  0.0270  0.0791  609 TYR A N   
2439  C CA  . TYR A 308 ? 0.8890 0.7146 0.6795 0.1712  0.0239  0.0759  609 TYR A CA  
2440  C C   . TYR A 308 ? 0.9785 0.8038 0.7537 0.1884  0.0221  0.0799  609 TYR A C   
2441  O O   . TYR A 308 ? 1.2045 1.0176 0.9620 0.2073  0.0195  0.0792  609 TYR A O   
2442  C CB  . TYR A 308 ? 0.9040 0.7669 0.7138 0.1744  0.0225  0.0670  609 TYR A CB  
2443  C CG  . TYR A 308 ? 0.8817 0.7345 0.6924 0.1710  0.0224  0.0624  609 TYR A CG  
2444  C CD1 . TYR A 308 ? 0.8690 0.7249 0.6952 0.1520  0.0245  0.0609  609 TYR A CD1 
2445  C CD2 . TYR A 308 ? 0.8187 0.6587 0.6136 0.1879  0.0201  0.0594  609 TYR A CD2 
2446  C CE1 . TYR A 308 ? 0.7586 0.6062 0.5848 0.1494  0.0242  0.0567  609 TYR A CE1 
2447  C CE2 . TYR A 308 ? 0.7260 0.5574 0.5209 0.1854  0.0200  0.0547  609 TYR A CE2 
2448  C CZ  . TYR A 308 ? 0.8537 0.6889 0.6643 0.1657  0.0220  0.0535  609 TYR A CZ  
2449  O OH  . TYR A 308 ? 0.9116 0.7389 0.7214 0.1635  0.0217  0.0487  609 TYR A OH  
2450  N N   . ASN A 309 ? 0.9446 0.7848 0.7259 0.1837  0.0233  0.0835  610 ASN A N   
2451  C CA  . ASN A 309 ? 0.9331 0.7656 0.6963 0.1973  0.0223  0.0896  610 ASN A CA  
2452  C C   . ASN A 309 ? 0.8982 0.7449 0.6524 0.2222  0.0180  0.0857  610 ASN A C   
2453  O O   . ASN A 309 ? 0.8042 0.6235 0.5327 0.2389  0.0161  0.0898  610 ASN A O   
2454  C CB  . ASN A 309 ? 0.9032 0.6875 0.6412 0.1940  0.0244  0.0991  610 ASN A CB  
2455  C CG  . ASN A 309 ? 0.9921 0.7666 0.7112 0.2041  0.0244  0.1073  610 ASN A CG  
2456  O OD1 . ASN A 309 ? 1.0773 0.8827 0.8062 0.2076  0.0237  0.1064  610 ASN A OD1 
2457  N ND2 . ASN A 309 ? 1.0049 0.7351 0.6955 0.2088  0.0252  0.1152  610 ASN A ND2 
2458  N N   . ILE A 310 ? 0.8611 0.7519 0.6361 0.2247  0.0162  0.0777  611 ILE A N   
2459  C CA  . ILE A 310 ? 0.9721 0.8850 0.7430 0.2470  0.0122  0.0723  611 ILE A CA  
2460  C C   . ILE A 310 ? 0.9789 0.9220 0.7524 0.2564  0.0100  0.0721  611 ILE A C   
2461  O O   . ILE A 310 ? 1.0169 0.9891 0.7922 0.2732  0.0064  0.0662  611 ILE A O   
2462  C CB  . ILE A 310 ? 0.9782 0.9213 0.7690 0.2448  0.0116  0.0625  611 ILE A CB  
2463  C CG1 . ILE A 310 ? 0.9333 0.9090 0.7523 0.2247  0.0137  0.0585  611 ILE A CG1 
2464  C CG2 . ILE A 310 ? 1.0109 0.9244 0.7946 0.2414  0.0128  0.0619  611 ILE A CG2 
2465  C CD1 . ILE A 310 ? 0.8779 0.8925 0.7159 0.2249  0.0129  0.0491  611 ILE A CD1 
2466  N N   . LEU A 311 ? 0.9744 0.9140 0.7487 0.2461  0.0119  0.0777  612 LEU A N   
2467  C CA  . LEU A 311 ? 0.8891 0.8563 0.6641 0.2554  0.0095  0.0774  612 LEU A CA  
2468  C C   . LEU A 311 ? 1.0059 0.9623 0.7550 0.2821  0.0057  0.0807  612 LEU A C   
2469  O O   . LEU A 311 ? 1.0179 1.0084 0.7700 0.2975  0.0017  0.0755  612 LEU A O   
2470  C CB  . LEU A 311 ? 0.6877 0.6471 0.4637 0.2409  0.0126  0.0837  612 LEU A CB  
2471  C CG  . LEU A 311 ? 0.5780 0.5583 0.3806 0.2182  0.0153  0.0793  612 LEU A CG  
2472  C CD1 . LEU A 311 ? 0.4939 0.4602 0.2919 0.2074  0.0184  0.0866  612 LEU A CD1 
2473  C CD2 . LEU A 311 ? 0.5127 0.5406 0.3354 0.2197  0.0124  0.0697  612 LEU A CD2 
2474  N N   . GLU A 312 ? 1.0363 0.9450 0.7588 0.2877  0.0068  0.0894  613 GLU A N   
2475  C CA  . GLU A 312 ? 1.0905 0.9839 0.7872 0.3107  0.0039  0.0915  613 GLU A CA  
2476  C C   . GLU A 312 ? 1.0649 0.9825 0.7660 0.3267  0.0004  0.0810  613 GLU A C   
2477  O O   . GLU A 312 ? 1.0361 0.9771 0.7330 0.3426  -0.0024 0.0760  613 GLU A O   
2478  C CB  . GLU A 312 ? 1.2438 1.0804 0.9158 0.3053  0.0072  0.0990  613 GLU A CB  
2479  C CG  . GLU A 312 ? 1.3297 1.1450 0.9762 0.3180  0.0068  0.1023  613 GLU A CG  
2480  C CD  . GLU A 312 ? 1.3726 1.1334 0.9974 0.3072  0.0105  0.1111  613 GLU A CD  
2481  O OE1 . GLU A 312 ? 1.3487 1.0966 0.9792 0.2874  0.0143  0.1176  613 GLU A OE1 
2482  O OE2 . GLU A 312 ? 1.3574 1.0892 0.9594 0.3182  0.0097  0.1111  613 GLU A OE2 
2483  N N   . GLU A 313 ? 1.0223 0.9374 0.7325 0.3223  0.0008  0.0771  614 GLU A N   
2484  C CA  . GLU A 313 ? 1.0282 0.9648 0.7413 0.3366  -0.0019 0.0671  614 GLU A CA  
2485  C C   . GLU A 313 ? 0.8385 0.8360 0.5752 0.3414  -0.0046 0.0587  614 GLU A C   
2486  O O   . GLU A 313 ? 0.7567 0.7791 0.4911 0.3567  -0.0071 0.0510  614 GLU A O   
2487  C CB  . GLU A 313 ? 1.0084 0.9287 0.7267 0.3291  -0.0004 0.0652  614 GLU A CB  
2488  C CG  . GLU A 313 ? 1.1027 0.9985 0.8012 0.3418  -0.0013 0.0611  614 GLU A CG  
2489  C CD  . GLU A 313 ? 1.2343 1.1704 0.9458 0.3527  -0.0035 0.0501  614 GLU A CD  
2490  O OE1 . GLU A 313 ? 1.3116 1.2892 1.0304 0.3632  -0.0058 0.0447  614 GLU A OE1 
2491  O OE2 . GLU A 313 ? 1.2503 1.1779 0.9650 0.3499  -0.0027 0.0466  614 GLU A OE2 
2492  N N   . VAL A 314 ? 0.7613 0.7838 0.5219 0.3232  -0.0030 0.0580  615 VAL A N   
2493  C CA  . VAL A 314 ? 0.7707 0.8504 0.5556 0.3219  -0.0049 0.0487  615 VAL A CA  
2494  C C   . VAL A 314 ? 0.9228 1.0229 0.6994 0.3380  -0.0089 0.0496  615 VAL A C   
2495  O O   . VAL A 314 ? 0.9874 1.1226 0.7671 0.3501  -0.0115 0.0411  615 VAL A O   
2496  C CB  . VAL A 314 ? 0.7498 0.8446 0.5612 0.2928  -0.0011 0.0461  615 VAL A CB  
2497  C CG1 . VAL A 314 ? 0.6059 0.7559 0.4397 0.2899  -0.0030 0.0372  615 VAL A CG1 
2498  C CG2 . VAL A 314 ? 0.8472 0.9298 0.6681 0.2792  0.0022  0.0438  615 VAL A CG2 
2499  N N   . ALA A 315 ? 0.8816 0.9598 0.6482 0.3322  -0.0077 0.0579  616 ALA A N   
2500  C CA  . ALA A 315 ? 0.7441 0.8379 0.5021 0.3427  -0.0099 0.0580  616 ALA A CA  
2501  C C   . ALA A 315 ? 0.7722 0.8644 0.5115 0.3632  -0.0115 0.0537  616 ALA A C   
2502  O O   . ALA A 315 ? 0.6715 0.8011 0.4145 0.3732  -0.0143 0.0466  616 ALA A O   
2503  C CB  . ALA A 315 ? 0.7797 0.8376 0.5223 0.3358  -0.0074 0.0695  616 ALA A CB  
2504  N N   . LYS A 316 ? 0.9290 0.9794 0.6480 0.3694  -0.0100 0.0570  617 LYS A N   
2505  C CA  . LYS A 316 ? 0.9266 0.9731 0.6256 0.3899  -0.0117 0.0528  617 LYS A CA  
2506  C C   . LYS A 316 ? 0.8715 0.9704 0.5866 0.3980  -0.0147 0.0405  617 LYS A C   
2507  O O   . LYS A 316 ? 0.9382 1.0684 0.6516 0.4098  -0.0171 0.0351  617 LYS A O   
2508  C CB  . LYS A 316 ? 0.9645 0.9589 0.6414 0.3931  -0.0100 0.0569  617 LYS A CB  
2509  C CG  . LYS A 316 ? 1.0784 1.0208 0.7314 0.3898  -0.0075 0.0681  617 LYS A CG  
2510  C CD  . LYS A 316 ? 1.1625 1.0580 0.7882 0.3987  -0.0070 0.0699  617 LYS A CD  
2511  C CE  . LYS A 316 ? 1.1255 0.9723 0.7272 0.3947  -0.0044 0.0808  617 LYS A CE  
2512  N NZ  . LYS A 316 ? 1.0179 0.8485 0.6304 0.3711  -0.0008 0.0889  617 LYS A NZ  
2513  N N   . LYS A 317 ? 0.9288 1.0406 0.6607 0.3904  -0.0142 0.0358  618 LYS A N   
2514  C CA  . LYS A 317 ? 0.9196 1.0840 0.6686 0.3948  -0.0164 0.0242  618 LYS A CA  
2515  C C   . LYS A 317 ? 0.8814 1.0965 0.6510 0.3890  -0.0183 0.0190  618 LYS A C   
2516  O O   . LYS A 317 ? 0.8958 1.1555 0.6739 0.3948  -0.0205 0.0093  618 LYS A O   
2517  C CB  . LYS A 317 ? 0.9110 1.0824 0.6780 0.3838  -0.0148 0.0209  618 LYS A CB  
2518  C CG  . LYS A 317 ? 0.9832 1.1017 0.7346 0.3832  -0.0126 0.0267  618 LYS A CG  
2519  C CD  . LYS A 317 ? 0.7860 0.9118 0.5344 0.3924  -0.0132 0.0193  618 LYS A CD  
2520  C CE  . LYS A 317 ? 0.9295 1.0243 0.6453 0.4125  -0.0149 0.0199  618 LYS A CE  
2521  N NZ  . LYS A 317 ? 1.0072 1.1047 0.7152 0.4238  -0.0161 0.0130  618 LYS A NZ  
2522  N N   . MET A 318 ? 0.7697 0.9795 0.5466 0.3769  -0.0175 0.0248  619 MET A N   
2523  C CA  . MET A 318 ? 0.7568 1.0118 0.5511 0.3712  -0.0196 0.0195  619 MET A CA  
2524  C C   . MET A 318 ? 0.7760 1.0331 0.5520 0.3861  -0.0214 0.0199  619 MET A C   
2525  O O   . MET A 318 ? 0.8321 1.1285 0.6200 0.3835  -0.0236 0.0141  619 MET A O   
2526  C CB  . MET A 318 ? 0.6982 0.9504 0.5090 0.3520  -0.0184 0.0246  619 MET A CB  
2527  C CG  . MET A 318 ? 0.6983 0.9603 0.5332 0.3356  -0.0165 0.0223  619 MET A CG  
2528  S SD  . MET A 318 ? 0.6753 0.9322 0.5286 0.3035  -0.0125 0.0241  619 MET A SD  
2529  C CE  . MET A 318 ? 0.6136 0.9284 0.4822 0.3044  -0.0170 0.0145  619 MET A CE  
2530  N N   . ASN A 319 ? 0.8315 1.0468 0.5785 0.4009  -0.0205 0.0261  620 ASN A N   
2531  C CA  . ASN A 319 ? 0.9353 1.1461 0.6614 0.4170  -0.0217 0.0275  620 ASN A CA  
2532  C C   . ASN A 319 ? 0.9115 1.1149 0.6374 0.4093  -0.0210 0.0343  620 ASN A C   
2533  O O   . ASN A 319 ? 0.8830 1.1053 0.6032 0.4185  -0.0226 0.0320  620 ASN A O   
2534  C CB  . ASN A 319 ? 0.9329 1.1943 0.6636 0.4294  -0.0250 0.0158  620 ASN A CB  
2535  C CG  . ASN A 319 ? 0.9769 1.2279 0.6874 0.4488  -0.0258 0.0127  620 ASN A CG  
2536  O OD1 . ASN A 319 ? 1.1047 1.3173 0.7876 0.4631  -0.0252 0.0187  620 ASN A OD1 
2537  N ND2 . ASN A 319 ? 0.8544 1.1393 0.5774 0.4493  -0.0273 0.0034  620 ASN A ND2 
2538  N N   . LEU A 320 ? 0.9305 1.1065 0.6612 0.3931  -0.0185 0.0427  621 LEU A N   
2539  C CA  . LEU A 320 ? 0.9669 1.1388 0.6980 0.3846  -0.0178 0.0489  621 LEU A CA  
2540  C C   . LEU A 320 ? 0.9994 1.1285 0.7006 0.3950  -0.0158 0.0585  621 LEU A C   
2541  O O   . LEU A 320 ? 1.0023 1.0931 0.6829 0.4033  -0.0143 0.0627  621 LEU A O   
2542  C CB  . LEU A 320 ? 0.9336 1.0933 0.6796 0.3635  -0.0157 0.0542  621 LEU A CB  
2543  C CG  . LEU A 320 ? 0.8822 1.0861 0.6585 0.3530  -0.0178 0.0444  621 LEU A CG  
2544  C CD1 . LEU A 320 ? 0.8068 1.0002 0.5975 0.3332  -0.0161 0.0495  621 LEU A CD1 
2545  C CD2 . LEU A 320 ? 0.8900 1.1470 0.6802 0.3552  -0.0214 0.0342  621 LEU A CD2 
2546  N N   . ASP A 321 ? 0.9917 1.1284 0.6901 0.3943  -0.0159 0.0615  622 ASP A N   
2547  C CA  . ASP A 321 ? 0.9098 1.0057 0.5817 0.4001  -0.0134 0.0721  622 ASP A CA  
2548  C C   . ASP A 321 ? 0.8999 0.9552 0.5692 0.3819  -0.0092 0.0831  622 ASP A C   
2549  O O   . ASP A 321 ? 0.9192 0.9855 0.6018 0.3671  -0.0083 0.0854  622 ASP A O   
2550  C CB  . ASP A 321 ? 1.0823 1.2024 0.7528 0.4053  -0.0148 0.0713  622 ASP A CB  
2551  C CG  . ASP A 321 ? 1.1561 1.2345 0.8032 0.4050  -0.0113 0.0839  622 ASP A CG  
2552  O OD1 . ASP A 321 ? 1.2085 1.2966 0.8600 0.3969  -0.0106 0.0871  622 ASP A OD1 
2553  O OD2 . ASP A 321 ? 1.1348 1.1703 0.7588 0.4120  -0.0093 0.0906  622 ASP A OD2 
2554  N N   . MET A 322 ? 1.0455 1.0547 0.6974 0.3823  -0.0066 0.0893  623 MET A N   
2555  C CA  . MET A 322 ? 1.1170 1.0859 0.7651 0.3642  -0.0022 0.0993  623 MET A CA  
2556  C C   . MET A 322 ? 1.1904 1.1169 0.8124 0.3642  0.0012  0.1106  623 MET A C   
2557  O O   . MET A 322 ? 1.2488 1.1333 0.8607 0.3520  0.0050  0.1187  623 MET A O   
2558  C CB  . MET A 322 ? 1.0895 1.0359 0.7383 0.3606  -0.0015 0.0980  623 MET A CB  
2559  C CG  . MET A 322 ? 1.0841 1.0690 0.7602 0.3558  -0.0039 0.0887  623 MET A CG  
2560  S SD  . MET A 322 ? 1.0800 1.0473 0.7531 0.3610  -0.0043 0.0840  623 MET A SD  
2561  C CE  . MET A 322 ? 1.1115 1.0122 0.7640 0.3480  0.0007  0.0960  623 MET A CE  
2562  N N   . ARG A 323 ? 1.1874 1.1253 0.7985 0.3770  -0.0001 0.1110  624 ARG A N   
2563  C CA  . ARG A 323 ? 1.2643 1.1651 0.8505 0.3773  0.0031  0.1220  624 ARG A CA  
2564  C C   . ARG A 323 ? 1.2510 1.1537 0.8436 0.3600  0.0064  0.1292  624 ARG A C   
2565  O O   . ARG A 323 ? 1.4117 1.2765 0.9879 0.3505  0.0107  0.1400  624 ARG A O   
2566  C CB  . ARG A 323 ? 1.2480 1.1590 0.8179 0.3997  0.0003  0.1196  624 ARG A CB  
2567  C CG  . ARG A 323 ? 1.3122 1.2157 0.8691 0.4191  -0.0024 0.1137  624 ARG A CG  
2568  C CD  . ARG A 323 ? 1.4310 1.3592 0.9780 0.4413  -0.0055 0.1091  624 ARG A CD  
2569  N NE  . ARG A 323 ? 1.5268 1.5041 1.0950 0.4382  -0.0073 0.1039  624 ARG A NE  
2570  C CZ  . ARG A 323 ? 1.5497 1.5575 1.1152 0.4535  -0.0100 0.0991  624 ARG A CZ  
2571  N NH1 . ARG A 323 ? 1.5440 1.5384 1.0855 0.4745  -0.0111 0.0993  624 ARG A NH1 
2572  N NH2 . ARG A 323 ? 1.5322 1.5837 1.1184 0.4479  -0.0116 0.0938  624 ARG A NH2 
2573  N N   . LYS A 324 ? 1.0851 1.0316 0.7005 0.3551  0.0045  0.1232  625 LYS A N   
2574  C CA  . LYS A 324 ? 1.1277 1.0794 0.7489 0.3398  0.0076  0.1289  625 LYS A CA  
2575  C C   . LYS A 324 ? 1.0419 1.0213 0.6900 0.3253  0.0070  0.1234  625 LYS A C   
2576  O O   . LYS A 324 ? 1.0162 1.0317 0.6821 0.3307  0.0025  0.1127  625 LYS A O   
2577  C CB  . LYS A 324 ? 1.0002 0.9776 0.6169 0.3502  0.0058  0.1277  625 LYS A CB  
2578  C CG  . LYS A 324 ? 1.0541 1.0768 0.6822 0.3668  -0.0002 0.1150  625 LYS A CG  
2579  C CD  . LYS A 324 ? 1.1822 1.2242 0.8015 0.3792  -0.0019 0.1143  625 LYS A CD  
2580  C CE  . LYS A 324 ? 1.1473 1.2338 0.7767 0.3959  -0.0076 0.1010  625 LYS A CE  
2581  N NZ  . LYS A 324 ? 0.9226 1.0526 0.5819 0.3862  -0.0107 0.0899  625 LYS A NZ  
2582  N N   . THR A 325 ? 0.9976 0.9609 0.6480 0.3064  0.0118  0.1307  626 THR A N   
2583  C CA  . THR A 325 ? 0.9709 0.9540 0.6438 0.2917  0.0120  0.1269  626 THR A CA  
2584  C C   . THR A 325 ? 0.9215 0.9556 0.6128 0.2943  0.0074  0.1173  626 THR A C   
2585  O O   . THR A 325 ? 0.7485 0.8082 0.4627 0.2871  0.0052  0.1083  626 THR A O   
2586  C CB  . THR A 325 ? 0.9746 0.9328 0.6441 0.2720  0.0187  0.1367  626 THR A CB  
2587  O OG1 . THR A 325 ? 0.9305 0.9061 0.5988 0.2695  0.0201  0.1386  626 THR A OG1 
2588  C CG2 . THR A 325 ? 1.0399 0.9483 0.6875 0.2690  0.0231  0.1466  626 THR A CG2 
2589  N N   . SER A 326 ? 0.9302 0.9791 0.6145 0.3018  0.0065  0.1171  627 SER A N   
2590  C CA  . SER A 326 ? 0.8664 0.9623 0.5667 0.3027  0.0023  0.1075  627 SER A CA  
2591  C C   . SER A 326 ? 0.8185 0.9512 0.5340 0.3132  -0.0043 0.0945  627 SER A C   
2592  O O   . SER A 326 ? 0.8453 1.0188 0.5782 0.3101  -0.0083 0.0847  627 SER A O   
2593  C CB  . SER A 326 ? 0.8162 0.9175 0.5034 0.3098  0.0029  0.1102  627 SER A CB  
2594  O OG  . SER A 326 ? 0.7565 0.8252 0.4202 0.3211  0.0049  0.1183  627 SER A OG  
2595  N N   . SER A 327 ? 0.7159 0.8366 0.4256 0.3245  -0.0054 0.0934  628 SER A N   
2596  C CA  . SER A 327 ? 0.7465 0.9039 0.4732 0.3315  -0.0107 0.0809  628 SER A CA  
2597  C C   . SER A 327 ? 0.6430 0.8159 0.3925 0.3165  -0.0118 0.0762  628 SER A C   
2598  O O   . SER A 327 ? 0.6735 0.8846 0.4425 0.3169  -0.0159 0.0643  628 SER A O   
2599  C CB  . SER A 327 ? 0.7580 0.8978 0.4721 0.3469  -0.0109 0.0807  628 SER A CB  
2600  O OG  . SER A 327 ? 0.8588 0.9706 0.5738 0.3394  -0.0086 0.0845  628 SER A OG  
2601  N N   . LEU A 328 ? 0.5524 0.6959 0.3054 0.2972  -0.0057 0.0818  629 LEU A N   
2602  C CA  . LEU A 328 ? 0.7154 0.8651 0.4948 0.2759  -0.0031 0.0744  629 LEU A CA  
2603  C C   . LEU A 328 ? 0.7620 0.9159 0.5487 0.2811  -0.0050 0.0692  629 LEU A C   
2604  O O   . LEU A 328 ? 0.8594 1.0390 0.6698 0.2702  -0.0058 0.0590  629 LEU A O   
2605  C CB  . LEU A 328 ? 0.7311 0.9197 0.5337 0.2636  -0.0047 0.0631  629 LEU A CB  
2606  C CG  . LEU A 328 ? 0.6056 0.7945 0.4044 0.2569  -0.0028 0.0659  629 LEU A CG  
2607  C CD1 . LEU A 328 ? 0.5580 0.7765 0.3822 0.2401  -0.0035 0.0538  629 LEU A CD1 
2608  C CD2 . LEU A 328 ? 0.6166 0.7638 0.4030 0.2475  0.0038  0.0782  629 LEU A CD2 
2609  N N   . TRP A 329 ? 0.7389 0.8663 0.5037 0.2980  -0.0058 0.0764  630 TRP A N   
2610  C CA  . TRP A 329 ? 0.7763 0.9040 0.5463 0.3030  -0.0070 0.0719  630 TRP A CA  
2611  C C   . TRP A 329 ? 0.7706 0.8812 0.5566 0.2805  -0.0021 0.0710  630 TRP A C   
2612  O O   . TRP A 329 ? 0.8209 0.9541 0.6273 0.2734  -0.0027 0.0620  630 TRP A O   
2613  C CB  . TRP A 329 ? 0.7788 0.8754 0.5206 0.3245  -0.0081 0.0791  630 TRP A CB  
2614  C CG  . TRP A 329 ? 0.7929 0.8346 0.5121 0.3197  -0.0030 0.0917  630 TRP A CG  
2615  C CD1 . TRP A 329 ? 0.8534 0.8735 0.5535 0.3220  -0.0006 0.0994  630 TRP A CD1 
2616  C CD2 . TRP A 329 ? 0.8628 0.8654 0.5765 0.3112  0.0004  0.0972  630 TRP A CD2 
2617  N NE1 . TRP A 329 ? 0.9139 0.8847 0.5976 0.3139  0.0042  0.1094  630 TRP A NE1 
2618  C CE2 . TRP A 329 ? 0.9445 0.9036 0.6362 0.3070  0.0048  0.1079  630 TRP A CE2 
2619  C CE3 . TRP A 329 ? 0.8679 0.8691 0.5956 0.3031  0.0011  0.0922  630 TRP A CE3 
2620  C CZ2 . TRP A 329 ? 0.8619 0.7768 0.5437 0.2965  0.0089  0.1145  630 TRP A CZ2 
2621  C CZ3 . TRP A 329 ? 0.7446 0.7016 0.4620 0.2940  0.0051  0.0987  630 TRP A CZ3 
2622  C CH2 . TRP A 329 ? 0.8132 0.7274 0.5067 0.2918  0.0084  0.1105  630 TRP A CH2 
2623  N N   . LYS A 330 ? 0.7592 0.8316 0.5359 0.2688  0.0029  0.0804  631 LYS A N   
2624  C CA  . LYS A 330 ? 0.6931 0.7504 0.4845 0.2474  0.0074  0.0797  631 LYS A CA  
2625  C C   . LYS A 330 ? 0.7191 0.8120 0.5398 0.2316  0.0072  0.0691  631 LYS A C   
2626  O O   . LYS A 330 ? 0.8297 0.9297 0.6657 0.2236  0.0076  0.0632  631 LYS A O   
2627  C CB  . LYS A 330 ? 0.6648 0.6871 0.4454 0.2352  0.0125  0.0900  631 LYS A CB  
2628  C CG  . LYS A 330 ? 0.8533 0.8305 0.6089 0.2420  0.0143  0.0999  631 LYS A CG  
2629  C CD  . LYS A 330 ? 0.8803 0.8273 0.6311 0.2244  0.0201  0.1083  631 LYS A CD  
2630  C CE  . LYS A 330 ? 0.9354 0.8358 0.6576 0.2309  0.0219  0.1190  631 LYS A CE  
2631  N NZ  . LYS A 330 ? 0.9455 0.8197 0.6640 0.2118  0.0279  0.1269  631 LYS A NZ  
2632  N N   . ASP A 331 ? 0.7310 0.8455 0.5583 0.2272  0.0065  0.0664  632 ASP A N   
2633  C CA  . ASP A 331 ? 0.7211 0.8666 0.5738 0.2121  0.0061  0.0561  632 ASP A CA  
2634  C C   . ASP A 331 ? 0.6657 0.8444 0.5317 0.2173  0.0022  0.0459  632 ASP A C   
2635  O O   . ASP A 331 ? 0.7197 0.9101 0.6048 0.2032  0.0033  0.0393  632 ASP A O   
2636  C CB  . ASP A 331 ? 0.7030 0.8668 0.5569 0.2104  0.0050  0.0542  632 ASP A CB  
2637  C CG  . ASP A 331 ? 0.6136 0.7486 0.4530 0.2067  0.0090  0.0646  632 ASP A CG  
2638  O OD1 . ASP A 331 ? 0.6246 0.7392 0.4413 0.2200  0.0093  0.0739  632 ASP A OD1 
2639  O OD2 . ASP A 331 ? 0.5878 0.7208 0.4379 0.1907  0.0121  0.0635  632 ASP A OD2 
2640  N N   . GLN A 332 ? 0.5951 0.7902 0.4505 0.2378  -0.0021 0.0447  633 GLN A N   
2641  C CA  . GLN A 332 ? 0.5648 0.7977 0.4329 0.2438  -0.0059 0.0345  633 GLN A CA  
2642  C C   . GLN A 332 ? 0.6594 0.8812 0.5311 0.2429  -0.0042 0.0340  633 GLN A C   
2643  O O   . GLN A 332 ? 0.5916 0.8368 0.4827 0.2323  -0.0039 0.0258  633 GLN A O   
2644  C CB  . GLN A 332 ? 0.5155 0.7675 0.3694 0.2683  -0.0112 0.0339  633 GLN A CB  
2645  C CG  . GLN A 332 ? 0.7038 1.0080 0.5733 0.2701  -0.0158 0.0219  633 GLN A CG  
2646  C CD  . GLN A 332 ? 0.8344 1.1544 0.6870 0.2942  -0.0211 0.0230  633 GLN A CD  
2647  O OE1 . GLN A 332 ? 0.8311 1.1252 0.6603 0.3133  -0.0218 0.0317  633 GLN A OE1 
2648  N NE2 . GLN A 332 ? 0.9460 1.3070 0.8089 0.2936  -0.0251 0.0141  633 GLN A NE2 
2649  N N   . ALA A 333 ? 0.6145 0.7996 0.4663 0.2536  -0.0029 0.0427  634 ALA A N   
2650  C CA  . ALA A 333 ? 0.6412 0.8126 0.4936 0.2541  -0.0014 0.0423  634 ALA A CA  
2651  C C   . ALA A 333 ? 0.7395 0.9001 0.6085 0.2300  0.0030  0.0413  634 ALA A C   
2652  O O   . ALA A 333 ? 0.6585 0.8275 0.5383 0.2255  0.0038  0.0365  634 ALA A O   
2653  C CB  . ALA A 333 ? 0.6466 0.7759 0.4717 0.2697  -0.0012 0.0520  634 ALA A CB  
2654  N N   . LEU A 334 ? 0.8126 0.9564 0.6835 0.2152  0.0059  0.0457  635 LEU A N   
2655  C CA  . LEU A 334 ? 0.7125 0.8464 0.5981 0.1937  0.0097  0.0449  635 LEU A CA  
2656  C C   . LEU A 334 ? 0.6891 0.8586 0.5979 0.1822  0.0091  0.0347  635 LEU A C   
2657  O O   . LEU A 334 ? 0.6495 0.8164 0.5692 0.1707  0.0112  0.0323  635 LEU A O   
2658  C CB  . LEU A 334 ? 0.6516 0.7652 0.5347 0.1819  0.0126  0.0509  635 LEU A CB  
2659  C CG  . LEU A 334 ? 0.5621 0.6692 0.4610 0.1605  0.0161  0.0494  635 LEU A CG  
2660  C CD1 . LEU A 334 ? 0.5931 0.6749 0.4893 0.1569  0.0183  0.0525  635 LEU A CD1 
2661  C CD2 . LEU A 334 ? 0.7444 0.8384 0.6409 0.1516  0.0185  0.0542  635 LEU A CD2 
2662  N N   . VAL A 335 ? 0.6938 0.8963 0.6096 0.1843  0.0061  0.0285  636 VAL A N   
2663  C CA  . VAL A 335 ? 0.6044 0.8388 0.5413 0.1708  0.0057  0.0187  636 VAL A CA  
2664  C C   . VAL A 335 ? 0.6225 0.8753 0.5658 0.1752  0.0052  0.0137  636 VAL A C   
2665  O O   . VAL A 335 ? 0.5946 0.8525 0.5515 0.1607  0.0075  0.0101  636 VAL A O   
2666  C CB  . VAL A 335 ? 0.5279 0.7948 0.4704 0.1719  0.0022  0.0121  636 VAL A CB  
2667  C CG1 . VAL A 335 ? 0.3190 0.6230 0.2808 0.1618  0.0011  0.0012  636 VAL A CG1 
2668  C CG2 . VAL A 335 ? 0.4050 0.6588 0.3478 0.1608  0.0035  0.0142  636 VAL A CG2 
2669  N N   . GLU A 336 ? 0.5632 0.8267 0.4959 0.1959  0.0022  0.0136  637 GLU A N   
2670  C CA  . GLU A 336 ? 0.5628 0.8490 0.5015 0.2020  0.0016  0.0079  637 GLU A CA  
2671  C C   . GLU A 336 ? 0.6863 0.9463 0.6252 0.1946  0.0055  0.0112  637 GLU A C   
2672  O O   . GLU A 336 ? 0.5962 0.8756 0.5479 0.1874  0.0068  0.0057  637 GLU A O   
2673  C CB  . GLU A 336 ? 0.5129 0.8097 0.4367 0.2286  -0.0024 0.0081  637 GLU A CB  
2674  C CG  . GLU A 336 ? 0.5779 0.9111 0.5034 0.2379  -0.0071 0.0028  637 GLU A CG  
2675  C CD  . GLU A 336 ? 0.5965 0.9811 0.5443 0.2283  -0.0084 -0.0091 637 GLU A CD  
2676  O OE1 . GLU A 336 ? 0.6451 1.0347 0.6085 0.2089  -0.0050 -0.0126 637 GLU A OE1 
2677  O OE2 . GLU A 336 ? 0.7055 1.1264 0.6545 0.2397  -0.0128 -0.0150 637 GLU A OE2 
2678  N N   . ILE A 337 ? 0.6780 0.8951 0.6027 0.1957  0.0073  0.0199  638 ILE A N   
2679  C CA  . ILE A 337 ? 0.5402 0.7316 0.4646 0.1881  0.0106  0.0227  638 ILE A CA  
2680  C C   . ILE A 337 ? 0.5885 0.7866 0.5317 0.1648  0.0135  0.0196  638 ILE A C   
2681  O O   . ILE A 337 ? 0.6505 0.8541 0.6017 0.1582  0.0154  0.0167  638 ILE A O   
2682  C CB  . ILE A 337 ? 0.5506 0.6955 0.4566 0.1911  0.0119  0.0324  638 ILE A CB  
2683  C CG1 . ILE A 337 ? 0.6037 0.7360 0.4880 0.2150  0.0092  0.0357  638 ILE A CG1 
2684  C CG2 . ILE A 337 ? 0.4481 0.5677 0.3567 0.1784  0.0153  0.0346  638 ILE A CG2 
2685  C CD1 . ILE A 337 ? 0.6131 0.7051 0.4775 0.2183  0.0099  0.0455  638 ILE A CD1 
2686  N N   . ASN A 338 ? 0.5944 0.7913 0.5435 0.1528  0.0140  0.0203  639 ASN A N   
2687  C CA  . ASN A 338 ? 0.6685 0.8677 0.6329 0.1318  0.0165  0.0176  639 ASN A CA  
2688  C C   . ASN A 338 ? 0.6281 0.8652 0.6080 0.1251  0.0160  0.0089  639 ASN A C   
2689  O O   . ASN A 338 ? 0.3979 0.6360 0.3883 0.1097  0.0185  0.0068  639 ASN A O   
2690  C CB  . ASN A 338 ? 0.5467 0.7353 0.5120 0.1228  0.0168  0.0198  639 ASN A CB  
2691  C CG  . ASN A 338 ? 0.6195 0.7701 0.5743 0.1212  0.0190  0.0283  639 ASN A CG  
2692  O OD1 . ASN A 338 ? 0.7233 0.8579 0.6832 0.1087  0.0215  0.0300  639 ASN A OD1 
2693  N ND2 . ASN A 338 ? 0.6078 0.7441 0.5472 0.1340  0.0180  0.0339  639 ASN A ND2 
2694  N N   . ILE A 339 ? 0.5826 0.8514 0.5634 0.1361  0.0128  0.0037  640 ILE A N   
2695  C CA  . ILE A 339 ? 0.5328 0.8410 0.5277 0.1307  0.0125  -0.0050 640 ILE A CA  
2696  C C   . ILE A 339 ? 0.4892 0.7997 0.4841 0.1348  0.0145  -0.0052 640 ILE A C   
2697  O O   . ILE A 339 ? 0.5338 0.8605 0.5408 0.1215  0.0170  -0.0093 640 ILE A O   
2698  C CB  . ILE A 339 ? 0.4766 0.8208 0.4719 0.1433  0.0082  -0.0108 640 ILE A CB  
2699  C CG1 . ILE A 339 ? 0.4212 0.7740 0.4224 0.1327  0.0066  -0.0141 640 ILE A CG1 
2700  C CG2 . ILE A 339 ? 0.4271 0.8142 0.4336 0.1444  0.0078  -0.0191 640 ILE A CG2 
2701  C CD1 . ILE A 339 ? 0.5113 0.8913 0.5086 0.1473  0.0018  -0.0181 640 ILE A CD1 
2702  N N   . ALA A 340 ? 0.4551 0.7473 0.4351 0.1529  0.0137  -0.0006 641 ALA A N   
2703  C CA  . ALA A 340 ? 0.6163 0.9091 0.5937 0.1600  0.0151  -0.0012 641 ALA A CA  
2704  C C   . ALA A 340 ? 0.6007 0.8686 0.5817 0.1440  0.0191  0.0020  641 ALA A C   
2705  O O   . ALA A 340 ? 0.6022 0.8848 0.5906 0.1385  0.0214  -0.0013 641 ALA A O   
2706  C CB  . ALA A 340 ? 0.6396 0.9124 0.5973 0.1836  0.0128  0.0029  641 ALA A CB  
2707  N N   . VAL A 341 ? 0.5802 0.8118 0.5554 0.1369  0.0201  0.0085  642 VAL A N   
2708  C CA  . VAL A 341 ? 0.5029 0.7126 0.4817 0.1218  0.0234  0.0114  642 VAL A CA  
2709  C C   . VAL A 341 ? 0.5163 0.7481 0.5115 0.1034  0.0254  0.0068  642 VAL A C   
2710  O O   . VAL A 341 ? 0.4683 0.7013 0.4681 0.0955  0.0280  0.0061  642 VAL A O   
2711  C CB  . VAL A 341 ? 0.4108 0.5838 0.3825 0.1167  0.0238  0.0183  642 VAL A CB  
2712  C CG1 . VAL A 341 ? 0.5168 0.6738 0.4947 0.1002  0.0267  0.0200  642 VAL A CG1 
2713  C CG2 . VAL A 341 ? 0.4413 0.5868 0.3953 0.1319  0.0227  0.0235  642 VAL A CG2 
2714  N N   . LEU A 342 ? 0.4874 0.7357 0.4903 0.0961  0.0242  0.0035  643 LEU A N   
2715  C CA  . LEU A 342 ? 0.4876 0.7504 0.5039 0.0767  0.0263  -0.0004 643 LEU A CA  
2716  C C   . LEU A 342 ? 0.5606 0.8600 0.5852 0.0760  0.0273  -0.0066 643 LEU A C   
2717  O O   . LEU A 342 ? 0.4508 0.7553 0.4826 0.0616  0.0305  -0.0077 643 LEU A O   
2718  C CB  . LEU A 342 ? 0.3708 0.6396 0.3922 0.0682  0.0246  -0.0031 643 LEU A CB  
2719  C CG  . LEU A 342 ? 0.3683 0.6029 0.3835 0.0653  0.0245  0.0026  643 LEU A CG  
2720  C CD1 . LEU A 342 ? 0.3558 0.5972 0.3726 0.0632  0.0221  -0.0002 643 LEU A CD1 
2721  C CD2 . LEU A 342 ? 0.3502 0.5628 0.3683 0.0504  0.0274  0.0054  643 LEU A CD2 
2722  N N   . TYR A 343 ? 0.5561 0.8822 0.5792 0.0916  0.0248  -0.0104 644 TYR A N   
2723  C CA  . TYR A 343 ? 0.4264 0.7922 0.4583 0.0913  0.0260  -0.0169 644 TYR A CA  
2724  C C   . TYR A 343 ? 0.5622 0.9207 0.5906 0.0947  0.0290  -0.0148 644 TYR A C   
2725  O O   . TYR A 343 ? 0.5579 0.9408 0.5950 0.0856  0.0320  -0.0184 644 TYR A O   
2726  C CB  . TYR A 343 ? 0.3969 0.7935 0.4269 0.1103  0.0221  -0.0217 644 TYR A CB  
2727  C CG  . TYR A 343 ? 0.3422 0.7817 0.3792 0.1162  0.0228  -0.0283 644 TYR A CG  
2728  C CD1 . TYR A 343 ? 0.4182 0.8944 0.4707 0.0991  0.0249  -0.0348 644 TYR A CD1 
2729  C CD2 . TYR A 343 ? 0.3069 0.7512 0.3342 0.1393  0.0214  -0.0283 644 TYR A CD2 
2730  C CE1 . TYR A 343 ? 0.4188 0.9388 0.4786 0.1041  0.0259  -0.0412 644 TYR A CE1 
2731  C CE2 . TYR A 343 ? 0.3908 0.8782 0.4246 0.1465  0.0219  -0.0351 644 TYR A CE2 
2732  C CZ  . TYR A 343 ? 0.4959 1.0228 0.5467 0.1285  0.0244  -0.0415 644 TYR A CZ  
2733  O OH  . TYR A 343 ? 0.6713 1.2449 0.7296 0.1347  0.0254  -0.0484 644 TYR A OH  
2734  N N   . SER A 344 ? 0.5585 0.8837 0.5734 0.1073  0.0283  -0.0091 645 SER A N   
2735  C CA  . SER A 344 ? 0.4809 0.7991 0.4905 0.1134  0.0304  -0.0080 645 SER A CA  
2736  C C   . SER A 344 ? 0.4930 0.7963 0.5075 0.0940  0.0344  -0.0053 645 SER A C   
2737  O O   . SER A 344 ? 0.5839 0.9038 0.6025 0.0900  0.0375  -0.0075 645 SER A O   
2738  C CB  . SER A 344 ? 0.4783 0.7630 0.4706 0.1314  0.0281  -0.0032 645 SER A CB  
2739  O OG  . SER A 344 ? 0.4608 0.7634 0.4466 0.1524  0.0248  -0.0063 645 SER A OG  
2740  N N   . PHE A 345 ? 0.4895 0.7628 0.5032 0.0824  0.0346  -0.0005 646 PHE A N   
2741  C CA  . PHE A 345 ? 0.3890 0.6473 0.4065 0.0649  0.0378  0.0023  646 PHE A CA  
2742  C C   . PHE A 345 ? 0.5672 0.8549 0.5970 0.0487  0.0405  -0.0020 646 PHE A C   
2743  O O   . PHE A 345 ? 0.7039 0.9959 0.7358 0.0401  0.0441  -0.0016 646 PHE A O   
2744  C CB  . PHE A 345 ? 0.2884 0.5134 0.3031 0.0572  0.0369  0.0072  646 PHE A CB  
2745  C CG  . PHE A 345 ? 0.4203 0.6114 0.4236 0.0658  0.0360  0.0126  646 PHE A CG  
2746  C CD1 . PHE A 345 ? 0.3219 0.5073 0.3151 0.0836  0.0337  0.0132  646 PHE A CD1 
2747  C CD2 . PHE A 345 ? 0.4879 0.6524 0.4896 0.0559  0.0373  0.0169  646 PHE A CD2 
2748  C CE1 . PHE A 345 ? 0.4021 0.5543 0.3838 0.0895  0.0330  0.0179  646 PHE A CE1 
2749  C CE2 . PHE A 345 ? 0.4472 0.5825 0.4389 0.0622  0.0364  0.0212  646 PHE A CE2 
2750  C CZ  . PHE A 345 ? 0.4417 0.5703 0.4235 0.0781  0.0344  0.0217  646 PHE A CZ  
2751  N N   . GLN A 346 ? 0.5104 0.8182 0.5476 0.0434  0.0390  -0.0061 647 GLN A N   
2752  C CA  . GLN A 346 ? 0.4912 0.8247 0.5395 0.0254  0.0416  -0.0104 647 GLN A CA  
2753  C C   . GLN A 346 ? 0.5396 0.9088 0.5924 0.0281  0.0443  -0.0145 647 GLN A C   
2754  O O   . GLN A 346 ? 0.6697 1.0502 0.7281 0.0123  0.0484  -0.0151 647 GLN A O   
2755  C CB  . GLN A 346 ? 0.4722 0.8232 0.5270 0.0207  0.0389  -0.0154 647 GLN A CB  
2756  C CG  . GLN A 346 ? 0.6161 0.9355 0.6675 0.0153  0.0369  -0.0123 647 GLN A CG  
2757  C CD  . GLN A 346 ? 0.6263 0.9636 0.6816 0.0167  0.0332  -0.0177 647 GLN A CD  
2758  O OE1 . GLN A 346 ? 0.6815 1.0043 0.7373 0.0069  0.0322  -0.0180 647 GLN A OE1 
2759  N NE2 . GLN A 346 ? 0.5986 0.9685 0.6561 0.0298  0.0311  -0.0224 647 GLN A NE2 
2760  N N   . SER A 347 ? 0.3984 0.7857 0.4481 0.0485  0.0421  -0.0172 648 SER A N   
2761  C CA  . SER A 347 ? 0.3414 0.7662 0.3954 0.0539  0.0444  -0.0219 648 SER A CA  
2762  C C   . SER A 347 ? 0.5518 0.9626 0.6012 0.0509  0.0485  -0.0181 648 SER A C   
2763  O O   . SER A 347 ? 0.5633 1.0013 0.6189 0.0422  0.0526  -0.0207 648 SER A O   
2764  C CB  . SER A 347 ? 0.3252 0.7660 0.3737 0.0798  0.0404  -0.0252 648 SER A CB  
2765  O OG  . SER A 347 ? 0.4648 0.9278 0.5186 0.0828  0.0368  -0.0297 648 SER A OG  
2766  N N   . ASP A 348 ? 0.5100 0.8794 0.5481 0.0574  0.0474  -0.0122 649 ASP A N   
2767  C CA  . ASP A 348 ? 0.4553 0.8086 0.4878 0.0550  0.0507  -0.0087 649 ASP A CA  
2768  C C   . ASP A 348 ? 0.5807 0.9117 0.6151 0.0335  0.0534  -0.0038 649 ASP A C   
2769  O O   . ASP A 348 ? 0.5623 0.8695 0.5899 0.0320  0.0550  0.0006  649 ASP A O   
2770  C CB  . ASP A 348 ? 0.3438 0.6655 0.3626 0.0732  0.0479  -0.0056 649 ASP A CB  
2771  C CG  . ASP A 348 ? 0.5146 0.8547 0.5283 0.0963  0.0452  -0.0101 649 ASP A CG  
2772  O OD1 . ASP A 348 ? 0.4783 0.8598 0.5005 0.0990  0.0454  -0.0160 649 ASP A OD1 
2773  O OD2 . ASP A 348 ? 0.5863 0.8991 0.5870 0.1118  0.0426  -0.0080 649 ASP A OD2 
2774  N N   . LYS A 349 ? 0.6185 0.9557 0.6609 0.0176  0.0537  -0.0047 650 LYS A N   
2775  C CA  . LYS A 349 ? 0.5533 0.8699 0.5965 -0.0027 0.0562  -0.0006 650 LYS A CA  
2776  C C   . LYS A 349 ? 0.5483 0.8218 0.5817 0.0001  0.0551  0.0060  650 LYS A C   
2777  O O   . LYS A 349 ? 0.5716 0.8294 0.6016 -0.0098 0.0578  0.0102  650 LYS A O   
2778  C CB  . LYS A 349 ? 0.4766 0.8169 0.5241 -0.0166 0.0616  -0.0015 650 LYS A CB  
2779  C CG  . LYS A 349 ? 0.4632 0.8474 0.5224 -0.0239 0.0626  -0.0085 650 LYS A CG  
2780  C CD  . LYS A 349 ? 0.7146 1.1345 0.7781 -0.0291 0.0678  -0.0110 650 LYS A CD  
2781  C CE  . LYS A 349 ? 0.9349 1.3487 0.9989 -0.0539 0.0731  -0.0074 650 LYS A CE  
2782  N NZ  . LYS A 349 ? 1.0410 1.4813 1.1151 -0.0727 0.0746  -0.0123 650 LYS A NZ  
2783  N N   . VAL A 350 ? 0.4688 0.7241 0.4971 0.0138  0.0510  0.0070  651 VAL A N   
2784  C CA  . VAL A 350 ? 0.4411 0.6577 0.4617 0.0158  0.0493  0.0125  651 VAL A CA  
2785  C C   . VAL A 350 ? 0.5006 0.7033 0.5237 0.0091  0.0471  0.0134  651 VAL A C   
2786  O O   . VAL A 350 ? 0.4444 0.6576 0.4699 0.0153  0.0446  0.0104  651 VAL A O   
2787  C CB  . VAL A 350 ? 0.3886 0.5938 0.4005 0.0347  0.0468  0.0130  651 VAL A CB  
2788  C CG1 . VAL A 350 ? 0.4360 0.6037 0.4408 0.0351  0.0450  0.0182  651 VAL A CG1 
2789  C CG2 . VAL A 350 ? 0.3991 0.6195 0.4078 0.0429  0.0487  0.0109  651 VAL A CG2 
2790  N N   . THR A 351 ? 0.4633 0.6426 0.4849 -0.0025 0.0478  0.0172  652 THR A N   
2791  C CA  . THR A 351 ? 0.3858 0.5510 0.4090 -0.0091 0.0459  0.0177  652 THR A CA  
2792  C C   . THR A 351 ? 0.5069 0.6645 0.5277 0.0035  0.0425  0.0177  652 THR A C   
2793  O O   . THR A 351 ? 0.5164 0.6621 0.5309 0.0149  0.0415  0.0202  652 THR A O   
2794  C CB  . THR A 351 ? 0.4841 0.6204 0.5031 -0.0175 0.0465  0.0225  652 THR A CB  
2795  O OG1 . THR A 351 ? 0.6060 0.7464 0.6248 -0.0287 0.0499  0.0236  652 THR A OG1 
2796  C CG2 . THR A 351 ? 0.4343 0.5578 0.4547 -0.0239 0.0446  0.0221  652 THR A CG2 
2797  N N   . ILE A 352 ? 0.5086 0.6731 0.5333 0.0009  0.0408  0.0148  653 ILE A N   
2798  C CA  . ILE A 352 ? 0.4292 0.5839 0.4509 0.0102  0.0378  0.0157  653 ILE A CA  
2799  C C   . ILE A 352 ? 0.4933 0.6525 0.5196 0.0016  0.0367  0.0123  653 ILE A C   
2800  O O   . ILE A 352 ? 0.5125 0.6875 0.5445 -0.0095 0.0377  0.0083  653 ILE A O   
2801  C CB  . ILE A 352 ? 0.4498 0.6208 0.4690 0.0258  0.0363  0.0139  653 ILE A CB  
2802  C CG1 . ILE A 352 ? 0.3191 0.4725 0.3311 0.0366  0.0339  0.0171  653 ILE A CG1 
2803  C CG2 . ILE A 352 ? 0.3179 0.5227 0.3445 0.0242  0.0358  0.0075  653 ILE A CG2 
2804  C CD1 . ILE A 352 ? 0.2606 0.4213 0.2657 0.0538  0.0325  0.0170  653 ILE A CD1 
2805  N N   . VAL A 353 ? 0.5476 0.6930 0.5709 0.0061  0.0346  0.0137  654 VAL A N   
2806  C CA  . VAL A 353 ? 0.5110 0.6603 0.5374 0.0004  0.0330  0.0099  654 VAL A CA  
2807  C C   . VAL A 353 ? 0.4915 0.6453 0.5148 0.0128  0.0305  0.0097  654 VAL A C   
2808  O O   . VAL A 353 ? 0.5003 0.6388 0.5172 0.0220  0.0303  0.0147  654 VAL A O   
2809  C CB  . VAL A 353 ? 0.4679 0.5926 0.4927 -0.0087 0.0333  0.0118  654 VAL A CB  
2810  C CG1 . VAL A 353 ? 0.3688 0.4732 0.3883 -0.0008 0.0324  0.0164  654 VAL A CG1 
2811  C CG2 . VAL A 353 ? 0.5206 0.6507 0.5486 -0.0187 0.0322  0.0062  654 VAL A CG2 
2812  N N   . ASP A 354 ? 0.5442 0.7196 0.5711 0.0126  0.0286  0.0039  655 ASP A N   
2813  C CA  . ASP A 354 ? 0.5735 0.7544 0.5964 0.0244  0.0261  0.0037  655 ASP A CA  
2814  C C   . ASP A 354 ? 0.4848 0.6468 0.5046 0.0223  0.0255  0.0053  655 ASP A C   
2815  O O   . ASP A 354 ? 0.5072 0.6568 0.5292 0.0113  0.0262  0.0043  655 ASP A O   
2816  C CB  . ASP A 354 ? 0.5822 0.7956 0.6101 0.0256  0.0238  -0.0036 655 ASP A CB  
2817  C CG  . ASP A 354 ? 0.5915 0.8117 0.6259 0.0104  0.0233  -0.0101 655 ASP A CG  
2818  O OD1 . ASP A 354 ? 0.7460 0.9843 0.7873 0.0004  0.0242  -0.0148 655 ASP A OD1 
2819  O OD2 . ASP A 354 ? 0.6339 0.8407 0.6659 0.0078  0.0222  -0.0107 655 ASP A OD2 
2820  N N   . HIS A 355 ? 0.5033 0.6638 0.5170 0.0333  0.0241  0.0075  656 HIS A N   
2821  C CA  . HIS A 355 ? 0.4435 0.5873 0.4540 0.0319  0.0240  0.0094  656 HIS A CA  
2822  C C   . HIS A 355 ? 0.3948 0.5464 0.4097 0.0234  0.0224  0.0024  656 HIS A C   
2823  O O   . HIS A 355 ? 0.4682 0.6045 0.4818 0.0195  0.0227  0.0027  656 HIS A O   
2824  C CB  . HIS A 355 ? 0.3939 0.5339 0.3956 0.0445  0.0235  0.0140  656 HIS A CB  
2825  C CG  . HIS A 355 ? 0.5311 0.6933 0.5304 0.0547  0.0211  0.0113  656 HIS A CG  
2826  N ND1 . HIS A 355 ? 0.5598 0.7323 0.5572 0.0631  0.0207  0.0120  656 HIS A ND1 
2827  C CD2 . HIS A 355 ? 0.4434 0.6195 0.4406 0.0594  0.0188  0.0080  656 HIS A CD2 
2828  C CE1 . HIS A 355 ? 0.5037 0.6964 0.4983 0.0728  0.0180  0.0092  656 HIS A CE1 
2829  N NE2 . HIS A 355 ? 0.5207 0.7161 0.5151 0.0704  0.0168  0.0068  656 HIS A NE2 
2830  N N   . HIS A 356 ? 0.3844 0.5595 0.4043 0.0201  0.0207  -0.0046 657 HIS A N   
2831  C CA  . HIS A 356 ? 0.4244 0.6051 0.4474 0.0110  0.0190  -0.0120 657 HIS A CA  
2832  C C   . HIS A 356 ? 0.5234 0.6891 0.5495 -0.0035 0.0205  -0.0136 657 HIS A C   
2833  O O   . HIS A 356 ? 0.6233 0.7728 0.6470 -0.0081 0.0200  -0.0151 657 HIS A O   
2834  C CB  . HIS A 356 ? 0.4341 0.6465 0.4616 0.0111  0.0164  -0.0196 657 HIS A CB  
2835  C CG  . HIS A 356 ? 0.4548 0.6814 0.4774 0.0266  0.0143  -0.0185 657 HIS A CG  
2836  N ND1 . HIS A 356 ? 0.4947 0.7183 0.5117 0.0324  0.0126  -0.0189 657 HIS A ND1 
2837  C CD2 . HIS A 356 ? 0.4672 0.7101 0.4882 0.0384  0.0136  -0.0165 657 HIS A CD2 
2838  C CE1 . HIS A 356 ? 0.5367 0.7734 0.5483 0.0466  0.0111  -0.0168 657 HIS A CE1 
2839  N NE2 . HIS A 356 ? 0.4726 0.7205 0.4863 0.0510  0.0114  -0.0153 657 HIS A NE2 
2840  N N   . SER A 357 ? 0.6127 0.7834 0.6429 -0.0101 0.0222  -0.0131 658 SER A N   
2841  C CA  A SER A 357 ? 0.6205 0.7746 0.6514 -0.0238 0.0240  -0.0133 658 SER A CA  
2842  C CA  B SER A 357 ? 0.6097 0.7639 0.6406 -0.0237 0.0240  -0.0132 658 SER A CA  
2843  C C   . SER A 357 ? 0.5581 0.6826 0.5837 -0.0211 0.0252  -0.0068 658 SER A C   
2844  O O   . SER A 357 ? 0.5588 0.6653 0.5818 -0.0280 0.0249  -0.0082 658 SER A O   
2845  C CB  A SER A 357 ? 0.6080 0.7733 0.6431 -0.0300 0.0264  -0.0125 658 SER A CB  
2846  C CB  B SER A 357 ? 0.6047 0.7703 0.6399 -0.0295 0.0264  -0.0123 658 SER A CB  
2847  O OG  A SER A 357 ? 0.6131 0.7604 0.6471 -0.0431 0.0284  -0.0115 658 SER A OG  
2848  O OG  B SER A 357 ? 0.5778 0.7758 0.6186 -0.0292 0.0253  -0.0180 658 SER A OG  
2849  N N   . ALA A 358 ? 0.4442 0.5635 0.4675 -0.0108 0.0262  -0.0001 659 ALA A N   
2850  C CA  . ALA A 358 ? 0.4317 0.5268 0.4508 -0.0084 0.0273  0.0057  659 ALA A CA  
2851  C C   . ALA A 358 ? 0.5331 0.6183 0.5495 -0.0074 0.0258  0.0036  659 ALA A C   
2852  O O   . ALA A 358 ? 0.6087 0.6763 0.6232 -0.0122 0.0260  0.0037  659 ALA A O   
2853  C CB  . ALA A 358 ? 0.3350 0.4284 0.3515 0.0024  0.0282  0.0120  659 ALA A CB  
2854  N N   . THR A 359 ? 0.5009 0.5977 0.5162 -0.0001 0.0244  0.0017  660 THR A N   
2855  C CA  . THR A 359 ? 0.4017 0.4909 0.4138 0.0025  0.0234  0.0000  660 THR A CA  
2856  C C   . THR A 359 ? 0.3648 0.4493 0.3770 -0.0066 0.0218  -0.0074 660 THR A C   
2857  O O   . THR A 359 ? 0.4311 0.5005 0.4399 -0.0065 0.0214  -0.0084 660 THR A O   
2858  C CB  . THR A 359 ? 0.4938 0.5975 0.5033 0.0119  0.0223  -0.0006 660 THR A CB  
2859  O OG1 . THR A 359 ? 0.5082 0.6333 0.5204 0.0109  0.0203  -0.0064 660 THR A OG1 
2860  C CG2 . THR A 359 ? 0.4388 0.5401 0.4450 0.0209  0.0240  0.0075  660 THR A CG2 
2861  N N   . GLU A 360 ? 0.4290 0.5261 0.4445 -0.0145 0.0208  -0.0130 661 GLU A N   
2862  C CA  . GLU A 360 ? 0.5545 0.6443 0.5686 -0.0249 0.0193  -0.0203 661 GLU A CA  
2863  C C   . GLU A 360 ? 0.6139 0.6782 0.6247 -0.0316 0.0207  -0.0174 661 GLU A C   
2864  O O   . GLU A 360 ? 0.5941 0.6405 0.5996 -0.0337 0.0195  -0.0205 661 GLU A O   
2865  C CB  . GLU A 360 ? 0.5130 0.6235 0.5318 -0.0340 0.0182  -0.0270 661 GLU A CB  
2866  C CG  . GLU A 360 ? 0.6950 0.7969 0.7112 -0.0466 0.0165  -0.0355 661 GLU A CG  
2867  C CD  . GLU A 360 ? 0.9800 1.1034 1.0017 -0.0589 0.0159  -0.0421 661 GLU A CD  
2868  O OE1 . GLU A 360 ? 1.0461 1.1976 1.0740 -0.0544 0.0158  -0.0422 661 GLU A OE1 
2869  O OE2 . GLU A 360 ? 1.0709 1.1833 1.0901 -0.0732 0.0157  -0.0472 661 GLU A OE2 
2870  N N   . SER A 361 ? 0.6205 0.6826 0.6333 -0.0338 0.0230  -0.0115 662 SER A N   
2871  C CA  . SER A 361 ? 0.5140 0.5523 0.5226 -0.0385 0.0243  -0.0076 662 SER A CA  
2872  C C   . SER A 361 ? 0.4867 0.5080 0.4909 -0.0299 0.0236  -0.0050 662 SER A C   
2873  O O   . SER A 361 ? 0.5806 0.5815 0.5788 -0.0325 0.0228  -0.0063 662 SER A O   
2874  C CB  . SER A 361 ? 0.5003 0.5418 0.5115 -0.0393 0.0268  -0.0013 662 SER A CB  
2875  O OG  . SER A 361 ? 0.5571 0.6132 0.5718 -0.0491 0.0279  -0.0041 662 SER A OG  
2876  N N   . PHE A 362 ? 0.5138 0.5438 0.5200 -0.0194 0.0239  -0.0016 663 PHE A N   
2877  C CA  . PHE A 362 ? 0.5709 0.5891 0.5742 -0.0118 0.0237  0.0011  663 PHE A CA  
2878  C C   . PHE A 362 ? 0.6718 0.6844 0.6709 -0.0101 0.0216  -0.0053 663 PHE A C   
2879  O O   . PHE A 362 ? 0.7488 0.7459 0.7437 -0.0071 0.0211  -0.0051 663 PHE A O   
2880  C CB  . PHE A 362 ? 0.5126 0.5415 0.5181 -0.0029 0.0250  0.0061  663 PHE A CB  
2881  C CG  . PHE A 362 ? 0.6161 0.6366 0.6198 0.0034  0.0253  0.0091  663 PHE A CG  
2882  C CD1 . PHE A 362 ? 0.5444 0.5527 0.5477 0.0032  0.0261  0.0136  663 PHE A CD1 
2883  C CD2 . PHE A 362 ? 0.5471 0.5740 0.5494 0.0096  0.0250  0.0070  663 PHE A CD2 
2884  C CE1 . PHE A 362 ? 0.5527 0.5568 0.5552 0.0088  0.0263  0.0156  663 PHE A CE1 
2885  C CE2 . PHE A 362 ? 0.6727 0.6953 0.6740 0.0149  0.0257  0.0094  663 PHE A CE2 
2886  C CZ  . PHE A 362 ? 0.6322 0.6442 0.6341 0.0144  0.0263  0.0135  663 PHE A CZ  
2887  N N   . ILE A 363 ? 0.5646 0.5903 0.5644 -0.0112 0.0202  -0.0115 664 ILE A N   
2888  C CA  . ILE A 363 ? 0.5193 0.5384 0.5140 -0.0103 0.0179  -0.0189 664 ILE A CA  
2889  C C   . ILE A 363 ? 0.5990 0.5953 0.5878 -0.0187 0.0168  -0.0223 664 ILE A C   
2890  O O   . ILE A 363 ? 0.6149 0.5940 0.5971 -0.0149 0.0155  -0.0246 664 ILE A O   
2891  C CB  . ILE A 363 ? 0.4642 0.5028 0.4603 -0.0108 0.0161  -0.0257 664 ILE A CB  
2892  C CG1 . ILE A 363 ? 0.4377 0.4941 0.4361 -0.0004 0.0171  -0.0216 664 ILE A CG1 
2893  C CG2 . ILE A 363 ? 0.3320 0.3621 0.3218 -0.0113 0.0134  -0.0347 664 ILE A CG2 
2894  C CD1 . ILE A 363 ? 0.5231 0.5728 0.5180 0.0086  0.0178  -0.0196 664 ILE A CD1 
2895  N N   . LYS A 364 ? 0.6076 0.6031 0.5978 -0.0299 0.0175  -0.0222 665 LYS A N   
2896  C CA  . LYS A 364 ? 0.6571 0.6284 0.6400 -0.0393 0.0170  -0.0240 665 LYS A CA  
2897  C C   . LYS A 364 ? 0.6591 0.6094 0.6371 -0.0338 0.0178  -0.0174 665 LYS A C   
2898  O O   . LYS A 364 ? 0.5804 0.5066 0.5489 -0.0338 0.0163  -0.0196 665 LYS A O   
2899  C CB  . LYS A 364 ? 0.6081 0.5861 0.5940 -0.0530 0.0185  -0.0240 665 LYS A CB  
2900  C CG  . LYS A 364 ? 0.7054 0.6909 0.6910 -0.0638 0.0168  -0.0334 665 LYS A CG  
2901  C CD  . LYS A 364 ? 0.8035 0.8080 0.7959 -0.0755 0.0187  -0.0332 665 LYS A CD  
2902  C CE  . LYS A 364 ? 0.9311 0.9388 0.9220 -0.0903 0.0172  -0.0427 665 LYS A CE  
2903  N NZ  . LYS A 364 ? 0.9486 0.9855 0.9489 -0.0999 0.0189  -0.0437 665 LYS A NZ  
2904  N N   . HIS A 365 ? 0.6482 0.6072 0.6318 -0.0285 0.0198  -0.0098 666 HIS A N   
2905  C CA  . HIS A 365 ? 0.5842 0.5277 0.5643 -0.0227 0.0202  -0.0039 666 HIS A CA  
2906  C C   . HIS A 365 ? 0.6993 0.6378 0.6763 -0.0113 0.0185  -0.0058 666 HIS A C   
2907  O O   . HIS A 365 ? 0.7275 0.6473 0.6976 -0.0071 0.0174  -0.0049 666 HIS A O   
2908  C CB  . HIS A 365 ? 0.5555 0.5115 0.5425 -0.0201 0.0224  0.0035  666 HIS A CB  
2909  C CG  . HIS A 365 ? 0.6260 0.5722 0.6111 -0.0128 0.0225  0.0088  666 HIS A CG  
2910  N ND1 . HIS A 365 ? 0.6509 0.5788 0.6299 -0.0151 0.0223  0.0121  666 HIS A ND1 
2911  C CD2 . HIS A 365 ? 0.6524 0.6064 0.6410 -0.0037 0.0227  0.0115  666 HIS A CD2 
2912  C CE1 . HIS A 365 ? 0.6763 0.6023 0.6556 -0.0069 0.0219  0.0159  666 HIS A CE1 
2913  N NE2 . HIS A 365 ? 0.5651 0.5073 0.5507 -0.0007 0.0223  0.0155  666 HIS A NE2 
2914  N N   . MET A 366 ? 0.6496 0.6058 0.6311 -0.0054 0.0184  -0.0084 667 MET A N   
2915  C CA  . MET A 366 ? 0.6468 0.6031 0.6262 0.0054  0.0175  -0.0101 667 MET A CA  
2916  C C   . MET A 366 ? 0.6718 0.6091 0.6414 0.0065  0.0147  -0.0174 667 MET A C   
2917  O O   . MET A 366 ? 0.5899 0.5140 0.5540 0.0142  0.0136  -0.0173 667 MET A O   
2918  C CB  . MET A 366 ? 0.7205 0.6993 0.7050 0.0101  0.0183  -0.0114 667 MET A CB  
2919  C CG  . MET A 366 ? 0.7582 0.7423 0.7419 0.0209  0.0184  -0.0118 667 MET A CG  
2920  S SD  . MET A 366 ? 0.6953 0.7053 0.6839 0.0249  0.0203  -0.0106 667 MET A SD  
2921  C CE  . MET A 366 ? 0.6445 0.6614 0.6349 0.0340  0.0225  -0.0058 667 MET A CE  
2922  N N   . GLU A 367 ? 0.6825 0.6180 0.6493 -0.0009 0.0133  -0.0242 668 GLU A N   
2923  C CA  . GLU A 367 ? 0.7668 0.6807 0.7224 -0.0008 0.0105  -0.0319 668 GLU A CA  
2924  C C   . GLU A 367 ? 0.6981 0.5830 0.6443 -0.0026 0.0099  -0.0289 668 GLU A C   
2925  O O   . GLU A 367 ? 0.6680 0.5352 0.6051 0.0063  0.0079  -0.0311 668 GLU A O   
2926  C CB  . GLU A 367 ? 0.8087 0.7262 0.7633 -0.0114 0.0092  -0.0397 668 GLU A CB  
2927  C CG  . GLU A 367 ? 0.8052 0.7497 0.7660 -0.0062 0.0089  -0.0437 668 GLU A CG  
2928  C CD  . GLU A 367 ? 0.8703 0.8283 0.8339 -0.0167 0.0079  -0.0500 668 GLU A CD  
2929  O OE1 . GLU A 367 ? 0.8054 0.7613 0.7708 -0.0293 0.0085  -0.0492 668 GLU A OE1 
2930  O OE2 . GLU A 367 ? 0.8911 0.8645 0.8552 -0.0120 0.0064  -0.0560 668 GLU A OE2 
2931  N N   . ASN A 368 ? 0.8490 0.7299 0.7970 -0.0126 0.0117  -0.0232 669 ASN A N   
2932  C CA  . ASN A 368 ? 0.8273 0.6804 0.7650 -0.0145 0.0113  -0.0192 669 ASN A CA  
2933  C C   . ASN A 368 ? 0.7436 0.5931 0.6801 -0.0004 0.0108  -0.0145 669 ASN A C   
2934  O O   . ASN A 368 ? 0.6706 0.4952 0.5949 0.0054  0.0087  -0.0150 669 ASN A O   
2935  C CB  . ASN A 368 ? 0.8441 0.6993 0.7853 -0.0271 0.0141  -0.0133 669 ASN A CB  
2936  C CG  . ASN A 368 ? 0.7898 0.6153 0.7186 -0.0306 0.0140  -0.0088 669 ASN A CG  
2937  O OD1 . ASN A 368 ? 0.7683 0.5676 0.6841 -0.0366 0.0126  -0.0127 669 ASN A OD1 
2938  N ND2 . ASN A 368 ? 0.6303 0.4583 0.5617 -0.0269 0.0155  -0.0006 669 ASN A ND2 
2939  N N   . GLU A 369 ? 0.6563 0.5304 0.6046 0.0053  0.0126  -0.0099 670 GLU A N   
2940  C CA  . GLU A 369 ? 0.5415 0.4183 0.4908 0.0178  0.0121  -0.0063 670 GLU A CA  
2941  C C   . GLU A 369 ? 0.6971 0.5715 0.6413 0.0302  0.0098  -0.0125 670 GLU A C   
2942  O O   . GLU A 369 ? 0.7581 0.6264 0.6983 0.0408  0.0084  -0.0111 670 GLU A O   
2943  C CB  . GLU A 369 ? 0.4803 0.3839 0.4428 0.0190  0.0147  -0.0010 670 GLU A CB  
2944  C CG  . GLU A 369 ? 0.6506 0.5552 0.6168 0.0105  0.0166  0.0054  670 GLU A CG  
2945  C CD  . GLU A 369 ? 0.6684 0.5619 0.6307 0.0148  0.0159  0.0107  670 GLU A CD  
2946  O OE1 . GLU A 369 ? 0.6141 0.5219 0.5834 0.0199  0.0167  0.0145  670 GLU A OE1 
2947  O OE2 . GLU A 369 ? 0.6366 0.5065 0.5879 0.0132  0.0145  0.0107  670 GLU A OE2 
2948  N N   . TYR A 370 ? 0.6535 0.5351 0.5979 0.0301  0.0092  -0.0195 671 TYR A N   
2949  C CA  . TYR A 370 ? 0.7102 0.5871 0.6477 0.0423  0.0069  -0.0263 671 TYR A CA  
2950  C C   . TYR A 370 ? 0.7347 0.5768 0.6557 0.0429  0.0036  -0.0308 671 TYR A C   
2951  O O   . TYR A 370 ? 0.7654 0.5957 0.6778 0.0558  0.0013  -0.0332 671 TYR A O   
2952  C CB  . TYR A 370 ? 0.7331 0.6284 0.6745 0.0429  0.0071  -0.0328 671 TYR A CB  
2953  C CG  . TYR A 370 ? 0.6981 0.6245 0.6514 0.0483  0.0099  -0.0290 671 TYR A CG  
2954  C CD1 . TYR A 370 ? 0.6726 0.6165 0.6360 0.0405  0.0127  -0.0232 671 TYR A CD1 
2955  C CD2 . TYR A 370 ? 0.7994 0.7374 0.7529 0.0611  0.0099  -0.0311 671 TYR A CD2 
2956  C CE1 . TYR A 370 ? 0.7190 0.6872 0.6909 0.0446  0.0154  -0.0192 671 TYR A CE1 
2957  C CE2 . TYR A 370 ? 0.7582 0.7238 0.7216 0.0641  0.0130  -0.0271 671 TYR A CE2 
2958  C CZ  . TYR A 370 ? 0.7179 0.6966 0.6898 0.0554  0.0157  -0.0208 671 TYR A CZ  
2959  O OH  . TYR A 370 ? 0.5985 0.6005 0.5780 0.0576  0.0189  -0.0162 671 TYR A OH  
2960  N N   . ARG A 371 ? 0.8402 0.6653 0.7558 0.0290  0.0035  -0.0320 672 ARG A N   
2961  C CA  . ARG A 371 ? 1.0041 0.7918 0.9020 0.0267  0.0009  -0.0352 672 ARG A CA  
2962  C C   . ARG A 371 ? 0.9816 0.7505 0.8709 0.0363  -0.0002 -0.0293 672 ARG A C   
2963  O O   . ARG A 371 ? 1.0189 0.7669 0.8948 0.0483  -0.0034 -0.0333 672 ARG A O   
2964  C CB  . ARG A 371 ? 1.2065 0.9834 1.1024 0.0072  0.0022  -0.0346 672 ARG A CB  
2965  C CG  . ARG A 371 ? 1.3454 1.1109 1.2339 -0.0018 0.0003  -0.0448 672 ARG A CG  
2966  C CD  . ARG A 371 ? 1.4357 1.2345 1.3375 -0.0033 0.0009  -0.0501 672 ARG A CD  
2967  N NE  . ARG A 371 ? 1.5229 1.3341 1.4259 0.0132  -0.0005 -0.0545 672 ARG A NE  
2968  C CZ  . ARG A 371 ? 1.4789 1.3169 1.3903 0.0157  -0.0003 -0.0592 672 ARG A CZ  
2969  N NH1 . ARG A 371 ? 1.4323 1.2880 1.3519 0.0036  0.0007  -0.0605 672 ARG A NH1 
2970  N NH2 . ARG A 371 ? 1.4277 1.2760 1.3388 0.0307  -0.0011 -0.0625 672 ARG A NH2 
2971  N N   . CYS A 372 ? 0.9693 0.7465 0.8657 0.0324  0.0020  -0.0202 673 CYS A N   
2972  C CA  . CYS A 372 ? 1.0260 0.7824 0.9124 0.0380  0.0009  -0.0140 673 CYS A CA  
2973  C C   . CYS A 372 ? 0.8960 0.6728 0.7908 0.0518  0.0007  -0.0096 673 CYS A C   
2974  O O   . CYS A 372 ? 0.8271 0.5887 0.7129 0.0598  -0.0011 -0.0056 673 CYS A O   
2975  C CB  . CYS A 372 ? 0.9897 0.7369 0.8751 0.0226  0.0033  -0.0069 673 CYS A CB  
2976  S SG  . CYS A 372 ? 0.9865 0.7709 0.8927 0.0177  0.0072  0.0005  673 CYS A SG  
2977  N N   . ARG A 373 ? 0.8877 0.6981 0.7985 0.0542  0.0026  -0.0099 674 ARG A N   
2978  C CA  . ARG A 373 ? 0.7352 0.5676 0.6552 0.0642  0.0029  -0.0059 674 ARG A CA  
2979  C C   . ARG A 373 ? 0.7664 0.6194 0.6917 0.0766  0.0024  -0.0114 674 ARG A C   
2980  O O   . ARG A 373 ? 0.7246 0.5925 0.6543 0.0871  0.0018  -0.0096 674 ARG A O   
2981  C CB  . ARG A 373 ? 0.6263 0.4815 0.5611 0.0542  0.0064  0.0006  674 ARG A CB  
2982  C CG  . ARG A 373 ? 0.5821 0.4528 0.5239 0.0606  0.0065  0.0061  674 ARG A CG  
2983  C CD  . ARG A 373 ? 0.4924 0.3862 0.4483 0.0519  0.0099  0.0109  674 ARG A CD  
2984  N NE  . ARG A 373 ? 0.5482 0.4534 0.5091 0.0564  0.0096  0.0156  674 ARG A NE  
2985  C CZ  . ARG A 373 ? 0.5872 0.5134 0.5596 0.0521  0.0119  0.0191  674 ARG A CZ  
2986  N NH1 . ARG A 373 ? 0.6785 0.6159 0.6579 0.0445  0.0147  0.0191  674 ARG A NH1 
2987  N NH2 . ARG A 373 ? 0.4410 0.3764 0.4170 0.0556  0.0112  0.0224  674 ARG A NH2 
2988  N N   . GLY A 374 ? 0.7106 0.5665 0.6353 0.0755  0.0025  -0.0182 675 GLY A N   
2989  C CA  . GLY A 374 ? 0.7991 0.6752 0.7277 0.0872  0.0024  -0.0234 675 GLY A CA  
2990  C C   . GLY A 374 ? 0.8439 0.7535 0.7883 0.0828  0.0061  -0.0210 675 GLY A C   
2991  O O   . GLY A 374 ? 0.8905 0.8210 0.8394 0.0918  0.0069  -0.0238 675 GLY A O   
2992  N N   . GLY A 375 ? 0.7613 0.6763 0.7131 0.0697  0.0086  -0.0157 676 GLY A N   
2993  C CA  . GLY A 375 ? 0.7602 0.7027 0.7244 0.0655  0.0120  -0.0130 676 GLY A CA  
2994  C C   . GLY A 375 ? 0.6697 0.6144 0.6404 0.0540  0.0141  -0.0057 676 GLY A C   
2995  O O   . GLY A 375 ? 0.7072 0.6341 0.6735 0.0487  0.0131  -0.0031 676 GLY A O   
2996  N N   . CYS A 376 ? 0.5613 0.5276 0.5414 0.0508  0.0170  -0.0025 677 CYS A N   
2997  C CA  . CYS A 376 ? 0.5438 0.5144 0.5299 0.0417  0.0191  0.0039  677 CYS A CA  
2998  C C   . CYS A 376 ? 0.6335 0.6266 0.6275 0.0416  0.0221  0.0072  677 CYS A C   
2999  O O   . CYS A 376 ? 0.7743 0.7763 0.7690 0.0403  0.0233  0.0054  677 CYS A O   
3000  C CB  . CYS A 376 ? 0.5146 0.4756 0.4981 0.0325  0.0188  0.0023  677 CYS A CB  
3001  S SG  . CYS A 376 ? 0.5828 0.5555 0.5739 0.0240  0.0215  0.0085  677 CYS A SG  
3002  N N   . PRO A 377 ? 0.5931 0.5953 0.5923 0.0427  0.0235  0.0121  678 PRO A N   
3003  C CA  . PRO A 377 ? 0.5733 0.5941 0.5781 0.0416  0.0267  0.0156  678 PRO A CA  
3004  C C   . PRO A 377 ? 0.5922 0.6133 0.5982 0.0343  0.0284  0.0193  678 PRO A C   
3005  O O   . PRO A 377 ? 0.6389 0.6507 0.6449 0.0293  0.0278  0.0218  678 PRO A O   
3006  C CB  . PRO A 377 ? 0.6661 0.6934 0.6754 0.0425  0.0272  0.0194  678 PRO A CB  
3007  C CG  . PRO A 377 ? 0.6144 0.6251 0.6207 0.0421  0.0244  0.0197  678 PRO A CG  
3008  C CD  . PRO A 377 ? 0.6101 0.6059 0.6091 0.0451  0.0220  0.0143  678 PRO A CD  
3009  N N   . ALA A 378 ? 0.6523 0.6848 0.6584 0.0348  0.0304  0.0196  679 ALA A N   
3010  C CA  . ALA A 378 ? 0.5626 0.5965 0.5684 0.0304  0.0317  0.0227  679 ALA A CA  
3011  C C   . ALA A 378 ? 0.5623 0.6088 0.5680 0.0314  0.0348  0.0268  679 ALA A C   
3012  O O   . ALA A 378 ? 0.5105 0.5672 0.5162 0.0351  0.0362  0.0258  679 ALA A O   
3013  C CB  . ALA A 378 ? 0.4960 0.5273 0.4987 0.0298  0.0298  0.0175  679 ALA A CB  
3014  N N   . ASP A 379 ? 0.4947 0.5399 0.4992 0.0282  0.0361  0.0316  680 ASP A N   
3015  C CA  . ASP A 379 ? 0.4641 0.5161 0.4660 0.0281  0.0393  0.0371  680 ASP A CA  
3016  C C   . ASP A 379 ? 0.5784 0.6319 0.5755 0.0301  0.0390  0.0370  680 ASP A C   
3017  O O   . ASP A 379 ? 0.4954 0.5428 0.4913 0.0285  0.0384  0.0392  680 ASP A O   
3018  C CB  . ASP A 379 ? 0.5405 0.5863 0.5434 0.0232  0.0409  0.0431  680 ASP A CB  
3019  C CG  . ASP A 379 ? 0.5739 0.6228 0.5722 0.0216  0.0445  0.0493  680 ASP A CG  
3020  O OD1 . ASP A 379 ? 0.5791 0.6249 0.5783 0.0166  0.0461  0.0533  680 ASP A OD1 
3021  O OD2 . ASP A 379 ? 0.7002 0.7540 0.6932 0.0248  0.0457  0.0502  680 ASP A OD2 
3022  N N   . TRP A 380 ? 0.6278 0.6911 0.6221 0.0344  0.0391  0.0340  681 TRP A N   
3023  C CA  . TRP A 380 ? 0.3920 0.4603 0.3815 0.0376  0.0383  0.0331  681 TRP A CA  
3024  C C   . TRP A 380 ? 0.3879 0.4525 0.3722 0.0377  0.0401  0.0404  681 TRP A C   
3025  O O   . TRP A 380 ? 0.3968 0.4606 0.3791 0.0393  0.0384  0.0400  681 TRP A O   
3026  C CB  . TRP A 380 ? 0.5299 0.6104 0.5158 0.0425  0.0391  0.0303  681 TRP A CB  
3027  C CG  . TRP A 380 ? 0.3468 0.4350 0.3285 0.0464  0.0370  0.0263  681 TRP A CG  
3028  C CD1 . TRP A 380 ? 0.3074 0.3994 0.2904 0.0474  0.0337  0.0174  681 TRP A CD1 
3029  C CD2 . TRP A 380 ? 0.4057 0.4987 0.3805 0.0502  0.0378  0.0307  681 TRP A CD2 
3030  N NE1 . TRP A 380 ? 0.4857 0.5875 0.4642 0.0510  0.0323  0.0155  681 TRP A NE1 
3031  C CE2 . TRP A 380 ? 0.4648 0.5678 0.4380 0.0537  0.0346  0.0238  681 TRP A CE2 
3032  C CE3 . TRP A 380 ? 0.4517 0.5404 0.4201 0.0511  0.0407  0.0398  681 TRP A CE3 
3033  C CZ2 . TRP A 380 ? 0.5260 0.6371 0.4923 0.0592  0.0340  0.0257  681 TRP A CZ2 
3034  C CZ3 . TRP A 380 ? 0.4203 0.5138 0.3803 0.0570  0.0402  0.0422  681 TRP A CZ3 
3035  C CH2 . TRP A 380 ? 0.4878 0.5936 0.4472 0.0615  0.0368  0.0353  681 TRP A CH2 
3036  N N   . VAL A 381 ? 0.3459 0.4083 0.3272 0.0360  0.0435  0.0471  682 VAL A N   
3037  C CA  . VAL A 381 ? 0.2997 0.3538 0.2735 0.0359  0.0454  0.0545  682 VAL A CA  
3038  C C   . VAL A 381 ? 0.4963 0.5395 0.4715 0.0344  0.0434  0.0549  682 VAL A C   
3039  O O   . VAL A 381 ? 0.5564 0.5930 0.5242 0.0373  0.0435  0.0588  682 VAL A O   
3040  C CB  . VAL A 381 ? 0.3608 0.4124 0.3324 0.0311  0.0495  0.0608  682 VAL A CB  
3041  C CG1 . VAL A 381 ? 0.4778 0.5153 0.4402 0.0294  0.0513  0.0685  682 VAL A CG1 
3042  C CG2 . VAL A 381 ? 0.4055 0.4705 0.3744 0.0334  0.0520  0.0609  682 VAL A CG2 
3043  N N   . TRP A 382 ? 0.4837 0.5244 0.4670 0.0307  0.0416  0.0508  683 TRP A N   
3044  C CA  . TRP A 382 ? 0.5067 0.5389 0.4915 0.0290  0.0400  0.0508  683 TRP A CA  
3045  C C   . TRP A 382 ? 0.5981 0.6355 0.5869 0.0300  0.0371  0.0446  683 TRP A C   
3046  O O   . TRP A 382 ? 0.5913 0.6269 0.5791 0.0311  0.0361  0.0447  683 TRP A O   
3047  C CB  . TRP A 382 ? 0.5191 0.5434 0.5087 0.0232  0.0404  0.0518  683 TRP A CB  
3048  C CG  . TRP A 382 ? 0.5182 0.5344 0.5032 0.0201  0.0429  0.0581  683 TRP A CG  
3049  C CD1 . TRP A 382 ? 0.4252 0.4442 0.4072 0.0184  0.0459  0.0618  683 TRP A CD1 
3050  C CD2 . TRP A 382 ? 0.6320 0.6355 0.6143 0.0174  0.0429  0.0610  683 TRP A CD2 
3051  N NE1 . TRP A 382 ? 0.5694 0.5773 0.5468 0.0136  0.0477  0.0670  683 TRP A NE1 
3052  C CE2 . TRP A 382 ? 0.6498 0.6473 0.6271 0.0133  0.0456  0.0662  683 TRP A CE2 
3053  C CE3 . TRP A 382 ? 0.6651 0.6623 0.6483 0.0177  0.0409  0.0594  683 TRP A CE3 
3054  C CZ2 . TRP A 382 ? 0.6097 0.5930 0.5823 0.0095  0.0460  0.0694  683 TRP A CZ2 
3055  C CZ3 . TRP A 382 ? 0.7447 0.7290 0.7233 0.0152  0.0413  0.0624  683 TRP A CZ3 
3056  C CH2 . TRP A 382 ? 0.6973 0.6739 0.6705 0.0111  0.0436  0.0671  683 TRP A CH2 
3057  N N   . ILE A 383 ? 0.3082 0.3521 0.3012 0.0294  0.0358  0.0389  684 ILE A N   
3058  C CA  . ILE A 383 ? 0.3297 0.3774 0.3259 0.0280  0.0332  0.0328  684 ILE A CA  
3059  C C   . ILE A 383 ? 0.3736 0.4320 0.3666 0.0324  0.0322  0.0314  684 ILE A C   
3060  O O   . ILE A 383 ? 0.5337 0.5961 0.5287 0.0313  0.0308  0.0289  684 ILE A O   
3061  C CB  . ILE A 383 ? 0.2761 0.3249 0.2751 0.0264  0.0319  0.0268  684 ILE A CB  
3062  C CG1 . ILE A 383 ? 0.4792 0.5180 0.4810 0.0236  0.0323  0.0280  684 ILE A CG1 
3063  C CG2 . ILE A 383 ? 0.2581 0.3095 0.2590 0.0231  0.0294  0.0203  684 ILE A CG2 
3064  C CD1 . ILE A 383 ? 0.6391 0.6689 0.6428 0.0194  0.0320  0.0302  684 ILE A CD1 
3065  N N   . VAL A 384 ? 0.4675 0.5323 0.4551 0.0378  0.0330  0.0331  685 VAL A N   
3066  C CA  . VAL A 384 ? 0.4574 0.5344 0.4412 0.0434  0.0314  0.0312  685 VAL A CA  
3067  C C   . VAL A 384 ? 0.4662 0.5403 0.4463 0.0471  0.0315  0.0356  685 VAL A C   
3068  O O   . VAL A 384 ? 0.4624 0.5244 0.4372 0.0483  0.0336  0.0424  685 VAL A O   
3069  C CB  . VAL A 384 ? 0.4952 0.5788 0.4724 0.0491  0.0323  0.0327  685 VAL A CB  
3070  C CG1 . VAL A 384 ? 0.2782 0.3753 0.2503 0.0563  0.0302  0.0310  685 VAL A CG1 
3071  C CG2 . VAL A 384 ? 0.4512 0.5390 0.4319 0.0466  0.0317  0.0267  685 VAL A CG2 
3072  N N   . PRO A 385 ? 0.5074 0.5922 0.4897 0.0486  0.0292  0.0314  686 PRO A N   
3073  C CA  . PRO A 385 ? 0.5631 0.6467 0.5412 0.0542  0.0291  0.0348  686 PRO A CA  
3074  C C   . PRO A 385 ? 0.7037 0.7833 0.6699 0.0637  0.0299  0.0410  686 PRO A C   
3075  O O   . PRO A 385 ? 0.7878 0.8741 0.7497 0.0673  0.0298  0.0411  686 PRO A O   
3076  C CB  . PRO A 385 ? 0.4980 0.6014 0.4813 0.0549  0.0264  0.0278  686 PRO A CB  
3077  C CG  . PRO A 385 ? 0.5376 0.6443 0.5293 0.0451  0.0257  0.0214  686 PRO A CG  
3078  C CD  . PRO A 385 ? 0.4721 0.5687 0.4620 0.0433  0.0269  0.0230  686 PRO A CD  
3079  N N   . PRO A 386 ? 0.6703 0.7382 0.6294 0.0684  0.0307  0.0463  687 PRO A N   
3080  C CA  . PRO A 386 ? 0.6335 0.6920 0.5782 0.0773  0.0316  0.0533  687 PRO A CA  
3081  C C   . PRO A 386 ? 0.6568 0.7300 0.5947 0.0893  0.0290  0.0519  687 PRO A C   
3082  O O   . PRO A 386 ? 0.6254 0.6886 0.5490 0.0986  0.0294  0.0581  687 PRO A O   
3083  C CB  . PRO A 386 ? 0.6017 0.6405 0.5410 0.0776  0.0328  0.0580  687 PRO A CB  
3084  C CG  . PRO A 386 ? 0.6261 0.6742 0.5759 0.0747  0.0311  0.0520  687 PRO A CG  
3085  C CD  . PRO A 386 ? 0.5169 0.5778 0.4796 0.0656  0.0307  0.0461  687 PRO A CD  
3086  N N   . MET A 387 ? 0.4885 0.5847 0.4353 0.0894  0.0262  0.0439  688 MET A N   
3087  C CA  . MET A 387 ? 0.4716 0.5867 0.4135 0.1008  0.0231  0.0412  688 MET A CA  
3088  C C   . MET A 387 ? 0.6537 0.7922 0.6072 0.0948  0.0208  0.0318  688 MET A C   
3089  O O   . MET A 387 ? 0.6377 0.7768 0.6027 0.0833  0.0213  0.0273  688 MET A O   
3090  C CB  . MET A 387 ? 0.5322 0.6526 0.4717 0.1096  0.0213  0.0404  688 MET A CB  
3091  C CG  . MET A 387 ? 0.6270 0.7623 0.5812 0.1018  0.0204  0.0329  688 MET A CG  
3092  S SD  . MET A 387 ? 0.6164 0.7710 0.5692 0.1144  0.0176  0.0296  688 MET A SD  
3093  C CE  . MET A 387 ? 0.6571 0.8493 0.6168 0.1168  0.0137  0.0205  688 MET A CE  
3094  N N   . SER A 388 ? 0.6152 0.7716 0.5644 0.1027  0.0183  0.0290  689 SER A N   
3095  C CA  . SER A 388 ? 0.4906 0.6701 0.4494 0.0972  0.0155  0.0191  689 SER A CA  
3096  C C   . SER A 388 ? 0.4590 0.6291 0.4244 0.0848  0.0173  0.0167  689 SER A C   
3097  O O   . SER A 388 ? 0.4885 0.6677 0.4642 0.0753  0.0159  0.0086  689 SER A O   
3098  C CB  . SER A 388 ? 0.4016 0.6007 0.3714 0.0936  0.0132  0.0114  689 SER A CB  
3099  O OG  . SER A 388 ? 0.5536 0.7649 0.5179 0.1065  0.0113  0.0125  689 SER A OG  
3100  N N   . GLY A 389 ? 0.4553 0.6069 0.4141 0.0848  0.0204  0.0236  690 GLY A N   
3101  C CA  . GLY A 389 ? 0.4500 0.5930 0.4141 0.0753  0.0222  0.0218  690 GLY A CA  
3102  C C   . GLY A 389 ? 0.6123 0.7695 0.5820 0.0708  0.0196  0.0119  690 GLY A C   
3103  O O   . GLY A 389 ? 0.6588 0.8133 0.6374 0.0610  0.0191  0.0063  690 GLY A O   
3104  N N   . SER A 390 ? 0.5547 0.7259 0.5182 0.0778  0.0179  0.0096  691 SER A N   
3105  C CA  . SER A 390 ? 0.5305 0.7124 0.4971 0.0741  0.0157  0.0001  691 SER A CA  
3106  C C   . SER A 390 ? 0.5093 0.7070 0.4845 0.0678  0.0117  -0.0106 691 SER A C   
3107  O O   . SER A 390 ? 0.5053 0.7082 0.4832 0.0624  0.0096  -0.0194 691 SER A O   
3108  C CB  . SER A 390 ? 0.6381 0.8312 0.5943 0.0839  0.0150  0.0008  691 SER A CB  
3109  O OG  . SER A 390 ? 0.5756 0.7910 0.5297 0.0906  0.0108  -0.0041 691 SER A OG  
3110  N N   . ILE A 391 ? 0.4429 0.6490 0.4222 0.0680  0.0106  -0.0105 692 ILE A N   
3111  C CA  . ILE A 391 ? 0.5313 0.7527 0.5201 0.0591  0.0077  -0.0204 692 ILE A CA  
3112  C C   . ILE A 391 ? 0.5641 0.7697 0.5608 0.0466  0.0098  -0.0204 692 ILE A C   
3113  O O   . ILE A 391 ? 0.6232 0.8379 0.6273 0.0366  0.0082  -0.0278 692 ILE A O   
3114  C CB  . ILE A 391 ? 0.5490 0.7946 0.5387 0.0661  0.0052  -0.0218 692 ILE A CB  
3115  C CG1 . ILE A 391 ? 0.4785 0.7152 0.4685 0.0692  0.0076  -0.0141 692 ILE A CG1 
3116  C CG2 . ILE A 391 ? 0.5205 0.7799 0.5001 0.0804  0.0030  -0.0205 692 ILE A CG2 
3117  C CD1 . ILE A 391 ? 0.4052 0.6666 0.3953 0.0784  0.0050  -0.0159 692 ILE A CD1 
3118  N N   . THR A 392 ? 0.5773 0.7602 0.5720 0.0463  0.0132  -0.0126 693 THR A N   
3119  C CA  . THR A 392 ? 0.5415 0.7081 0.5419 0.0351  0.0148  -0.0132 693 THR A CA  
3120  C C   . THR A 392 ? 0.5344 0.6877 0.5333 0.0309  0.0149  -0.0164 693 THR A C   
3121  O O   . THR A 392 ? 0.6170 0.7672 0.6102 0.0378  0.0157  -0.0136 693 THR A O   
3122  C CB  . THR A 392 ? 0.5599 0.7100 0.5593 0.0370  0.0180  -0.0037 693 THR A CB  
3123  O OG1 . THR A 392 ? 0.6104 0.7480 0.6035 0.0428  0.0200  0.0025  693 THR A OG1 
3124  C CG2 . THR A 392 ? 0.5507 0.7121 0.5491 0.0441  0.0178  -0.0003 693 THR A CG2 
3125  N N   . PRO A 393 ? 0.5158 0.6601 0.5187 0.0200  0.0143  -0.0219 694 PRO A N   
3126  C CA  . PRO A 393 ? 0.5484 0.6812 0.5483 0.0175  0.0134  -0.0271 694 PRO A CA  
3127  C C   . PRO A 393 ? 0.6150 0.7300 0.6116 0.0220  0.0160  -0.0207 694 PRO A C   
3128  O O   . PRO A 393 ? 0.6330 0.7422 0.6261 0.0236  0.0154  -0.0247 694 PRO A O   
3129  C CB  . PRO A 393 ? 0.4417 0.5659 0.4449 0.0044  0.0122  -0.0334 694 PRO A CB  
3130  C CG  . PRO A 393 ? 0.5946 0.7182 0.6026 0.0007  0.0143  -0.0276 694 PRO A CG  
3131  C CD  . PRO A 393 ? 0.4994 0.6430 0.5082 0.0096  0.0144  -0.0238 694 PRO A CD  
3132  N N   . VAL A 394 ? 0.7116 0.8186 0.7093 0.0240  0.0189  -0.0117 695 VAL A N   
3133  C CA  . VAL A 394 ? 0.6230 0.7160 0.6187 0.0270  0.0212  -0.0063 695 VAL A CA  
3134  C C   . VAL A 394 ? 0.5479 0.6487 0.5385 0.0359  0.0226  -0.0029 695 VAL A C   
3135  O O   . VAL A 394 ? 0.4194 0.5140 0.4082 0.0384  0.0243  -0.0011 695 VAL A O   
3136  C CB  . VAL A 394 ? 0.5742 0.6562 0.5723 0.0254  0.0237  0.0018  695 VAL A CB  
3137  C CG1 . VAL A 394 ? 0.4774 0.5462 0.4787 0.0170  0.0232  -0.0002 695 VAL A CG1 
3138  C CG2 . VAL A 394 ? 0.3524 0.4432 0.3504 0.0285  0.0243  0.0065  695 VAL A CG2 
3139  N N   . PHE A 395 ? 0.5266 0.6418 0.5143 0.0411  0.0220  -0.0018 696 PHE A N   
3140  C CA  . PHE A 395 ? 0.5008 0.6234 0.4816 0.0495  0.0234  0.0017  696 PHE A CA  
3141  C C   . PHE A 395 ? 0.5127 0.6379 0.4912 0.0510  0.0227  -0.0045 696 PHE A C   
3142  O O   . PHE A 395 ? 0.4603 0.5838 0.4353 0.0549  0.0254  -0.0005 696 PHE A O   
3143  C CB  . PHE A 395 ? 0.5322 0.6708 0.5091 0.0554  0.0216  0.0017  696 PHE A CB  
3144  C CG  . PHE A 395 ? 0.5992 0.7441 0.5668 0.0644  0.0232  0.0067  696 PHE A CG  
3145  C CD1 . PHE A 395 ? 0.5611 0.6988 0.5227 0.0688  0.0262  0.0171  696 PHE A CD1 
3146  C CD2 . PHE A 395 ? 0.5955 0.7524 0.5590 0.0683  0.0217  0.0008  696 PHE A CD2 
3147  C CE1 . PHE A 395 ? 0.5667 0.7083 0.5179 0.0762  0.0281  0.0226  696 PHE A CE1 
3148  C CE2 . PHE A 395 ? 0.4499 0.6129 0.4037 0.0765  0.0235  0.0060  696 PHE A CE2 
3149  C CZ  . PHE A 395 ? 0.5000 0.6552 0.4474 0.0802  0.0268  0.0173  696 PHE A CZ  
3150  N N   . HIS A 396 ? 0.4786 0.6077 0.4587 0.0475  0.0192  -0.0146 697 HIS A N   
3151  C CA  . HIS A 396 ? 0.5795 0.7108 0.5560 0.0496  0.0178  -0.0223 697 HIS A CA  
3152  C C   . HIS A 396 ? 0.6317 0.7459 0.6098 0.0463  0.0182  -0.0249 697 HIS A C   
3153  O O   . HIS A 396 ? 0.6708 0.7834 0.6455 0.0476  0.0163  -0.0331 697 HIS A O   
3154  C CB  . HIS A 396 ? 0.6276 0.7705 0.6039 0.0471  0.0134  -0.0329 697 HIS A CB  
3155  C CG  . HIS A 396 ? 0.6376 0.7981 0.6137 0.0501  0.0123  -0.0308 697 HIS A CG  
3156  N ND1 . HIS A 396 ? 0.5798 0.7563 0.5492 0.0593  0.0118  -0.0300 697 HIS A ND1 
3157  C CD2 . HIS A 396 ? 0.6424 0.8075 0.6234 0.0465  0.0116  -0.0290 697 HIS A CD2 
3158  C CE1 . HIS A 396 ? 0.6456 0.8352 0.6154 0.0618  0.0105  -0.0280 697 HIS A CE1 
3159  N NE2 . HIS A 396 ? 0.6841 0.8680 0.6613 0.0543  0.0103  -0.0277 697 HIS A NE2 
3160  N N   . GLN A 397 ? 0.6238 0.7252 0.6060 0.0428  0.0202  -0.0186 698 GLN A N   
3161  C CA  . GLN A 397 ? 0.5342 0.6190 0.5174 0.0405  0.0202  -0.0203 698 GLN A CA  
3162  C C   . GLN A 397 ? 0.5728 0.6579 0.5555 0.0463  0.0237  -0.0138 698 GLN A C   
3163  O O   . GLN A 397 ? 0.6122 0.6979 0.5972 0.0458  0.0265  -0.0050 698 GLN A O   
3164  C CB  . GLN A 397 ? 0.4105 0.4823 0.3981 0.0324  0.0199  -0.0179 698 GLN A CB  
3165  C CG  . GLN A 397 ? 0.4538 0.5071 0.4410 0.0310  0.0198  -0.0185 698 GLN A CG  
3166  C CD  . GLN A 397 ? 0.5713 0.6157 0.5532 0.0309  0.0168  -0.0285 698 GLN A CD  
3167  O OE1 . GLN A 397 ? 0.5616 0.6036 0.5421 0.0243  0.0142  -0.0350 698 GLN A OE1 
3168  N NE2 . GLN A 397 ? 0.4696 0.5095 0.4480 0.0383  0.0169  -0.0303 698 GLN A NE2 
3169  N N   . GLU A 398 ? 0.4714 0.5569 0.4508 0.0516  0.0235  -0.0187 699 GLU A N   
3170  C CA  . GLU A 398 ? 0.5205 0.6078 0.5009 0.0560  0.0267  -0.0136 699 GLU A CA  
3171  C C   . GLU A 398 ? 0.6021 0.6746 0.5869 0.0521  0.0267  -0.0102 699 GLU A C   
3172  O O   . GLU A 398 ? 0.5395 0.5975 0.5243 0.0479  0.0239  -0.0142 699 GLU A O   
3173  C CB  . GLU A 398 ? 0.4891 0.5814 0.4650 0.0636  0.0261  -0.0206 699 GLU A CB  
3174  C CG  . GLU A 398 ? 0.5163 0.6273 0.4876 0.0690  0.0278  -0.0209 699 GLU A CG  
3175  C CD  . GLU A 398 ? 0.6302 0.7464 0.5962 0.0769  0.0267  -0.0298 699 GLU A CD  
3176  O OE1 . GLU A 398 ? 0.6865 0.8183 0.6476 0.0819  0.0277  -0.0314 699 GLU A OE1 
3177  O OE2 . GLU A 398 ? 0.6642 0.7685 0.6298 0.0790  0.0248  -0.0352 699 GLU A OE2 
3178  N N   . MET A 399 ? 0.5144 0.5907 0.5024 0.0527  0.0300  -0.0026 700 MET A N   
3179  C CA  . MET A 399 ? 0.5706 0.6360 0.5630 0.0492  0.0302  0.0016  700 MET A CA  
3180  C C   . MET A 399 ? 0.6321 0.7056 0.6269 0.0530  0.0328  0.0048  700 MET A C   
3181  O O   . MET A 399 ? 0.7176 0.8039 0.7131 0.0530  0.0363  0.0102  700 MET A O   
3182  C CB  . MET A 399 ? 0.5269 0.5890 0.5220 0.0428  0.0312  0.0086  700 MET A CB  
3183  C CG  . MET A 399 ? 0.5224 0.5788 0.5169 0.0382  0.0288  0.0056  700 MET A CG  
3184  S SD  . MET A 399 ? 0.6160 0.6741 0.6122 0.0343  0.0305  0.0136  700 MET A SD  
3185  C CE  . MET A 399 ? 0.3336 0.3925 0.3298 0.0304  0.0275  0.0079  700 MET A CE  
3186  N N   . LEU A 400 ? 0.5816 0.6480 0.5772 0.0560  0.0310  0.0016  701 LEU A N   
3187  C CA  . LEU A 400 ? 0.6606 0.7364 0.6598 0.0595  0.0329  0.0041  701 LEU A CA  
3188  C C   . LEU A 400 ? 0.6706 0.7415 0.6750 0.0532  0.0337  0.0110  701 LEU A C   
3189  O O   . LEU A 400 ? 0.5688 0.6240 0.5729 0.0495  0.0313  0.0112  701 LEU A O   
3190  C CB  . LEU A 400 ? 0.6141 0.6852 0.6107 0.0680  0.0300  -0.0031 701 LEU A CB  
3191  C CG  . LEU A 400 ? 0.6192 0.6981 0.6105 0.0758  0.0296  -0.0105 701 LEU A CG  
3192  C CD1 . LEU A 400 ? 0.6510 0.7175 0.6369 0.0843  0.0258  -0.0182 701 LEU A CD1 
3193  C CD2 . LEU A 400 ? 0.6443 0.7485 0.6385 0.0789  0.0340  -0.0077 701 LEU A CD2 
3194  N N   . ASN A 401 ? 0.6504 0.7349 0.6589 0.0512  0.0371  0.0164  702 ASN A N   
3195  C CA  . ASN A 401 ? 0.6516 0.7322 0.6641 0.0442  0.0380  0.0228  702 ASN A CA  
3196  C C   . ASN A 401 ? 0.6263 0.7172 0.6441 0.0460  0.0383  0.0230  702 ASN A C   
3197  O O   . ASN A 401 ? 0.6981 0.8075 0.7182 0.0476  0.0412  0.0234  702 ASN A O   
3198  C CB  . ASN A 401 ? 0.6228 0.7078 0.6345 0.0380  0.0417  0.0295  702 ASN A CB  
3199  C CG  . ASN A 401 ? 0.5253 0.6020 0.5392 0.0307  0.0420  0.0352  702 ASN A CG  
3200  O OD1 . ASN A 401 ? 0.6310 0.6966 0.6464 0.0299  0.0392  0.0340  702 ASN A OD1 
3201  N ND2 . ASN A 401 ? 0.5833 0.6643 0.5962 0.0254  0.0456  0.0413  702 ASN A ND2 
3202  N N   . TYR A 402 ? 0.6440 0.7247 0.6635 0.0455  0.0355  0.0229  703 TYR A N   
3203  C CA  . TYR A 402 ? 0.6641 0.7558 0.6886 0.0479  0.0350  0.0227  703 TYR A CA  
3204  C C   . TYR A 402 ? 0.6967 0.7757 0.7225 0.0433  0.0328  0.0256  703 TYR A C   
3205  O O   . TYR A 402 ? 0.7123 0.7736 0.7344 0.0401  0.0314  0.0267  703 TYR A O   
3206  C CB  . TYR A 402 ? 0.5192 0.6155 0.5418 0.0597  0.0326  0.0158  703 TYR A CB  
3207  C CG  . TYR A 402 ? 0.5847 0.6588 0.5996 0.0646  0.0287  0.0112  703 TYR A CG  
3208  C CD1 . TYR A 402 ? 0.6501 0.7070 0.6622 0.0660  0.0251  0.0110  703 TYR A CD1 
3209  C CD2 . TYR A 402 ? 0.5966 0.6664 0.6063 0.0671  0.0287  0.0071  703 TYR A CD2 
3210  C CE1 . TYR A 402 ? 0.6339 0.6684 0.6375 0.0687  0.0220  0.0073  703 TYR A CE1 
3211  C CE2 . TYR A 402 ? 0.5403 0.5890 0.5425 0.0696  0.0252  0.0025  703 TYR A CE2 
3212  C CZ  . TYR A 402 ? 0.6129 0.6433 0.6119 0.0699  0.0221  0.0028  703 TYR A CZ  
3213  O OH  . TYR A 402 ? 0.6829 0.6907 0.6732 0.0706  0.0191  -0.0013 703 TYR A OH  
3214  N N   . ARG A 403 ? 0.6221 0.7127 0.6532 0.0428  0.0326  0.0266  704 ARG A N   
3215  C CA  . ARG A 403 ? 0.6248 0.7075 0.6574 0.0376  0.0309  0.0296  704 ARG A CA  
3216  C C   . ARG A 403 ? 0.6664 0.7449 0.6976 0.0460  0.0265  0.0262  704 ARG A C   
3217  O O   . ARG A 403 ? 0.6369 0.7325 0.6721 0.0516  0.0256  0.0239  704 ARG A O   
3218  C CB  . ARG A 403 ? 0.7045 0.8029 0.7434 0.0295  0.0335  0.0330  704 ARG A CB  
3219  C CG  . ARG A 403 ? 0.8393 0.9378 0.8769 0.0209  0.0379  0.0375  704 ARG A CG  
3220  C CD  . ARG A 403 ? 0.9625 1.0492 0.9991 0.0114  0.0383  0.0420  704 ARG A CD  
3221  N NE  . ARG A 403 ? 1.0554 1.1433 1.0955 0.0105  0.0352  0.0410  704 ARG A NE  
3222  C CZ  . ARG A 403 ? 1.0825 1.1880 1.1287 0.0068  0.0356  0.0405  704 ARG A CZ  
3223  N NH1 . ARG A 403 ? 1.0282 1.1518 1.0780 0.0026  0.0394  0.0414  704 ARG A NH1 
3224  N NH2 . ARG A 403 ? 1.1531 1.2595 1.2018 0.0069  0.0322  0.0391  704 ARG A NH2 
3225  N N   . LEU A 404 ? 0.5640 0.6207 0.5891 0.0468  0.0239  0.0263  705 LEU A N   
3226  C CA  . LEU A 404 ? 0.5740 0.6224 0.5955 0.0535  0.0198  0.0249  705 LEU A CA  
3227  C C   . LEU A 404 ? 0.5176 0.5647 0.5414 0.0472  0.0190  0.0287  705 LEU A C   
3228  O O   . LEU A 404 ? 0.5420 0.5865 0.5677 0.0377  0.0212  0.0322  705 LEU A O   
3229  C CB  . LEU A 404 ? 0.5136 0.5374 0.5255 0.0567  0.0177  0.0233  705 LEU A CB  
3230  C CG  . LEU A 404 ? 0.5176 0.5398 0.5258 0.0623  0.0180  0.0185  705 LEU A CG  
3231  C CD1 . LEU A 404 ? 0.5223 0.5181 0.5201 0.0631  0.0158  0.0167  705 LEU A CD1 
3232  C CD2 . LEU A 404 ? 0.5689 0.6062 0.5782 0.0737  0.0166  0.0145  705 LEU A CD2 
3233  N N   . THR A 405 ? 0.5488 0.5975 0.5714 0.0538  0.0154  0.0277  706 THR A N   
3234  C CA  A THR A 405 ? 0.5042 0.5482 0.5265 0.0494  0.0137  0.0307  706 THR A CA  
3235  C CA  B THR A 405 ? 0.5033 0.5479 0.5258 0.0497  0.0136  0.0306  706 THR A CA  
3236  C C   . THR A 405 ? 0.5384 0.5606 0.5504 0.0553  0.0103  0.0311  706 THR A C   
3237  O O   . THR A 405 ? 0.5738 0.5884 0.5795 0.0652  0.0082  0.0285  706 THR A O   
3238  C CB  A THR A 405 ? 0.4474 0.5152 0.4774 0.0502  0.0125  0.0296  706 THR A CB  
3239  C CB  B THR A 405 ? 0.4470 0.5146 0.4765 0.0515  0.0120  0.0294  706 THR A CB  
3240  O OG1 A THR A 405 ? 0.4911 0.5575 0.5229 0.0409  0.0125  0.0325  706 THR A OG1 
3241  O OG1 B THR A 405 ? 0.3418 0.4166 0.3692 0.0650  0.0088  0.0256  706 THR A OG1 
3242  C CG2 A THR A 405 ? 0.4171 0.4885 0.4436 0.0634  0.0079  0.0268  706 THR A CG2 
3243  C CG2 B THR A 405 ? 0.4791 0.5679 0.5180 0.0434  0.0158  0.0295  706 THR A CG2 
3244  N N   . PRO A 406 ? 0.5934 0.6036 0.6021 0.0496  0.0098  0.0346  707 PRO A N   
3245  C CA  . PRO A 406 ? 0.5434 0.5569 0.5564 0.0393  0.0116  0.0374  707 PRO A CA  
3246  C C   . PRO A 406 ? 0.6257 0.6392 0.6420 0.0315  0.0156  0.0382  707 PRO A C   
3247  O O   . PRO A 406 ? 0.7304 0.7354 0.7435 0.0328  0.0167  0.0373  707 PRO A O   
3248  C CB  . PRO A 406 ? 0.5099 0.5045 0.5144 0.0382  0.0101  0.0401  707 PRO A CB  
3249  C CG  . PRO A 406 ? 0.5281 0.5121 0.5240 0.0485  0.0068  0.0393  707 PRO A CG  
3250  C CD  . PRO A 406 ? 0.6072 0.5949 0.6044 0.0542  0.0073  0.0358  707 PRO A CD  
3251  N N   . SER A 407 ? 0.6373 0.6597 0.6589 0.0239  0.0176  0.0397  708 SER A N   
3252  C CA  . SER A 407 ? 0.6555 0.6760 0.6781 0.0177  0.0212  0.0411  708 SER A CA  
3253  C C   . SER A 407 ? 0.5546 0.5713 0.5771 0.0099  0.0222  0.0436  708 SER A C   
3254  O O   . SER A 407 ? 0.6593 0.6788 0.6825 0.0081  0.0203  0.0436  708 SER A O   
3255  C CB  . SER A 407 ? 0.5586 0.5949 0.5866 0.0176  0.0236  0.0400  708 SER A CB  
3256  O OG  . SER A 407 ? 0.5806 0.6316 0.6141 0.0130  0.0239  0.0404  708 SER A OG  
3257  N N   . PHE A 408 ? 0.4767 0.4865 0.4972 0.0061  0.0248  0.0452  709 PHE A N   
3258  C CA  . PHE A 408 ? 0.4317 0.4375 0.4508 -0.0003 0.0262  0.0473  709 PHE A CA  
3259  C C   . PHE A 408 ? 0.5432 0.5583 0.5653 -0.0046 0.0287  0.0483  709 PHE A C   
3260  O O   . PHE A 408 ? 0.6991 0.7215 0.7231 -0.0024 0.0304  0.0480  709 PHE A O   
3261  C CB  . PHE A 408 ? 0.3558 0.3497 0.3699 -0.0006 0.0274  0.0486  709 PHE A CB  
3262  C CG  . PHE A 408 ? 0.4132 0.3987 0.4239 0.0011  0.0256  0.0482  709 PHE A CG  
3263  C CD1 . PHE A 408 ? 0.4713 0.4526 0.4802 0.0040  0.0255  0.0474  709 PHE A CD1 
3264  C CD2 . PHE A 408 ? 0.4184 0.4003 0.4270 -0.0008 0.0242  0.0486  709 PHE A CD2 
3265  C CE1 . PHE A 408 ? 0.4964 0.4697 0.5013 0.0041  0.0245  0.0477  709 PHE A CE1 
3266  C CE2 . PHE A 408 ? 0.3431 0.3180 0.3476 0.0007  0.0230  0.0488  709 PHE A CE2 
3267  C CZ  . PHE A 408 ? 0.5193 0.4898 0.5218 0.0027  0.0234  0.0488  709 PHE A CZ  
3268  N N   . GLU A 409 ? 0.5010 0.5159 0.5229 -0.0111 0.0290  0.0492  710 GLU A N   
3269  C CA  . GLU A 409 ? 0.5606 0.5840 0.5848 -0.0175 0.0315  0.0504  710 GLU A CA  
3270  C C   . GLU A 409 ? 0.5833 0.5925 0.6009 -0.0242 0.0329  0.0528  710 GLU A C   
3271  O O   . GLU A 409 ? 0.6301 0.6283 0.6439 -0.0244 0.0309  0.0521  710 GLU A O   
3272  C CB  . GLU A 409 ? 0.6522 0.6926 0.6833 -0.0204 0.0299  0.0480  710 GLU A CB  
3273  C CG  . GLU A 409 ? 0.7414 0.7955 0.7776 -0.0120 0.0278  0.0451  710 GLU A CG  
3274  C CD  . GLU A 409 ? 0.8681 0.9343 0.9073 -0.0092 0.0305  0.0450  710 GLU A CD  
3275  O OE1 . GLU A 409 ? 0.9182 0.9851 0.9563 -0.0152 0.0343  0.0477  710 GLU A OE1 
3276  O OE2 . GLU A 409 ? 0.8935 0.9675 0.9350 -0.0005 0.0288  0.0423  710 GLU A OE2 
3277  N N   . TYR A 410 ? 0.5606 0.5692 0.5757 -0.0292 0.0363  0.0556  711 TYR A N   
3278  C CA  . TYR A 410 ? 0.5744 0.5681 0.5818 -0.0363 0.0375  0.0579  711 TYR A CA  
3279  C C   . TYR A 410 ? 0.5927 0.5921 0.6032 -0.0455 0.0364  0.0559  711 TYR A C   
3280  O O   . TYR A 410 ? 0.6116 0.6309 0.6309 -0.0475 0.0358  0.0538  711 TYR A O   
3281  C CB  . TYR A 410 ? 0.6276 0.6170 0.6293 -0.0393 0.0417  0.0622  711 TYR A CB  
3282  C CG  . TYR A 410 ? 0.6925 0.6772 0.6904 -0.0305 0.0425  0.0638  711 TYR A CG  
3283  C CD1 . TYR A 410 ? 0.8170 0.8155 0.8192 -0.0263 0.0440  0.0638  711 TYR A CD1 
3284  C CD2 . TYR A 410 ? 0.7607 0.7289 0.7506 -0.0258 0.0415  0.0645  711 TYR A CD2 
3285  C CE1 . TYR A 410 ? 0.9127 0.9082 0.9115 -0.0188 0.0443  0.0644  711 TYR A CE1 
3286  C CE2 . TYR A 410 ? 0.8918 0.8590 0.8791 -0.0179 0.0420  0.0652  711 TYR A CE2 
3287  C CZ  . TYR A 410 ? 0.9461 0.9267 0.9378 -0.0150 0.0433  0.0651  711 TYR A CZ  
3288  O OH  . TYR A 410 ? 1.0170 0.9976 1.0060 -0.0077 0.0433  0.0651  711 TYR A OH  
3289  N N   . GLN A 411 ? 0.5963 0.5787 0.5991 -0.0509 0.0358  0.0561  712 GLN A N   
3290  C CA  . GLN A 411 ? 0.6760 0.6617 0.6802 -0.0618 0.0349  0.0540  712 GLN A CA  
3291  C C   . GLN A 411 ? 0.6150 0.5773 0.6067 -0.0696 0.0369  0.0566  712 GLN A C   
3292  O O   . GLN A 411 ? 0.7631 0.7061 0.7450 -0.0635 0.0375  0.0590  712 GLN A O   
3293  C CB  . GLN A 411 ? 0.7118 0.7010 0.7191 -0.0597 0.0302  0.0493  712 GLN A CB  
3294  C CG  . GLN A 411 ? 0.7689 0.7409 0.7690 -0.0517 0.0284  0.0490  712 GLN A CG  
3295  C CD  . GLN A 411 ? 0.7221 0.6989 0.7246 -0.0495 0.0240  0.0449  712 GLN A CD  
3296  O OE1 . GLN A 411 ? 0.6042 0.5965 0.6133 -0.0538 0.0219  0.0419  712 GLN A OE1 
3297  N NE2 . GLN A 411 ? 0.6986 0.6637 0.6954 -0.0425 0.0228  0.0445  712 GLN A NE2 
3298  N N   . PRO A 412 ? 0.5613 0.5247 0.5524 -0.0829 0.0379  0.0562  713 PRO A N   
3299  C CA  . PRO A 412 ? 0.7134 0.6502 0.6901 -0.0911 0.0400  0.0590  713 PRO A CA  
3300  C C   . PRO A 412 ? 0.8286 0.7421 0.7952 -0.0867 0.0366  0.0563  713 PRO A C   
3301  O O   . PRO A 412 ? 0.7530 0.6737 0.7248 -0.0821 0.0327  0.0516  713 PRO A O   
3302  C CB  . PRO A 412 ? 0.6430 0.5901 0.6234 -0.1080 0.0412  0.0576  713 PRO A CB  
3303  C CG  . PRO A 412 ? 0.5554 0.5319 0.5514 -0.1064 0.0377  0.0520  713 PRO A CG  
3304  C CD  . PRO A 412 ? 0.4836 0.4728 0.4865 -0.0915 0.0374  0.0530  713 PRO A CD  
3305  N N   . ASP A 413 ? 0.8686 0.7537 0.8194 -0.0873 0.0383  0.0595  714 ASP A N   
3306  C CA  . ASP A 413 ? 0.8696 0.7314 0.8089 -0.0816 0.0354  0.0568  714 ASP A CA  
3307  C C   . ASP A 413 ? 0.9295 0.7893 0.8689 -0.0913 0.0321  0.0508  714 ASP A C   
3308  O O   . ASP A 413 ? 1.0050 0.8672 0.9453 -0.1062 0.0332  0.0503  714 ASP A O   
3309  C CB  . ASP A 413 ? 0.9643 0.7949 0.8848 -0.0802 0.0377  0.0613  714 ASP A CB  
3310  C CG  . ASP A 413 ? 1.0430 0.8751 0.9620 -0.0678 0.0399  0.0663  714 ASP A CG  
3311  O OD1 . ASP A 413 ? 0.9969 0.8473 0.9264 -0.0577 0.0385  0.0646  714 ASP A OD1 
3312  O OD2 . ASP A 413 ? 1.1464 0.9610 1.0529 -0.0686 0.0428  0.0717  714 ASP A OD2 
3313  N N   . PRO A 414 ? 0.8410 0.6974 0.7790 -0.0839 0.0282  0.0461  715 PRO A N   
3314  C CA  . PRO A 414 ? 0.7870 0.6452 0.7260 -0.0922 0.0245  0.0396  715 PRO A CA  
3315  C C   . PRO A 414 ? 0.9139 0.7468 0.8391 -0.1054 0.0248  0.0382  715 PRO A C   
3316  O O   . PRO A 414 ? 0.9255 0.7668 0.8550 -0.1186 0.0231  0.0338  715 PRO A O   
3317  C CB  . PRO A 414 ? 0.7177 0.5722 0.6538 -0.0793 0.0212  0.0360  715 PRO A CB  
3318  C CG  . PRO A 414 ? 0.8196 0.6857 0.7621 -0.0665 0.0229  0.0401  715 PRO A CG  
3319  C CD  . PRO A 414 ? 0.8391 0.6961 0.7770 -0.0680 0.0271  0.0461  715 PRO A CD  
3320  N N   . TRP A 415 ? 0.9669 0.7686 0.8750 -0.1022 0.0267  0.0415  716 TRP A N   
3321  C CA  . TRP A 415 ? 0.9591 0.7310 0.8509 -0.1145 0.0268  0.0402  716 TRP A CA  
3322  C C   . TRP A 415 ? 1.0361 0.8102 0.9291 -0.1323 0.0307  0.0442  716 TRP A C   
3323  O O   . TRP A 415 ? 1.1001 0.8522 0.9812 -0.1466 0.0309  0.0426  716 TRP A O   
3324  C CB  . TRP A 415 ? 1.0042 0.7397 0.8749 -0.1038 0.0273  0.0427  716 TRP A CB  
3325  C CG  . TRP A 415 ? 1.0569 0.7916 0.9258 -0.0940 0.0311  0.0507  716 TRP A CG  
3326  C CD1 . TRP A 415 ? 1.0653 0.7855 0.9249 -0.1005 0.0353  0.0577  716 TRP A CD1 
3327  C CD2 . TRP A 415 ? 0.9727 0.7222 0.8484 -0.0765 0.0310  0.0523  716 TRP A CD2 
3328  N NE1 . TRP A 415 ? 0.9110 0.6367 0.7712 -0.0869 0.0375  0.0633  716 TRP A NE1 
3329  C CE2 . TRP A 415 ? 0.8681 0.6122 0.7387 -0.0726 0.0348  0.0598  716 TRP A CE2 
3330  C CE3 . TRP A 415 ? 0.9165 0.6834 0.8015 -0.0646 0.0282  0.0482  716 TRP A CE3 
3331  C CZ2 . TRP A 415 ? 0.7938 0.5504 0.6692 -0.0575 0.0354  0.0624  716 TRP A CZ2 
3332  C CZ3 . TRP A 415 ? 0.9175 0.6958 0.8071 -0.0507 0.0293  0.0513  716 TRP A CZ3 
3333  C CH2 . TRP A 415 ? 0.8610 0.6347 0.7462 -0.0473 0.0327  0.0579  716 TRP A CH2 
3334  N N   . ASN A 416 ? 1.0204 0.8200 0.9266 -0.1321 0.0341  0.0491  717 ASN A N   
3335  C CA  . ASN A 416 ? 0.8837 0.6916 0.7930 -0.1495 0.0382  0.0525  717 ASN A CA  
3336  C C   . ASN A 416 ? 0.8546 0.6910 0.7790 -0.1634 0.0361  0.0462  717 ASN A C   
3337  O O   . ASN A 416 ? 0.8857 0.7205 0.8080 -0.1825 0.0382  0.0461  717 ASN A O   
3338  C CB  . ASN A 416 ? 0.8584 0.6849 0.7758 -0.1434 0.0425  0.0595  717 ASN A CB  
3339  C CG  . ASN A 416 ? 0.9054 0.7041 0.8063 -0.1325 0.0450  0.0663  717 ASN A CG  
3340  O OD1 . ASN A 416 ? 0.9485 0.7112 0.8294 -0.1356 0.0455  0.0680  717 ASN A OD1 
3341  N ND2 . ASN A 416 ? 0.8533 0.6679 0.7615 -0.1192 0.0464  0.0698  717 ASN A ND2 
3342  N N   . THR A 417 ? 0.8284 0.6907 0.7673 -0.1546 0.0320  0.0409  718 THR A N   
3343  C CA  . THR A 417 ? 0.8360 0.7307 0.7905 -0.1648 0.0296  0.0351  718 THR A CA  
3344  C C   . THR A 417 ? 0.8529 0.7450 0.8061 -0.1662 0.0236  0.0264  718 THR A C   
3345  O O   . THR A 417 ? 0.6884 0.6026 0.6511 -0.1784 0.0214  0.0209  718 THR A O   
3346  C CB  . THR A 417 ? 0.7384 0.6701 0.7116 -0.1536 0.0294  0.0358  718 THR A CB  
3347  O OG1 . THR A 417 ? 0.7949 0.7236 0.7681 -0.1356 0.0260  0.0345  718 THR A OG1 
3348  C CG2 . THR A 417 ? 0.6959 0.6314 0.6702 -0.1517 0.0352  0.0436  718 THR A CG2 
3349  N N   . HIS A 418 ? 0.8626 0.7306 0.8043 -0.1541 0.0208  0.0248  719 HIS A N   
3350  C CA  . HIS A 418 ? 0.8854 0.7527 0.8254 -0.1536 0.0151  0.0165  719 HIS A CA  
3351  C C   . HIS A 418 ? 0.8952 0.7443 0.8249 -0.1724 0.0138  0.0112  719 HIS A C   
3352  O O   . HIS A 418 ? 0.9652 0.7824 0.8793 -0.1801 0.0168  0.0144  719 HIS A O   
3353  C CB  . HIS A 418 ? 0.8995 0.7462 0.8289 -0.1360 0.0131  0.0162  719 HIS A CB  
3354  C CG  . HIS A 418 ? 0.8944 0.7359 0.8185 -0.1353 0.0076  0.0077  719 HIS A CG  
3355  N ND1 . HIS A 418 ? 0.8697 0.7402 0.8062 -0.1335 0.0034  0.0026  719 HIS A ND1 
3356  C CD2 . HIS A 418 ? 0.9073 0.7177 0.8139 -0.1356 0.0055  0.0033  719 HIS A CD2 
3357  C CE1 . HIS A 418 ? 0.9218 0.7805 0.8491 -0.1331 -0.0010 -0.0046 719 HIS A CE1 
3358  N NE2 . HIS A 418 ? 0.9179 0.7401 0.8272 -0.1345 0.0002  -0.0046 719 HIS A NE2 
3359  N N   . VAL A 419 ? 0.9404 0.8089 0.8777 -0.1797 0.0091  0.0031  720 VAL A N   
3360  C CA  . VAL A 419 ? 1.0557 0.9103 0.9844 -0.1983 0.0068  -0.0039 720 VAL A CA  
3361  C C   . VAL A 419 ? 1.0710 0.9088 0.9889 -0.1898 0.0011  -0.0114 720 VAL A C   
3362  O O   . VAL A 419 ? 1.0872 0.9487 1.0147 -0.1790 -0.0030 -0.0153 720 VAL A O   
3363  C CB  . VAL A 419 ? 1.0870 0.9801 1.0328 -0.2146 0.0055  -0.0086 720 VAL A CB  
3364  C CG1 . VAL A 419 ? 1.1047 0.9924 1.0448 -0.2292 0.0004  -0.0191 720 VAL A CG1 
3365  C CG2 . VAL A 419 ? 1.1380 1.0359 1.0871 -0.2297 0.0119  -0.0024 720 VAL A CG2 
3366  N N   . TRP A 420 ? 1.0539 0.8501 0.9508 -0.1942 0.0010  -0.0134 721 TRP A N   
3367  C CA  . TRP A 420 ? 1.1270 0.9009 1.0100 -0.1822 -0.0034 -0.0192 721 TRP A CA  
3368  C C   . TRP A 420 ? 1.2230 1.0086 1.1078 -0.1910 -0.0097 -0.0307 721 TRP A C   
3369  O O   . TRP A 420 ? 1.2790 1.0632 1.1627 -0.2118 -0.0106 -0.0356 721 TRP A O   
3370  C CB  . TRP A 420 ? 1.0700 0.7937 0.9282 -0.1819 -0.0013 -0.0173 721 TRP A CB  
3371  C CG  . TRP A 420 ? 1.0349 0.7477 0.8894 -0.1658 0.0033  -0.0074 721 TRP A CG  
3372  C CD1 . TRP A 420 ? 1.0106 0.7219 0.8670 -0.1700 0.0089  0.0018  721 TRP A CD1 
3373  C CD2 . TRP A 420 ? 1.0012 0.7064 0.8501 -0.1431 0.0026  -0.0062 721 TRP A CD2 
3374  N NE1 . TRP A 420 ? 0.8808 0.5835 0.7329 -0.1509 0.0113  0.0084  721 TRP A NE1 
3375  C CE2 . TRP A 420 ? 1.0043 0.7039 0.8523 -0.1347 0.0075  0.0035  721 TRP A CE2 
3376  C CE3 . TRP A 420 ? 0.9354 0.6394 0.7798 -0.1294 -0.0016 -0.0125 721 TRP A CE3 
3377  C CZ2 . TRP A 420 ? 1.0343 0.7289 0.8781 -0.1138 0.0082  0.0066  721 TRP A CZ2 
3378  C CZ3 . TRP A 420 ? 0.9402 0.6393 0.7804 -0.1090 -0.0004 -0.0089 721 TRP A CZ3 
3379  C CH2 . TRP A 420 ? 0.9829 0.6779 0.8233 -0.1016 0.0043  0.0003  721 TRP A CH2 
3380  N N   . LYS A 421 ? 1.2169 1.0143 1.1039 -0.1754 -0.0139 -0.0348 722 LYS A N   
3381  C CA  . LYS A 421 ? 1.1943 1.0055 1.0825 -0.1794 -0.0205 -0.0457 722 LYS A CA  
3382  C C   . LYS A 421 ? 1.2813 1.0568 1.1492 -0.1904 -0.0236 -0.0546 722 LYS A C   
3383  O O   . LYS A 421 ? 1.2911 1.0755 1.1610 -0.2075 -0.0273 -0.0630 722 LYS A O   
3384  C CB  . LYS A 421 ? 1.1456 0.9710 1.0364 -0.1582 -0.0234 -0.0466 722 LYS A CB  
3385  C CG  . LYS A 421 ? 1.1731 1.0340 1.0828 -0.1471 -0.0218 -0.0395 722 LYS A CG  
3386  C CD  . LYS A 421 ? 1.1439 1.0434 1.0713 -0.1577 -0.0243 -0.0424 722 LYS A CD  
3387  C CE  . LYS A 421 ? 1.0366 0.9570 0.9792 -0.1566 -0.0196 -0.0336 722 LYS A CE  
3388  N NZ  . LYS A 421 ? 0.9836 0.9413 0.9427 -0.1681 -0.0217 -0.0370 722 LYS A NZ  
3389  N N   . ARG B 3   ? 1.0205 1.5170 1.0216 -0.1313 -0.0530 -0.0294 304 ARG B N   
3390  C CA  . ARG B 3   ? 1.1434 1.6341 1.1380 -0.1624 -0.0509 -0.0400 304 ARG B CA  
3391  C C   . ARG B 3   ? 1.2753 1.7039 1.2586 -0.1692 -0.0437 -0.0418 304 ARG B C   
3392  O O   . ARG B 3   ? 1.3882 1.8034 1.3772 -0.1628 -0.0390 -0.0364 304 ARG B O   
3393  C CB  . ARG B 3   ? 1.1830 1.6854 1.1674 -0.1761 -0.0562 -0.0488 304 ARG B CB  
3394  C CG  . ARG B 3   ? 1.2555 1.8226 1.2504 -0.1691 -0.0638 -0.0470 304 ARG B CG  
3395  C CD  . ARG B 3   ? 1.3154 1.8875 1.2991 -0.1714 -0.0696 -0.0524 304 ARG B CD  
3396  N NE  . ARG B 3   ? 1.4371 2.0086 1.4095 -0.2033 -0.0705 -0.0659 304 ARG B NE  
3397  C CZ  . ARG B 3   ? 1.5589 2.0766 1.5130 -0.2172 -0.0667 -0.0736 304 ARG B CZ  
3398  N NH1 . ARG B 3   ? 1.6246 2.0895 1.5719 -0.2017 -0.0618 -0.0690 304 ARG B NH1 
3399  N NH2 . ARG B 3   ? 1.5650 2.0820 1.5063 -0.2464 -0.0678 -0.0863 304 ARG B NH2 
3400  N N   . PHE B 4   ? 1.2130 1.6048 1.1794 -0.1807 -0.0430 -0.0493 305 PHE B N   
3401  C CA  . PHE B 4   ? 0.9795 1.3126 0.9324 -0.1856 -0.0365 -0.0514 305 PHE B CA  
3402  C C   . PHE B 4   ? 0.8817 1.1817 0.8218 -0.1748 -0.0373 -0.0528 305 PHE B C   
3403  O O   . PHE B 4   ? 1.0792 1.3945 1.0136 -0.1784 -0.0419 -0.0578 305 PHE B O   
3404  C CB  . PHE B 4   ? 0.9989 1.3182 0.9396 -0.2159 -0.0333 -0.0611 305 PHE B CB  
3405  C CG  . PHE B 4   ? 1.0636 1.4320 1.0162 -0.2329 -0.0345 -0.0623 305 PHE B CG  
3406  C CD1 . PHE B 4   ? 1.1757 1.5919 1.1317 -0.2454 -0.0408 -0.0680 305 PHE B CD1 
3407  C CD2 . PHE B 4   ? 1.0080 1.3784 0.9687 -0.2363 -0.0295 -0.0576 305 PHE B CD2 
3408  C CE1 . PHE B 4   ? 1.2396 1.7072 1.2078 -0.2615 -0.0421 -0.0690 305 PHE B CE1 
3409  C CE2 . PHE B 4   ? 1.0699 1.4898 1.0423 -0.2521 -0.0301 -0.0583 305 PHE B CE2 
3410  C CZ  . PHE B 4   ? 1.2377 1.7077 1.2145 -0.2650 -0.0365 -0.0640 305 PHE B CZ  
3411  N N   . LEU B 5   ? 0.6524 0.9105 0.5883 -0.1617 -0.0328 -0.0483 306 LEU B N   
3412  C CA  . LEU B 5   ? 0.5530 0.7888 0.4820 -0.1458 -0.0334 -0.0462 306 LEU B CA  
3413  C C   . LEU B 5   ? 0.6066 0.7913 0.5178 -0.1502 -0.0282 -0.0514 306 LEU B C   
3414  O O   . LEU B 5   ? 0.6970 0.8543 0.6056 -0.1526 -0.0230 -0.0504 306 LEU B O   
3415  C CB  . LEU B 5   ? 0.5051 0.7431 0.4461 -0.1220 -0.0335 -0.0346 306 LEU B CB  
3416  C CG  . LEU B 5   ? 0.4312 0.7145 0.3876 -0.1126 -0.0379 -0.0281 306 LEU B CG  
3417  C CD1 . LEU B 5   ? 0.4505 0.7243 0.4128 -0.0897 -0.0375 -0.0176 306 LEU B CD1 
3418  C CD2 . LEU B 5   ? 0.4888 0.8063 0.4440 -0.1144 -0.0441 -0.0310 306 LEU B CD2 
3419  N N   . LYS B 6   ? 0.6124 0.7853 0.5106 -0.1495 -0.0295 -0.0567 307 LYS B N   
3420  C CA  . LYS B 6   ? 0.6806 0.8076 0.5598 -0.1504 -0.0248 -0.0621 307 LYS B CA  
3421  C C   . LYS B 6   ? 0.7023 0.8149 0.5839 -0.1284 -0.0233 -0.0547 307 LYS B C   
3422  O O   . LYS B 6   ? 0.7429 0.8795 0.6342 -0.1162 -0.0270 -0.0485 307 LYS B O   
3423  C CB  . LYS B 6   ? 0.8528 0.9753 0.7136 -0.1632 -0.0266 -0.0736 307 LYS B CB  
3424  C CG  . LYS B 6   ? 0.9287 1.0790 0.7886 -0.1860 -0.0304 -0.0812 307 LYS B CG  
3425  C CD  . LYS B 6   ? 0.9246 1.0379 0.7604 -0.2074 -0.0267 -0.0931 307 LYS B CD  
3426  C CE  . LYS B 6   ? 0.9278 1.0702 0.7623 -0.2336 -0.0305 -0.1010 307 LYS B CE  
3427  N NZ  . LYS B 6   ? 0.9936 1.0970 0.8064 -0.2570 -0.0258 -0.1100 307 LYS B NZ  
3428  N N   . VAL B 7   ? 0.7129 0.7871 0.5848 -0.1234 -0.0179 -0.0550 308 VAL B N   
3429  C CA  . VAL B 7   ? 0.6761 0.7370 0.5473 -0.1054 -0.0162 -0.0500 308 VAL B CA  
3430  C C   . VAL B 7   ? 0.6987 0.7268 0.5476 -0.1069 -0.0125 -0.0586 308 VAL B C   
3431  O O   . VAL B 7   ? 0.8522 0.8567 0.6859 -0.1199 -0.0099 -0.0665 308 VAL B O   
3432  C CB  . VAL B 7   ? 0.7307 0.7810 0.6128 -0.0937 -0.0133 -0.0408 308 VAL B CB  
3433  C CG1 . VAL B 7   ? 0.7357 0.8121 0.6353 -0.0948 -0.0160 -0.0346 308 VAL B CG1 
3434  C CG2 . VAL B 7   ? 0.7335 0.7464 0.6031 -0.0963 -0.0076 -0.0441 308 VAL B CG2 
3435  N N   . LYS B 8   ? 0.5352 0.5615 0.3804 -0.0939 -0.0121 -0.0571 309 LYS B N   
3436  C CA  . LYS B 8   ? 0.4916 0.4911 0.3147 -0.0923 -0.0087 -0.0655 309 LYS B CA  
3437  C C   . LYS B 8   ? 0.5767 0.5641 0.4002 -0.0738 -0.0049 -0.0599 309 LYS B C   
3438  O O   . LYS B 8   ? 0.6236 0.6315 0.4632 -0.0637 -0.0064 -0.0504 309 LYS B O   
3439  C CB  . LYS B 8   ? 0.7019 0.7187 0.5165 -0.0969 -0.0125 -0.0721 309 LYS B CB  
3440  C CG  . LYS B 8   ? 0.8145 0.8052 0.6050 -0.0926 -0.0089 -0.0810 309 LYS B CG  
3441  C CD  . LYS B 8   ? 0.9540 0.9662 0.7378 -0.0950 -0.0129 -0.0863 309 LYS B CD  
3442  C CE  . LYS B 8   ? 0.9829 0.9684 0.7409 -0.0893 -0.0089 -0.0957 309 LYS B CE  
3443  N NZ  . LYS B 8   ? 0.9848 0.9926 0.7364 -0.0890 -0.0123 -0.0998 309 LYS B NZ  
3444  N N   . ASN B 9   ? 0.6521 0.6059 0.4563 -0.0695 0.0002  -0.0657 310 ASN B N   
3445  C CA  . ASN B 9   ? 0.6521 0.5963 0.4539 -0.0514 0.0043  -0.0618 310 ASN B CA  
3446  C C   . ASN B 9   ? 0.7725 0.7167 0.5587 -0.0458 0.0052  -0.0683 310 ASN B C   
3447  O O   . ASN B 9   ? 0.8295 0.7481 0.5923 -0.0503 0.0073  -0.0790 310 ASN B O   
3448  C CB  . ASN B 9   ? 0.7446 0.6531 0.5344 -0.0468 0.0096  -0.0632 310 ASN B CB  
3449  C CG  . ASN B 9   ? 0.9643 0.8705 0.7559 -0.0272 0.0132  -0.0576 310 ASN B CG  
3450  O OD1 . ASN B 9   ? 1.0995 1.0043 0.8798 -0.0169 0.0154  -0.0610 310 ASN B OD1 
3451  N ND2 . ASN B 9   ? 0.9457 0.8538 0.7510 -0.0219 0.0138  -0.0493 310 ASN B ND2 
3452  N N   . TRP B 10  ? 0.7204 0.6915 0.5176 -0.0365 0.0039  -0.0620 311 TRP B N   
3453  C CA  . TRP B 10  ? 0.7761 0.7530 0.5599 -0.0320 0.0044  -0.0676 311 TRP B CA  
3454  C C   . TRP B 10  ? 0.8158 0.7697 0.5816 -0.0175 0.0107  -0.0720 311 TRP B C   
3455  O O   . TRP B 10  ? 0.8190 0.7769 0.5719 -0.0113 0.0121  -0.0769 311 TRP B O   
3456  C CB  . TRP B 10  ? 0.7008 0.7139 0.5006 -0.0276 0.0014  -0.0586 311 TRP B CB  
3457  C CG  . TRP B 10  ? 0.6262 0.6610 0.4370 -0.0394 -0.0048 -0.0564 311 TRP B CG  
3458  C CD1 . TRP B 10  ? 0.6499 0.6961 0.4792 -0.0433 -0.0078 -0.0485 311 TRP B CD1 
3459  C CD2 . TRP B 10  ? 0.7539 0.8031 0.5568 -0.0479 -0.0089 -0.0627 311 TRP B CD2 
3460  N NE1 . TRP B 10  ? 0.6958 0.7640 0.5297 -0.0523 -0.0134 -0.0488 311 TRP B NE1 
3461  C CE2 . TRP B 10  ? 0.7526 0.8243 0.5711 -0.0558 -0.0144 -0.0574 311 TRP B CE2 
3462  C CE3 . TRP B 10  ? 0.7818 0.8283 0.5652 -0.0488 -0.0085 -0.0723 311 TRP B CE3 
3463  C CZ2 . TRP B 10  ? 0.7400 0.8341 0.5563 -0.0645 -0.0198 -0.0610 311 TRP B CZ2 
3464  C CZ3 . TRP B 10  ? 0.8313 0.8984 0.6120 -0.0588 -0.0140 -0.0765 311 TRP B CZ3 
3465  C CH2 . TRP B 10  ? 0.8300 0.9221 0.6276 -0.0665 -0.0197 -0.0706 311 TRP B CH2 
3466  N N   . GLU B 11  ? 0.7883 0.7195 0.5520 -0.0107 0.0145  -0.0702 312 GLU B N   
3467  C CA  . GLU B 11  ? 0.8050 0.7127 0.5491 0.0052  0.0206  -0.0747 312 GLU B CA  
3468  C C   . GLU B 11  ? 0.9842 0.8469 0.7005 0.0003  0.0235  -0.0857 312 GLU B C   
3469  O O   . GLU B 11  ? 1.1718 1.0110 0.8637 0.0121  0.0281  -0.0929 312 GLU B O   
3470  C CB  . GLU B 11  ? 0.7831 0.6964 0.5407 0.0191  0.0233  -0.0649 312 GLU B CB  
3471  C CG  . GLU B 11  ? 1.0417 0.9576 0.7900 0.0398  0.0285  -0.0651 312 GLU B CG  
3472  C CD  . GLU B 11  ? 1.1631 1.0874 0.9248 0.0525  0.0307  -0.0558 312 GLU B CD  
3473  O OE1 . GLU B 11  ? 0.9225 0.8417 0.6962 0.0461  0.0287  -0.0507 312 GLU B OE1 
3474  O OE2 . GLU B 11  ? 1.3445 1.2830 1.1043 0.0692  0.0343  -0.0540 312 GLU B OE2 
3475  N N   . THR B 12  ? 1.0171 0.8666 0.7348 -0.0169 0.0211  -0.0871 313 THR B N   
3476  C CA  . THR B 12  ? 0.9668 0.7716 0.6573 -0.0258 0.0237  -0.0968 313 THR B CA  
3477  C C   . THR B 12  ? 1.0547 0.8603 0.7392 -0.0496 0.0194  -0.1050 313 THR B C   
3478  O O   . THR B 12  ? 1.1486 0.9161 0.8064 -0.0602 0.0215  -0.1150 313 THR B O   
3479  C CB  . THR B 12  ? 0.9185 0.7030 0.6128 -0.0264 0.0259  -0.0910 313 THR B CB  
3480  O OG1 . THR B 12  ? 0.9523 0.7594 0.6690 -0.0437 0.0212  -0.0860 313 THR B OG1 
3481  C CG2 . THR B 12  ? 0.8618 0.6573 0.5690 -0.0049 0.0285  -0.0812 313 THR B CG2 
3482  N N   . GLU B 13  ? 1.0720 0.9196 0.7792 -0.0584 0.0135  -0.1011 314 GLU B N   
3483  C CA  . GLU B 13  ? 1.0800 0.9411 0.7881 -0.0807 0.0082  -0.1069 314 GLU B CA  
3484  C C   . GLU B 13  ? 1.0491 0.8975 0.7597 -0.0981 0.0079  -0.1067 314 GLU B C   
3485  O O   . GLU B 13  ? 1.0546 0.9085 0.7611 -0.1190 0.0044  -0.1133 314 GLU B O   
3486  C CB  . GLU B 13  ? 1.1403 0.9842 0.8199 -0.0874 0.0082  -0.1209 314 GLU B CB  
3487  C CG  . GLU B 13  ? 1.1467 1.0173 0.8285 -0.0747 0.0068  -0.1206 314 GLU B CG  
3488  C CD  . GLU B 13  ? 1.1561 1.0056 0.8065 -0.0780 0.0077  -0.1350 314 GLU B CD  
3489  O OE1 . GLU B 13  ? 1.2032 1.0542 0.8448 -0.0985 0.0035  -0.1438 314 GLU B OE1 
3490  O OE2 . GLU B 13  ? 1.2004 1.0330 0.8342 -0.0600 0.0127  -0.1379 314 GLU B OE2 
3491  N N   . VAL B 14  ? 1.0127 0.8475 0.7306 -0.0905 0.0112  -0.0990 315 VAL B N   
3492  C CA  . VAL B 14  ? 0.9349 0.7621 0.6576 -0.1061 0.0113  -0.0970 315 VAL B CA  
3493  C C   . VAL B 14  ? 0.8991 0.7739 0.6512 -0.1155 0.0052  -0.0908 315 VAL B C   
3494  O O   . VAL B 14  ? 0.8826 0.7885 0.6568 -0.1030 0.0027  -0.0819 315 VAL B O   
3495  C CB  . VAL B 14  ? 0.9483 0.7519 0.6717 -0.0930 0.0163  -0.0896 315 VAL B CB  
3496  C CG1 . VAL B 14  ? 0.9359 0.7489 0.6758 -0.1049 0.0154  -0.0832 315 VAL B CG1 
3497  C CG2 . VAL B 14  ? 0.9663 0.7160 0.6548 -0.0889 0.0224  -0.0971 315 VAL B CG2 
3498  N N   . VAL B 15  ? 0.8465 0.7270 0.5973 -0.1377 0.0029  -0.0955 316 VAL B N   
3499  C CA  . VAL B 15  ? 0.7932 0.7191 0.5699 -0.1464 -0.0025 -0.0900 316 VAL B CA  
3500  C C   . VAL B 15  ? 0.9650 0.8846 0.7485 -0.1561 -0.0003 -0.0858 316 VAL B C   
3501  O O   . VAL B 15  ? 1.0767 0.9629 0.8403 -0.1702 0.0035  -0.0918 316 VAL B O   
3502  C CB  . VAL B 15  ? 0.7155 0.6655 0.4882 -0.1642 -0.0079 -0.0987 316 VAL B CB  
3503  C CG1 . VAL B 15  ? 0.6364 0.6360 0.4355 -0.1709 -0.0133 -0.0926 316 VAL B CG1 
3504  C CG2 . VAL B 15  ? 0.5733 0.5310 0.3398 -0.1532 -0.0099 -0.1018 316 VAL B CG2 
3505  N N   . LEU B 16  ? 0.8822 0.8315 0.6915 -0.1483 -0.0022 -0.0754 317 LEU B N   
3506  C CA  . LEU B 16  ? 0.8748 0.8275 0.6941 -0.1563 -0.0006 -0.0705 317 LEU B CA  
3507  C C   . LEU B 16  ? 0.8963 0.8985 0.7364 -0.1649 -0.0062 -0.0682 317 LEU B C   
3508  O O   . LEU B 16  ? 0.9688 1.0019 0.8210 -0.1560 -0.0109 -0.0657 317 LEU B O   
3509  C CB  . LEU B 16  ? 0.7208 0.6640 0.5506 -0.1376 0.0023  -0.0604 317 LEU B CB  
3510  C CG  . LEU B 16  ? 0.6603 0.5632 0.4728 -0.1234 0.0071  -0.0611 317 LEU B CG  
3511  C CD1 . LEU B 16  ? 0.4892 0.3936 0.3154 -0.1041 0.0084  -0.0510 317 LEU B CD1 
3512  C CD2 . LEU B 16  ? 0.6936 0.5523 0.4796 -0.1350 0.0124  -0.0676 317 LEU B CD2 
3513  N N   . THR B 17  ? 0.9085 0.9190 0.7516 -0.1821 -0.0053 -0.0689 318 THR B N   
3514  C CA  . THR B 17  ? 0.8549 0.9157 0.7170 -0.1906 -0.0101 -0.0671 318 THR B CA  
3515  C C   . THR B 17  ? 0.7622 0.8380 0.6433 -0.1820 -0.0086 -0.0571 318 THR B C   
3516  O O   . THR B 17  ? 0.9459 0.9962 0.8213 -0.1862 -0.0034 -0.0553 318 THR B O   
3517  C CB  . THR B 17  ? 0.9191 0.9866 0.7708 -0.2192 -0.0106 -0.0763 318 THR B CB  
3518  O OG1 . THR B 17  ? 0.9693 1.0033 0.7952 -0.2277 -0.0098 -0.0867 318 THR B OG1 
3519  C CG2 . THR B 17  ? 0.8440 0.9708 0.7137 -0.2253 -0.0173 -0.0764 318 THR B CG2 
3520  N N   . ASP B 18  ? 0.6652 0.7800 0.5666 -0.1691 -0.0131 -0.0505 319 ASP B N   
3521  C CA  . ASP B 18  ? 0.6827 0.8101 0.6008 -0.1561 -0.0121 -0.0409 319 ASP B CA  
3522  C C   . ASP B 18  ? 0.7448 0.9187 0.6776 -0.1649 -0.0146 -0.0397 319 ASP B C   
3523  O O   . ASP B 18  ? 0.6333 0.8449 0.5747 -0.1623 -0.0201 -0.0398 319 ASP B O   
3524  C CB  . ASP B 18  ? 0.7276 0.8589 0.6545 -0.1325 -0.0147 -0.0337 319 ASP B CB  
3525  C CG  . ASP B 18  ? 0.6629 0.7940 0.6016 -0.1184 -0.0129 -0.0248 319 ASP B CG  
3526  O OD1 . ASP B 18  ? 0.5720 0.7298 0.5219 -0.1206 -0.0133 -0.0220 319 ASP B OD1 
3527  O OD2 . ASP B 18  ? 0.6149 0.7207 0.5511 -0.1050 -0.0112 -0.0210 319 ASP B OD2 
3528  N N   . THR B 19  ? 0.7150 0.8880 0.6502 -0.1745 -0.0105 -0.0382 320 THR B N   
3529  C CA  . THR B 19  ? 0.5802 0.7996 0.5317 -0.1784 -0.0118 -0.0352 320 THR B CA  
3530  C C   . THR B 19  ? 0.5510 0.7737 0.5147 -0.1604 -0.0096 -0.0260 320 THR B C   
3531  O O   . THR B 19  ? 0.5232 0.7874 0.5016 -0.1558 -0.0113 -0.0223 320 THR B O   
3532  C CB  . THR B 19  ? 0.6096 0.8343 0.5550 -0.2065 -0.0086 -0.0407 320 THR B CB  
3533  O OG1 . THR B 19  ? 0.7116 0.8867 0.6416 -0.2130 -0.0019 -0.0410 320 THR B OG1 
3534  C CG2 . THR B 19  ? 0.6083 0.8436 0.5443 -0.2261 -0.0122 -0.0503 320 THR B CG2 
3535  N N   . LEU B 20  ? 0.5871 0.7686 0.5441 -0.1496 -0.0060 -0.0227 321 LEU B N   
3536  C CA  . LEU B 20  ? 0.6273 0.8093 0.5935 -0.1343 -0.0039 -0.0150 321 LEU B CA  
3537  C C   . LEU B 20  ? 0.6003 0.8110 0.5799 -0.1138 -0.0087 -0.0094 321 LEU B C   
3538  O O   . LEU B 20  ? 0.4650 0.6925 0.4541 -0.1035 -0.0079 -0.0042 321 LEU B O   
3539  C CB  . LEU B 20  ? 0.4959 0.6304 0.4518 -0.1262 -0.0001 -0.0129 321 LEU B CB  
3540  C CG  . LEU B 20  ? 0.6195 0.7449 0.5807 -0.1119 0.0025  -0.0060 321 LEU B CG  
3541  C CD1 . LEU B 20  ? 0.4833 0.6247 0.4488 -0.1211 0.0064  -0.0043 321 LEU B CD1 
3542  C CD2 . LEU B 20  ? 0.6212 0.7020 0.5705 -0.1053 0.0054  -0.0051 321 LEU B CD2 
3543  N N   . HIS B 21  ? 0.6149 0.8310 0.5934 -0.1076 -0.0134 -0.0105 322 HIS B N   
3544  C CA  . HIS B 21  ? 0.5957 0.8327 0.5829 -0.0875 -0.0177 -0.0045 322 HIS B CA  
3545  C C   . HIS B 21  ? 0.5285 0.8132 0.5278 -0.0852 -0.0197 -0.0025 322 HIS B C   
3546  O O   . HIS B 21  ? 0.6307 0.9297 0.6358 -0.0658 -0.0221 0.0035  322 HIS B O   
3547  C CB  . HIS B 21  ? 0.7339 0.9709 0.7163 -0.0838 -0.0221 -0.0060 322 HIS B CB  
3548  C CG  . HIS B 21  ? 0.6076 0.8788 0.5911 -0.0966 -0.0258 -0.0115 322 HIS B CG  
3549  N ND1 . HIS B 21  ? 0.5941 0.8563 0.5683 -0.1177 -0.0247 -0.0201 322 HIS B ND1 
3550  C CD2 . HIS B 21  ? 0.6081 0.9233 0.6000 -0.0913 -0.0306 -0.0098 322 HIS B CD2 
3551  C CE1 . HIS B 21  ? 0.6821 0.9824 0.6596 -0.1267 -0.0290 -0.0240 322 HIS B CE1 
3552  N NE2 . HIS B 21  ? 0.6700 1.0051 0.6590 -0.1104 -0.0327 -0.0176 322 HIS B NE2 
3553  N N   . LEU B 22  ? 0.5160 0.8263 0.5184 -0.1043 -0.0186 -0.0073 323 LEU B N   
3554  C CA  . LEU B 22  ? 0.4843 0.8464 0.4996 -0.1018 -0.0202 -0.0052 323 LEU B CA  
3555  C C   . LEU B 22  ? 0.5524 0.9161 0.5739 -0.0908 -0.0161 0.0003  323 LEU B C   
3556  O O   . LEU B 22  ? 0.6369 1.0384 0.6681 -0.0775 -0.0176 0.0043  323 LEU B O   
3557  C CB  . LEU B 22  ? 0.4727 0.8650 0.4895 -0.1283 -0.0202 -0.0121 323 LEU B CB  
3558  C CG  . LEU B 22  ? 0.5896 0.9892 0.6000 -0.1421 -0.0247 -0.0192 323 LEU B CG  
3559  C CD1 . LEU B 22  ? 0.4699 0.8860 0.4775 -0.1735 -0.0232 -0.0271 323 LEU B CD1 
3560  C CD2 . LEU B 22  ? 0.6983 1.1397 0.7167 -0.1264 -0.0316 -0.0165 323 LEU B CD2 
3561  N N   . LYS B 23  ? 0.5921 0.9155 0.6069 -0.0940 -0.0110 0.0009  324 LYS B N   
3562  C CA  . LYS B 23  ? 0.6495 0.9690 0.6679 -0.0823 -0.0071 0.0060  324 LYS B CA  
3563  C C   . LYS B 23  ? 0.7400 1.0389 0.7566 -0.0568 -0.0091 0.0115  324 LYS B C   
3564  O O   . LYS B 23  ? 0.8889 1.1693 0.9040 -0.0482 -0.0059 0.0146  324 LYS B O   
3565  C CB  . LYS B 23  ? 0.6862 0.9717 0.6966 -0.0965 -0.0010 0.0045  324 LYS B CB  
3566  C CG  . LYS B 23  ? 0.7663 1.0787 0.7817 -0.1115 0.0037  0.0042  324 LYS B CG  
3567  C CD  . LYS B 23  ? 0.9344 1.2804 0.9526 -0.1339 0.0021  -0.0014 324 LYS B CD  
3568  C CE  . LYS B 23  ? 0.9877 1.3826 1.0167 -0.1436 0.0050  -0.0004 324 LYS B CE  
3569  N NZ  . LYS B 23  ? 0.9213 1.2994 0.9476 -0.1452 0.0120  0.0032  324 LYS B NZ  
3570  N N   . SER B 24  ? 0.7172 1.0177 0.7325 -0.0456 -0.0142 0.0128  325 SER B N   
3571  C CA  . SER B 24  ? 0.7556 1.0334 0.7666 -0.0241 -0.0159 0.0180  325 SER B CA  
3572  C C   . SER B 24  ? 0.8045 1.1124 0.8205 -0.0046 -0.0177 0.0227  325 SER B C   
3573  O O   . SER B 24  ? 0.8954 1.2461 0.9185 -0.0048 -0.0200 0.0222  325 SER B O   
3574  C CB  . SER B 24  ? 0.8747 1.1361 0.8793 -0.0224 -0.0199 0.0178  325 SER B CB  
3575  O OG  . SER B 24  ? 1.0102 1.2515 1.0094 -0.0036 -0.0217 0.0234  325 SER B OG  
3576  N N   . THR B 25  ? 0.8561 1.1418 0.8672 0.0128  -0.0168 0.0271  326 THR B N   
3577  C CA  . THR B 25  ? 1.0070 1.3154 1.0196 0.0334  -0.0175 0.0312  326 THR B CA  
3578  C C   . THR B 25  ? 1.0402 1.3289 1.0424 0.0550  -0.0210 0.0364  326 THR B C   
3579  O O   . THR B 25  ? 1.2146 1.5284 1.2164 0.0724  -0.0232 0.0397  326 THR B O   
3580  C CB  . THR B 25  ? 1.0262 1.3296 1.0396 0.0370  -0.0125 0.0316  326 THR B CB  
3581  O OG1 . THR B 25  ? 0.9397 1.2107 0.9504 0.0212  -0.0091 0.0290  326 THR B OG1 
3582  C CG2 . THR B 25  ? 1.0101 1.3644 1.0347 0.0342  -0.0104 0.0307  326 THR B CG2 
3583  N N   . LEU B 26  ? 0.8521 1.0974 0.8449 0.0545  -0.0215 0.0374  327 LEU B N   
3584  C CA  . LEU B 26  ? 0.8049 1.0260 0.7853 0.0724  -0.0242 0.0426  327 LEU B CA  
3585  C C   . LEU B 26  ? 0.8529 1.0683 0.8291 0.0693  -0.0280 0.0441  327 LEU B C   
3586  O O   . LEU B 26  ? 0.8661 1.0825 0.8469 0.0522  -0.0280 0.0403  327 LEU B O   
3587  C CB  . LEU B 26  ? 0.8344 1.0122 0.8059 0.0741  -0.0221 0.0432  327 LEU B CB  
3588  C CG  . LEU B 26  ? 0.8737 1.0529 0.8472 0.0774  -0.0182 0.0417  327 LEU B CG  
3589  C CD1 . LEU B 26  ? 0.8470 1.0255 0.8289 0.0573  -0.0146 0.0371  327 LEU B CD1 
3590  C CD2 . LEU B 26  ? 0.8433 0.9855 0.8025 0.0906  -0.0181 0.0441  327 LEU B CD2 
3591  N N   . GLU B 27  ? 0.6949 0.9019 0.6600 0.0868  -0.0308 0.0499  328 GLU B N   
3592  C CA  . GLU B 27  ? 0.7243 0.9245 0.6831 0.0859  -0.0342 0.0527  328 GLU B CA  
3593  C C   . GLU B 27  ? 0.7320 0.8936 0.6856 0.0739  -0.0330 0.0520  328 GLU B C   
3594  O O   . GLU B 27  ? 0.6202 0.7538 0.5701 0.0728  -0.0306 0.0517  328 GLU B O   
3595  C CB  . GLU B 27  ? 0.6632 0.8589 0.6081 0.1088  -0.0369 0.0601  328 GLU B CB  
3596  C CG  . GLU B 27  ? 0.6062 0.8483 0.5563 0.1223  -0.0391 0.0614  328 GLU B CG  
3597  C CD  . GLU B 27  ? 0.7207 0.9547 0.6544 0.1496  -0.0409 0.0690  328 GLU B CD  
3598  O OE1 . GLU B 27  ? 0.7885 1.0612 0.7256 0.1649  -0.0423 0.0705  328 GLU B OE1 
3599  O OE2 . GLU B 27  ? 0.7114 0.9008 0.6277 0.1559  -0.0408 0.0736  328 GLU B OE2 
3600  N N   . THR B 28  ? 0.6695 0.8327 0.6226 0.0649  -0.0348 0.0517  329 THR B N   
3601  C CA  . THR B 28  ? 0.5477 0.6799 0.4957 0.0553  -0.0338 0.0518  329 THR B CA  
3602  C C   . THR B 28  ? 0.5661 0.6747 0.4993 0.0650  -0.0355 0.0591  329 THR B C   
3603  O O   . THR B 28  ? 0.6872 0.7684 0.6149 0.0585  -0.0343 0.0603  329 THR B O   
3604  C CB  . THR B 28  ? 0.5894 0.7340 0.5430 0.0403  -0.0340 0.0471  329 THR B CB  
3605  O OG1 . THR B 28  ? 0.5674 0.7386 0.5199 0.0451  -0.0376 0.0488  329 THR B OG1 
3606  C CG2 . THR B 28  ? 0.3519 0.5078 0.3161 0.0271  -0.0314 0.0396  329 THR B CG2 
3607  N N   . GLY B 29  ? 0.6137 0.7332 0.5395 0.0802  -0.0382 0.0644  330 GLY B N   
3608  C CA  . GLY B 29  ? 0.6543 0.7528 0.5634 0.0892  -0.0399 0.0722  330 GLY B CA  
3609  C C   . GLY B 29  ? 0.7239 0.8446 0.6322 0.0892  -0.0428 0.0743  330 GLY B C   
3610  O O   . GLY B 29  ? 0.6633 0.7751 0.5568 0.1014  -0.0447 0.0820  330 GLY B O   
3611  N N   . CYS B 30  ? 0.6617 0.8093 0.5833 0.0761  -0.0431 0.0677  331 CYS B N   
3612  C CA  . CYS B 30  ? 0.5109 0.6794 0.4313 0.0735  -0.0459 0.0682  331 CYS B CA  
3613  C C   . CYS B 30  ? 0.6449 0.8516 0.5677 0.0858  -0.0496 0.0693  331 CYS B C   
3614  O O   . CYS B 30  ? 0.7034 0.9293 0.6343 0.0911  -0.0494 0.0670  331 CYS B O   
3615  C CB  . CYS B 30  ? 0.4059 0.5844 0.3369 0.0540  -0.0446 0.0595  331 CYS B CB  
3616  S SG  . CYS B 30  ? 0.6079 0.7501 0.5366 0.0411  -0.0405 0.0580  331 CYS B SG  
3617  N N   . THR B 31  ? 0.4825 0.7029 0.3980 0.0908  -0.0528 0.0733  332 THR B N   
3618  C CA  . THR B 31  ? 0.5908 0.8559 0.5108 0.0986  -0.0570 0.0728  332 THR B CA  
3619  C C   . THR B 31  ? 0.6508 0.9364 0.5733 0.0852  -0.0593 0.0683  332 THR B C   
3620  O O   . THR B 31  ? 0.7592 1.0225 0.6784 0.0729  -0.0573 0.0665  332 THR B O   
3621  C CB  . THR B 31  ? 0.6417 0.9067 0.5468 0.1239  -0.0596 0.0833  332 THR B CB  
3622  O OG1 . THR B 31  ? 0.6157 0.8616 0.5048 0.1270  -0.0608 0.0905  332 THR B OG1 
3623  C CG2 . THR B 31  ? 0.5154 0.7495 0.4131 0.1369  -0.0568 0.0874  332 THR B CG2 
3624  N N   . GLU B 32  ? 0.6710 1.0015 0.5988 0.0878  -0.0636 0.0661  333 GLU B N   
3625  C CA  . GLU B 32  ? 0.6467 0.9976 0.5734 0.0775  -0.0666 0.0622  333 GLU B CA  
3626  C C   . GLU B 32  ? 0.5822 0.9082 0.4920 0.0846  -0.0669 0.0705  333 GLU B C   
3627  O O   . GLU B 32  ? 0.6438 0.9726 0.5509 0.0732  -0.0675 0.0668  333 GLU B O   
3628  C CB  . GLU B 32  ? 0.8286 1.2341 0.7612 0.0826  -0.0721 0.0604  333 GLU B CB  
3629  C CG  . GLU B 32  ? 0.9233 1.3609 0.8728 0.0653  -0.0722 0.0493  333 GLU B CG  
3630  C CD  . GLU B 32  ? 1.0963 1.5431 1.0552 0.0734  -0.0702 0.0505  333 GLU B CD  
3631  O OE1 . GLU B 32  ? 1.0467 1.4632 0.9990 0.0894  -0.0676 0.0579  333 GLU B OE1 
3632  O OE2 . GLU B 32  ? 1.2176 1.7027 1.1897 0.0629  -0.0711 0.0436  333 GLU B OE2 
3633  N N   . TYR B 33  ? 0.5424 0.8411 0.4391 0.1021  -0.0660 0.0813  334 TYR B N   
3634  C CA  . TYR B 33  ? 0.6175 0.8936 0.4957 0.1099  -0.0662 0.0910  334 TYR B CA  
3635  C C   . TYR B 33  ? 0.5991 0.8253 0.4685 0.1041  -0.0613 0.0951  334 TYR B C   
3636  O O   . TYR B 33  ? 0.6351 0.8438 0.4904 0.1044  -0.0607 0.1018  334 TYR B O   
3637  C CB  . TYR B 33  ? 0.8226 1.1055 0.6869 0.1355  -0.0695 0.1018  334 TYR B CB  
3638  C CG  . TYR B 33  ? 0.8703 1.2079 0.7417 0.1417  -0.0750 0.0990  334 TYR B CG  
3639  C CD1 . TYR B 33  ? 0.9290 1.2894 0.7965 0.1371  -0.0785 0.0984  334 TYR B CD1 
3640  C CD2 . TYR B 33  ? 0.8712 1.2411 0.7538 0.1509  -0.0769 0.0963  334 TYR B CD2 
3641  C CE1 . TYR B 33  ? 0.9715 1.3849 0.8456 0.1411  -0.0842 0.0952  334 TYR B CE1 
3642  C CE2 . TYR B 33  ? 0.9020 1.3274 0.7923 0.1549  -0.0822 0.0935  334 TYR B CE2 
3643  C CZ  . TYR B 33  ? 0.9251 1.3718 0.8109 0.1496  -0.0861 0.0928  334 TYR B CZ  
3644  O OH  . TYR B 33  ? 0.9413 1.4376 0.8370 0.1497  -0.0891 0.0876  334 TYR B OH  
3645  N N   . ILE B 34  ? 0.7267 0.9310 0.6030 0.0988  -0.0578 0.0917  335 ILE B N   
3646  C CA  . ILE B 34  ? 0.6755 0.8372 0.5446 0.0916  -0.0535 0.0948  335 ILE B CA  
3647  C C   . ILE B 34  ? 0.6705 0.8277 0.5555 0.0765  -0.0504 0.0851  335 ILE B C   
3648  O O   . ILE B 34  ? 0.7594 0.9279 0.6546 0.0788  -0.0505 0.0805  335 ILE B O   
3649  C CB  . ILE B 34  ? 0.6351 0.7621 0.4871 0.1065  -0.0526 0.1048  335 ILE B CB  
3650  C CG1 . ILE B 34  ? 0.9426 1.0766 0.7778 0.1267  -0.0561 0.1146  335 ILE B CG1 
3651  C CG2 . ILE B 34  ? 0.5442 0.6323 0.3847 0.0969  -0.0492 0.1097  335 ILE B CG2 
3652  C CD1 . ILE B 34  ? 1.0739 1.2144 0.9059 0.1475  -0.0578 0.1170  335 ILE B CD1 
3653  N N   . CYS B 35  ? 0.6622 0.8047 0.5487 0.0620  -0.0474 0.0822  336 CYS B N   
3654  C CA  . CYS B 35  ? 0.5843 0.7187 0.4831 0.0490  -0.0442 0.0740  336 CYS B CA  
3655  C C   . CYS B 35  ? 0.6500 0.7487 0.5427 0.0472  -0.0410 0.0785  336 CYS B C   
3656  O O   . CYS B 35  ? 0.5811 0.6633 0.4631 0.0450  -0.0399 0.0846  336 CYS B O   
3657  C CB  . CYS B 35  ? 0.4157 0.5613 0.3203 0.0350  -0.0429 0.0664  336 CYS B CB  
3658  S SG  . CYS B 35  ? 0.5895 0.7149 0.5029 0.0224  -0.0382 0.0597  336 CYS B SG  
3659  N N   . MET B 36  ? 0.5887 0.6771 0.4882 0.0464  -0.0395 0.0750  337 MET B N   
3660  C CA  . MET B 36  ? 0.4765 0.5327 0.3700 0.0448  -0.0372 0.0784  337 MET B CA  
3661  C C   . MET B 36  ? 0.5031 0.5540 0.4074 0.0320  -0.0342 0.0716  337 MET B C   
3662  O O   . MET B 36  ? 0.4817 0.5114 0.3843 0.0303  -0.0327 0.0723  337 MET B O   
3663  C CB  . MET B 36  ? 0.5092 0.5538 0.3974 0.0577  -0.0381 0.0812  337 MET B CB  
3664  C CG  . MET B 36  ? 0.6907 0.7371 0.5654 0.0740  -0.0409 0.0889  337 MET B CG  
3665  S SD  . MET B 36  ? 0.7980 0.8147 0.6589 0.0891  -0.0407 0.0932  337 MET B SD  
3666  C CE  . MET B 36  ? 0.8486 0.8635 0.6890 0.1093  -0.0436 0.1036  337 MET B CE  
3667  N N   . GLY B 37  ? 0.5912 0.6596 0.5046 0.0234  -0.0333 0.0650  338 GLY B N   
3668  C CA  . GLY B 37  ? 0.6088 0.6724 0.5308 0.0140  -0.0303 0.0585  338 GLY B CA  
3669  C C   . GLY B 37  ? 0.5744 0.6194 0.4929 0.0082  -0.0280 0.0613  338 GLY B C   
3670  O O   . GLY B 37  ? 0.5932 0.6361 0.5182 0.0021  -0.0256 0.0563  338 GLY B O   
3671  N N   . SER B 38  ? 0.6057 0.6383 0.5133 0.0096  -0.0285 0.0692  339 SER B N   
3672  C CA  . SER B 38  ? 0.5832 0.6003 0.4867 0.0023  -0.0265 0.0726  339 SER B CA  
3673  C C   . SER B 38  ? 0.6117 0.6036 0.5047 0.0050  -0.0275 0.0785  339 SER B C   
3674  O O   . SER B 38  ? 0.5758 0.5534 0.4626 -0.0027 -0.0263 0.0823  339 SER B O   
3675  C CB  . SER B 38  ? 0.6774 0.7006 0.5746 -0.0022 -0.0255 0.0771  339 SER B CB  
3676  O OG  . SER B 38  ? 0.7189 0.7343 0.6026 0.0036  -0.0274 0.0853  339 SER B OG  
3677  N N   . ILE B 39  ? 0.6039 0.5905 0.4931 0.0156  -0.0295 0.0794  340 ILE B N   
3678  C CA  . ILE B 39  ? 0.6493 0.6090 0.5268 0.0203  -0.0303 0.0831  340 ILE B CA  
3679  C C   . ILE B 39  ? 0.7226 0.6782 0.6091 0.0173  -0.0293 0.0768  340 ILE B C   
3680  O O   . ILE B 39  ? 0.7530 0.7264 0.6528 0.0188  -0.0289 0.0705  340 ILE B O   
3681  C CB  . ILE B 39  ? 0.6423 0.6009 0.5111 0.0360  -0.0325 0.0866  340 ILE B CB  
3682  C CG1 . ILE B 39  ? 0.7229 0.6850 0.5810 0.0397  -0.0336 0.0937  340 ILE B CG1 
3683  C CG2 . ILE B 39  ? 0.7857 0.7133 0.6400 0.0429  -0.0329 0.0895  340 ILE B CG2 
3684  C CD1 . ILE B 39  ? 0.8466 0.7772 0.6847 0.0356  -0.0329 0.1023  340 ILE B CD1 
3685  N N   . MET B 40  ? 0.6553 0.5868 0.5333 0.0121  -0.0291 0.0786  341 MET B N   
3686  C CA  . MET B 40  ? 0.7056 0.6343 0.5914 0.0080  -0.0283 0.0729  341 MET B CA  
3687  C C   . MET B 40  ? 0.7805 0.7082 0.6678 0.0196  -0.0289 0.0696  341 MET B C   
3688  O O   . MET B 40  ? 0.6931 0.6341 0.5930 0.0190  -0.0279 0.0637  341 MET B O   
3689  C CB  . MET B 40  ? 0.7563 0.6613 0.6312 -0.0016 -0.0284 0.0754  341 MET B CB  
3690  C CG  . MET B 40  ? 0.9403 0.8392 0.8194 -0.0041 -0.0284 0.0699  341 MET B CG  
3691  S SD  . MET B 40  ? 1.0047 0.9278 0.9026 -0.0133 -0.0267 0.0642  341 MET B SD  
3692  C CE  . MET B 40  ? 1.0115 0.9359 0.9052 -0.0281 -0.0262 0.0688  341 MET B CE  
3693  N N   . HIS B 41  ? 0.8407 0.7526 0.7138 0.0310  -0.0303 0.0736  342 HIS B N   
3694  C CA  . HIS B 41  ? 0.7760 0.6910 0.6494 0.0448  -0.0307 0.0712  342 HIS B CA  
3695  C C   . HIS B 41  ? 0.7554 0.6808 0.6236 0.0581  -0.0320 0.0755  342 HIS B C   
3696  O O   . HIS B 41  ? 0.7624 0.6665 0.6123 0.0694  -0.0331 0.0807  342 HIS B O   
3697  C CB  . HIS B 41  ? 0.8214 0.7054 0.6797 0.0491  -0.0309 0.0713  342 HIS B CB  
3698  C CG  . HIS B 41  ? 0.8843 0.7540 0.7424 0.0344  -0.0305 0.0690  342 HIS B CG  
3699  N ND1 . HIS B 41  ? 0.8458 0.7301 0.7191 0.0279  -0.0294 0.0630  342 HIS B ND1 
3700  C CD2 . HIS B 41  ? 0.9210 0.7650 0.7650 0.0244  -0.0311 0.0720  342 HIS B CD2 
3701  C CE1 . HIS B 41  ? 0.8883 0.7595 0.7580 0.0160  -0.0297 0.0623  342 HIS B CE1 
3702  N NE2 . HIS B 41  ? 0.9301 0.7778 0.7827 0.0124  -0.0307 0.0675  342 HIS B NE2 
3703  N N   . PRO B 42  ? 0.7897 0.7472 0.6719 0.0577  -0.0322 0.0735  343 PRO B N   
3704  C CA  . PRO B 42  ? 0.7543 0.7255 0.6312 0.0697  -0.0342 0.0779  343 PRO B CA  
3705  C C   . PRO B 42  ? 0.8824 0.8607 0.7565 0.0873  -0.0349 0.0779  343 PRO B C   
3706  O O   . PRO B 42  ? 0.8957 0.8659 0.7547 0.1022  -0.0364 0.0840  343 PRO B O   
3707  C CB  . PRO B 42  ? 0.7180 0.7222 0.6109 0.0613  -0.0343 0.0741  343 PRO B CB  
3708  C CG  . PRO B 42  ? 0.7471 0.7562 0.6541 0.0490  -0.0320 0.0669  343 PRO B CG  
3709  C CD  . PRO B 42  ? 0.7875 0.7676 0.6879 0.0459  -0.0308 0.0672  343 PRO B CD  
3710  N N   . SER B 43  ? 1.0093 1.0013 0.8957 0.0868  -0.0335 0.0718  344 SER B N   
3711  C CA  . SER B 43  ? 0.9147 0.9224 0.8017 0.1030  -0.0336 0.0712  344 SER B CA  
3712  C C   . SER B 43  ? 0.8567 0.8372 0.7331 0.1103  -0.0321 0.0703  344 SER B C   
3713  O O   . SER B 43  ? 0.8461 0.8070 0.7230 0.0990  -0.0307 0.0673  344 SER B O   
3714  C CB  . SER B 43  ? 0.8710 0.9187 0.7792 0.0968  -0.0326 0.0651  344 SER B CB  
3715  O OG  . SER B 43  ? 0.9428 1.0164 0.8530 0.1122  -0.0330 0.0655  344 SER B OG  
3716  N N   . GLN B 44  ? 0.8998 0.8802 0.7655 0.1306  -0.0325 0.0728  345 GLN B N   
3717  C CA  . GLN B 44  ? 0.9958 0.9587 0.8528 0.1405  -0.0308 0.0706  345 GLN B CA  
3718  C C   . GLN B 44  ? 1.0843 1.0854 0.9545 0.1509  -0.0293 0.0672  345 GLN B C   
3719  O O   . GLN B 44  ? 1.0442 1.0365 0.9060 0.1641  -0.0277 0.0658  345 GLN B O   
3720  C CB  . GLN B 44  ? 0.9878 0.9115 0.8161 0.1573  -0.0317 0.0760  345 GLN B CB  
3721  C CG  . GLN B 44  ? 1.0255 0.9088 0.8383 0.1450  -0.0327 0.0796  345 GLN B CG  
3722  C CD  . GLN B 44  ? 1.1899 1.0331 0.9712 0.1615  -0.0335 0.0860  345 GLN B CD  
3723  O OE1 . GLN B 44  ? 1.3137 1.1561 1.0855 0.1688  -0.0349 0.0929  345 GLN B OE1 
3724  N NE2 . GLN B 44  ? 1.1632 0.9714 0.9261 0.1681  -0.0324 0.0839  345 GLN B NE2 
3725  N N   . HIS B 45  ? 1.1406 1.1843 1.0304 0.1442  -0.0297 0.0656  346 HIS B N   
3726  C CA  . HIS B 45  ? 1.1172 1.2023 1.0216 0.1494  -0.0280 0.0623  346 HIS B CA  
3727  C C   . HIS B 45  ? 1.1278 1.2073 1.0392 0.1403  -0.0245 0.0569  346 HIS B C   
3728  O O   . HIS B 45  ? 1.1323 1.2053 1.0525 0.1208  -0.0236 0.0537  346 HIS B O   
3729  C CB  . HIS B 45  ? 1.0234 1.1507 0.9463 0.1376  -0.0292 0.0607  346 HIS B CB  
3730  C CG  . HIS B 45  ? 0.9955 1.1716 0.9303 0.1458  -0.0286 0.0594  346 HIS B CG  
3731  N ND1 . HIS B 45  ? 0.9928 1.2083 0.9465 0.1298  -0.0283 0.0553  346 HIS B ND1 
3732  C CD2 . HIS B 45  ? 0.9921 1.1856 0.9219 0.1682  -0.0282 0.0616  346 HIS B CD2 
3733  C CE1 . HIS B 45  ? 0.9848 1.2426 0.9460 0.1401  -0.0279 0.0551  346 HIS B CE1 
3734  N NE2 . HIS B 45  ? 0.9863 1.2335 0.9340 0.1645  -0.0277 0.0590  346 HIS B NE2 
3735  N N   . ALA B 46  ? 1.1140 1.1962 1.0199 0.1558  -0.0225 0.0562  347 ALA B N   
3736  C CA  . ALA B 46  ? 0.9857 1.0635 0.8957 0.1504  -0.0190 0.0516  347 ALA B CA  
3737  C C   . ALA B 46  ? 0.9396 1.0628 0.8625 0.1570  -0.0162 0.0498  347 ALA B C   
3738  O O   . ALA B 46  ? 0.8248 0.9731 0.7458 0.1750  -0.0169 0.0524  347 ALA B O   
3739  C CB  . ALA B 46  ? 0.8810 0.9149 0.7693 0.1617  -0.0187 0.0516  347 ALA B CB  
3740  N N   . ARG B 47  ? 1.0756 1.2103 1.0108 0.1427  -0.0129 0.0458  348 ARG B N   
3741  C CA  . ARG B 47  ? 1.1516 1.3327 1.1011 0.1429  -0.0096 0.0443  348 ARG B CA  
3742  C C   . ARG B 47  ? 1.2776 1.4659 1.2189 0.1647  -0.0069 0.0444  348 ARG B C   
3743  O O   . ARG B 47  ? 1.3215 1.5539 1.2741 0.1680  -0.0041 0.0439  348 ARG B O   
3744  C CB  . ARG B 47  ? 1.1153 1.3019 1.0778 0.1191  -0.0065 0.0407  348 ARG B CB  
3745  C CG  . ARG B 47  ? 1.0831 1.2886 1.0585 0.0993  -0.0079 0.0397  348 ARG B CG  
3746  C CD  . ARG B 47  ? 1.1458 1.3393 1.1272 0.0768  -0.0052 0.0366  348 ARG B CD  
3747  N NE  . ARG B 47  ? 1.2483 1.4596 1.2354 0.0722  -0.0001 0.0350  348 ARG B NE  
3748  C CZ  . ARG B 47  ? 1.2315 1.4822 1.2303 0.0621  0.0024  0.0340  348 ARG B CZ  
3749  N NH1 . ARG B 47  ? 1.1636 1.4414 1.1701 0.0556  -0.0002 0.0336  348 ARG B NH1 
3750  N NH2 . ARG B 47  ? 1.1964 1.4604 1.1986 0.0575  0.0076  0.0334  348 ARG B NH2 
3751  N N   . ARG B 48  ? 1.2957 1.4428 1.2166 0.1796  -0.0075 0.0448  349 ARG B N   
3752  C CA  . ARG B 48  ? 1.2112 1.3583 1.1199 0.2026  -0.0049 0.0443  349 ARG B CA  
3753  C C   . ARG B 48  ? 1.2789 1.3851 1.1617 0.2236  -0.0077 0.0469  349 ARG B C   
3754  O O   . ARG B 48  ? 1.3076 1.3824 1.1828 0.2160  -0.0113 0.0489  349 ARG B O   
3755  C CB  . ARG B 48  ? 1.1475 1.2801 1.0554 0.1944  -0.0012 0.0402  349 ARG B CB  
3756  C CG  . ARG B 48  ? 1.0724 1.1677 0.9792 0.1730  -0.0028 0.0385  349 ARG B CG  
3757  C CD  . ARG B 48  ? 1.0639 1.1340 0.9609 0.1729  -0.0005 0.0349  349 ARG B CD  
3758  N NE  . ARG B 48  ? 1.1113 1.1635 0.9874 0.1973  -0.0001 0.0342  349 ARG B NE  
3759  C CZ  . ARG B 48  ? 1.2811 1.3550 1.1556 0.2121  0.0041  0.0326  349 ARG B CZ  
3760  N NH1 . ARG B 48  ? 1.3227 1.4379 1.2164 0.2027  0.0082  0.0322  349 ARG B NH1 
3761  N NH2 . ARG B 48  ? 1.3559 1.4093 1.2083 0.2361  0.0045  0.0316  349 ARG B NH2 
3762  N N   . PRO B 49  ? 1.4608 1.5638 1.3273 0.2501  -0.0060 0.0470  350 PRO B N   
3763  C CA  . PRO B 49  ? 1.5773 1.6356 1.4151 0.2701  -0.0085 0.0497  350 PRO B CA  
3764  C C   . PRO B 49  ? 1.6950 1.6917 1.5130 0.2612  -0.0095 0.0470  350 PRO B C   
3765  O O   . PRO B 49  ? 1.6409 1.6286 1.4698 0.2362  -0.0100 0.0446  350 PRO B O   
3766  C CB  . PRO B 49  ? 1.6094 1.6861 1.4360 0.3017  -0.0056 0.0498  350 PRO B CB  
3767  C CG  . PRO B 49  ? 1.6465 1.7507 1.4879 0.2942  -0.0009 0.0450  350 PRO B CG  
3768  C CD  . PRO B 49  ? 1.5847 1.7220 1.4558 0.2638  -0.0012 0.0448  350 PRO B CD  
3769  N N   . GLU B 50  ? 1.8147 1.7686 1.6020 0.2816  -0.0098 0.0471  351 GLU B N   
3770  C CA  . GLU B 50  ? 1.8017 1.6949 1.5671 0.2717  -0.0115 0.0446  351 GLU B CA  
3771  C C   . GLU B 50  ? 1.6216 1.5076 1.3866 0.2657  -0.0088 0.0377  351 GLU B C   
3772  O O   . GLU B 50  ? 1.5057 1.3782 1.2778 0.2419  -0.0099 0.0349  351 GLU B O   
3773  C CB  . GLU B 50  ? 1.8870 1.7316 1.6157 0.2944  -0.0128 0.0471  351 GLU B CB  
3774  C CG  . GLU B 50  ? 1.8451 1.6730 1.5661 0.2926  -0.0163 0.0543  351 GLU B CG  
3775  C CD  . GLU B 50  ? 1.7827 1.5433 1.4751 0.2822  -0.0187 0.0547  351 GLU B CD  
3776  O OE1 . GLU B 50  ? 1.7630 1.5015 1.4547 0.2630  -0.0188 0.0492  351 GLU B OE1 
3777  O OE2 . GLU B 50  ? 1.7232 1.4539 1.3930 0.2928  -0.0204 0.0607  351 GLU B OE2 
3778  N N   . ASP B 51  ? 1.5794 1.4760 1.3355 0.2881  -0.0053 0.0351  352 ASP B N   
3779  C CA  . ASP B 51  ? 1.5454 1.4302 1.2946 0.2873  -0.0026 0.0285  352 ASP B CA  
3780  C C   . ASP B 51  ? 1.4912 1.4346 1.2658 0.2881  0.0020  0.0273  352 ASP B C   
3781  O O   . ASP B 51  ? 1.3958 1.3837 1.1980 0.2759  0.0023  0.0305  352 ASP B O   
3782  C CB  . ASP B 51  ? 1.4955 1.3343 1.2068 0.3127  -0.0021 0.0258  352 ASP B CB  
3783  C CG  . ASP B 51  ? 1.4392 1.2111 1.1236 0.3012  -0.0060 0.0241  352 ASP B CG  
3784  O OD1 . ASP B 51  ? 1.3655 1.1226 1.0535 0.2789  -0.0072 0.0197  352 ASP B OD1 
3785  O OD2 . ASP B 51  ? 1.4189 1.1548 1.0789 0.3132  -0.0080 0.0276  352 ASP B OD2 
3786  N N   . VAL B 52  ? 1.5288 1.4713 1.2926 0.3014  0.0058  0.0227  353 VAL B N   
3787  C CA  . VAL B 52  ? 1.4942 1.4896 1.2799 0.3001  0.0108  0.0217  353 VAL B CA  
3788  C C   . VAL B 52  ? 1.5522 1.6029 1.3537 0.3147  0.0128  0.0264  353 VAL B C   
3789  O O   . VAL B 52  ? 1.5699 1.6223 1.3554 0.3437  0.0136  0.0276  353 VAL B O   
3790  C CB  . VAL B 52  ? 1.3174 1.2991 1.0849 0.3141  0.0146  0.0158  353 VAL B CB  
3791  C CG1 . VAL B 52  ? 1.3976 1.3495 1.1327 0.3465  0.0149  0.0144  353 VAL B CG1 
3792  C CG2 . VAL B 52  ? 1.1313 1.1708 0.9205 0.3136  0.0208  0.0157  353 VAL B CG2 
3793  N N   . ALA B 53  ? 1.4244 1.5209 1.2563 0.2947  0.0136  0.0289  354 ALA B N   
3794  C CA  . ALA B 53  ? 1.2024 1.3535 1.0520 0.3018  0.0142  0.0333  354 ALA B CA  
3795  C C   . ALA B 53  ? 1.0945 1.2969 0.9510 0.3185  0.0201  0.0327  354 ALA B C   
3796  O O   . ALA B 53  ? 1.1161 1.3227 0.9735 0.3145  0.0246  0.0294  354 ALA B O   
3797  C CB  . ALA B 53  ? 1.1316 1.3089 1.0087 0.2715  0.0126  0.0353  354 ALA B CB  
3798  N N   . THR B 54  ? 0.9904 1.2346 0.8518 0.3381  0.0204  0.0362  355 THR B N   
3799  C CA  . THR B 54  ? 0.9115 1.2188 0.7856 0.3507  0.0260  0.0365  355 THR B CA  
3800  C C   . THR B 54  ? 0.8362 1.1887 0.7407 0.3189  0.0289  0.0367  355 THR B C   
3801  O O   . THR B 54  ? 0.8708 1.2056 0.7856 0.2899  0.0262  0.0366  355 THR B O   
3802  C CB  . THR B 54  ? 0.9128 1.2596 0.7873 0.3771  0.0247  0.0407  355 THR B CB  
3803  O OG1 . THR B 54  ? 0.9424 1.2990 0.8308 0.3611  0.0194  0.0444  355 THR B OG1 
3804  C CG2 . THR B 54  ? 0.8755 1.1701 0.7124 0.4042  0.0233  0.0401  355 THR B CG2 
3805  N N   . LYS B 55  ? 0.8327 1.2435 0.7501 0.3244  0.0347  0.0370  356 LYS B N   
3806  C CA  . LYS B 55  ? 0.7598 1.2130 0.7033 0.2936  0.0381  0.0376  356 LYS B CA  
3807  C C   . LYS B 55  ? 0.6644 1.1514 0.6283 0.2761  0.0342  0.0404  356 LYS B C   
3808  O O   . LYS B 55  ? 0.6715 1.1579 0.6496 0.2441  0.0338  0.0402  356 LYS B O   
3809  C CB  . LYS B 55  ? 0.7170 1.2274 0.6687 0.3029  0.0457  0.0376  356 LYS B CB  
3810  C CG  . LYS B 55  ? 0.6577 1.2069 0.6327 0.2695  0.0501  0.0386  356 LYS B CG  
3811  C CD  . LYS B 55  ? 0.7069 1.3062 0.6869 0.2776  0.0584  0.0388  356 LYS B CD  
3812  C CE  . LYS B 55  ? 0.6258 1.2529 0.6247 0.2415  0.0632  0.0402  356 LYS B CE  
3813  N NZ  . LYS B 55  ? 0.7148 1.4061 0.7226 0.2475  0.0710  0.0417  356 LYS B NZ  
3814  N N   . ASP B 56  ? 0.7661 1.2822 0.7301 0.2973  0.0313  0.0431  357 ASP B N   
3815  C CA  . ASP B 56  ? 0.7394 1.2896 0.7218 0.2810  0.0271  0.0454  357 ASP B CA  
3816  C C   . ASP B 56  ? 0.6771 1.1728 0.6542 0.2642  0.0209  0.0452  357 ASP B C   
3817  O O   . ASP B 56  ? 0.7638 1.2795 0.7566 0.2418  0.0181  0.0458  357 ASP B O   
3818  C CB  . ASP B 56  ? 0.7332 1.3310 0.7164 0.3098  0.0251  0.0486  357 ASP B CB  
3819  C CG  . ASP B 56  ? 0.8531 1.3968 0.8058 0.3396  0.0212  0.0498  357 ASP B CG  
3820  O OD1 . ASP B 56  ? 0.8870 1.4474 0.8268 0.3580  0.0205  0.0517  357 ASP B OD1 
3821  O OD2 . ASP B 56  ? 0.8885 1.3674 0.8258 0.3402  0.0190  0.0487  357 ASP B OD2 
3822  N N   . GLN B 57  ? 0.6235 1.0522 0.5782 0.2735  0.0190  0.0441  358 GLN B N   
3823  C CA  . GLN B 57  ? 0.6877 1.0651 0.6379 0.2549  0.0141  0.0438  358 GLN B CA  
3824  C C   . GLN B 57  ? 0.7555 1.1202 0.7166 0.2225  0.0163  0.0411  358 GLN B C   
3825  O O   . GLN B 57  ? 0.7324 1.1029 0.7067 0.1981  0.0142  0.0412  358 GLN B O   
3826  C CB  . GLN B 57  ? 0.7563 1.0688 0.6783 0.2738  0.0115  0.0435  358 GLN B CB  
3827  C CG  . GLN B 57  ? 0.8838 1.1832 0.7931 0.2926  0.0063  0.0474  358 GLN B CG  
3828  C CD  . GLN B 57  ? 1.0024 1.2583 0.8807 0.3238  0.0063  0.0476  358 GLN B CD  
3829  O OE1 . GLN B 57  ? 1.0428 1.2656 0.9073 0.3269  0.0090  0.0439  358 GLN B OE1 
3830  N NE2 . GLN B 57  ? 0.9713 1.2257 0.8365 0.3474  0.0032  0.0519  358 GLN B NE2 
3831  N N   . LEU B 58  ? 0.7977 1.1443 0.7516 0.2229  0.0206  0.0387  359 LEU B N   
3832  C CA  . LEU B 58  ? 0.6820 1.0039 0.6403 0.1961  0.0221  0.0367  359 LEU B CA  
3833  C C   . LEU B 58  ? 0.6232 0.9903 0.6025 0.1721  0.0263  0.0371  359 LEU B C   
3834  O O   . LEU B 58  ? 0.5051 0.8579 0.4913 0.1466  0.0256  0.0366  359 LEU B O   
3835  C CB  . LEU B 58  ? 0.6553 0.9418 0.5970 0.2050  0.0248  0.0341  359 LEU B CB  
3836  C CG  . LEU B 58  ? 0.6590 0.9238 0.6041 0.1803  0.0268  0.0326  359 LEU B CG  
3837  C CD1 . LEU B 58  ? 0.6072 0.8358 0.5525 0.1632  0.0214  0.0326  359 LEU B CD1 
3838  C CD2 . LEU B 58  ? 0.6259 0.8625 0.5547 0.1898  0.0296  0.0298  359 LEU B CD2 
3839  N N   . PHE B 59  ? 0.5994 1.0208 0.5881 0.1793  0.0309  0.0381  360 PHE B N   
3840  C CA  . PHE B 59  ? 0.5719 1.0328 0.5781 0.1536  0.0357  0.0385  360 PHE B CA  
3841  C C   . PHE B 59  ? 0.6005 1.0745 0.6202 0.1291  0.0323  0.0388  360 PHE B C   
3842  O O   . PHE B 59  ? 0.5021 0.9680 0.5272 0.1017  0.0346  0.0381  360 PHE B O   
3843  C CB  . PHE B 59  ? 0.5417 1.0658 0.5568 0.1648  0.0412  0.0399  360 PHE B CB  
3844  C CG  . PHE B 59  ? 0.6448 1.2063 0.6752 0.1363  0.0471  0.0406  360 PHE B CG  
3845  C CD1 . PHE B 59  ? 0.7014 1.2464 0.7267 0.1262  0.0531  0.0406  360 PHE B CD1 
3846  C CD2 . PHE B 59  ? 0.5481 1.1586 0.5959 0.1181  0.0465  0.0414  360 PHE B CD2 
3847  C CE1 . PHE B 59  ? 0.6417 1.2160 0.6780 0.0989  0.0589  0.0421  360 PHE B CE1 
3848  C CE2 . PHE B 59  ? 0.5842 1.2248 0.6433 0.0891  0.0520  0.0421  360 PHE B CE2 
3849  C CZ  . PHE B 59  ? 0.6772 1.2982 0.7299 0.0795  0.0586  0.0428  360 PHE B CZ  
3850  N N   . PRO B 60  ? 0.5940 1.0877 0.6180 0.1373  0.0271  0.0396  361 PRO B N   
3851  C CA  . PRO B 60  ? 0.4321 0.9411 0.4684 0.1124  0.0241  0.0390  361 PRO B CA  
3852  C C   . PRO B 60  ? 0.4498 0.9035 0.4800 0.0936  0.0217  0.0374  361 PRO B C   
3853  O O   . PRO B 60  ? 0.4666 0.9242 0.5044 0.0665  0.0225  0.0359  361 PRO B O   
3854  C CB  . PRO B 60  ? 0.5039 1.0378 0.5417 0.1313  0.0185  0.0405  361 PRO B CB  
3855  C CG  . PRO B 60  ? 0.5590 1.1161 0.5912 0.1630  0.0209  0.0424  361 PRO B CG  
3856  C CD  . PRO B 60  ? 0.5348 1.0420 0.5520 0.1696  0.0242  0.0413  361 PRO B CD  
3857  N N   . LEU B 61  ? 0.5135 0.9154 0.5288 0.1073  0.0189  0.0374  362 LEU B N   
3858  C CA  . LEU B 61  ? 0.5724 0.9238 0.5816 0.0912  0.0172  0.0360  362 LEU B CA  
3859  C C   . LEU B 61  ? 0.6312 0.9747 0.6420 0.0722  0.0228  0.0351  362 LEU B C   
3860  O O   . LEU B 61  ? 0.5134 0.8407 0.5262 0.0500  0.0229  0.0340  362 LEU B O   
3861  C CB  . LEU B 61  ? 0.5093 0.8117 0.5020 0.1091  0.0141  0.0362  362 LEU B CB  
3862  C CG  . LEU B 61  ? 0.5665 0.8650 0.5517 0.1303  0.0090  0.0380  362 LEU B CG  
3863  C CD1 . LEU B 61  ? 0.6483 0.8939 0.6145 0.1436  0.0070  0.0379  362 LEU B CD1 
3864  C CD2 . LEU B 61  ? 0.6231 0.9267 0.6153 0.1176  0.0046  0.0385  362 LEU B CD2 
3865  N N   . ALA B 62  ? 0.6833 1.0371 0.6912 0.0818  0.0278  0.0357  363 ALA B N   
3866  C CA  . ALA B 62  ? 0.6730 1.0165 0.6794 0.0666  0.0334  0.0358  363 ALA B CA  
3867  C C   . ALA B 62  ? 0.6283 1.0075 0.6468 0.0418  0.0375  0.0363  363 ALA B C   
3868  O O   . ALA B 62  ? 0.5679 0.9260 0.5840 0.0207  0.0401  0.0363  363 ALA B O   
3869  C CB  . ALA B 62  ? 0.6583 1.0066 0.6575 0.0849  0.0376  0.0362  363 ALA B CB  
3870  N N   . LYS B 63  ? 0.6132 1.0466 0.6434 0.0437  0.0383  0.0368  364 LYS B N   
3871  C CA  . LYS B 63  ? 0.6245 1.0937 0.6658 0.0171  0.0416  0.0368  364 LYS B CA  
3872  C C   . LYS B 63  ? 0.5949 1.0390 0.6359 -0.0045 0.0378  0.0346  364 LYS B C   
3873  O O   . LYS B 63  ? 0.6070 1.0481 0.6481 -0.0308 0.0413  0.0341  364 LYS B O   
3874  C CB  . LYS B 63  ? 0.5845 1.1207 0.6394 0.0238  0.0417  0.0374  364 LYS B CB  
3875  C CG  . LYS B 63  ? 0.6800 1.2592 0.7463 -0.0061 0.0460  0.0373  364 LYS B CG  
3876  C CD  . LYS B 63  ? 0.6554 1.3072 0.7369 -0.0012 0.0451  0.0376  364 LYS B CD  
3877  C CE  . LYS B 63  ? 0.6738 1.3666 0.7656 -0.0355 0.0491  0.0370  364 LYS B CE  
3878  N NZ  . LYS B 63  ? 0.6354 1.2950 0.7231 -0.0638 0.0461  0.0338  364 LYS B NZ  
3879  N N   . GLU B 64  ? 0.4865 0.9094 0.5247 0.0064  0.0310  0.0334  365 GLU B N   
3880  C CA  . GLU B 64  ? 0.6207 1.0201 0.6575 -0.0120 0.0276  0.0310  365 GLU B CA  
3881  C C   . GLU B 64  ? 0.5829 0.9303 0.6086 -0.0243 0.0299  0.0306  365 GLU B C   
3882  O O   . GLU B 64  ? 0.5907 0.9276 0.6145 -0.0475 0.0314  0.0290  365 GLU B O   
3883  C CB  . GLU B 64  ? 0.7478 1.1367 0.7832 0.0040  0.0202  0.0305  365 GLU B CB  
3884  C CG  . GLU B 64  ? 0.9121 1.2935 0.9487 -0.0134 0.0164  0.0277  365 GLU B CG  
3885  C CD  . GLU B 64  ? 1.0647 1.3905 1.0904 -0.0134 0.0139  0.0270  365 GLU B CD  
3886  O OE1 . GLU B 64  ? 1.1225 1.4210 1.1429 -0.0308 0.0167  0.0255  365 GLU B OE1 
3887  O OE2 . GLU B 64  ? 1.1004 1.4104 1.1221 0.0044  0.0094  0.0282  365 GLU B OE2 
3888  N N   . PHE B 65  ? 0.6383 0.9525 0.6550 -0.0088 0.0302  0.0320  366 PHE B N   
3889  C CA  . PHE B 65  ? 0.6081 0.8756 0.6142 -0.0178 0.0318  0.0320  366 PHE B CA  
3890  C C   . PHE B 65  ? 0.6990 0.9705 0.7027 -0.0354 0.0390  0.0335  366 PHE B C   
3891  O O   . PHE B 65  ? 0.7600 1.0066 0.7572 -0.0536 0.0408  0.0329  366 PHE B O   
3892  C CB  . PHE B 65  ? 0.6817 0.9173 0.6789 0.0021  0.0300  0.0328  366 PHE B CB  
3893  C CG  . PHE B 65  ? 0.6781 0.8729 0.6649 -0.0049 0.0319  0.0333  366 PHE B CG  
3894  C CD1 . PHE B 65  ? 0.6459 0.8118 0.6286 -0.0156 0.0296  0.0321  366 PHE B CD1 
3895  C CD2 . PHE B 65  ? 0.6552 0.8422 0.6354 0.0003  0.0360  0.0350  366 PHE B CD2 
3896  C CE1 . PHE B 65  ? 0.5807 0.7117 0.5533 -0.0197 0.0313  0.0328  366 PHE B CE1 
3897  C CE2 . PHE B 65  ? 0.6080 0.7600 0.5782 -0.0048 0.0374  0.0359  366 PHE B CE2 
3898  C CZ  . PHE B 65  ? 0.5878 0.7124 0.5543 -0.0143 0.0350  0.0350  366 PHE B CZ  
3899  N N   . ILE B 66  ? 0.6637 0.9645 0.6707 -0.0295 0.0436  0.0356  367 ILE B N   
3900  C CA  . ILE B 66  ? 0.6428 0.9509 0.6471 -0.0471 0.0512  0.0379  367 ILE B CA  
3901  C C   . ILE B 66  ? 0.6758 1.0004 0.6842 -0.0745 0.0528  0.0366  367 ILE B C   
3902  O O   . ILE B 66  ? 0.6670 0.9652 0.6656 -0.0943 0.0566  0.0373  367 ILE B O   
3903  C CB  . ILE B 66  ? 0.6184 0.9653 0.6276 -0.0355 0.0559  0.0402  367 ILE B CB  
3904  C CG1 . ILE B 66  ? 0.5278 0.8562 0.5306 -0.0075 0.0536  0.0401  367 ILE B CG1 
3905  C CG2 . ILE B 66  ? 0.6136 0.9659 0.6184 -0.0539 0.0643  0.0435  367 ILE B CG2 
3906  C CD1 . ILE B 66  ? 0.4921 0.7741 0.4811 -0.0072 0.0550  0.0412  367 ILE B CD1 
3907  N N   . ASP B 67  ? 0.6620 1.0291 0.6830 -0.0757 0.0498  0.0346  368 ASP B N   
3908  C CA  . ASP B 67  ? 0.6369 1.0215 0.6615 -0.1024 0.0500  0.0322  368 ASP B CA  
3909  C C   . ASP B 67  ? 0.6249 0.9590 0.6377 -0.1149 0.0476  0.0295  368 ASP B C   
3910  O O   . ASP B 67  ? 0.5575 0.8768 0.5619 -0.1399 0.0513  0.0286  368 ASP B O   
3911  C CB  . ASP B 67  ? 0.5655 1.0004 0.6047 -0.0967 0.0450  0.0301  368 ASP B CB  
3912  C CG  . ASP B 67  ? 0.6141 1.1096 0.6655 -0.0907 0.0486  0.0324  368 ASP B CG  
3913  O OD1 . ASP B 67  ? 0.6989 1.1976 0.7475 -0.0926 0.0553  0.0355  368 ASP B OD1 
3914  O OD2 . ASP B 67  ? 0.6406 1.1824 0.7041 -0.0831 0.0447  0.0313  368 ASP B OD2 
3915  N N   . GLN B 68  ? 0.5664 0.8734 0.5771 -0.0977 0.0415  0.0281  369 GLN B N   
3916  C CA  . GLN B 68  ? 0.5870 0.8475 0.5863 -0.1058 0.0393  0.0257  369 GLN B CA  
3917  C C   . GLN B 68  ? 0.6319 0.8504 0.6162 -0.1136 0.0448  0.0279  369 GLN B C   
3918  O O   . GLN B 68  ? 0.6858 0.8790 0.6589 -0.1328 0.0471  0.0264  369 GLN B O   
3919  C CB  . GLN B 68  ? 0.5993 0.8417 0.5995 -0.0842 0.0326  0.0249  369 GLN B CB  
3920  C CG  . GLN B 68  ? 0.6027 0.8009 0.5923 -0.0888 0.0303  0.0226  369 GLN B CG  
3921  C CD  . GLN B 68  ? 0.7037 0.8867 0.6942 -0.0680 0.0244  0.0228  369 GLN B CD  
3922  O OE1 . GLN B 68  ? 0.7340 0.9415 0.7328 -0.0534 0.0209  0.0236  369 GLN B OE1 
3923  N NE2 . GLN B 68  ? 0.7632 0.9057 0.7439 -0.0661 0.0236  0.0225  369 GLN B NE2 
3924  N N   . TYR B 69  ? 0.7050 0.9147 0.6868 -0.0985 0.0471  0.0317  370 TYR B N   
3925  C CA  . TYR B 69  ? 0.6656 0.8357 0.6322 -0.1031 0.0518  0.0345  370 TYR B CA  
3926  C C   . TYR B 69  ? 0.6258 0.8015 0.5857 -0.1274 0.0593  0.0364  370 TYR B C   
3927  O O   . TYR B 69  ? 0.6196 0.7570 0.5633 -0.1403 0.0625  0.0372  370 TYR B O   
3928  C CB  . TYR B 69  ? 0.6787 0.8419 0.6438 -0.0822 0.0523  0.0376  370 TYR B CB  
3929  C CG  . TYR B 69  ? 0.6562 0.7916 0.6068 -0.0878 0.0583  0.0416  370 TYR B CG  
3930  C CD1 . TYR B 69  ? 0.6776 0.7674 0.6141 -0.0879 0.0578  0.0420  370 TYR B CD1 
3931  C CD2 . TYR B 69  ? 0.6087 0.7652 0.5589 -0.0924 0.0648  0.0452  370 TYR B CD2 
3932  C CE1 . TYR B 69  ? 0.7010 0.7651 0.6224 -0.0917 0.0633  0.0464  370 TYR B CE1 
3933  C CE2 . TYR B 69  ? 0.8172 0.9476 0.7524 -0.0976 0.0706  0.0497  370 TYR B CE2 
3934  C CZ  . TYR B 69  ? 0.7888 0.8720 0.7091 -0.0967 0.0696  0.0504  370 TYR B CZ  
3935  O OH  . TYR B 69  ? 0.7255 0.7828 0.6293 -0.1000 0.0753  0.0555  370 TYR B OH  
3936  N N   . TYR B 70  ? 0.4932 0.7159 0.4638 -0.1339 0.0625  0.0376  371 TYR B N   
3937  C CA  . TYR B 70  ? 0.4941 0.7238 0.4579 -0.1600 0.0700  0.0397  371 TYR B CA  
3938  C C   . TYR B 70  ? 0.6044 0.8285 0.5638 -0.1850 0.0691  0.0354  371 TYR B C   
3939  O O   . TYR B 70  ? 0.7012 0.9030 0.6455 -0.2082 0.0747  0.0366  371 TYR B O   
3940  C CB  . TYR B 70  ? 0.5574 0.8434 0.5343 -0.1609 0.0742  0.0423  371 TYR B CB  
3941  C CG  . TYR B 70  ? 0.6935 0.9722 0.6648 -0.1473 0.0792  0.0476  371 TYR B CG  
3942  C CD1 . TYR B 70  ? 0.6865 0.9764 0.6651 -0.1184 0.0760  0.0478  371 TYR B CD1 
3943  C CD2 . TYR B 70  ? 0.7063 0.9624 0.6621 -0.1632 0.0870  0.0524  371 TYR B CD2 
3944  C CE1 . TYR B 70  ? 0.7069 0.9889 0.6787 -0.1062 0.0802  0.0517  371 TYR B CE1 
3945  C CE2 . TYR B 70  ? 0.6849 0.9347 0.6345 -0.1505 0.0914  0.0572  371 TYR B CE2 
3946  C CZ  . TYR B 70  ? 0.7315 0.9954 0.6896 -0.1221 0.0878  0.0565  371 TYR B CZ  
3947  O OH  . TYR B 70  ? 0.7771 1.0346 0.7278 -0.1095 0.0919  0.0604  371 TYR B OH  
3948  N N   . SER B 71  ? 0.7133 0.9538 0.6832 -0.1805 0.0621  0.0304  372 SER B N   
3949  C CA  . SER B 71  ? 0.7827 1.0122 0.7462 -0.2022 0.0602  0.0252  372 SER B CA  
3950  C C   . SER B 71  ? 0.7399 0.9044 0.6821 -0.2039 0.0607  0.0243  372 SER B C   
3951  O O   . SER B 71  ? 0.8766 1.0151 0.8024 -0.2272 0.0642  0.0224  372 SER B O   
3952  C CB  . SER B 71  ? 0.9146 1.1758 0.8934 -0.1935 0.0522  0.0205  372 SER B CB  
3953  O OG  . SER B 71  ? 0.9581 1.2824 0.9552 -0.1925 0.0519  0.0213  372 SER B OG  
3954  N N   . SER B 72  ? 0.6381 0.7758 0.5789 -0.1793 0.0574  0.0256  373 SER B N   
3955  C CA  . SER B 72  ? 0.6443 0.7248 0.5658 -0.1769 0.0578  0.0253  373 SER B CA  
3956  C C   . SER B 72  ? 0.7920 0.8396 0.6925 -0.1941 0.0657  0.0286  373 SER B C   
3957  O O   . SER B 72  ? 0.7916 0.7967 0.6724 -0.2042 0.0672  0.0265  373 SER B O   
3958  C CB  . SER B 72  ? 0.6530 0.7173 0.5770 -0.1492 0.0547  0.0280  373 SER B CB  
3959  O OG  . SER B 72  ? 0.7151 0.7709 0.6328 -0.1449 0.0600  0.0338  373 SER B OG  
3960  N N   . ILE B 73  ? 0.7762 0.8416 0.6786 -0.1972 0.0712  0.0340  374 ILE B N   
3961  C CA  . ILE B 73  ? 0.8931 0.9239 0.7739 -0.2090 0.0791  0.0392  374 ILE B CA  
3962  C C   . ILE B 73  ? 0.8591 0.9100 0.7361 -0.2399 0.0853  0.0398  374 ILE B C   
3963  O O   . ILE B 73  ? 0.8939 0.9403 0.7612 -0.2490 0.0927  0.0458  374 ILE B O   
3964  C CB  . ILE B 73  ? 0.7999 0.8294 0.6814 -0.1895 0.0815  0.0457  374 ILE B CB  
3965  C CG1 . ILE B 73  ? 0.7705 0.8573 0.6760 -0.1792 0.0798  0.0461  374 ILE B CG1 
3966  C CG2 . ILE B 73  ? 0.6764 0.6708 0.5525 -0.1652 0.0768  0.0456  374 ILE B CG2 
3967  C CD1 . ILE B 73  ? 0.5041 0.6054 0.4085 -0.1760 0.0862  0.0526  374 ILE B CD1 
3968  N N   . LYS B 74  ? 0.9076 0.9813 0.7914 -0.2572 0.0824  0.0336  375 LYS B N   
3969  C CA  . LYS B 74  ? 1.0260 1.1137 0.9030 -0.2915 0.0878  0.0328  375 LYS B CA  
3970  C C   . LYS B 74  ? 1.0186 1.1541 0.9078 -0.2976 0.0934  0.0385  375 LYS B C   
3971  O O   . LYS B 74  ? 1.0538 1.1829 0.9292 -0.3221 0.1012  0.0423  375 LYS B O   
3972  C CB  . LYS B 74  ? 1.1050 1.1275 0.9482 -0.3103 0.0935  0.0335  375 LYS B CB  
3973  C CG  . LYS B 74  ? 1.0381 1.0081 0.8663 -0.2978 0.0889  0.0289  375 LYS B CG  
3974  C CD  . LYS B 74  ? 1.0431 0.9962 0.8575 -0.3230 0.0878  0.0209  375 LYS B CD  
3975  C CE  . LYS B 74  ? 0.9592 0.8810 0.7684 -0.3054 0.0815  0.0151  375 LYS B CE  
3976  N NZ  . LYS B 74  ? 0.8601 0.8262 0.6994 -0.2812 0.0733  0.0132  375 LYS B NZ  
3977  N N   . ARG B 75  ? 0.9276 1.1102 0.8413 -0.2746 0.0896  0.0393  376 ARG B N   
3978  C CA  . ARG B 75  ? 0.9062 1.1486 0.8361 -0.2791 0.0936  0.0428  376 ARG B CA  
3979  C C   . ARG B 75  ? 0.9571 1.2592 0.9119 -0.2746 0.0870  0.0376  376 ARG B C   
3980  O O   . ARG B 75  ? 0.8493 1.1609 0.8046 -0.2947 0.0842  0.0321  376 ARG B O   
3981  C CB  . ARG B 75  ? 0.7407 0.9836 0.6729 -0.2548 0.0965  0.0491  376 ARG B CB  
3982  C CG  . ARG B 75  ? 0.7916 0.9672 0.6993 -0.2493 0.0995  0.0531  376 ARG B CG  
3983  C CD  . ARG B 75  ? 1.0323 1.2087 0.9307 -0.2542 0.1084  0.0610  376 ARG B CD  
3984  N NE  . ARG B 75  ? 1.1643 1.3021 1.0376 -0.2829 0.1156  0.0641  376 ARG B NE  
3985  C CZ  . ARG B 75  ? 1.2500 1.3707 1.1070 -0.2897 0.1240  0.0720  376 ARG B CZ  
3986  N NH1 . ARG B 75  ? 1.3253 1.4057 1.1564 -0.3164 0.1305  0.0749  376 ARG B NH1 
3987  N NH2 . ARG B 75  ? 1.1985 1.3403 1.0632 -0.2696 0.1261  0.0768  376 ARG B NH2 
3988  N N   . PHE B 76  ? 0.9671 1.3071 0.9406 -0.2473 0.0842  0.0391  377 PHE B N   
3989  C CA  . PHE B 76  ? 0.8944 1.3002 0.8911 -0.2408 0.0797  0.0363  377 PHE B CA  
3990  C C   . PHE B 76  ? 0.8932 1.3544 0.8976 -0.2648 0.0862  0.0385  377 PHE B C   
3991  O O   . PHE B 76  ? 0.8660 1.3253 0.8621 -0.2985 0.0892  0.0368  377 PHE B O   
3992  C CB  . PHE B 76  ? 0.8830 1.2885 0.8836 -0.2451 0.0716  0.0293  377 PHE B CB  
3993  C CG  . PHE B 76  ? 0.7821 1.2539 0.8054 -0.2338 0.0663  0.0272  377 PHE B CG  
3994  C CD1 . PHE B 76  ? 0.8141 1.3411 0.8475 -0.2576 0.0670  0.0250  377 PHE B CD1 
3995  C CD2 . PHE B 76  ? 0.7874 1.2668 0.8206 -0.1991 0.0607  0.0277  377 PHE B CD2 
3996  C CE1 . PHE B 76  ? 0.9070 1.4983 0.9610 -0.2449 0.0620  0.0235  377 PHE B CE1 
3997  C CE2 . PHE B 76  ? 0.8077 1.3459 0.8592 -0.1862 0.0561  0.0265  377 PHE B CE2 
3998  C CZ  . PHE B 76  ? 0.8933 1.4887 0.9556 -0.2080 0.0567  0.0246  377 PHE B CZ  
3999  N N   . GLY B 77  ? 0.8928 1.4042 0.9121 -0.2479 0.0885  0.0421  378 GLY B N   
4000  C CA  . GLY B 77  ? 0.8581 1.4246 0.8852 -0.2661 0.0948  0.0449  378 GLY B CA  
4001  C C   . GLY B 77  ? 0.9065 1.4480 0.9188 -0.2746 0.1035  0.0510  378 GLY B C   
4002  O O   . GLY B 77  ? 0.9824 1.5617 1.0001 -0.2781 0.1058  0.0529  378 GLY B O   
4003  N N   . SER B 78  ? 0.8496 1.3252 0.8417 -0.2754 0.1069  0.0538  379 SER B N   
4004  C CA  . SER B 78  ? 0.6749 1.1238 0.6506 -0.2822 0.1160  0.0609  379 SER B CA  
4005  C C   . SER B 78  ? 0.6984 1.1871 0.6856 -0.2570 0.1192  0.0651  379 SER B C   
4006  O O   . SER B 78  ? 0.6439 1.1646 0.6478 -0.2291 0.1136  0.0623  379 SER B O   
4007  C CB  . SER B 78  ? 0.6643 1.0327 0.6175 -0.2733 0.1148  0.0619  379 SER B CB  
4008  O OG  . SER B 78  ? 0.7202 1.0788 0.6805 -0.2365 0.1084  0.0604  379 SER B OG  
4009  N N   . LYS B 79  ? 0.6836 1.1636 0.6594 -0.2639 0.1269  0.0712  380 LYS B N   
4010  C CA  . LYS B 79  ? 0.6338 1.1482 0.6178 -0.2396 0.1306  0.0750  380 LYS B CA  
4011  C C   . LYS B 79  ? 0.6607 1.1413 0.6417 -0.2042 0.1256  0.0737  380 LYS B C   
4012  O O   . LYS B 79  ? 0.6420 1.1556 0.6369 -0.1762 0.1221  0.0715  380 LYS B O   
4013  C CB  . LYS B 79  ? 0.6563 1.1595 0.6266 -0.2524 0.1385  0.0812  380 LYS B CB  
4014  C CG  . LYS B 79  ? 0.8592 1.4241 0.8444 -0.2412 0.1406  0.0824  380 LYS B CG  
4015  C CD  . LYS B 79  ? 0.9255 1.4940 0.9019 -0.2663 0.1464  0.0865  380 LYS B CD  
4016  C CE  . LYS B 79  ? 0.9385 1.5577 0.9290 -0.2857 0.1422  0.0822  380 LYS B CE  
4017  N NZ  . LYS B 79  ? 0.8666 1.5555 0.8805 -0.2627 0.1379  0.0792  380 LYS B NZ  
4018  N N   . ALA B 80  ? 0.6561 1.0676 0.6184 -0.2037 0.1235  0.0741  381 ALA B N   
4019  C CA  . ALA B 80  ? 0.6576 1.0334 0.6163 -0.1717 0.1173  0.0722  381 ALA B CA  
4020  C C   . ALA B 80  ? 0.6239 1.0205 0.5997 -0.1509 0.1079  0.0656  381 ALA B C   
4021  O O   . ALA B 80  ? 0.5024 0.9023 0.4824 -0.1217 0.1043  0.0642  381 ALA B O   
4022  C CB  . ALA B 80  ? 0.6764 0.9807 0.6142 -0.1771 0.1158  0.0730  381 ALA B CB  
4023  N N   . HIS B 81  ? 0.7699 1.1794 0.7540 -0.1662 0.1039  0.0616  382 HIS B N   
4024  C CA  . HIS B 81  ? 0.6785 1.1050 0.6769 -0.1473 0.0950  0.0560  382 HIS B CA  
4025  C C   . HIS B 81  ? 0.6094 1.1017 0.6254 -0.1308 0.0955  0.0560  382 HIS B C   
4026  O O   . HIS B 81  ? 0.6001 1.0963 0.6211 -0.1012 0.0904  0.0539  382 HIS B O   
4027  C CB  . HIS B 81  ? 0.7207 1.1441 0.7215 -0.1689 0.0908  0.0518  382 HIS B CB  
4028  C CG  . HIS B 81  ? 0.8116 1.2591 0.8271 -0.1527 0.0822  0.0469  382 HIS B CG  
4029  N ND1 . HIS B 81  ? 0.8661 1.3329 0.8887 -0.1700 0.0784  0.0427  382 HIS B ND1 
4030  C CD2 . HIS B 81  ? 0.8354 1.2886 0.8578 -0.1210 0.0767  0.0456  382 HIS B CD2 
4031  C CE1 . HIS B 81  ? 0.8605 1.3455 0.8943 -0.1486 0.0709  0.0397  382 HIS B CE1 
4032  N NE2 . HIS B 81  ? 0.8552 1.3307 0.8884 -0.1190 0.0700  0.0415  382 HIS B NE2 
4033  N N   . MET B 82  ? 0.5773 1.1217 0.6012 -0.1495 0.1021  0.0584  383 MET B N   
4034  C CA  . MET B 82  ? 0.6151 1.2276 0.6558 -0.1326 0.1031  0.0586  383 MET B CA  
4035  C C   . MET B 82  ? 0.6639 1.2720 0.6994 -0.1030 0.1059  0.0609  383 MET B C   
4036  O O   . MET B 82  ? 0.7061 1.3389 0.7493 -0.0734 0.1024  0.0588  383 MET B O   
4037  C CB  . MET B 82  ? 0.5730 1.2444 0.6229 -0.1609 0.1101  0.0611  383 MET B CB  
4038  C CG  . MET B 82  ? 0.5460 1.2228 0.6002 -0.1881 0.1044  0.0567  383 MET B CG  
4039  S SD  . MET B 82  ? 0.6905 1.3737 0.7563 -0.1689 0.0942  0.0510  383 MET B SD  
4040  C CE  . MET B 82  ? 0.7522 1.5085 0.8360 -0.1378 0.0910  0.0507  383 MET B CE  
4041  N N   . GLU B 83  ? 0.6389 1.2134 0.6594 -0.1098 0.1122  0.0650  384 GLU B N   
4042  C CA  . GLU B 83  ? 0.5628 1.1271 0.5756 -0.0827 0.1144  0.0665  384 GLU B CA  
4043  C C   . GLU B 83  ? 0.5571 1.0800 0.5651 -0.0544 0.1055  0.0620  384 GLU B C   
4044  O O   . GLU B 83  ? 0.5714 1.1062 0.5799 -0.0253 0.1041  0.0603  384 GLU B O   
4045  C CB  . GLU B 83  ? 0.5814 1.1104 0.5766 -0.0969 0.1217  0.0719  384 GLU B CB  
4046  C CG  . GLU B 83  ? 0.7556 1.3287 0.7532 -0.1199 0.1322  0.0775  384 GLU B CG  
4047  C CD  . GLU B 83  ? 0.8379 1.3671 0.8160 -0.1437 0.1386  0.0833  384 GLU B CD  
4048  O OE1 . GLU B 83  ? 0.8049 1.2717 0.7692 -0.1437 0.1343  0.0825  384 GLU B OE1 
4049  O OE2 . GLU B 83  ? 0.9300 1.4874 0.9059 -0.1619 0.1480  0.0889  384 GLU B OE2 
4050  N N   . ARG B 84  ? 0.4804 0.9540 0.4822 -0.0629 0.0996  0.0600  385 ARG B N   
4051  C CA  . ARG B 84  ? 0.5568 0.9905 0.5538 -0.0398 0.0913  0.0561  385 ARG B CA  
4052  C C   . ARG B 84  ? 0.6425 1.1085 0.6517 -0.0182 0.0856  0.0523  385 ARG B C   
4053  O O   . ARG B 84  ? 0.7312 1.1834 0.7354 0.0090  0.0820  0.0502  385 ARG B O   
4054  C CB  . ARG B 84  ? 0.5356 0.9198 0.5257 -0.0551 0.0868  0.0548  385 ARG B CB  
4055  C CG  . ARG B 84  ? 0.5656 0.9061 0.5491 -0.0350 0.0791  0.0517  385 ARG B CG  
4056  C CD  . ARG B 84  ? 0.4712 0.7752 0.4395 -0.0260 0.0811  0.0536  385 ARG B CD  
4057  N NE  . ARG B 84  ? 0.5744 0.8398 0.5370 -0.0092 0.0734  0.0502  385 ARG B NE  
4058  C CZ  . ARG B 84  ? 0.6026 0.8673 0.5632 0.0151  0.0701  0.0476  385 ARG B CZ  
4059  N NH1 . ARG B 84  ? 0.5991 0.8984 0.5620 0.0281  0.0740  0.0478  385 ARG B NH1 
4060  N NH2 . ARG B 84  ? 0.4825 0.7109 0.4370 0.0262  0.0632  0.0446  385 ARG B NH2 
4061  N N   . LEU B 85  ? 0.5522 1.0604 0.5755 -0.0300 0.0846  0.0516  386 LEU B N   
4062  C CA  . LEU B 85  ? 0.5420 1.0862 0.5762 -0.0082 0.0797  0.0490  386 LEU B CA  
4063  C C   . LEU B 85  ? 0.5371 1.1142 0.5713 0.0179  0.0837  0.0500  386 LEU B C   
4064  O O   . LEU B 85  ? 0.5026 1.0720 0.5329 0.0474  0.0794  0.0477  386 LEU B O   
4065  C CB  . LEU B 85  ? 0.5311 1.1244 0.5809 -0.0272 0.0790  0.0485  386 LEU B CB  
4066  C CG  . LEU B 85  ? 0.4650 1.0280 0.5140 -0.0491 0.0738  0.0461  386 LEU B CG  
4067  C CD1 . LEU B 85  ? 0.5205 1.1372 0.5841 -0.0690 0.0733  0.0450  386 LEU B CD1 
4068  C CD2 . LEU B 85  ? 0.3546 0.8779 0.3988 -0.0286 0.0652  0.0432  386 LEU B CD2 
4069  N N   . GLU B 86  ? 0.6322 1.2444 0.6689 0.0076  0.0925  0.0534  387 GLU B N   
4070  C CA  . GLU B 86  ? 0.6747 1.3195 0.7102 0.0326  0.0973  0.0542  387 GLU B CA  
4071  C C   . GLU B 86  ? 0.6280 1.2203 0.6453 0.0539  0.0963  0.0528  387 GLU B C   
4072  O O   . GLU B 86  ? 0.5991 1.2012 0.6113 0.0839  0.0964  0.0510  387 GLU B O   
4073  C CB  . GLU B 86  ? 0.8674 1.5606 0.9088 0.0139  0.1075  0.0587  387 GLU B CB  
4074  C CG  . GLU B 86  ? 1.1041 1.8725 1.1641 0.0105  0.1083  0.0592  387 GLU B CG  
4075  C CD  . GLU B 86  ? 1.2806 2.0607 1.3500 -0.0274 0.1064  0.0596  387 GLU B CD  
4076  O OE1 . GLU B 86  ? 1.3371 2.1093 1.4022 -0.0561 0.1117  0.0626  387 GLU B OE1 
4077  O OE2 . GLU B 86  ? 1.3148 2.1091 1.3938 -0.0283 0.0996  0.0567  387 GLU B OE2 
4078  N N   . GLU B 87  ? 0.5743 1.1107 0.5802 0.0396  0.0954  0.0534  388 GLU B N   
4079  C CA  . GLU B 87  ? 0.6545 1.1418 0.6430 0.0574  0.0937  0.0517  388 GLU B CA  
4080  C C   . GLU B 87  ? 0.6538 1.1117 0.6377 0.0805  0.0847  0.0468  388 GLU B C   
4081  O O   . GLU B 87  ? 0.4462 0.8911 0.4188 0.1062  0.0836  0.0441  388 GLU B O   
4082  C CB  . GLU B 87  ? 0.6630 1.1025 0.6412 0.0362  0.0946  0.0540  388 GLU B CB  
4083  C CG  . GLU B 87  ? 0.6690 1.0762 0.6301 0.0483  0.0966  0.0541  388 GLU B CG  
4084  C CD  . GLU B 87  ? 0.7229 1.0763 0.6727 0.0338  0.0946  0.0556  388 GLU B CD  
4085  O OE1 . GLU B 87  ? 0.7561 1.0940 0.7103 0.0155  0.0918  0.0562  388 GLU B OE1 
4086  O OE2 . GLU B 87  ? 0.7665 1.0934 0.7021 0.0419  0.0957  0.0560  388 GLU B OE2 
4087  N N   . VAL B 88  ? 0.6480 1.0939 0.6388 0.0712  0.0783  0.0457  389 VAL B N   
4088  C CA  . VAL B 88  ? 0.6330 1.0533 0.6195 0.0911  0.0701  0.0420  389 VAL B CA  
4089  C C   . VAL B 88  ? 0.6669 1.1278 0.6572 0.1167  0.0699  0.0409  389 VAL B C   
4090  O O   . VAL B 88  ? 0.6513 1.0900 0.6296 0.1425  0.0664  0.0382  389 VAL B O   
4091  C CB  . VAL B 88  ? 0.5595 0.9621 0.5527 0.0742  0.0641  0.0415  389 VAL B CB  
4092  C CG1 . VAL B 88  ? 0.5413 0.9205 0.5297 0.0942  0.0560  0.0386  389 VAL B CG1 
4093  C CG2 . VAL B 88  ? 0.4942 0.8537 0.4807 0.0529  0.0644  0.0425  389 VAL B CG2 
4094  N N   . ASN B 89  ? 0.6396 1.1603 0.6453 0.1102  0.0738  0.0431  390 ASN B N   
4095  C CA  . ASN B 89  ? 0.7138 1.2799 0.7239 0.1362  0.0740  0.0427  390 ASN B CA  
4096  C C   . ASN B 89  ? 0.7343 1.2947 0.7295 0.1642  0.0777  0.0412  390 ASN B C   
4097  O O   . ASN B 89  ? 0.7541 1.2976 0.7375 0.1930  0.0739  0.0386  390 ASN B O   
4098  C CB  . ASN B 89  ? 0.7452 1.3831 0.7748 0.1214  0.0788  0.0455  390 ASN B CB  
4099  C CG  . ASN B 89  ? 0.8829 1.5690 0.9209 0.1441  0.0761  0.0452  390 ASN B CG  
4100  O OD1 . ASN B 89  ? 0.8949 1.5964 0.9257 0.1752  0.0779  0.0446  390 ASN B OD1 
4101  N ND2 . ASN B 89  ? 0.9718 1.6821 1.0236 0.1296  0.0717  0.0456  390 ASN B ND2 
4102  N N   . LYS B 90  ? 0.6480 1.2189 0.6409 0.1559  0.0854  0.0428  391 LYS B N   
4103  C CA  . LYS B 90  ? 0.6500 1.2185 0.6279 0.1818  0.0895  0.0410  391 LYS B CA  
4104  C C   . LYS B 90  ? 0.5984 1.0972 0.5547 0.1958  0.0840  0.0367  391 LYS B C   
4105  O O   . LYS B 90  ? 0.6803 1.1681 0.6208 0.2247  0.0840  0.0332  391 LYS B O   
4106  C CB  . LYS B 90  ? 0.7445 1.3366 0.7241 0.1664  0.0989  0.0443  391 LYS B CB  
4107  C CG  . LYS B 90  ? 0.8226 1.3746 0.7818 0.1768  0.1012  0.0423  391 LYS B CG  
4108  C CD  . LYS B 90  ? 0.9445 1.5017 0.9051 0.1505  0.1086  0.0469  391 LYS B CD  
4109  C CE  . LYS B 90  ? 0.8990 1.4194 0.8390 0.1605  0.1108  0.0452  391 LYS B CE  
4110  N NZ  . LYS B 90  ? 0.8342 1.3957 0.7695 0.1792  0.1190  0.0453  391 LYS B NZ  
4111  N N   . GLU B 91  ? 0.4049 0.8569 0.3592 0.1756  0.0793  0.0366  392 GLU B N   
4112  C CA  . GLU B 91  ? 0.5394 0.9284 0.4746 0.1849  0.0737  0.0326  392 GLU B CA  
4113  C C   . GLU B 91  ? 0.8019 1.1718 0.7291 0.2076  0.0669  0.0294  392 GLU B C   
4114  O O   . GLU B 91  ? 0.7150 1.0528 0.6222 0.2292  0.0650  0.0253  392 GLU B O   
4115  C CB  . GLU B 91  ? 0.4022 0.7533 0.3394 0.1581  0.0704  0.0338  392 GLU B CB  
4116  C CG  . GLU B 91  ? 0.7678 1.0614 0.6861 0.1631  0.0662  0.0303  392 GLU B CG  
4117  C CD  . GLU B 91  ? 0.7925 1.0594 0.7115 0.1385  0.0659  0.0325  392 GLU B CD  
4118  O OE1 . GLU B 91  ? 0.8616 1.0864 0.7666 0.1410  0.0622  0.0299  392 GLU B OE1 
4119  O OE2 . GLU B 91  ? 0.6364 0.9240 0.5684 0.1170  0.0693  0.0368  392 GLU B OE2 
4120  N N   . ILE B 92  ? 0.8883 1.2752 0.8289 0.2023  0.0630  0.0312  393 ILE B N   
4121  C CA  . ILE B 92  ? 0.8057 1.1786 0.7384 0.2244  0.0571  0.0295  393 ILE B CA  
4122  C C   . ILE B 92  ? 0.8264 1.2262 0.7497 0.2570  0.0606  0.0283  393 ILE B C   
4123  O O   . ILE B 92  ? 0.8820 1.2486 0.7854 0.2815  0.0572  0.0253  393 ILE B O   
4124  C CB  . ILE B 92  ? 0.8655 1.2608 0.8155 0.2122  0.0531  0.0323  393 ILE B CB  
4125  C CG1 . ILE B 92  ? 0.7589 1.1175 0.7131 0.1847  0.0488  0.0326  393 ILE B CG1 
4126  C CG2 . ILE B 92  ? 0.9215 1.3123 0.8631 0.2383  0.0481  0.0318  393 ILE B CG2 
4127  C CD1 . ILE B 92  ? 0.6533 1.0425 0.6271 0.1649  0.0471  0.0351  393 ILE B CD1 
4128  N N   . ASP B 93  ? 0.9434 1.4033 0.8796 0.2576  0.0677  0.0306  394 ASP B N   
4129  C CA  . ASP B 93  ? 0.9726 1.4653 0.9007 0.2896  0.0723  0.0295  394 ASP B CA  
4130  C C   . ASP B 93  ? 1.0142 1.4619 0.9153 0.3097  0.0735  0.0246  394 ASP B C   
4131  O O   . ASP B 93  ? 1.1407 1.5831 1.0242 0.3424  0.0736  0.0219  394 ASP B O   
4132  C CB  . ASP B 93  ? 0.9622 1.5261 0.9089 0.2809  0.0808  0.0329  394 ASP B CB  
4133  C CG  . ASP B 93  ? 1.0433 1.6683 1.0126 0.2755  0.0803  0.0366  394 ASP B CG  
4134  O OD1 . ASP B 93  ? 1.0756 1.7008 1.0399 0.2956  0.0738  0.0367  394 ASP B OD1 
4135  O OD2 . ASP B 93  ? 1.0915 1.7568 1.0803 0.2474  0.0840  0.0398  394 ASP B OD2 
4136  N N   . THR B 94  ? 0.8221 1.2374 0.7180 0.2912  0.0745  0.0233  395 THR B N   
4137  C CA  . THR B 94  ? 0.8501 1.2332 0.7223 0.3068  0.0767  0.0185  395 THR B CA  
4138  C C   . THR B 94  ? 0.9182 1.2272 0.7695 0.3055  0.0694  0.0138  395 THR B C   
4139  O O   . THR B 94  ? 1.0845 1.3607 0.9106 0.3259  0.0692  0.0083  395 THR B O   
4140  C CB  . THR B 94  ? 0.8203 1.2270 0.6995 0.2896  0.0841  0.0205  395 THR B CB  
4141  O OG1 . THR B 94  ? 0.9062 1.2966 0.7976 0.2559  0.0819  0.0236  395 THR B OG1 
4142  C CG2 . THR B 94  ? 0.6681 1.1501 0.5656 0.2916  0.0920  0.0248  395 THR B CG2 
4143  N N   . THR B 95  ? 0.9033 1.1858 0.7632 0.2823  0.0635  0.0155  396 THR B N   
4144  C CA  . THR B 95  ? 0.9168 1.1346 0.7591 0.2786  0.0565  0.0115  396 THR B CA  
4145  C C   . THR B 95  ? 0.9441 1.1396 0.7879 0.2773  0.0493  0.0126  396 THR B C   
4146  O O   . THR B 95  ? 0.9623 1.1070 0.7937 0.2707  0.0433  0.0100  396 THR B O   
4147  C CB  . THR B 95  ? 1.0014 1.2011 0.8492 0.2509  0.0560  0.0123  396 THR B CB  
4148  O OG1 . THR B 95  ? 1.0782 1.2969 0.9493 0.2267  0.0551  0.0175  396 THR B OG1 
4149  C CG2 . THR B 95  ? 0.9988 1.2207 0.8448 0.2505  0.0635  0.0123  396 THR B CG2 
4150  N N   . SER B 96  ? 0.8434 1.0778 0.7022 0.2822  0.0496  0.0165  397 SER B N   
4151  C CA  . SER B 96  ? 0.8947 1.1136 0.7549 0.2828  0.0432  0.0182  397 SER B CA  
4152  C C   . SER B 96  ? 0.7880 0.9864 0.6604 0.2528  0.0387  0.0200  397 SER B C   
4153  O O   . SER B 96  ? 0.7562 0.9303 0.6260 0.2510  0.0329  0.0208  397 SER B O   
4154  C CB  . SER B 96  ? 1.0946 1.2632 0.9254 0.3068  0.0391  0.0146  397 SER B CB  
4155  O OG  . SER B 96  ? 1.1853 1.3740 1.0037 0.3388  0.0429  0.0135  397 SER B OG  
4156  N N   . THR B 97  ? 0.8009 1.0086 0.6853 0.2300  0.0415  0.0209  398 THR B N   
4157  C CA  . THR B 97  ? 0.7807 0.9681 0.6748 0.2032  0.0379  0.0223  398 THR B CA  
4158  C C   . THR B 97  ? 0.7038 0.9234 0.6148 0.1820  0.0434  0.0252  398 THR B C   
4159  O O   . THR B 97  ? 0.6608 0.9242 0.5796 0.1863  0.0494  0.0268  398 THR B O   
4160  C CB  . THR B 97  ? 0.8248 0.9556 0.7006 0.2009  0.0334  0.0186  398 THR B CB  
4161  O OG1 . THR B 97  ? 0.7974 0.9111 0.6825 0.1776  0.0298  0.0201  398 THR B OG1 
4162  C CG2 . THR B 97  ? 0.9170 1.0411 0.7820 0.2037  0.0373  0.0157  398 THR B CG2 
4163  N N   . TYR B 98  ? 0.6217 0.8201 0.5375 0.1594  0.0416  0.0261  399 TYR B N   
4164  C CA  . TYR B 98  ? 0.5570 0.7722 0.4820 0.1398  0.0470  0.0289  399 TYR B CA  
4165  C C   . TYR B 98  ? 0.5481 0.7231 0.4686 0.1238  0.0438  0.0287  399 TYR B C   
4166  O O   . TYR B 98  ? 0.6726 0.8133 0.5859 0.1261  0.0376  0.0264  399 TYR B O   
4167  C CB  . TYR B 98  ? 0.5641 0.8229 0.5084 0.1254  0.0500  0.0325  399 TYR B CB  
4168  C CG  . TYR B 98  ? 0.5809 0.8294 0.5344 0.1097  0.0451  0.0333  399 TYR B CG  
4169  C CD1 . TYR B 98  ? 0.5262 0.7612 0.4838 0.0861  0.0459  0.0349  399 TYR B CD1 
4170  C CD2 . TYR B 98  ? 0.5451 0.7974 0.5014 0.1195  0.0400  0.0325  399 TYR B CD2 
4171  C CE1 . TYR B 98  ? 0.4930 0.7184 0.4572 0.0731  0.0417  0.0350  399 TYR B CE1 
4172  C CE2 . TYR B 98  ? 0.5383 0.7822 0.5018 0.1059  0.0357  0.0331  399 TYR B CE2 
4173  C CZ  . TYR B 98  ? 0.5936 0.8249 0.5615 0.0827  0.0366  0.0340  399 TYR B CZ  
4174  O OH  . TYR B 98  ? 0.6959 0.9190 0.6697 0.0703  0.0325  0.0339  399 TYR B OH  
4175  N N   . GLN B 99  ? 0.5603 0.7408 0.4840 0.1078  0.0485  0.0314  400 GLN B N   
4176  C CA  . GLN B 99  ? 0.5531 0.6991 0.4697 0.0967  0.0468  0.0317  400 GLN B CA  
4177  C C   . GLN B 99  ? 0.5828 0.7340 0.5092 0.0741  0.0493  0.0357  400 GLN B C   
4178  O O   . GLN B 99  ? 0.5866 0.7678 0.5204 0.0647  0.0554  0.0388  400 GLN B O   
4179  C CB  . GLN B 99  ? 0.5366 0.6759 0.4403 0.1031  0.0505  0.0312  400 GLN B CB  
4180  C CG  . GLN B 99  ? 0.6019 0.7314 0.4921 0.1251  0.0483  0.0262  400 GLN B CG  
4181  C CD  . GLN B 99  ? 0.6967 0.7872 0.5779 0.1287  0.0402  0.0223  400 GLN B CD  
4182  O OE1 . GLN B 99  ? 0.7512 0.8198 0.6330 0.1159  0.0368  0.0231  400 GLN B OE1 
4183  N NE2 . GLN B 99  ? 0.7820 0.8636 0.6537 0.1461  0.0372  0.0183  400 GLN B NE2 
4184  N N   . LEU B 100 ? 0.5632 0.6845 0.4881 0.0652  0.0448  0.0355  401 LEU B N   
4185  C CA  . LEU B 100 ? 0.6164 0.7362 0.5477 0.0457  0.0463  0.0384  401 LEU B CA  
4186  C C   . LEU B 100 ? 0.5673 0.6761 0.4904 0.0365  0.0513  0.0419  401 LEU B C   
4187  O O   . LEU B 100 ? 0.5344 0.6198 0.4467 0.0428  0.0495  0.0414  401 LEU B O   
4188  C CB  . LEU B 100 ? 0.5433 0.6368 0.4754 0.0423  0.0397  0.0367  401 LEU B CB  
4189  C CG  . LEU B 100 ? 0.4798 0.5823 0.4193 0.0489  0.0349  0.0344  401 LEU B CG  
4190  C CD1 . LEU B 100 ? 0.5359 0.6103 0.4735 0.0471  0.0287  0.0330  401 LEU B CD1 
4191  C CD2 . LEU B 100 ? 0.3662 0.4992 0.3178 0.0383  0.0375  0.0358  401 LEU B CD2 
4192  N N   . LYS B 101 ? 0.5094 0.6347 0.4361 0.0212  0.0575  0.0456  402 LYS B N   
4193  C CA  . LYS B 101 ? 0.5059 0.6120 0.4225 0.0097  0.0619  0.0498  402 LYS B CA  
4194  C C   . LYS B 101 ? 0.5515 0.6206 0.4619 0.0083  0.0567  0.0492  402 LYS B C   
4195  O O   . LYS B 101 ? 0.6689 0.7317 0.5857 0.0093  0.0511  0.0461  402 LYS B O   
4196  C CB  . LYS B 101 ? 0.4695 0.5920 0.3894 -0.0107 0.0686  0.0536  402 LYS B CB  
4197  C CG  . LYS B 101 ? 0.5667 0.7275 0.4905 -0.0120 0.0755  0.0559  402 LYS B CG  
4198  C CD  . LYS B 101 ? 0.5838 0.7469 0.5001 0.0064  0.0766  0.0556  402 LYS B CD  
4199  C CE  . LYS B 101 ? 0.6580 0.8598 0.5766 0.0045  0.0847  0.0586  402 LYS B CE  
4200  N NZ  . LYS B 101 ? 0.6937 0.9121 0.6115 0.0278  0.0838  0.0552  402 LYS B NZ  
4201  N N   . ASP B 102 ? 0.5863 0.6329 0.4839 0.0067  0.0588  0.0525  403 ASP B N   
4202  C CA  . ASP B 102 ? 0.5784 0.5937 0.4696 0.0071  0.0544  0.0524  403 ASP B CA  
4203  C C   . ASP B 102 ? 0.5741 0.5806 0.4685 -0.0065 0.0546  0.0527  403 ASP B C   
4204  O O   . ASP B 102 ? 0.6202 0.6107 0.5158 -0.0041 0.0493  0.0504  403 ASP B O   
4205  C CB  . ASP B 102 ? 0.6899 0.6860 0.5655 0.0084  0.0575  0.0569  403 ASP B CB  
4206  C CG  . ASP B 102 ? 0.8291 0.8276 0.6994 0.0231  0.0553  0.0553  403 ASP B CG  
4207  O OD1 . ASP B 102 ? 0.7828 0.7943 0.6601 0.0322  0.0515  0.0504  403 ASP B OD1 
4208  O OD2 . ASP B 102 ? 0.9271 0.9129 0.7842 0.0258  0.0574  0.0590  403 ASP B OD2 
4209  N N   . THR B 103 ? 0.6384 0.6538 0.5323 -0.0217 0.0609  0.0555  404 THR B N   
4210  C CA  . THR B 103 ? 0.7083 0.7149 0.6034 -0.0362 0.0612  0.0548  404 THR B CA  
4211  C C   . THR B 103 ? 0.6591 0.6843 0.5697 -0.0342 0.0556  0.0496  404 THR B C   
4212  O O   . THR B 103 ? 0.5067 0.5169 0.4183 -0.0352 0.0514  0.0471  404 THR B O   
4213  C CB  . THR B 103 ? 0.7073 0.7214 0.5975 -0.0553 0.0693  0.0585  404 THR B CB  
4214  O OG1 . THR B 103 ? 0.6675 0.7184 0.5662 -0.0549 0.0727  0.0593  404 THR B OG1 
4215  C CG2 . THR B 103 ? 0.6896 0.6718 0.5596 -0.0595 0.0744  0.0641  404 THR B CG2 
4216  N N   . GLU B 104 ? 0.6773 0.7355 0.5989 -0.0296 0.0557  0.0483  405 GLU B N   
4217  C CA  . GLU B 104 ? 0.6195 0.6958 0.5541 -0.0237 0.0502  0.0441  405 GLU B CA  
4218  C C   . GLU B 104 ? 0.6924 0.7461 0.6258 -0.0116 0.0430  0.0416  405 GLU B C   
4219  O O   . GLU B 104 ? 0.8442 0.8929 0.7821 -0.0146 0.0391  0.0393  405 GLU B O   
4220  C CB  . GLU B 104 ? 0.6212 0.7323 0.5637 -0.0139 0.0514  0.0437  405 GLU B CB  
4221  C CG  . GLU B 104 ? 0.5045 0.6491 0.4527 -0.0282 0.0579  0.0458  405 GLU B CG  
4222  C CD  . GLU B 104 ? 0.5455 0.7241 0.4984 -0.0170 0.0610  0.0465  405 GLU B CD  
4223  O OE1 . GLU B 104 ? 0.6635 0.8717 0.6202 -0.0284 0.0673  0.0489  405 GLU B OE1 
4224  O OE2 . GLU B 104 ? 0.6969 0.8726 0.6483 0.0028  0.0576  0.0445  405 GLU B OE2 
4225  N N   . LEU B 105 ? 0.7003 0.7404 0.6267 0.0008  0.0414  0.0418  406 LEU B N   
4226  C CA  . LEU B 105 ? 0.5705 0.5928 0.4959 0.0107  0.0346  0.0393  406 LEU B CA  
4227  C C   . LEU B 105 ? 0.6330 0.6323 0.5547 0.0041  0.0329  0.0397  406 LEU B C   
4228  O O   . LEU B 105 ? 0.6370 0.6295 0.5621 0.0072  0.0276  0.0374  406 LEU B O   
4229  C CB  . LEU B 105 ? 0.5875 0.6008 0.5047 0.0229  0.0332  0.0390  406 LEU B CB  
4230  C CG  . LEU B 105 ? 0.5678 0.5635 0.4820 0.0313  0.0263  0.0363  406 LEU B CG  
4231  C CD1 . LEU B 105 ? 0.5839 0.5870 0.5011 0.0412  0.0223  0.0329  406 LEU B CD1 
4232  C CD2 . LEU B 105 ? 0.3852 0.3664 0.2881 0.0364  0.0259  0.0370  406 LEU B CD2 
4233  N N   . ILE B 106 ? 0.5336 0.5194 0.4465 -0.0042 0.0375  0.0427  407 ILE B N   
4234  C CA  . ILE B 106 ? 0.5673 0.5302 0.4746 -0.0076 0.0361  0.0428  407 ILE B CA  
4235  C C   . ILE B 106 ? 0.7156 0.6832 0.6291 -0.0179 0.0358  0.0405  407 ILE B C   
4236  O O   . ILE B 106 ? 0.7010 0.6588 0.6156 -0.0166 0.0320  0.0385  407 ILE B O   
4237  C CB  . ILE B 106 ? 0.5311 0.4732 0.4234 -0.0111 0.0412  0.0471  407 ILE B CB  
4238  C CG1 . ILE B 106 ? 0.4550 0.3925 0.3406 0.0007  0.0403  0.0491  407 ILE B CG1 
4239  C CG2 . ILE B 106 ? 0.5818 0.5004 0.4667 -0.0138 0.0406  0.0470  407 ILE B CG2 
4240  C CD1 . ILE B 106 ? 0.4724 0.4025 0.3452 -0.0029 0.0470  0.0542  407 ILE B CD1 
4241  N N   . TYR B 107 ? 0.6798 0.6650 0.5973 -0.0288 0.0397  0.0407  408 TYR B N   
4242  C CA  . TYR B 107 ? 0.7096 0.7037 0.6330 -0.0399 0.0390  0.0379  408 TYR B CA  
4243  C C   . TYR B 107 ? 0.6717 0.6781 0.6064 -0.0313 0.0325  0.0347  408 TYR B C   
4244  O O   . TYR B 107 ? 0.5942 0.5912 0.5292 -0.0333 0.0295  0.0325  408 TYR B O   
4245  C CB  . TYR B 107 ? 0.6977 0.7171 0.6253 -0.0525 0.0439  0.0386  408 TYR B CB  
4246  C CG  . TYR B 107 ? 0.7711 0.8086 0.7071 -0.0634 0.0423  0.0352  408 TYR B CG  
4247  C CD1 . TYR B 107 ? 0.8458 0.8660 0.7735 -0.0788 0.0439  0.0334  408 TYR B CD1 
4248  C CD2 . TYR B 107 ? 0.7403 0.8112 0.6905 -0.0574 0.0389  0.0335  408 TYR B CD2 
4249  C CE1 . TYR B 107 ? 0.8044 0.8424 0.7389 -0.0897 0.0420  0.0295  408 TYR B CE1 
4250  C CE2 . TYR B 107 ? 0.6257 0.7165 0.5835 -0.0669 0.0369  0.0304  408 TYR B CE2 
4251  C CZ  . TYR B 107 ? 0.7647 0.8399 0.7151 -0.0839 0.0383  0.0282  408 TYR B CZ  
4252  O OH  . TYR B 107 ? 0.9087 1.0043 0.8656 -0.0942 0.0359  0.0245  408 TYR B OH  
4253  N N   . GLY B 108 ? 0.6174 0.6427 0.5594 -0.0207 0.0304  0.0347  409 GLY B N   
4254  C CA  . GLY B 108 ? 0.5420 0.5758 0.4917 -0.0121 0.0246  0.0325  409 GLY B CA  
4255  C C   . GLY B 108 ? 0.6402 0.6511 0.5860 -0.0057 0.0200  0.0318  409 GLY B C   
4256  O O   . GLY B 108 ? 0.8170 0.8282 0.7668 -0.0054 0.0162  0.0303  409 GLY B O   
4257  N N   . ALA B 109 ? 0.5931 0.5866 0.5312 -0.0006 0.0204  0.0332  410 ALA B N   
4258  C CA  . ALA B 109 ? 0.5921 0.5689 0.5274 0.0045  0.0160  0.0326  410 ALA B CA  
4259  C C   . ALA B 109 ? 0.5510 0.5179 0.4849 -0.0025 0.0162  0.0319  410 ALA B C   
4260  O O   . ALA B 109 ? 0.6050 0.5696 0.5418 -0.0006 0.0123  0.0306  410 ALA B O   
4261  C CB  . ALA B 109 ? 0.4695 0.4335 0.3966 0.0104  0.0164  0.0340  410 ALA B CB  
4262  N N   . LYS B 110 ? 0.5808 0.5402 0.5086 -0.0109 0.0210  0.0326  411 LYS B N   
4263  C CA  . LYS B 110 ? 0.5521 0.4982 0.4752 -0.0167 0.0216  0.0313  411 LYS B CA  
4264  C C   . LYS B 110 ? 0.6253 0.5854 0.5564 -0.0228 0.0195  0.0283  411 LYS B C   
4265  O O   . LYS B 110 ? 0.6949 0.6488 0.6253 -0.0229 0.0174  0.0265  411 LYS B O   
4266  C CB  . LYS B 110 ? 0.5703 0.5004 0.4811 -0.0250 0.0276  0.0328  411 LYS B CB  
4267  C CG  . LYS B 110 ? 0.5481 0.4551 0.4465 -0.0176 0.0290  0.0354  411 LYS B CG  
4268  C CD  . LYS B 110 ? 0.5804 0.4755 0.4668 -0.0217 0.0349  0.0390  411 LYS B CD  
4269  C CE  . LYS B 110 ? 0.6114 0.4830 0.4835 -0.0120 0.0359  0.0421  411 LYS B CE  
4270  N NZ  . LYS B 110 ? 0.5449 0.3979 0.4006 -0.0170 0.0425  0.0464  411 LYS B NZ  
4271  N N   . HIS B 111 ? 0.6119 0.5937 0.5505 -0.0268 0.0201  0.0280  412 HIS B N   
4272  C CA  . HIS B 111 ? 0.6400 0.6383 0.5857 -0.0327 0.0180  0.0253  412 HIS B CA  
4273  C C   . HIS B 111 ? 0.7700 0.7767 0.7229 -0.0226 0.0123  0.0252  412 HIS B C   
4274  O O   . HIS B 111 ? 0.7537 0.7671 0.7097 -0.0254 0.0098  0.0233  412 HIS B O   
4275  C CB  . HIS B 111 ? 0.5505 0.5733 0.5016 -0.0409 0.0207  0.0252  412 HIS B CB  
4276  C CG  . HIS B 111 ? 0.5955 0.6112 0.5390 -0.0574 0.0255  0.0240  412 HIS B CG  
4277  N ND1 . HIS B 111 ? 0.6963 0.6838 0.6265 -0.0605 0.0297  0.0256  412 HIS B ND1 
4278  C CD2 . HIS B 111 ? 0.6893 0.7203 0.6346 -0.0724 0.0268  0.0214  412 HIS B CD2 
4279  C CE1 . HIS B 111 ? 0.7271 0.7087 0.6494 -0.0770 0.0337  0.0241  412 HIS B CE1 
4280  N NE2 . HIS B 111 ? 0.7189 0.7276 0.6506 -0.0856 0.0320  0.0212  412 HIS B NE2 
4281  N N   . ALA B 112 ? 0.6311 0.6357 0.5846 -0.0115 0.0103  0.0271  413 ALA B N   
4282  C CA  . ALA B 112 ? 0.5970 0.6022 0.5533 -0.0037 0.0053  0.0273  413 ALA B CA  
4283  C C   . ALA B 112 ? 0.6171 0.6072 0.5702 -0.0049 0.0036  0.0268  413 ALA B C   
4284  O O   . ALA B 112 ? 0.5774 0.5712 0.5330 -0.0045 0.0006  0.0264  413 ALA B O   
4285  C CB  . ALA B 112 ? 0.6075 0.6092 0.5619 0.0067  0.0037  0.0288  413 ALA B CB  
4286  N N   . TRP B 113 ? 0.5249 0.4994 0.4717 -0.0054 0.0057  0.0270  414 TRP B N   
4287  C CA  . TRP B 113 ? 0.5594 0.5231 0.5028 -0.0056 0.0049  0.0263  414 TRP B CA  
4288  C C   . TRP B 113 ? 0.6140 0.5787 0.5563 -0.0133 0.0063  0.0237  414 TRP B C   
4289  O O   . TRP B 113 ? 0.6465 0.6119 0.5895 -0.0129 0.0042  0.0227  414 TRP B O   
4290  C CB  . TRP B 113 ? 0.4354 0.3838 0.3708 -0.0027 0.0073  0.0275  414 TRP B CB  
4291  C CG  . TRP B 113 ? 0.5513 0.4912 0.4826 0.0002  0.0067  0.0270  414 TRP B CG  
4292  C CD1 . TRP B 113 ? 0.5408 0.4860 0.4754 0.0001  0.0043  0.0259  414 TRP B CD1 
4293  C CD2 . TRP B 113 ? 0.5730 0.4996 0.4953 0.0051  0.0089  0.0281  414 TRP B CD2 
4294  N NE1 . TRP B 113 ? 0.5368 0.4747 0.4658 0.0046  0.0051  0.0258  414 TRP B NE1 
4295  C CE2 . TRP B 113 ? 0.5909 0.5173 0.5122 0.0086  0.0077  0.0272  414 TRP B CE2 
4296  C CE3 . TRP B 113 ? 0.6719 0.5877 0.5861 0.0081  0.0119  0.0301  414 TRP B CE3 
4297  C CZ2 . TRP B 113 ? 0.7195 0.6366 0.6322 0.0162  0.0093  0.0281  414 TRP B CZ2 
4298  C CZ3 . TRP B 113 ? 0.6101 0.5142 0.5147 0.0154  0.0133  0.0314  414 TRP B CZ3 
4299  C CH2 . TRP B 113 ? 0.7182 0.6238 0.6224 0.0201  0.0119  0.0303  414 TRP B CH2 
4300  N N   . ARG B 114 ? 0.5962 0.5612 0.5357 -0.0214 0.0099  0.0224  415 ARG B N   
4301  C CA  . ARG B 114 ? 0.5120 0.4753 0.4477 -0.0309 0.0113  0.0190  415 ARG B CA  
4302  C C   . ARG B 114 ? 0.6750 0.6588 0.6191 -0.0329 0.0077  0.0174  415 ARG B C   
4303  O O   . ARG B 114 ? 0.8223 0.8051 0.7634 -0.0383 0.0073  0.0142  415 ARG B O   
4304  C CB  . ARG B 114 ? 0.4050 0.3644 0.3349 -0.0417 0.0161  0.0182  415 ARG B CB  
4305  C CG  . ARG B 114 ? 0.4058 0.3601 0.3286 -0.0543 0.0179  0.0139  415 ARG B CG  
4306  C CD  . ARG B 114 ? 0.4544 0.4130 0.3741 -0.0685 0.0219  0.0133  415 ARG B CD  
4307  N NE  . ARG B 114 ? 0.5545 0.4966 0.4612 -0.0820 0.0245  0.0088  415 ARG B NE  
4308  C CZ  . ARG B 114 ? 0.6081 0.5491 0.5083 -0.0985 0.0284  0.0074  415 ARG B CZ  
4309  N NH1 . ARG B 114 ? 0.6134 0.5350 0.4988 -0.1117 0.0304  0.0026  415 ARG B NH1 
4310  N NH2 . ARG B 114 ? 0.6423 0.6015 0.5497 -0.1022 0.0304  0.0108  415 ARG B NH2 
4311  N N   . ASN B 115 ? 0.6188 0.6201 0.5717 -0.0277 0.0051  0.0197  416 ASN B N   
4312  C CA  . ASN B 115 ? 0.5029 0.5242 0.4626 -0.0267 0.0015  0.0194  416 ASN B CA  
4313  C C   . ASN B 115 ? 0.5887 0.6062 0.5492 -0.0182 -0.0023 0.0214  416 ASN B C   
4314  O O   . ASN B 115 ? 0.6871 0.7183 0.6511 -0.0154 -0.0054 0.0223  416 ASN B O   
4315  C CB  . ASN B 115 ? 0.4260 0.4677 0.3923 -0.0233 0.0012  0.0212  416 ASN B CB  
4316  C CG  . ASN B 115 ? 0.5702 0.6229 0.5372 -0.0338 0.0051  0.0195  416 ASN B CG  
4317  O OD1 . ASN B 115 ? 0.5729 0.6169 0.5344 -0.0457 0.0075  0.0165  416 ASN B OD1 
4318  N ND2 . ASN B 115 ? 0.6257 0.6969 0.5981 -0.0300 0.0060  0.0213  416 ASN B ND2 
4319  N N   . ALA B 116 ? 0.5255 0.5263 0.4821 -0.0140 -0.0022 0.0227  417 ALA B N   
4320  C CA  . ALA B 116 ? 0.5582 0.5564 0.5152 -0.0080 -0.0056 0.0251  417 ALA B CA  
4321  C C   . ALA B 116 ? 0.6569 0.6570 0.6126 -0.0114 -0.0063 0.0234  417 ALA B C   
4322  O O   . ALA B 116 ? 0.5871 0.5777 0.5383 -0.0131 -0.0044 0.0216  417 ALA B O   
4323  C CB  . ALA B 116 ? 0.3954 0.3801 0.3494 -0.0039 -0.0054 0.0266  417 ALA B CB  
4324  N N   . SER B 117 ? 0.5703 0.5831 0.5284 -0.0110 -0.0089 0.0243  418 SER B N   
4325  C CA  A SER B 117 ? 0.5971 0.6146 0.5535 -0.0146 -0.0096 0.0223  418 SER B CA  
4326  C CA  B SER B 117 ? 0.5948 0.6124 0.5512 -0.0145 -0.0096 0.0224  418 SER B CA  
4327  C C   . SER B 117 ? 0.6389 0.6484 0.5924 -0.0121 -0.0099 0.0239  418 SER B C   
4328  O O   . SER B 117 ? 0.6372 0.6476 0.5874 -0.0145 -0.0092 0.0214  418 SER B O   
4329  C CB  A SER B 117 ? 0.5590 0.5936 0.5180 -0.0132 -0.0128 0.0238  418 SER B CB  
4330  C CB  B SER B 117 ? 0.5591 0.5936 0.5182 -0.0130 -0.0128 0.0240  418 SER B CB  
4331  O OG  A SER B 117 ? 0.5330 0.5656 0.4918 -0.0055 -0.0153 0.0291  418 SER B OG  
4332  O OG  B SER B 117 ? 0.5049 0.5541 0.4671 -0.0172 -0.0124 0.0214  418 SER B OG  
4333  N N   . ARG B 118 ? 0.4709 0.4738 0.4248 -0.0079 -0.0109 0.0275  419 ARG B N   
4334  C CA  . ARG B 118 ? 0.3660 0.3665 0.3182 -0.0071 -0.0114 0.0294  419 ARG B CA  
4335  C C   . ARG B 118 ? 0.5231 0.5169 0.4736 -0.0060 -0.0088 0.0277  419 ARG B C   
4336  O O   . ARG B 118 ? 0.5842 0.5809 0.5340 -0.0050 -0.0088 0.0288  419 ARG B O   
4337  C CB  . ARG B 118 ? 0.4097 0.4074 0.3616 -0.0053 -0.0141 0.0342  419 ARG B CB  
4338  C CG  . ARG B 118 ? 0.5519 0.5539 0.5027 -0.0034 -0.0165 0.0368  419 ARG B CG  
4339  C CD  . ARG B 118 ? 0.5354 0.5278 0.4812 -0.0015 -0.0189 0.0417  419 ARG B CD  
4340  N NE  . ARG B 118 ? 0.5525 0.5474 0.4940 0.0010  -0.0209 0.0454  419 ARG B NE  
4341  C CZ  . ARG B 118 ? 0.6706 0.6536 0.6041 0.0043  -0.0229 0.0500  419 ARG B CZ  
4342  N NH1 . ARG B 118 ? 0.6871 0.6549 0.6164 0.0041  -0.0233 0.0505  419 ARG B NH1 
4343  N NH2 . ARG B 118 ? 0.6635 0.6481 0.5913 0.0082  -0.0245 0.0540  419 ARG B NH2 
4344  N N   . CYS B 119 ? 0.4977 0.4839 0.4466 -0.0057 -0.0065 0.0253  420 CYS B N   
4345  C CA  . CYS B 119 ? 0.5250 0.5034 0.4706 -0.0022 -0.0044 0.0248  420 CYS B CA  
4346  C C   . CYS B 119 ? 0.4562 0.4291 0.3950 -0.0015 -0.0012 0.0211  420 CYS B C   
4347  O O   . CYS B 119 ? 0.4079 0.3727 0.3418 -0.0052 0.0011  0.0178  420 CYS B O   
4348  C CB  . CYS B 119 ? 0.5909 0.5613 0.5358 -0.0011 -0.0033 0.0250  420 CYS B CB  
4349  S SG  . CYS B 119 ? 0.6209 0.5813 0.5594 0.0051  -0.0006 0.0251  420 CYS B SG  
4350  N N   . VAL B 120 ? 0.4489 0.4255 0.3858 0.0030  -0.0007 0.0214  421 VAL B N   
4351  C CA  . VAL B 120 ? 0.4664 0.4353 0.3940 0.0069  0.0028  0.0178  421 VAL B CA  
4352  C C   . VAL B 120 ? 0.5944 0.5462 0.5134 0.0117  0.0059  0.0169  421 VAL B C   
4353  O O   . VAL B 120 ? 0.6208 0.5574 0.5277 0.0137  0.0094  0.0132  421 VAL B O   
4354  C CB  . VAL B 120 ? 0.5326 0.5144 0.4609 0.0123  0.0027  0.0189  421 VAL B CB  
4355  C CG1 . VAL B 120 ? 0.4872 0.4762 0.4191 0.0180  0.0020  0.0224  421 VAL B CG1 
4356  C CG2 . VAL B 120 ? 0.5007 0.4747 0.4174 0.0176  0.0064  0.0143  421 VAL B CG2 
4357  N N   . GLY B 121 ? 0.6147 0.5661 0.5373 0.0135  0.0050  0.0200  422 GLY B N   
4358  C CA  . GLY B 121 ? 0.5405 0.4774 0.4546 0.0195  0.0077  0.0205  422 GLY B CA  
4359  C C   . GLY B 121 ? 0.6392 0.5594 0.5472 0.0139  0.0102  0.0196  422 GLY B C   
4360  O O   . GLY B 121 ? 0.7131 0.6206 0.6135 0.0186  0.0125  0.0212  422 GLY B O   
4361  N N   . ARG B 122 ? 0.5372 0.4583 0.4476 0.0039  0.0100  0.0172  423 ARG B N   
4362  C CA  . ARG B 122 ? 0.5609 0.4729 0.4682 -0.0037 0.0122  0.0168  423 ARG B CA  
4363  C C   . ARG B 122 ? 0.6359 0.5224 0.5259 -0.0058 0.0172  0.0144  423 ARG B C   
4364  O O   . ARG B 122 ? 0.7331 0.6122 0.6195 -0.0143 0.0196  0.0143  423 ARG B O   
4365  C CB  . ARG B 122 ? 0.4186 0.3444 0.3340 -0.0137 0.0103  0.0151  423 ARG B CB  
4366  C CG  . ARG B 122 ? 0.4362 0.3814 0.3651 -0.0120 0.0061  0.0180  423 ARG B CG  
4367  C CD  . ARG B 122 ? 0.5695 0.5291 0.5042 -0.0195 0.0044  0.0162  423 ARG B CD  
4368  N NE  . ARG B 122 ? 0.4829 0.4502 0.4189 -0.0193 0.0022  0.0148  423 ARG B NE  
4369  C CZ  . ARG B 122 ? 0.6427 0.6223 0.5812 -0.0252 0.0006  0.0127  423 ARG B CZ  
4370  N NH1 . ARG B 122 ? 0.4814 0.4696 0.4224 -0.0321 0.0010  0.0114  423 ARG B NH1 
4371  N NH2 . ARG B 122 ? 0.6297 0.6160 0.5682 -0.0241 -0.0014 0.0119  423 ARG B NH2 
4372  N N   . ILE B 123 ? 0.5678 0.4401 0.4457 0.0015  0.0193  0.0126  424 ILE B N   
4373  C CA  . ILE B 123 ? 0.5763 0.4176 0.4334 0.0010  0.0244  0.0108  424 ILE B CA  
4374  C C   . ILE B 123 ? 0.6953 0.5248 0.5470 0.0039  0.0268  0.0155  424 ILE B C   
4375  O O   . ILE B 123 ? 0.6713 0.4762 0.5075 -0.0024 0.0312  0.0152  424 ILE B O   
4376  C CB  . ILE B 123 ? 0.5351 0.3627 0.3782 0.0130  0.0263  0.0085  424 ILE B CB  
4377  C CG1 . ILE B 123 ? 0.6195 0.4084 0.4364 0.0126  0.0320  0.0061  424 ILE B CG1 
4378  C CG2 . ILE B 123 ? 0.6678 0.5071 0.5155 0.0295  0.0249  0.0129  424 ILE B CG2 
4379  C CD1 . ILE B 123 ? 0.7183 0.4937 0.5259 -0.0036 0.0335  -0.0003 424 ILE B CD1 
4380  N N   . GLN B 124 ? 0.7224 0.5690 0.5858 0.0118  0.0239  0.0198  425 GLN B N   
4381  C CA  . GLN B 124 ? 0.7201 0.5590 0.5788 0.0166  0.0255  0.0244  425 GLN B CA  
4382  C C   . GLN B 124 ? 0.8101 0.6597 0.6786 0.0068  0.0249  0.0261  425 GLN B C   
4383  O O   . GLN B 124 ? 0.9520 0.7998 0.8186 0.0111  0.0256  0.0299  425 GLN B O   
4384  C CB  . GLN B 124 ? 0.7713 0.6251 0.6363 0.0305  0.0223  0.0276  425 GLN B CB  
4385  C CG  . GLN B 124 ? 0.8653 0.7211 0.7263 0.0415  0.0219  0.0263  425 GLN B CG  
4386  C CD  . GLN B 124 ? 1.0196 0.8491 0.8588 0.0533  0.0265  0.0275  425 GLN B CD  
4387  O OE1 . GLN B 124 ? 1.0621 0.8713 0.8890 0.0534  0.0297  0.0302  425 GLN B OE1 
4388  N NE2 . GLN B 124 ? 1.1893 1.0184 1.0220 0.0645  0.0271  0.0257  425 GLN B NE2 
4389  N N   . TRP B 125 ? 0.8647 0.7273 0.7431 -0.0048 0.0236  0.0234  426 TRP B N   
4390  C CA  . TRP B 125 ? 0.7289 0.6107 0.6204 -0.0097 0.0217  0.0249  426 TRP B CA  
4391  C C   . TRP B 125 ? 0.7287 0.6009 0.6130 -0.0127 0.0258  0.0280  426 TRP B C   
4392  O O   . TRP B 125 ? 0.6827 0.5672 0.5743 -0.0096 0.0244  0.0305  426 TRP B O   
4393  C CB  . TRP B 125 ? 0.6789 0.5760 0.5794 -0.0206 0.0203  0.0217  426 TRP B CB  
4394  C CG  . TRP B 125 ? 0.6047 0.4901 0.4953 -0.0335 0.0245  0.0193  426 TRP B CG  
4395  C CD1 . TRP B 125 ? 0.6274 0.4951 0.5055 -0.0387 0.0266  0.0154  426 TRP B CD1 
4396  C CD2 . TRP B 125 ? 0.6035 0.4937 0.4943 -0.0442 0.0276  0.0203  426 TRP B CD2 
4397  N NE1 . TRP B 125 ? 0.7456 0.6046 0.6151 -0.0538 0.0305  0.0138  426 TRP B NE1 
4398  C CE2 . TRP B 125 ? 0.6507 0.5253 0.5288 -0.0578 0.0313  0.0171  426 TRP B CE2 
4399  C CE3 . TRP B 125 ? 0.6777 0.5844 0.5772 -0.0439 0.0277  0.0235  426 TRP B CE3 
4400  C CZ2 . TRP B 125 ? 0.5291 0.4066 0.4043 -0.0728 0.0351  0.0173  426 TRP B CZ2 
4401  C CZ3 . TRP B 125 ? 0.6804 0.5918 0.5777 -0.0568 0.0318  0.0239  426 TRP B CZ3 
4402  C CH2 . TRP B 125 ? 0.5047 0.4027 0.3905 -0.0720 0.0354  0.0211  426 TRP B CH2 
4403  N N   . SER B 126 ? 0.6954 0.5444 0.5635 -0.0193 0.0310  0.0279  427 SER B N   
4404  C CA  . SER B 126 ? 0.7396 0.5787 0.5991 -0.0240 0.0355  0.0315  427 SER B CA  
4405  C C   . SER B 126 ? 0.8374 0.6617 0.6863 -0.0108 0.0368  0.0362  427 SER B C   
4406  O O   . SER B 126 ? 0.8096 0.6264 0.6508 -0.0130 0.0405  0.0401  427 SER B O   
4407  C CB  . SER B 126 ? 0.8619 0.6796 0.7059 -0.0388 0.0409  0.0298  427 SER B CB  
4408  O OG  . SER B 126 ? 1.0005 0.7896 0.8272 -0.0339 0.0425  0.0280  427 SER B OG  
4409  N N   . LYS B 127 ? 0.8164 0.6388 0.6644 0.0028  0.0339  0.0362  428 LYS B N   
4410  C CA  . LYS B 127 ? 0.8985 0.7131 0.7379 0.0170  0.0340  0.0406  428 LYS B CA  
4411  C C   . LYS B 127 ? 0.8592 0.7014 0.7156 0.0241  0.0280  0.0409  428 LYS B C   
4412  O O   . LYS B 127 ? 0.9945 0.8459 0.8552 0.0337  0.0243  0.0404  428 LYS B O   
4413  C CB  . LYS B 127 ? 0.9213 0.7154 0.7452 0.0281  0.0354  0.0405  428 LYS B CB  
4414  C CG  . LYS B 127 ? 1.0838 0.8706 0.8967 0.0444  0.0358  0.0455  428 LYS B CG  
4415  C CD  . LYS B 127 ? 1.1264 0.9086 0.9318 0.0597  0.0349  0.0448  428 LYS B CD  
4416  C CE  . LYS B 127 ? 1.1307 0.9207 0.9322 0.0772  0.0331  0.0495  428 LYS B CE  
4417  N NZ  . LYS B 127 ? 1.1273 0.8938 0.9061 0.0941  0.0365  0.0520  428 LYS B NZ  
4418  N N   . LEU B 128 ? 0.6839 0.5400 0.5497 0.0181  0.0273  0.0414  429 LEU B N   
4419  C CA  . LEU B 128 ? 0.5590 0.4367 0.4380 0.0225  0.0220  0.0410  429 LEU B CA  
4420  C C   . LEU B 128 ? 0.7640 0.6408 0.6375 0.0260  0.0234  0.0444  429 LEU B C   
4421  O O   . LEU B 128 ? 0.9431 0.8093 0.8079 0.0208  0.0286  0.0467  429 LEU B O   
4422  C CB  . LEU B 128 ? 0.3861 0.2810 0.2796 0.0145  0.0196  0.0379  429 LEU B CB  
4423  C CG  . LEU B 128 ? 0.3500 0.2619 0.2540 0.0181  0.0144  0.0370  429 LEU B CG  
4424  C CD1 . LEU B 128 ? 0.3420 0.2598 0.2503 0.0235  0.0094  0.0360  429 LEU B CD1 
4425  C CD2 . LEU B 128 ? 0.3534 0.2779 0.2673 0.0118  0.0136  0.0349  429 LEU B CD2 
4426  N N   . GLN B 129 ? 0.6040 0.4923 0.4815 0.0338  0.0189  0.0446  430 GLN B N   
4427  C CA  . GLN B 129 ? 0.5197 0.4087 0.3912 0.0384  0.0194  0.0472  430 GLN B CA  
4428  C C   . GLN B 129 ? 0.6502 0.5554 0.5323 0.0360  0.0159  0.0444  430 GLN B C   
4429  O O   . GLN B 129 ? 0.7445 0.6600 0.6344 0.0376  0.0104  0.0416  430 GLN B O   
4430  C CB  . GLN B 129 ? 0.5876 0.4761 0.4519 0.0501  0.0169  0.0494  430 GLN B CB  
4431  C CG  . GLN B 129 ? 0.6665 0.5562 0.5230 0.0556  0.0170  0.0522  430 GLN B CG  
4432  C CD  . GLN B 129 ? 0.7377 0.6085 0.5792 0.0550  0.0241  0.0571  430 GLN B CD  
4433  O OE1 . GLN B 129 ? 0.7378 0.5900 0.5674 0.0578  0.0278  0.0601  430 GLN B OE1 
4434  N NE2 . GLN B 129 ? 0.8002 0.6743 0.6405 0.0513  0.0265  0.0580  430 GLN B NE2 
4435  N N   . VAL B 130 ? 0.6990 0.6060 0.5800 0.0321  0.0195  0.0451  431 VAL B N   
4436  C CA  . VAL B 130 ? 0.5467 0.4671 0.4351 0.0318  0.0172  0.0423  431 VAL B CA  
4437  C C   . VAL B 130 ? 0.6311 0.5525 0.5118 0.0386  0.0166  0.0433  431 VAL B C   
4438  O O   . VAL B 130 ? 0.6844 0.5999 0.5555 0.0395  0.0213  0.0471  431 VAL B O   
4439  C CB  . VAL B 130 ? 0.4702 0.3972 0.3629 0.0243  0.0218  0.0423  431 VAL B CB  
4440  C CG1 . VAL B 130 ? 0.4416 0.3824 0.3402 0.0274  0.0197  0.0396  431 VAL B CG1 
4441  C CG2 . VAL B 130 ? 0.5712 0.4978 0.4702 0.0170  0.0221  0.0410  431 VAL B CG2 
4442  N N   . PHE B 131 ? 0.5511 0.4787 0.4342 0.0425  0.0109  0.0398  432 PHE B N   
4443  C CA  . PHE B 131 ? 0.5083 0.4377 0.3835 0.0484  0.0092  0.0391  432 PHE B CA  
4444  C C   . PHE B 131 ? 0.6038 0.5389 0.4809 0.0490  0.0092  0.0357  432 PHE B C   
4445  O O   . PHE B 131 ? 0.6348 0.5707 0.5156 0.0489  0.0046  0.0316  432 PHE B O   
4446  C CB  . PHE B 131 ? 0.5702 0.5016 0.4441 0.0515  0.0025  0.0370  432 PHE B CB  
4447  C CG  . PHE B 131 ? 0.6590 0.5884 0.5297 0.0546  0.0025  0.0406  432 PHE B CG  
4448  C CD1 . PHE B 131 ? 0.5760 0.4977 0.4368 0.0586  0.0077  0.0457  432 PHE B CD1 
4449  C CD2 . PHE B 131 ? 0.6604 0.5955 0.5368 0.0541  -0.0022 0.0393  432 PHE B CD2 
4450  C CE1 . PHE B 131 ? 0.5370 0.4542 0.3923 0.0640  0.0081  0.0493  432 PHE B CE1 
4451  C CE2 . PHE B 131 ? 0.6405 0.5758 0.5131 0.0597  -0.0018 0.0426  432 PHE B CE2 
4452  C CZ  . PHE B 131 ? 0.6139 0.5391 0.4754 0.0656  0.0032  0.0475  432 PHE B CZ  
4453  N N   . ASP B 132 ? 0.5591 0.4974 0.4319 0.0500  0.0148  0.0377  433 ASP B N   
4454  C CA  . ASP B 132 ? 0.4756 0.4218 0.3491 0.0531  0.0158  0.0348  433 ASP B CA  
4455  C C   . ASP B 132 ? 0.5712 0.5139 0.4357 0.0600  0.0111  0.0305  433 ASP B C   
4456  O O   . ASP B 132 ? 0.7732 0.7137 0.6284 0.0632  0.0110  0.0316  433 ASP B O   
4457  C CB  . ASP B 132 ? 0.3819 0.3364 0.2531 0.0518  0.0235  0.0385  433 ASP B CB  
4458  C CG  . ASP B 132 ? 0.5229 0.4902 0.3955 0.0567  0.0253  0.0358  433 ASP B CG  
4459  O OD1 . ASP B 132 ? 0.6629 0.6426 0.5367 0.0540  0.0319  0.0389  433 ASP B OD1 
4460  O OD2 . ASP B 132 ? 0.4599 0.4248 0.3314 0.0631  0.0206  0.0308  433 ASP B OD2 
4461  N N   . ALA B 133 ? 0.5294 0.4700 0.3946 0.0624  0.0073  0.0257  434 ALA B N   
4462  C CA  . ALA B 133 ? 0.3940 0.3266 0.2485 0.0669  0.0022  0.0204  434 ALA B CA  
4463  C C   . ALA B 133 ? 0.5759 0.5072 0.4257 0.0740  0.0031  0.0165  434 ALA B C   
4464  O O   . ALA B 133 ? 0.5312 0.4499 0.3723 0.0764  -0.0018 0.0112  434 ALA B O   
4465  C CB  . ALA B 133 ? 0.5245 0.4489 0.3803 0.0616  -0.0049 0.0179  434 ALA B CB  
4466  N N   . ARG B 134 ? 0.4468 0.3910 0.3012 0.0771  0.0094  0.0191  435 ARG B N   
4467  C CA  . ARG B 134 ? 0.5699 0.5171 0.4201 0.0866  0.0110  0.0159  435 ARG B CA  
4468  C C   . ARG B 134 ? 0.6950 0.6376 0.5293 0.0958  0.0114  0.0119  435 ARG B C   
4469  O O   . ARG B 134 ? 0.8958 0.8357 0.7221 0.1061  0.0118  0.0080  435 ARG B O   
4470  C CB  . ARG B 134 ? 0.5858 0.5545 0.4472 0.0863  0.0176  0.0201  435 ARG B CB  
4471  C CG  . ARG B 134 ? 0.5886 0.5606 0.4638 0.0778  0.0164  0.0226  435 ARG B CG  
4472  C CD  . ARG B 134 ? 0.5438 0.5387 0.4297 0.0745  0.0225  0.0263  435 ARG B CD  
4473  N NE  . ARG B 134 ? 0.5459 0.5459 0.4330 0.0656  0.0275  0.0308  435 ARG B NE  
4474  C CZ  . ARG B 134 ? 0.6330 0.6527 0.5264 0.0601  0.0338  0.0342  435 ARG B CZ  
4475  N NH1 . ARG B 134 ? 0.6607 0.7016 0.5617 0.0636  0.0355  0.0334  435 ARG B NH1 
4476  N NH2 . ARG B 134 ? 0.6169 0.6358 0.5080 0.0509  0.0386  0.0387  435 ARG B NH2 
4477  N N   . ASP B 135 ? 0.6447 0.5858 0.4726 0.0935  0.0111  0.0127  436 ASP B N   
4478  C CA  . ASP B 135 ? 0.6738 0.6100 0.4850 0.1017  0.0108  0.0083  436 ASP B CA  
4479  C C   . ASP B 135 ? 0.7324 0.6472 0.5310 0.1017  0.0028  0.0010  436 ASP B C   
4480  O O   . ASP B 135 ? 0.8653 0.7723 0.6474 0.1083  0.0016  -0.0044 436 ASP B O   
4481  C CB  . ASP B 135 ? 0.6349 0.5787 0.4428 0.0995  0.0136  0.0125  436 ASP B CB  
4482  C CG  . ASP B 135 ? 0.7637 0.7004 0.5728 0.0917  0.0081  0.0138  436 ASP B CG  
4483  O OD1 . ASP B 135 ? 0.7856 0.7262 0.5897 0.0916  0.0093  0.0174  436 ASP B OD1 
4484  O OD2 . ASP B 135 ? 0.8187 0.7472 0.6334 0.0863  0.0027  0.0117  436 ASP B OD2 
4485  N N   . CYS B 136 ? 0.6435 0.5487 0.4484 0.0938  -0.0024 0.0005  437 CYS B N   
4486  C CA  . CYS B 136 ? 0.6128 0.4990 0.4064 0.0892  -0.0101 -0.0056 437 CYS B CA  
4487  C C   . CYS B 136 ? 0.6553 0.5214 0.4321 0.0972  -0.0115 -0.0125 437 CYS B C   
4488  O O   . CYS B 136 ? 0.6259 0.4921 0.4048 0.1052  -0.0080 -0.0115 437 CYS B O   
4489  C CB  . CYS B 136 ? 0.5599 0.4443 0.3656 0.0780  -0.0141 -0.0031 437 CYS B CB  
4490  S SG  . CYS B 136 ? 0.7058 0.5751 0.5015 0.0671  -0.0233 -0.0088 437 CYS B SG  
4491  N N   . THR B 137 ? 0.7748 0.6233 0.5329 0.0957  -0.0167 -0.0196 438 THR B N   
4492  C CA  . THR B 137 ? 0.6866 0.5095 0.4232 0.1038  -0.0181 -0.0271 438 THR B CA  
4493  C C   . THR B 137 ? 0.6705 0.4654 0.3921 0.0930  -0.0259 -0.0334 438 THR B C   
4494  O O   . THR B 137 ? 0.7095 0.4770 0.4129 0.0987  -0.0268 -0.0385 438 THR B O   
4495  C CB  . THR B 137 ? 0.7382 0.5615 0.4581 0.1157  -0.0152 -0.0318 438 THR B CB  
4496  O OG1 . THR B 137 ? 0.7273 0.5418 0.4332 0.1082  -0.0210 -0.0376 438 THR B OG1 
4497  C CG2 . THR B 137 ? 0.6061 0.4601 0.3403 0.1219  -0.0077 -0.0249 438 THR B CG2 
4498  N N   . THR B 138 ? 0.7064 0.5068 0.4334 0.0778  -0.0314 -0.0333 439 THR B N   
4499  C CA  . THR B 138 ? 0.5793 0.3559 0.2918 0.0647  -0.0387 -0.0394 439 THR B CA  
4500  C C   . THR B 138 ? 0.7580 0.5461 0.4881 0.0492  -0.0422 -0.0345 439 THR B C   
4501  O O   . THR B 138 ? 0.6838 0.4989 0.4355 0.0483  -0.0400 -0.0275 439 THR B O   
4502  C CB  . THR B 138 ? 0.7540 0.5260 0.4488 0.0595  -0.0437 -0.0471 439 THR B CB  
4503  O OG1 . THR B 138 ? 0.7374 0.5410 0.4480 0.0546  -0.0447 -0.0428 439 THR B OG1 
4504  C CG2 . THR B 138 ? 0.7754 0.5349 0.4499 0.0752  -0.0404 -0.0529 439 THR B CG2 
4505  N N   . ALA B 139 ? 0.7671 0.5324 0.4852 0.0367  -0.0476 -0.0387 440 ALA B N   
4506  C CA  . ALA B 139 ? 0.7608 0.5375 0.4919 0.0197  -0.0518 -0.0355 440 ALA B CA  
4507  C C   . ALA B 139 ? 0.8247 0.6332 0.5680 0.0138  -0.0544 -0.0341 440 ALA B C   
4508  O O   . ALA B 139 ? 0.8643 0.6965 0.6277 0.0087  -0.0543 -0.0280 440 ALA B O   
4509  C CB  . ALA B 139 ? 0.7770 0.5234 0.4879 0.0048  -0.0575 -0.0415 440 ALA B CB  
4510  N N   . HIS B 140 ? 0.8897 0.6993 0.6195 0.0159  -0.0566 -0.0398 441 HIS B N   
4511  C CA  . HIS B 140 ? 0.6673 0.5073 0.4058 0.0125  -0.0595 -0.0385 441 HIS B CA  
4512  C C   . HIS B 140 ? 0.6241 0.4887 0.3822 0.0246  -0.0533 -0.0296 441 HIS B C   
4513  O O   . HIS B 140 ? 0.7204 0.6091 0.4943 0.0209  -0.0542 -0.0242 441 HIS B O   
4514  C CB  . HIS B 140 ? 0.7628 0.5973 0.4805 0.0137  -0.0629 -0.0466 441 HIS B CB  
4515  C CG  . HIS B 140 ? 0.6871 0.5107 0.3889 -0.0045 -0.0713 -0.0550 441 HIS B CG  
4516  N ND1 . HIS B 140 ? 0.7183 0.5034 0.3956 -0.0098 -0.0733 -0.0633 441 HIS B ND1 
4517  C CD2 . HIS B 140 ? 0.6585 0.5050 0.3642 -0.0193 -0.0781 -0.0565 441 HIS B CD2 
4518  C CE1 . HIS B 140 ? 0.7775 0.5602 0.4436 -0.0293 -0.0810 -0.0698 441 HIS B CE1 
4519  N NE2 . HIS B 140 ? 0.6915 0.5142 0.3760 -0.0356 -0.0842 -0.0658 441 HIS B NE2 
4520  N N   . GLY B 141 ? 0.6171 0.4761 0.3730 0.0390  -0.0468 -0.0280 442 GLY B N   
4521  C CA  . GLY B 141 ? 0.6699 0.5479 0.4430 0.0478  -0.0403 -0.0193 442 GLY B CA  
4522  C C   . GLY B 141 ? 0.7647 0.6485 0.5565 0.0433  -0.0386 -0.0132 442 GLY B C   
4523  O O   . GLY B 141 ? 0.7879 0.6897 0.5938 0.0447  -0.0361 -0.0066 442 GLY B O   
4524  N N   . MET B 142 ? 0.7328 0.5994 0.5228 0.0385  -0.0398 -0.0151 443 MET B N   
4525  C CA  . MET B 142 ? 0.6222 0.4947 0.4287 0.0333  -0.0388 -0.0098 443 MET B CA  
4526  C C   . MET B 142 ? 0.6542 0.5456 0.4704 0.0233  -0.0430 -0.0077 443 MET B C   
4527  O O   . MET B 142 ? 0.5611 0.4688 0.3926 0.0248  -0.0404 -0.0017 443 MET B O   
4528  C CB  . MET B 142 ? 0.6477 0.4972 0.4470 0.0291  -0.0403 -0.0123 443 MET B CB  
4529  C CG  . MET B 142 ? 0.6286 0.4693 0.4286 0.0407  -0.0347 -0.0103 443 MET B CG  
4530  S SD  . MET B 142 ? 0.7791 0.5859 0.5617 0.0386  -0.0374 -0.0143 443 MET B SD  
4531  C CE  . MET B 142 ? 0.6922 0.5080 0.4936 0.0326  -0.0363 -0.0071 443 MET B CE  
4532  N N   . PHE B 143 ? 0.7104 0.6009 0.5165 0.0134  -0.0496 -0.0130 444 PHE B N   
4533  C CA  . PHE B 143 ? 0.5491 0.4630 0.3643 0.0042  -0.0540 -0.0115 444 PHE B CA  
4534  C C   . PHE B 143 ? 0.5803 0.5183 0.4035 0.0137  -0.0521 -0.0067 444 PHE B C   
4535  O O   . PHE B 143 ? 0.7175 0.6760 0.5535 0.0129  -0.0523 -0.0020 444 PHE B O   
4536  C CB  . PHE B 143 ? 0.6356 0.5451 0.4365 -0.0094 -0.0616 -0.0189 444 PHE B CB  
4537  C CG  . PHE B 143 ? 0.6756 0.6164 0.4842 -0.0176 -0.0667 -0.0182 444 PHE B CG  
4538  C CD1 . PHE B 143 ? 0.6240 0.5803 0.4257 -0.0154 -0.0704 -0.0211 444 PHE B CD1 
4539  C CD2 . PHE B 143 ? 0.5435 0.5007 0.3658 -0.0266 -0.0680 -0.0145 444 PHE B CD2 
4540  C CE1 . PHE B 143 ? 0.6859 0.6752 0.4949 -0.0215 -0.0754 -0.0202 444 PHE B CE1 
4541  C CE2 . PHE B 143 ? 0.5818 0.5723 0.4118 -0.0328 -0.0725 -0.0137 444 PHE B CE2 
4542  C CZ  . PHE B 143 ? 0.6850 0.6926 0.5087 -0.0298 -0.0764 -0.0165 444 PHE B CZ  
4543  N N   . ASN B 144 ? 0.6963 0.6314 0.5106 0.0236  -0.0498 -0.0076 445 ASN B N   
4544  C CA  . ASN B 144 ? 0.6996 0.6534 0.5180 0.0333  -0.0473 -0.0022 445 ASN B CA  
4545  C C   . ASN B 144 ? 0.6627 0.6174 0.4937 0.0405  -0.0401 0.0055  445 ASN B C   
4546  O O   . ASN B 144 ? 0.6938 0.6630 0.5315 0.0452  -0.0387 0.0111  445 ASN B O   
4547  C CB  . ASN B 144 ? 0.6260 0.5749 0.4295 0.0413  -0.0464 -0.0050 445 ASN B CB  
4548  C CG  . ASN B 144 ? 0.7904 0.7544 0.5949 0.0522  -0.0430 0.0016  445 ASN B CG  
4549  O OD1 . ASN B 144 ? 0.8141 0.7717 0.6127 0.0612  -0.0373 0.0039  445 ASN B OD1 
4550  N ND2 . ASN B 144 ? 0.8044 0.7887 0.6150 0.0520  -0.0462 0.0050  445 ASN B ND2 
4551  N N   . TYR B 145 ? 0.7139 0.6528 0.5468 0.0418  -0.0356 0.0056  446 TYR B N   
4552  C CA  . TYR B 145 ? 0.7570 0.6969 0.6016 0.0457  -0.0293 0.0119  446 TYR B CA  
4553  C C   . TYR B 145 ? 0.6525 0.6000 0.5092 0.0394  -0.0311 0.0142  446 TYR B C   
4554  O O   . TYR B 145 ? 0.6116 0.5661 0.4759 0.0430  -0.0277 0.0194  446 TYR B O   
4555  C CB  . TYR B 145 ? 0.6821 0.6081 0.5260 0.0480  -0.0249 0.0109  446 TYR B CB  
4556  C CG  . TYR B 145 ? 0.5839 0.5097 0.4228 0.0567  -0.0189 0.0130  446 TYR B CG  
4557  C CD1 . TYR B 145 ? 0.5364 0.4538 0.3642 0.0614  -0.0181 0.0086  446 TYR B CD1 
4558  C CD2 . TYR B 145 ? 0.5253 0.4580 0.3691 0.0600  -0.0134 0.0194  446 TYR B CD2 
4559  C CE1 . TYR B 145 ? 0.5171 0.4380 0.3413 0.0689  -0.0118 0.0109  446 TYR B CE1 
4560  C CE2 . TYR B 145 ? 0.4931 0.4262 0.3321 0.0656  -0.0074 0.0220  446 TYR B CE2 
4561  C CZ  . TYR B 145 ? 0.5581 0.4877 0.3883 0.0700  -0.0065 0.0179  446 TYR B CZ  
4562  O OH  . TYR B 145 ? 0.7422 0.6761 0.5683 0.0752  0.0002  0.0210  446 TYR B OH  
4563  N N   . ILE B 146 ? 0.6628 0.6077 0.5195 0.0298  -0.0363 0.0102  447 ILE B N   
4564  C CA  . ILE B 146 ? 0.6537 0.6074 0.5217 0.0232  -0.0377 0.0123  447 ILE B CA  
4565  C C   . ILE B 146 ? 0.6534 0.6302 0.5256 0.0240  -0.0404 0.0146  447 ILE B C   
4566  O O   . ILE B 146 ? 0.7405 0.7276 0.6223 0.0263  -0.0383 0.0188  447 ILE B O   
4567  C CB  . ILE B 146 ? 0.5949 0.5378 0.4593 0.0116  -0.0420 0.0081  447 ILE B CB  
4568  C CG1 . ILE B 146 ? 0.6536 0.5763 0.5166 0.0139  -0.0384 0.0080  447 ILE B CG1 
4569  C CG2 . ILE B 146 ? 0.5520 0.5096 0.4260 0.0029  -0.0446 0.0099  447 ILE B CG2 
4570  C CD1 . ILE B 146 ? 0.6071 0.5128 0.4624 0.0041  -0.0420 0.0046  447 ILE B CD1 
4571  N N   . CYS B 147 ? 0.5687 0.5549 0.4329 0.0235  -0.0449 0.0117  448 CYS B N   
4572  C CA  . CYS B 147 ? 0.4645 0.4769 0.3322 0.0263  -0.0479 0.0140  448 CYS B CA  
4573  C C   . CYS B 147 ? 0.5550 0.5704 0.4245 0.0408  -0.0423 0.0206  448 CYS B C   
4574  O O   . CYS B 147 ? 0.5944 0.6271 0.4697 0.0459  -0.0423 0.0245  448 CYS B O   
4575  C CB  . CYS B 147 ? 0.6165 0.6389 0.4737 0.0236  -0.0539 0.0094  448 CYS B CB  
4576  S SG  . CYS B 147 ? 0.6557 0.6845 0.5094 0.0038  -0.0625 0.0019  448 CYS B SG  
4577  N N   . ASN B 148 ? 0.6457 0.6443 0.5083 0.0478  -0.0372 0.0221  449 ASN B N   
4578  C CA  . ASN B 148 ? 0.5310 0.5273 0.3923 0.0595  -0.0313 0.0288  449 ASN B CA  
4579  C C   . ASN B 148 ? 0.5957 0.5853 0.4663 0.0589  -0.0268 0.0318  449 ASN B C   
4580  O O   . ASN B 148 ? 0.6386 0.6314 0.5095 0.0667  -0.0240 0.0366  449 ASN B O   
4581  C CB  . ASN B 148 ? 0.6135 0.5949 0.4649 0.0646  -0.0266 0.0298  449 ASN B CB  
4582  C CG  . ASN B 148 ? 0.5450 0.5326 0.3851 0.0664  -0.0308 0.0264  449 ASN B CG  
4583  O OD1 . ASN B 148 ? 0.5217 0.5268 0.3605 0.0654  -0.0371 0.0245  449 ASN B OD1 
4584  N ND2 . ASN B 148 ? 0.5744 0.5499 0.4061 0.0688  -0.0274 0.0256  449 ASN B ND2 
4585  N N   . HIS B 149 ? 0.6055 0.5849 0.4819 0.0506  -0.0261 0.0291  450 HIS B N   
4586  C CA  . HIS B 149 ? 0.6645 0.6399 0.5499 0.0485  -0.0228 0.0310  450 HIS B CA  
4587  C C   . HIS B 149 ? 0.5721 0.5648 0.4638 0.0487  -0.0257 0.0322  450 HIS B C   
4588  O O   . HIS B 149 ? 0.5836 0.5771 0.4762 0.0556  -0.0222 0.0359  450 HIS B O   
4589  C CB  . HIS B 149 ? 0.6677 0.6332 0.5574 0.0399  -0.0233 0.0276  450 HIS B CB  
4590  C CG  . HIS B 149 ? 0.6350 0.5970 0.5332 0.0372  -0.0203 0.0293  450 HIS B CG  
4591  N ND1 . HIS B 149 ? 0.6757 0.6443 0.5781 0.0402  -0.0186 0.0322  450 HIS B ND1 
4592  C CD2 . HIS B 149 ? 0.5912 0.5444 0.4933 0.0328  -0.0188 0.0281  450 HIS B CD2 
4593  C CE1 . HIS B 149 ? 0.6262 0.5895 0.5347 0.0366  -0.0162 0.0324  450 HIS B CE1 
4594  N NE2 . HIS B 149 ? 0.6433 0.5986 0.5523 0.0319  -0.0165 0.0302  450 HIS B NE2 
4595  N N   . VAL B 150 ? 0.3638 0.3704 0.2585 0.0408  -0.0319 0.0288  451 VAL B N   
4596  C CA  . VAL B 150 ? 0.3497 0.3789 0.2515 0.0399  -0.0347 0.0298  451 VAL B CA  
4597  C C   . VAL B 150 ? 0.5964 0.6386 0.4947 0.0539  -0.0334 0.0339  451 VAL B C   
4598  O O   . VAL B 150 ? 0.6562 0.7062 0.5584 0.0604  -0.0312 0.0369  451 VAL B O   
4599  C CB  . VAL B 150 ? 0.4392 0.4833 0.3420 0.0275  -0.0418 0.0254  451 VAL B CB  
4600  C CG1 . VAL B 150 ? 0.4096 0.4858 0.3189 0.0285  -0.0449 0.0269  451 VAL B CG1 
4601  C CG2 . VAL B 150 ? 0.3825 0.4127 0.2881 0.0148  -0.0423 0.0228  451 VAL B CG2 
4602  N N   . LYS B 151 ? 0.6614 0.7051 0.5506 0.0602  -0.0347 0.0343  452 LYS B N   
4603  C CA  . LYS B 151 ? 0.4597 0.5173 0.3434 0.0749  -0.0344 0.0388  452 LYS B CA  
4604  C C   . LYS B 151 ? 0.4014 0.4384 0.2790 0.0867  -0.0268 0.0441  452 LYS B C   
4605  O O   . LYS B 151 ? 0.4482 0.4932 0.3237 0.0985  -0.0252 0.0478  452 LYS B O   
4606  C CB  . LYS B 151 ? 0.4820 0.5459 0.3558 0.0786  -0.0377 0.0381  452 LYS B CB  
4607  C CG  . LYS B 151 ? 0.4647 0.5404 0.3301 0.0964  -0.0369 0.0439  452 LYS B CG  
4608  C CD  . LYS B 151 ? 0.4969 0.5881 0.3541 0.0989  -0.0423 0.0426  452 LYS B CD  
4609  C CE  . LYS B 151 ? 0.4191 0.5286 0.2683 0.1176  -0.0428 0.0485  452 LYS B CE  
4610  N NZ  . LYS B 151 ? 0.5814 0.7072 0.4214 0.1203  -0.0483 0.0472  452 LYS B NZ  
4611  N N   . TYR B 152 ? 0.5030 0.5133 0.3761 0.0838  -0.0218 0.0444  453 TYR B N   
4612  C CA  . TYR B 152 ? 0.5411 0.5293 0.4075 0.0907  -0.0144 0.0488  453 TYR B CA  
4613  C C   . TYR B 152 ? 0.5969 0.5848 0.4714 0.0886  -0.0128 0.0482  453 TYR B C   
4614  O O   . TYR B 152 ? 0.6553 0.6384 0.5238 0.0991  -0.0095 0.0515  453 TYR B O   
4615  C CB  . TYR B 152 ? 0.6009 0.5665 0.4634 0.0845  -0.0098 0.0486  453 TYR B CB  
4616  C CG  . TYR B 152 ? 0.6612 0.6037 0.5175 0.0865  -0.0023 0.0522  453 TYR B CG  
4617  C CD1 . TYR B 152 ? 0.6572 0.5842 0.4977 0.0958  0.0025  0.0577  453 TYR B CD1 
4618  C CD2 . TYR B 152 ? 0.7304 0.6657 0.5946 0.0784  -0.0001 0.0501  453 TYR B CD2 
4619  C CE1 . TYR B 152 ? 0.7416 0.6442 0.5735 0.0954  0.0095  0.0607  453 TYR B CE1 
4620  C CE2 . TYR B 152 ? 0.7580 0.6719 0.6150 0.0784  0.0063  0.0525  453 TYR B CE2 
4621  C CZ  . TYR B 152 ? 0.8012 0.6977 0.6415 0.0861  0.0112  0.0577  453 TYR B CZ  
4622  O OH  . TYR B 152 ? 0.8976 0.7693 0.7277 0.0840  0.0178  0.0599  453 TYR B OH  
4623  N N   . ALA B 153 ? 0.6079 0.5994 0.4940 0.0760  -0.0150 0.0440  454 ALA B N   
4624  C CA  . ALA B 153 ? 0.5085 0.4991 0.4018 0.0729  -0.0132 0.0434  454 ALA B CA  
4625  C C   . ALA B 153 ? 0.5356 0.5480 0.4315 0.0809  -0.0152 0.0446  454 ALA B C   
4626  O O   . ALA B 153 ? 0.5660 0.5731 0.4600 0.0873  -0.0115 0.0459  454 ALA B O   
4627  C CB  . ALA B 153 ? 0.3733 0.3655 0.2770 0.0588  -0.0158 0.0394  454 ALA B CB  
4628  N N   . THR B 154 ? 0.5527 0.5911 0.4520 0.0810  -0.0210 0.0438  455 THR B N   
4629  C CA  . THR B 154 ? 0.4457 0.5127 0.3497 0.0877  -0.0233 0.0448  455 THR B CA  
4630  C C   . THR B 154 ? 0.6182 0.6837 0.5104 0.1082  -0.0200 0.0495  455 THR B C   
4631  O O   . THR B 154 ? 0.6872 0.7591 0.5789 0.1180  -0.0175 0.0510  455 THR B O   
4632  C CB  . THR B 154 ? 0.4778 0.5751 0.3886 0.0793  -0.0307 0.0424  455 THR B CB  
4633  O OG1 . THR B 154 ? 0.4024 0.4935 0.3200 0.0607  -0.0332 0.0382  455 THR B OG1 
4634  C CG2 . THR B 154 ? 0.3906 0.5251 0.3081 0.0848  -0.0333 0.0435  455 THR B CG2 
4635  N N   . ASN B 155 ? 0.7469 0.8028 0.6276 0.1159  -0.0195 0.0520  456 ASN B N   
4636  C CA  . ASN B 155 ? 0.6884 0.7317 0.5528 0.1358  -0.0152 0.0575  456 ASN B CA  
4637  C C   . ASN B 155 ? 0.5743 0.6470 0.4391 0.1516  -0.0169 0.0596  456 ASN B C   
4638  O O   . ASN B 155 ? 0.6272 0.6867 0.4805 0.1676  -0.0121 0.0629  456 ASN B O   
4639  C CB  . ASN B 155 ? 0.6933 0.6971 0.5477 0.1367  -0.0074 0.0589  456 ASN B CB  
4640  C CG  . ASN B 155 ? 0.7929 0.7725 0.6256 0.1538  -0.0023 0.0648  456 ASN B CG  
4641  O OD1 . ASN B 155 ? 0.8902 0.8786 0.7149 0.1640  -0.0043 0.0682  456 ASN B OD1 
4642  N ND2 . ASN B 155 ? 0.7652 0.7125 0.5863 0.1567  0.0043  0.0659  456 ASN B ND2 
4643  N N   . LYS B 156 ? 0.5555 0.6686 0.4323 0.1470  -0.0238 0.0576  457 LYS B N   
4644  C CA  . LYS B 156 ? 0.6217 0.7730 0.5014 0.1612  -0.0263 0.0595  457 LYS B CA  
4645  C C   . LYS B 156 ? 0.8291 0.9846 0.7144 0.1642  -0.0229 0.0589  457 LYS B C   
4646  O O   . LYS B 156 ? 0.9545 1.1268 0.8349 0.1836  -0.0214 0.0618  457 LYS B O   
4647  C CB  . LYS B 156 ? 0.6959 0.8453 0.5579 0.1860  -0.0247 0.0655  457 LYS B CB  
4648  C CG  . LYS B 156 ? 0.7495 0.8941 0.6039 0.1844  -0.0277 0.0666  457 LYS B CG  
4649  C CD  . LYS B 156 ? 0.8541 1.0276 0.6997 0.2053  -0.0310 0.0713  457 LYS B CD  
4650  C CE  . LYS B 156 ? 0.7680 0.9760 0.6218 0.1942  -0.0396 0.0681  457 LYS B CE  
4651  N NZ  . LYS B 156 ? 0.8904 1.1396 0.7402 0.2142  -0.0439 0.0720  457 LYS B NZ  
4652  N N   . GLY B 157 ? 0.8406 0.9816 0.7351 0.1463  -0.0216 0.0551  458 GLY B N   
4653  C CA  . GLY B 157 ? 0.6806 0.8254 0.5807 0.1466  -0.0185 0.0539  458 GLY B CA  
4654  C C   . GLY B 157 ? 0.6849 0.7862 0.5732 0.1512  -0.0113 0.0541  458 GLY B C   
4655  O O   . GLY B 157 ? 0.8511 0.9497 0.7449 0.1454  -0.0091 0.0518  458 GLY B O   
4656  N N   . ASN B 158 ? 0.6246 0.6920 0.4957 0.1605  -0.0075 0.0568  459 ASN B N   
4657  C CA  . ASN B 158 ? 0.5850 0.6091 0.4430 0.1617  -0.0007 0.0566  459 ASN B CA  
4658  C C   . ASN B 158 ? 0.6546 0.6574 0.5182 0.1409  -0.0006 0.0541  459 ASN B C   
4659  O O   . ASN B 158 ? 0.6450 0.6249 0.4991 0.1395  0.0013  0.0559  459 ASN B O   
4660  C CB  . ASN B 158 ? 0.5024 0.4991 0.3365 0.1814  0.0040  0.0615  459 ASN B CB  
4661  C CG  . ASN B 158 ? 0.6742 0.6218 0.4927 0.1773  0.0108  0.0611  459 ASN B CG  
4662  O OD1 . ASN B 158 ? 0.8601 0.7976 0.6823 0.1686  0.0130  0.0573  459 ASN B OD1 
4663  N ND2 . ASN B 158 ? 0.7253 0.6433 0.5259 0.1820  0.0141  0.0652  459 ASN B ND2 
4664  N N   . LEU B 159 ? 0.6480 0.6592 0.5263 0.1254  -0.0022 0.0501  460 LEU B N   
4665  C CA  . LEU B 159 ? 0.5553 0.5569 0.4415 0.1071  -0.0037 0.0477  460 LEU B CA  
4666  C C   . LEU B 159 ? 0.5637 0.5279 0.4390 0.1038  0.0018  0.0479  460 LEU B C   
4667  O O   . LEU B 159 ? 0.7191 0.6612 0.5816 0.1113  0.0070  0.0487  460 LEU B O   
4668  C CB  . LEU B 159 ? 0.4788 0.4955 0.3806 0.0931  -0.0063 0.0443  460 LEU B CB  
4669  C CG  . LEU B 159 ? 0.6019 0.6564 0.5156 0.0913  -0.0112 0.0438  460 LEU B CG  
4670  C CD1 . LEU B 159 ? 0.6527 0.7129 0.5788 0.0729  -0.0140 0.0411  460 LEU B CD1 
4671  C CD2 . LEU B 159 ? 0.5230 0.6000 0.4373 0.0951  -0.0158 0.0452  460 LEU B CD2 
4672  N N   . ARG B 160 ? 0.4821 0.4396 0.3616 0.0918  0.0007  0.0469  461 ARG B N   
4673  C CA  . ARG B 160 ? 0.4772 0.4069 0.3497 0.0852  0.0053  0.0471  461 ARG B CA  
4674  C C   . ARG B 160 ? 0.5658 0.5002 0.4514 0.0698  0.0032  0.0437  461 ARG B C   
4675  O O   . ARG B 160 ? 0.6162 0.5691 0.5119 0.0650  -0.0020 0.0422  461 ARG B O   
4676  C CB  . ARG B 160 ? 0.5359 0.4545 0.3965 0.0907  0.0070  0.0508  461 ARG B CB  
4677  C CG  . ARG B 160 ? 0.6881 0.5922 0.5305 0.1066  0.0107  0.0552  461 ARG B CG  
4678  C CD  . ARG B 160 ? 0.8124 0.7045 0.6416 0.1116  0.0125  0.0597  461 ARG B CD  
4679  N NE  . ARG B 160 ? 0.7510 0.6698 0.5863 0.1161  0.0066  0.0601  461 ARG B NE  
4680  C CZ  . ARG B 160 ? 0.8003 0.7164 0.6244 0.1237  0.0068  0.0641  461 ARG B CZ  
4681  N NH1 . ARG B 160 ? 0.8511 0.7376 0.6570 0.1275  0.0132  0.0688  461 ARG B NH1 
4682  N NH2 . ARG B 160 ? 0.7168 0.6593 0.5468 0.1262  0.0007  0.0635  461 ARG B NH2 
4683  N N   . SER B 161 ? 0.5772 0.4949 0.4615 0.0619  0.0069  0.0425  462 SER B N   
4684  C CA  . SER B 161 ? 0.6789 0.6025 0.5747 0.0499  0.0050  0.0398  462 SER B CA  
4685  C C   . SER B 161 ? 0.6713 0.5928 0.5658 0.0474  0.0049  0.0406  462 SER B C   
4686  O O   . SER B 161 ? 0.5495 0.4579 0.4334 0.0504  0.0088  0.0432  462 SER B O   
4687  C CB  . SER B 161 ? 0.6965 0.6087 0.5924 0.0424  0.0084  0.0379  462 SER B CB  
4688  O OG  . SER B 161 ? 0.8106 0.7160 0.7004 0.0472  0.0105  0.0374  462 SER B OG  
4689  N N   . ALA B 162 ? 0.5817 0.5143 0.4851 0.0420  0.0008  0.0384  463 ALA B N   
4690  C CA  . ALA B 162 ? 0.4712 0.4023 0.3726 0.0408  0.0009  0.0384  463 ALA B CA  
4691  C C   . ALA B 162 ? 0.5213 0.4584 0.4306 0.0347  -0.0023 0.0355  463 ALA B C   
4692  O O   . ALA B 162 ? 0.5236 0.4678 0.4389 0.0318  -0.0062 0.0338  463 ALA B O   
4693  C CB  . ALA B 162 ? 0.5554 0.4916 0.4508 0.0477  -0.0017 0.0396  463 ALA B CB  
4694  N N   . ILE B 163 ? 0.6033 0.5373 0.5111 0.0334  -0.0002 0.0351  464 ILE B N   
4695  C CA  . ILE B 163 ? 0.5554 0.4925 0.4667 0.0312  -0.0028 0.0325  464 ILE B CA  
4696  C C   . ILE B 163 ? 0.6417 0.5774 0.5459 0.0353  -0.0025 0.0321  464 ILE B C   
4697  O O   . ILE B 163 ? 0.5468 0.4799 0.4452 0.0379  0.0015  0.0345  464 ILE B O   
4698  C CB  . ILE B 163 ? 0.4324 0.3711 0.3495 0.0272  -0.0001 0.0322  464 ILE B CB  
4699  C CG1 . ILE B 163 ? 0.4580 0.3989 0.3776 0.0274  -0.0034 0.0300  464 ILE B CG1 
4700  C CG2 . ILE B 163 ? 0.3321 0.2706 0.2463 0.0269  0.0054  0.0336  464 ILE B CG2 
4701  C CD1 . ILE B 163 ? 0.4022 0.3492 0.3274 0.0255  -0.0011 0.0300  464 ILE B CD1 
4702  N N   . THR B 164 ? 0.5739 0.5094 0.4763 0.0358  -0.0066 0.0291  465 THR B N   
4703  C CA  . THR B 164 ? 0.5816 0.5149 0.4758 0.0401  -0.0068 0.0273  465 THR B CA  
4704  C C   . THR B 164 ? 0.6050 0.5356 0.4990 0.0414  -0.0069 0.0248  465 THR B C   
4705  O O   . THR B 164 ? 0.6687 0.5948 0.5635 0.0390  -0.0107 0.0229  465 THR B O   
4706  C CB  . THR B 164 ? 0.5907 0.5239 0.4787 0.0403  -0.0124 0.0250  465 THR B CB  
4707  O OG1 . THR B 164 ? 0.5026 0.4411 0.3890 0.0428  -0.0118 0.0279  465 THR B OG1 
4708  C CG2 . THR B 164 ? 0.5771 0.5052 0.4548 0.0440  -0.0136 0.0215  465 THR B CG2 
4709  N N   . ILE B 165 ? 0.4918 0.4257 0.3837 0.0456  -0.0024 0.0253  466 ILE B N   
4710  C CA  . ILE B 165 ? 0.5648 0.5006 0.4577 0.0493  -0.0014 0.0238  466 ILE B CA  
4711  C C   . ILE B 165 ? 0.5080 0.4389 0.3894 0.0571  -0.0018 0.0204  466 ILE B C   
4712  O O   . ILE B 165 ? 0.5596 0.4963 0.4370 0.0610  0.0021  0.0212  466 ILE B O   
4713  C CB  . ILE B 165 ? 0.6746 0.6234 0.5755 0.0478  0.0043  0.0266  466 ILE B CB  
4714  C CG1 . ILE B 165 ? 0.5812 0.5312 0.4896 0.0397  0.0052  0.0292  466 ILE B CG1 
4715  C CG2 . ILE B 165 ? 0.7455 0.7003 0.6499 0.0516  0.0040  0.0255  466 ILE B CG2 
4716  C CD1 . ILE B 165 ? 0.4930 0.4550 0.4085 0.0351  0.0102  0.0312  466 ILE B CD1 
4717  N N   . PHE B 166 ? 0.5494 0.4682 0.4238 0.0595  -0.0062 0.0168  467 PHE B N   
4718  C CA  . PHE B 166 ? 0.5889 0.4971 0.4487 0.0673  -0.0074 0.0124  467 PHE B CA  
4719  C C   . PHE B 166 ? 0.6314 0.5463 0.4902 0.0776  -0.0032 0.0123  467 PHE B C   
4720  O O   . PHE B 166 ? 0.9029 0.8321 0.7733 0.0771  -0.0002 0.0156  467 PHE B O   
4721  C CB  . PHE B 166 ? 0.5395 0.4281 0.3899 0.0634  -0.0138 0.0087  467 PHE B CB  
4722  C CG  . PHE B 166 ? 0.6470 0.5349 0.4970 0.0545  -0.0178 0.0081  467 PHE B CG  
4723  C CD1 . PHE B 166 ? 0.7076 0.5969 0.5494 0.0562  -0.0183 0.0059  467 PHE B CD1 
4724  C CD2 . PHE B 166 ? 0.4674 0.3565 0.3251 0.0451  -0.0209 0.0098  467 PHE B CD2 
4725  C CE1 . PHE B 166 ? 0.7416 0.6348 0.5834 0.0491  -0.0224 0.0055  467 PHE B CE1 
4726  C CE2 . PHE B 166 ? 0.6749 0.5687 0.5330 0.0380  -0.0246 0.0094  467 PHE B CE2 
4727  C CZ  . PHE B 166 ? 0.6674 0.5640 0.5179 0.0402  -0.0255 0.0073  467 PHE B CZ  
4728  N N   . PRO B 167 ? 0.6503 0.5572 0.4949 0.0877  -0.0029 0.0083  468 PRO B N   
4729  C CA  . PRO B 167 ? 0.6366 0.5557 0.4807 0.0999  0.0019  0.0086  468 PRO B CA  
4730  C C   . PRO B 167 ? 0.7686 0.6865 0.6162 0.1037  0.0008  0.0096  468 PRO B C   
4731  O O   . PRO B 167 ? 0.7996 0.6963 0.6403 0.1015  -0.0041 0.0081  468 PRO B O   
4732  C CB  . PRO B 167 ? 0.6514 0.5559 0.4756 0.1108  0.0014  0.0030  468 PRO B CB  
4733  C CG  . PRO B 167 ? 0.6723 0.5634 0.4893 0.1022  -0.0027 0.0004  468 PRO B CG  
4734  C CD  . PRO B 167 ? 0.6703 0.5567 0.4970 0.0893  -0.0070 0.0027  468 PRO B CD  
4735  N N   . GLN B 168 ? 0.7977 0.7399 0.6555 0.1091  0.0054  0.0126  469 GLN B N   
4736  C CA  . GLN B 168 ? 0.6683 0.6147 0.5308 0.1133  0.0044  0.0143  469 GLN B CA  
4737  C C   . GLN B 168 ? 0.7830 0.7081 0.6267 0.1288  0.0022  0.0109  469 GLN B C   
4738  O O   . GLN B 168 ? 0.8468 0.7549 0.6737 0.1362  0.0019  0.0066  469 GLN B O   
4739  C CB  . GLN B 168 ? 0.5792 0.5609 0.4565 0.1152  0.0096  0.0177  469 GLN B CB  
4740  C CG  . GLN B 168 ? 0.5590 0.5559 0.4300 0.1311  0.0139  0.0164  469 GLN B CG  
4741  C CD  . GLN B 168 ? 0.5775 0.6101 0.4626 0.1260  0.0202  0.0195  469 GLN B CD  
4742  O OE1 . GLN B 168 ? 0.4996 0.5365 0.3941 0.1102  0.0214  0.0219  469 GLN B OE1 
4743  N NE2 . GLN B 168 ? 0.6303 0.6889 0.5158 0.1392  0.0244  0.0197  469 GLN B NE2 
4744  N N   . ARG B 169 ? 0.7691 0.6936 0.6137 0.1341  0.0007  0.0130  470 ARG B N   
4745  C CA  . ARG B 169 ? 0.7586 0.6598 0.5831 0.1503  -0.0011 0.0109  470 ARG B CA  
4746  C C   . ARG B 169 ? 0.7874 0.7102 0.6090 0.1699  0.0038  0.0104  470 ARG B C   
4747  O O   . ARG B 169 ? 0.8522 0.8137 0.6918 0.1697  0.0079  0.0134  470 ARG B O   
4748  C CB  . ARG B 169 ? 0.8476 0.7404 0.6731 0.1495  -0.0044 0.0143  470 ARG B CB  
4749  C CG  . ARG B 169 ? 0.9784 0.8406 0.7794 0.1664  -0.0062 0.0130  470 ARG B CG  
4750  C CD  . ARG B 169 ? 0.8429 0.6989 0.6441 0.1669  -0.0089 0.0177  470 ARG B CD  
4751  N NE  . ARG B 169 ? 0.7846 0.6118 0.5808 0.1497  -0.0134 0.0181  470 ARG B NE  
4752  C CZ  . ARG B 169 ? 0.9609 0.7991 0.7722 0.1365  -0.0151 0.0222  470 ARG B CZ  
4753  N NH1 . ARG B 169 ? 0.8861 0.7605 0.7172 0.1379  -0.0131 0.0256  470 ARG B NH1 
4754  N NH2 . ARG B 169 ? 1.0741 0.8885 0.8803 0.1214  -0.0187 0.0225  470 ARG B NH2 
4755  N N   . THR B 170 ? 0.7875 0.6855 0.5854 0.1865  0.0036  0.0062  471 THR B N   
4756  C CA  . THR B 170 ? 0.8320 0.7500 0.6244 0.2082  0.0085  0.0052  471 THR B CA  
4757  C C   . THR B 170 ? 0.9394 0.8405 0.7141 0.2294  0.0073  0.0055  471 THR B C   
4758  O O   . THR B 170 ? 0.8712 0.8031 0.6573 0.2391  0.0091  0.0098  471 THR B O   
4759  C CB  . THR B 170 ? 0.8555 0.7632 0.6335 0.2131  0.0107  -0.0004 471 THR B CB  
4760  O OG1 . THR B 170 ? 0.8966 0.7544 0.6474 0.2149  0.0063  -0.0060 471 THR B OG1 
4761  C CG2 . THR B 170 ? 0.6174 0.5431 0.4119 0.1937  0.0123  0.0004  471 THR B CG2 
4762  N N   . ASP B 171 ? 0.9618 0.8144 0.7076 0.2368  0.0042  0.0013  472 ASP B N   
4763  C CA  . ASP B 171 ? 0.9487 0.7778 0.6726 0.2584  0.0033  0.0019  472 ASP B CA  
4764  C C   . ASP B 171 ? 1.0055 0.7912 0.7164 0.2475  -0.0023 0.0034  472 ASP B C   
4765  O O   . ASP B 171 ? 1.1138 0.8672 0.7998 0.2637  -0.0035 0.0038  472 ASP B O   
4766  C CB  . ASP B 171 ? 1.0395 0.8442 0.7336 0.2811  0.0057  -0.0043 472 ASP B CB  
4767  C CG  . ASP B 171 ? 1.1033 0.8551 0.7722 0.2706  0.0020  -0.0111 472 ASP B CG  
4768  O OD1 . ASP B 171 ? 1.1693 0.9226 0.8511 0.2461  -0.0004 -0.0121 472 ASP B OD1 
4769  O OD2 . ASP B 171 ? 1.1589 0.8672 0.7938 0.2867  0.0013  -0.0156 472 ASP B OD2 
4770  N N   . GLY B 172 ? 0.9831 0.7672 0.7087 0.2212  -0.0055 0.0045  473 GLY B N   
4771  C CA  . GLY B 172 ? 0.9813 0.7303 0.6970 0.2088  -0.0104 0.0065  473 GLY B CA  
4772  C C   . GLY B 172 ? 1.0688 0.7646 0.7549 0.2025  -0.0137 0.0007  473 GLY B C   
4773  O O   . GLY B 172 ? 0.9282 0.6000 0.6103 0.1843  -0.0177 0.0019  473 GLY B O   
4774  N N   . LYS B 173 ? 1.2066 0.8842 0.8711 0.2161  -0.0120 -0.0057 474 LYS B N   
4775  C CA  . LYS B 173 ? 1.3702 0.9985 1.0057 0.2080  -0.0153 -0.0127 474 LYS B CA  
4776  C C   . LYS B 173 ? 1.3408 0.9829 0.9869 0.1917  -0.0161 -0.0178 474 LYS B C   
4777  O O   . LYS B 173 ? 1.4105 1.0177 1.0337 0.1843  -0.0190 -0.0247 474 LYS B O   
4778  C CB  . LYS B 173 ? 1.5415 1.1334 1.1404 0.2339  -0.0135 -0.0176 474 LYS B CB  
4779  C CG  . LYS B 173 ? 1.6125 1.1737 1.1899 0.2500  -0.0137 -0.0131 474 LYS B CG  
4780  C CD  . LYS B 173 ? 1.6983 1.2089 1.2314 0.2733  -0.0126 -0.0193 474 LYS B CD  
4781  C CE  . LYS B 173 ? 1.6950 1.2361 1.2291 0.3029  -0.0069 -0.0215 474 LYS B CE  
4782  N NZ  . LYS B 173 ? 1.6287 1.1991 1.1721 0.3271  -0.0039 -0.0138 474 LYS B NZ  
4783  N N   . HIS B 174 ? 1.2348 0.9258 0.9129 0.1861  -0.0136 -0.0147 475 HIS B N   
4784  C CA  . HIS B 174 ? 1.1148 0.8212 0.8034 0.1719  -0.0140 -0.0181 475 HIS B CA  
4785  C C   . HIS B 174 ? 0.9774 0.7114 0.6957 0.1509  -0.0155 -0.0127 475 HIS B C   
4786  O O   . HIS B 174 ? 0.9879 0.7526 0.7253 0.1446  -0.0135 -0.0118 475 HIS B O   
4787  C CB  . HIS B 174 ? 1.1444 0.8807 0.8387 0.1869  -0.0084 -0.0197 475 HIS B CB  
4788  C CG  . HIS B 174 ? 1.1543 0.8674 0.8195 0.2103  -0.0062 -0.0253 475 HIS B CG  
4789  N ND1 . HIS B 174 ? 1.1559 0.8186 0.7888 0.2170  -0.0092 -0.0293 475 HIS B ND1 
4790  C CD2 . HIS B 174 ? 1.1413 0.8738 0.8031 0.2292  -0.0009 -0.0276 475 HIS B CD2 
4791  C CE1 . HIS B 174 ? 1.2106 0.8608 0.8204 0.2406  -0.0059 -0.0342 475 HIS B CE1 
4792  N NE2 . HIS B 174 ? 1.2337 0.9281 0.8615 0.2487  -0.0008 -0.0333 475 HIS B NE2 
4793  N N   . ASP B 175 ? 0.9575 0.6791 0.6780 0.1406  -0.0187 -0.0090 476 ASP B N   
4794  C CA  . ASP B 175 ? 0.9484 0.6960 0.6958 0.1234  -0.0197 -0.0038 476 ASP B CA  
4795  C C   . ASP B 175 ? 0.8527 0.6009 0.6042 0.1050  -0.0228 -0.0068 476 ASP B C   
4796  O O   . ASP B 175 ? 0.8730 0.5920 0.6047 0.0981  -0.0266 -0.0119 476 ASP B O   
4797  C CB  . ASP B 175 ? 1.0089 0.7417 0.7549 0.1174  -0.0224 0.0006  476 ASP B CB  
4798  C CG  . ASP B 175 ? 1.0097 0.7590 0.7632 0.1323  -0.0194 0.0058  476 ASP B CG  
4799  O OD1 . ASP B 175 ? 0.9759 0.7309 0.7224 0.1519  -0.0161 0.0045  476 ASP B OD1 
4800  O OD2 . ASP B 175 ? 1.0162 0.7746 0.7821 0.1248  -0.0205 0.0111  476 ASP B OD2 
4801  N N   . PHE B 176 ? 0.8012 0.5826 0.5774 0.0968  -0.0213 -0.0034 477 PHE B N   
4802  C CA  . PHE B 176 ? 0.7448 0.5313 0.5285 0.0794  -0.0245 -0.0041 477 PHE B CA  
4803  C C   . PHE B 176 ? 0.8514 0.6395 0.6458 0.0662  -0.0271 0.0002  477 PHE B C   
4804  O O   . PHE B 176 ? 1.0164 0.8220 0.8264 0.0682  -0.0247 0.0053  477 PHE B O   
4805  C CB  . PHE B 176 ? 0.7908 0.6084 0.5916 0.0794  -0.0211 -0.0024 477 PHE B CB  
4806  C CG  . PHE B 176 ? 0.8183 0.6339 0.6071 0.0876  -0.0195 -0.0070 477 PHE B CG  
4807  C CD1 . PHE B 176 ? 0.8437 0.6562 0.6222 0.1044  -0.0158 -0.0089 477 PHE B CD1 
4808  C CD2 . PHE B 176 ? 0.8512 0.6693 0.6379 0.0796  -0.0219 -0.0096 477 PHE B CD2 
4809  C CE1 . PHE B 176 ? 0.7889 0.5999 0.5551 0.1127  -0.0141 -0.0134 477 PHE B CE1 
4810  C CE2 . PHE B 176 ? 0.8025 0.6187 0.5767 0.0873  -0.0206 -0.0140 477 PHE B CE2 
4811  C CZ  . PHE B 176 ? 0.7639 0.5759 0.5277 0.1036  -0.0165 -0.0160 477 PHE B CZ  
4812  N N   . ARG B 177 ? 0.8299 0.6018 0.6158 0.0520  -0.0319 -0.0020 478 ARG B N   
4813  C CA  . ARG B 177 ? 0.8583 0.6317 0.6525 0.0390  -0.0342 0.0021  478 ARG B CA  
4814  C C   . ARG B 177 ? 0.8424 0.6248 0.6415 0.0224  -0.0380 0.0006  478 ARG B C   
4815  O O   . ARG B 177 ? 1.0479 0.8166 0.8322 0.0168  -0.0413 -0.0048 478 ARG B O   
4816  C CB  . ARG B 177 ? 0.9139 0.6538 0.6884 0.0380  -0.0362 0.0023  478 ARG B CB  
4817  C CG  . ARG B 177 ? 0.9394 0.6709 0.7081 0.0555  -0.0330 0.0050  478 ARG B CG  
4818  C CD  . ARG B 177 ? 0.9573 0.7211 0.7505 0.0593  -0.0299 0.0110  478 ARG B CD  
4819  N NE  . ARG B 177 ? 0.8882 0.6597 0.6927 0.0454  -0.0316 0.0153  478 ARG B NE  
4820  C CZ  . ARG B 177 ? 0.8121 0.5701 0.6104 0.0445  -0.0324 0.0193  478 ARG B CZ  
4821  N NH1 . ARG B 177 ? 0.6950 0.4289 0.4746 0.0576  -0.0319 0.0199  478 ARG B NH1 
4822  N NH2 . ARG B 177 ? 0.7846 0.5538 0.5944 0.0316  -0.0335 0.0231  478 ARG B NH2 
4823  N N   . VAL B 178 ? 0.7947 0.6010 0.6134 0.0151  -0.0376 0.0051  479 VAL B N   
4824  C CA  . VAL B 178 ? 0.7234 0.5389 0.5465 -0.0009 -0.0414 0.0050  479 VAL B CA  
4825  C C   . VAL B 178 ? 0.7725 0.5715 0.5888 -0.0108 -0.0433 0.0073  479 VAL B C   
4826  O O   . VAL B 178 ? 0.8059 0.6112 0.6317 -0.0085 -0.0411 0.0123  479 VAL B O   
4827  C CB  . VAL B 178 ? 0.6056 0.4539 0.4510 -0.0014 -0.0395 0.0088  479 VAL B CB  
4828  C CG1 . VAL B 178 ? 0.4277 0.2897 0.2783 -0.0158 -0.0432 0.0092  479 VAL B CG1 
4829  C CG2 . VAL B 178 ? 0.6171 0.4777 0.4662 0.0078  -0.0373 0.0074  479 VAL B CG2 
4830  N N   . TRP B 179 ? 0.7395 0.5161 0.5374 -0.0226 -0.0474 0.0037  480 TRP B N   
4831  C CA  . TRP B 179 ? 0.7293 0.4860 0.5170 -0.0336 -0.0488 0.0064  480 TRP B CA  
4832  C C   . TRP B 179 ? 0.7643 0.5479 0.5693 -0.0474 -0.0496 0.0107  480 TRP B C   
4833  O O   . TRP B 179 ? 0.7884 0.5632 0.5905 -0.0543 -0.0493 0.0150  480 TRP B O   
4834  C CB  . TRP B 179 ? 0.7282 0.4496 0.4881 -0.0446 -0.0527 0.0009  480 TRP B CB  
4835  C CG  . TRP B 179 ? 0.8470 0.5329 0.5843 -0.0294 -0.0513 -0.0025 480 TRP B CG  
4836  C CD1 . TRP B 179 ? 0.8630 0.5554 0.6045 -0.0089 -0.0479 -0.0035 480 TRP B CD1 
4837  C CD2 . TRP B 179 ? 0.7899 0.4283 0.4954 -0.0324 -0.0528 -0.0050 480 TRP B CD2 
4838  N NE1 . TRP B 179 ? 0.9024 0.5578 0.6181 0.0026  -0.0472 -0.0067 480 TRP B NE1 
4839  C CE2 . TRP B 179 ? 0.8311 0.4502 0.5231 -0.0106 -0.0502 -0.0077 480 TRP B CE2 
4840  C CE3 . TRP B 179 ? 0.8808 0.4901 0.5665 -0.0516 -0.0558 -0.0050 480 TRP B CE3 
4841  C CZ2 . TRP B 179 ? 0.8262 0.3961 0.4844 -0.0051 -0.0505 -0.0107 480 TRP B CZ2 
4842  C CZ3 . TRP B 179 ? 0.9344 0.4913 0.5853 -0.0483 -0.0561 -0.0079 480 TRP B CZ3 
4843  C CH2 . TRP B 179 ? 0.9210 0.4577 0.5579 -0.0240 -0.0535 -0.0108 480 TRP B CH2 
4844  N N   . ASN B 180 ? 0.6618 0.4776 0.4830 -0.0508 -0.0505 0.0099  481 ASN B N   
4845  C CA  . ASN B 180 ? 0.6391 0.4842 0.4777 -0.0595 -0.0504 0.0142  481 ASN B CA  
4846  C C   . ASN B 180 ? 0.7576 0.6130 0.6105 -0.0479 -0.0459 0.0193  481 ASN B C   
4847  O O   . ASN B 180 ? 0.7387 0.5962 0.5966 -0.0332 -0.0429 0.0190  481 ASN B O   
4848  C CB  . ASN B 180 ? 0.6005 0.4781 0.4519 -0.0612 -0.0519 0.0125  481 ASN B CB  
4849  C CG  . ASN B 180 ? 0.6102 0.4827 0.4485 -0.0720 -0.0569 0.0066  481 ASN B CG  
4850  O OD1 . ASN B 180 ? 0.6369 0.4902 0.4621 -0.0658 -0.0576 0.0020  481 ASN B OD1 
4851  N ND2 . ASN B 180 ? 0.6154 0.5082 0.4573 -0.0883 -0.0603 0.0066  481 ASN B ND2 
4852  N N   . SER B 181 ? 0.7137 0.5772 0.5726 -0.0555 -0.0452 0.0239  482 SER B N   
4853  C CA  . SER B 181 ? 0.6534 0.5297 0.5259 -0.0463 -0.0414 0.0282  482 SER B CA  
4854  C C   . SER B 181 ? 0.6164 0.5234 0.5068 -0.0406 -0.0396 0.0282  482 SER B C   
4855  O O   . SER B 181 ? 0.6351 0.5474 0.5335 -0.0290 -0.0362 0.0291  482 SER B O   
4856  C CB  . SER B 181 ? 0.6000 0.4762 0.4720 -0.0562 -0.0412 0.0330  482 SER B CB  
4857  O OG  . SER B 181 ? 0.8121 0.6995 0.6835 -0.0729 -0.0439 0.0328  482 SER B OG  
4858  N N   . GLN B 182 ? 0.6043 0.5315 0.4998 -0.0484 -0.0417 0.0272  483 GLN B N   
4859  C CA  . GLN B 182 ? 0.6734 0.6243 0.5805 -0.0403 -0.0405 0.0266  483 GLN B CA  
4860  C C   . GLN B 182 ? 0.7576 0.7133 0.6595 -0.0434 -0.0441 0.0228  483 GLN B C   
4861  O O   . GLN B 182 ? 0.8700 0.8194 0.7624 -0.0563 -0.0480 0.0205  483 GLN B O   
4862  C CB  . GLN B 182 ? 0.6396 0.6177 0.5594 -0.0421 -0.0391 0.0297  483 GLN B CB  
4863  C CG  . GLN B 182 ? 0.6823 0.6583 0.6070 -0.0393 -0.0357 0.0331  483 GLN B CG  
4864  C CD  . GLN B 182 ? 0.7541 0.7529 0.6862 -0.0465 -0.0355 0.0359  483 GLN B CD  
4865  O OE1 . GLN B 182 ? 0.7670 0.7906 0.7076 -0.0426 -0.0347 0.0361  483 GLN B OE1 
4866  N NE2 . GLN B 182 ? 0.7204 0.7112 0.6479 -0.0565 -0.0359 0.0385  483 GLN B NE2 
4867  N N   . LEU B 183 ? 0.7186 0.6846 0.6252 -0.0323 -0.0426 0.0220  484 LEU B N   
4868  C CA  . LEU B 183 ? 0.5848 0.5576 0.4862 -0.0332 -0.0460 0.0186  484 LEU B CA  
4869  C C   . LEU B 183 ? 0.6115 0.6086 0.5159 -0.0455 -0.0503 0.0182  484 LEU B C   
4870  O O   . LEU B 183 ? 0.6434 0.6384 0.5386 -0.0560 -0.0549 0.0144  484 LEU B O   
4871  C CB  . LEU B 183 ? 0.5197 0.5017 0.4258 -0.0186 -0.0431 0.0195  484 LEU B CB  
4872  C CG  . LEU B 183 ? 0.4416 0.4035 0.3440 -0.0082 -0.0389 0.0195  484 LEU B CG  
4873  C CD1 . LEU B 183 ? 0.3887 0.3579 0.2923 0.0034  -0.0362 0.0206  484 LEU B CD1 
4874  C CD2 . LEU B 183 ? 0.3819 0.3205 0.2707 -0.0114 -0.0411 0.0155  484 LEU B CD2 
4875  N N   . ILE B 184 ? 0.6710 0.6924 0.5875 -0.0453 -0.0488 0.0218  485 ILE B N   
4876  C CA  . ILE B 184 ? 0.5495 0.6025 0.4716 -0.0554 -0.0521 0.0222  485 ILE B CA  
4877  C C   . ILE B 184 ? 0.6785 0.7343 0.6044 -0.0663 -0.0510 0.0252  485 ILE B C   
4878  O O   . ILE B 184 ? 0.6413 0.7025 0.5754 -0.0581 -0.0468 0.0286  485 ILE B O   
4879  C CB  . ILE B 184 ? 0.5331 0.6173 0.4652 -0.0421 -0.0509 0.0242  485 ILE B CB  
4880  C CG1 . ILE B 184 ? 0.5744 0.6527 0.5011 -0.0300 -0.0512 0.0224  485 ILE B CG1 
4881  C CG2 . ILE B 184 ? 0.4455 0.5686 0.3842 -0.0510 -0.0545 0.0246  485 ILE B CG2 
4882  C CD1 . ILE B 184 ? 0.6614 0.7590 0.5943 -0.0131 -0.0484 0.0256  485 ILE B CD1 
4883  N N   . ARG B 185 ? 0.6410 0.6913 0.5591 -0.0853 -0.0545 0.0239  486 ARG B N   
4884  C CA  . ARG B 185 ? 0.6609 0.7181 0.5814 -0.0985 -0.0537 0.0274  486 ARG B CA  
4885  C C   . ARG B 185 ? 0.7509 0.8237 0.6669 -0.1204 -0.0586 0.0256  486 ARG B C   
4886  O O   . ARG B 185 ? 0.6148 0.6790 0.5206 -0.1274 -0.0629 0.0208  486 ARG B O   
4887  C CB  . ARG B 185 ? 0.7315 0.7508 0.6419 -0.1009 -0.0515 0.0291  486 ARG B CB  
4888  C CG  . ARG B 185 ? 0.7193 0.7247 0.6338 -0.0824 -0.0470 0.0308  486 ARG B CG  
4889  C CD  . ARG B 185 ? 0.7767 0.7548 0.6831 -0.0856 -0.0452 0.0336  486 ARG B CD  
4890  N NE  . ARG B 185 ? 0.8608 0.8568 0.7734 -0.0945 -0.0437 0.0381  486 ARG B NE  
4891  C CZ  . ARG B 185 ? 0.8266 0.8049 0.7324 -0.0993 -0.0422 0.0419  486 ARG B CZ  
4892  N NH1 . ARG B 185 ? 0.6818 0.6244 0.5745 -0.0949 -0.0421 0.0417  486 ARG B NH1 
4893  N NH2 . ARG B 185 ? 0.9549 0.9523 0.8662 -0.1076 -0.0406 0.0461  486 ARG B NH2 
4894  N N   . TYR B 186 ? 0.6983 0.7942 0.6208 -0.1326 -0.0578 0.0293  487 TYR B N   
4895  C CA  . TYR B 186 ? 0.6448 0.7602 0.5639 -0.1565 -0.0620 0.0282  487 TYR B CA  
4896  C C   . TYR B 186 ? 0.8058 0.8800 0.7051 -0.1763 -0.0631 0.0279  487 TYR B C   
4897  O O   . TYR B 186 ? 0.9902 1.0310 0.8823 -0.1716 -0.0598 0.0308  487 TYR B O   
4898  C CB  . TYR B 186 ? 0.5120 0.6758 0.4469 -0.1609 -0.0603 0.0326  487 TYR B CB  
4899  C CG  . TYR B 186 ? 0.5798 0.7838 0.5310 -0.1403 -0.0593 0.0328  487 TYR B CG  
4900  C CD1 . TYR B 186 ? 0.5709 0.7846 0.5325 -0.1219 -0.0539 0.0366  487 TYR B CD1 
4901  C CD2 . TYR B 186 ? 0.6181 0.8473 0.5716 -0.1382 -0.0637 0.0292  487 TYR B CD2 
4902  C CE1 . TYR B 186 ? 0.5246 0.7691 0.4971 -0.1018 -0.0526 0.0369  487 TYR B CE1 
4903  C CE2 . TYR B 186 ? 0.5788 0.8421 0.5445 -0.1170 -0.0626 0.0302  487 TYR B CE2 
4904  C CZ  . TYR B 186 ? 0.5528 0.8216 0.5271 -0.0986 -0.0568 0.0342  487 TYR B CZ  
4905  O OH  . TYR B 186 ? 0.5446 0.8409 0.5272 -0.0763 -0.0551 0.0354  487 TYR B OH  
4906  N N   . ALA B 187 ? 0.9173 0.9930 0.8061 -0.1984 -0.0681 0.0242  488 ALA B N   
4907  C CA  . ALA B 187 ? 0.9242 0.9565 0.7895 -0.2190 -0.0695 0.0233  488 ALA B CA  
4908  C C   . ALA B 187 ? 0.8915 0.9343 0.7571 -0.2388 -0.0673 0.0294  488 ALA B C   
4909  O O   . ALA B 187 ? 0.9185 1.0117 0.8013 -0.2452 -0.0669 0.0322  488 ALA B O   
4910  C CB  . ALA B 187 ? 0.9295 0.9564 0.7805 -0.2366 -0.0758 0.0159  488 ALA B CB  
4911  N N   . GLY B 188 ? 0.8272 0.8217 0.6721 -0.2479 -0.0658 0.0318  489 GLY B N   
4912  C CA  . GLY B 188 ? 0.7717 0.7675 0.6115 -0.2689 -0.0635 0.0381  489 GLY B CA  
4913  C C   . GLY B 188 ? 0.8927 0.8504 0.7040 -0.2980 -0.0666 0.0361  489 GLY B C   
4914  O O   . GLY B 188 ? 0.9771 0.8806 0.7648 -0.2950 -0.0679 0.0324  489 GLY B O   
4915  N N   . TYR B 189 ? 0.8862 0.8711 0.6980 -0.3265 -0.0674 0.0385  490 TYR B N   
4916  C CA  . TYR B 189 ? 0.8271 0.7820 0.6120 -0.3589 -0.0709 0.0355  490 TYR B CA  
4917  C C   . TYR B 189 ? 0.9347 0.8713 0.7058 -0.3802 -0.0670 0.0440  490 TYR B C   
4918  O O   . TYR B 189 ? 0.8964 0.8767 0.6867 -0.3828 -0.0634 0.0509  490 TYR B O   
4919  C CB  . TYR B 189 ? 0.8828 0.8886 0.6782 -0.3791 -0.0763 0.0299  490 TYR B CB  
4920  C CG  . TYR B 189 ? 0.8551 0.8785 0.6614 -0.3594 -0.0806 0.0219  490 TYR B CG  
4921  C CD1 . TYR B 189 ? 0.8065 0.8944 0.6437 -0.3434 -0.0807 0.0223  490 TYR B CD1 
4922  C CD2 . TYR B 189 ? 0.8746 0.8490 0.6585 -0.3557 -0.0841 0.0141  490 TYR B CD2 
4923  C CE1 . TYR B 189 ? 0.8476 0.9499 0.6927 -0.3251 -0.0843 0.0160  490 TYR B CE1 
4924  C CE2 . TYR B 189 ? 0.9229 0.9141 0.7157 -0.3381 -0.0876 0.0073  490 TYR B CE2 
4925  C CZ  . TYR B 189 ? 0.9179 0.9730 0.7414 -0.3234 -0.0878 0.0086  490 TYR B CZ  
4926  O OH  . TYR B 189 ? 0.8930 0.9639 0.7239 -0.3054 -0.0910 0.0029  490 TYR B OH  
4927  N N   . LYS B 190 ? 0.9651 0.8359 0.7008 -0.3950 -0.0675 0.0435  491 LYS B N   
4928  C CA  . LYS B 190 ? 0.9861 0.8254 0.7018 -0.4100 -0.0631 0.0519  491 LYS B CA  
4929  C C   . LYS B 190 ? 1.1439 1.0000 0.8495 -0.4373 -0.0639 0.0503  491 LYS B C   
4930  O O   . LYS B 190 ? 1.2574 1.0738 0.9354 -0.4484 -0.0664 0.0444  491 LYS B O   
4931  C CB  . LYS B 190 ? 1.0758 0.8343 0.7577 -0.3978 -0.0619 0.0522  491 LYS B CB  
4932  C CG  . LYS B 190 ? 1.1991 0.9254 0.8624 -0.4000 -0.0565 0.0616  491 LYS B CG  
4933  C CD  . LYS B 190 ? 1.2314 0.9937 0.9198 -0.3898 -0.0519 0.0714  491 LYS B CD  
4934  C CE  . LYS B 190 ? 1.2901 1.0273 0.9602 -0.3950 -0.0470 0.0804  491 LYS B CE  
4935  N NZ  . LYS B 190 ? 1.2953 1.0736 0.9897 -0.3876 -0.0424 0.0896  491 LYS B NZ  
4936  N N   . GLN B 191 ? 1.3275 1.2424 1.0542 -0.4479 -0.0614 0.0556  492 GLN B N   
4937  C CA  . GLN B 191 ? 1.4183 1.3630 1.1407 -0.4737 -0.0624 0.0542  492 GLN B CA  
4938  C C   . GLN B 191 ? 1.4998 1.3874 1.1845 -0.4918 -0.0605 0.0565  492 GLN B C   
4939  O O   . GLN B 191 ? 1.5395 1.3756 1.2061 -0.4829 -0.0572 0.0616  492 GLN B O   
4940  C CB  . GLN B 191 ? 1.3076 1.3278 1.0603 -0.4771 -0.0594 0.0601  492 GLN B CB  
4941  C CG  . GLN B 191 ? 1.1811 1.2646 0.9707 -0.4595 -0.0611 0.0578  492 GLN B CG  
4942  C CD  . GLN B 191 ? 1.1436 1.2616 0.9403 -0.4659 -0.0667 0.0491  492 GLN B CD  
4943  O OE1 . GLN B 191 ? 1.1522 1.2376 0.9250 -0.4815 -0.0698 0.0434  492 GLN B OE1 
4944  N NE2 . GLN B 191 ? 1.0794 1.2638 0.9082 -0.4525 -0.0677 0.0482  492 GLN B NE2 
4945  N N   . PRO B 192 ? 1.4479 1.3438 1.1192 -0.5170 -0.0624 0.0528  493 PRO B N   
4946  C CA  . PRO B 192 ? 1.4465 1.2893 1.0806 -0.5362 -0.0606 0.0550  493 PRO B CA  
4947  C C   . PRO B 192 ? 1.5154 1.3652 1.1498 -0.5417 -0.0552 0.0655  493 PRO B C   
4948  O O   . PRO B 192 ? 1.4799 1.2722 1.0837 -0.5468 -0.0527 0.0693  493 PRO B O   
4949  C CB  . PRO B 192 ? 1.3074 1.1742 0.9341 -0.5630 -0.0639 0.0488  493 PRO B CB  
4950  C CG  . PRO B 192 ? 1.1893 1.1391 0.8553 -0.5590 -0.0659 0.0469  493 PRO B CG  
4951  C CD  . PRO B 192 ? 1.2607 1.2104 0.9472 -0.5283 -0.0666 0.0460  493 PRO B CD  
4952  N N   . ASP B 193 ? 1.4796 1.3989 1.1472 -0.5396 -0.0532 0.0702  494 ASP B N   
4953  C CA  . ASP B 193 ? 1.3591 1.2917 1.0297 -0.5436 -0.0480 0.0800  494 ASP B CA  
4954  C C   . ASP B 193 ? 1.3848 1.2993 1.0642 -0.5172 -0.0444 0.0863  494 ASP B C   
4955  O O   . ASP B 193 ? 1.4242 1.3719 1.1193 -0.5141 -0.0402 0.0940  494 ASP B O   
4956  C CB  . ASP B 193 ? 1.2857 1.3034 0.9852 -0.5540 -0.0473 0.0820  494 ASP B CB  
4957  C CG  . ASP B 193 ? 1.2174 1.2938 0.9519 -0.5369 -0.0497 0.0774  494 ASP B CG  
4958  O OD1 . ASP B 193 ? 1.0751 1.1800 0.8345 -0.5159 -0.0470 0.0816  494 ASP B OD1 
4959  O OD2 . ASP B 193 ? 1.1870 1.2806 0.9231 -0.5443 -0.0542 0.0698  494 ASP B OD2 
4960  N N   . GLY B 194 ? 1.3065 1.1707 0.9758 -0.4979 -0.0458 0.0833  495 GLY B N   
4961  C CA  . GLY B 194 ? 1.1187 0.9591 0.7913 -0.4737 -0.0423 0.0897  495 GLY B CA  
4962  C C   . GLY B 194 ? 1.1835 1.0777 0.8937 -0.4543 -0.0415 0.0908  495 GLY B C   
4963  O O   . GLY B 194 ? 1.1857 1.0580 0.8991 -0.4319 -0.0398 0.0939  495 GLY B O   
4964  N N   . SER B 195 ? 1.3500 1.3145 1.0877 -0.4616 -0.0427 0.0885  496 SER B N   
4965  C CA  . SER B 195 ? 1.3603 1.3803 1.1339 -0.4429 -0.0418 0.0892  496 SER B CA  
4966  C C   . SER B 195 ? 1.2844 1.2907 1.0638 -0.4280 -0.0463 0.0817  496 SER B C   
4967  O O   . SER B 195 ? 1.3221 1.2742 1.0772 -0.4301 -0.0497 0.0763  496 SER B O   
4968  C CB  . SER B 195 ? 1.3966 1.4957 1.1952 -0.4529 -0.0415 0.0890  496 SER B CB  
4969  O OG  . SER B 195 ? 1.3906 1.5076 1.1882 -0.4662 -0.0467 0.0809  496 SER B OG  
4970  N N   . THR B 196 ? 1.1706 1.2259 0.9814 -0.4117 -0.0463 0.0810  497 THR B N   
4971  C CA  . THR B 196 ? 1.1759 1.2177 0.9925 -0.3865 -0.0500 0.0729  497 THR B CA  
4972  C C   . THR B 196 ? 1.1484 1.2597 0.9978 -0.3723 -0.0516 0.0687  497 THR B C   
4973  O O   . THR B 196 ? 1.1815 1.3336 1.0526 -0.3559 -0.0476 0.0727  497 THR B O   
4974  C CB  . THR B 196 ? 1.1524 1.1526 0.9645 -0.3555 -0.0469 0.0754  497 THR B CB  
4975  O OG1 . THR B 196 ? 1.2258 1.1614 1.0056 -0.3661 -0.0454 0.0801  497 THR B OG1 
4976  C CG2 . THR B 196 ? 1.0074 0.9935 0.8240 -0.3300 -0.0505 0.0669  497 THR B CG2 
4977  N N   . LEU B 197 ? 1.0622 1.1842 0.9128 -0.3771 -0.0575 0.0604  498 LEU B N   
4978  C CA  . LEU B 197 ? 1.0031 1.1848 0.8808 -0.3612 -0.0597 0.0560  498 LEU B CA  
4979  C C   . LEU B 197 ? 0.9748 1.1313 0.8551 -0.3285 -0.0610 0.0508  498 LEU B C   
4980  O O   . LEU B 197 ? 1.0127 1.1129 0.8721 -0.3272 -0.0631 0.0469  498 LEU B O   
4981  C CB  . LEU B 197 ? 0.9984 1.2140 0.8763 -0.3874 -0.0658 0.0505  498 LEU B CB  
4982  C CG  . LEU B 197 ? 0.8729 1.1167 0.7635 -0.3716 -0.0711 0.0424  498 LEU B CG  
4983  C CD1 . LEU B 197 ? 0.7336 1.0576 0.6549 -0.3588 -0.0704 0.0440  498 LEU B CD1 
4984  C CD2 . LEU B 197 ? 0.9572 1.1883 0.8300 -0.3987 -0.0782 0.0348  498 LEU B CD2 
4985  N N   . GLY B 198 ? 0.8891 1.0864 0.7935 -0.3023 -0.0593 0.0507  499 GLY B N   
4986  C CA  . GLY B 198 ? 0.8134 0.9923 0.7216 -0.2721 -0.0599 0.0465  499 GLY B CA  
4987  C C   . GLY B 198 ? 0.9338 1.0897 0.8450 -0.2486 -0.0543 0.0508  499 GLY B C   
4988  O O   . GLY B 198 ? 0.9390 1.1225 0.8623 -0.2441 -0.0499 0.0562  499 GLY B O   
4989  N N   . ASP B 199 ? 0.9745 1.0824 0.8745 -0.2336 -0.0546 0.0482  500 ASP B N   
4990  C CA  . ASP B 199 ? 1.0124 1.0976 0.9140 -0.2123 -0.0500 0.0515  500 ASP B CA  
4991  C C   . ASP B 199 ? 1.0553 1.0857 0.9335 -0.2213 -0.0493 0.0542  500 ASP B C   
4992  O O   . ASP B 199 ? 1.1508 1.1403 1.0120 -0.2208 -0.0519 0.0501  500 ASP B O   
4993  C CB  . ASP B 199 ? 1.0849 1.1625 0.9929 -0.1860 -0.0503 0.0469  500 ASP B CB  
4994  C CG  . ASP B 199 ? 1.0960 1.1616 1.0094 -0.1644 -0.0457 0.0498  500 ASP B CG  
4995  O OD1 . ASP B 199 ? 1.1038 1.1373 1.0057 -0.1663 -0.0437 0.0534  500 ASP B OD1 
4996  O OD2 . ASP B 199 ? 1.0378 1.1256 0.9658 -0.1455 -0.0440 0.0485  500 ASP B OD2 
4997  N N   . PRO B 200 ? 0.8635 0.8904 0.7382 -0.2284 -0.0455 0.0612  501 PRO B N   
4998  C CA  . PRO B 200 ? 0.8752 0.8486 0.7240 -0.2384 -0.0450 0.0648  501 PRO B CA  
4999  C C   . PRO B 200 ? 0.8907 0.8195 0.7291 -0.2164 -0.0447 0.0632  501 PRO B C   
5000  O O   . PRO B 200 ? 0.8981 0.7777 0.7114 -0.2221 -0.0454 0.0640  501 PRO B O   
5001  C CB  . PRO B 200 ? 0.8263 0.8147 0.6779 -0.2457 -0.0404 0.0733  501 PRO B CB  
5002  C CG  . PRO B 200 ? 0.7665 0.8168 0.6402 -0.2528 -0.0400 0.0732  501 PRO B CG  
5003  C CD  . PRO B 200 ? 0.6556 0.7291 0.5468 -0.2320 -0.0420 0.0664  501 PRO B CD  
5004  N N   . ALA B 201 ? 0.7490 0.6935 0.6046 -0.1917 -0.0434 0.0610  502 ALA B N   
5005  C CA  . ALA B 201 ? 0.7604 0.6699 0.6085 -0.1712 -0.0429 0.0595  502 ALA B CA  
5006  C C   . ALA B 201 ? 0.9294 0.8072 0.7621 -0.1713 -0.0465 0.0532  502 ALA B C   
5007  O O   . ALA B 201 ? 0.9865 0.8230 0.8020 -0.1621 -0.0464 0.0530  502 ALA B O   
5008  C CB  . ALA B 201 ? 0.6783 0.6147 0.5481 -0.1484 -0.0407 0.0580  502 ALA B CB  
5009  N N   . ASN B 202 ? 0.9221 0.8204 0.7600 -0.1806 -0.0498 0.0480  503 ASN B N   
5010  C CA  . ASN B 202 ? 0.8441 0.7197 0.6701 -0.1787 -0.0534 0.0410  503 ASN B CA  
5011  C C   . ASN B 202 ? 0.9799 0.8232 0.7801 -0.2022 -0.0566 0.0390  503 ASN B C   
5012  O O   . ASN B 202 ? 1.1692 0.9935 0.9571 -0.2034 -0.0600 0.0323  503 ASN B O   
5013  C CB  . ASN B 202 ? 0.7173 0.6341 0.5625 -0.1737 -0.0554 0.0361  503 ASN B CB  
5014  C CG  . ASN B 202 ? 0.7970 0.7365 0.6628 -0.1497 -0.0521 0.0373  503 ASN B CG  
5015  O OD1 . ASN B 202 ? 0.8017 0.7178 0.6644 -0.1330 -0.0499 0.0377  503 ASN B OD1 
5016  N ND2 . ASN B 202 ? 0.7305 0.7158 0.6163 -0.1478 -0.0516 0.0379  503 ASN B ND2 
5017  N N   . VAL B 203 ? 0.9739 0.8089 0.7638 -0.2215 -0.0554 0.0447  504 VAL B N   
5018  C CA  . VAL B 203 ? 1.0046 0.8065 0.7674 -0.2474 -0.0582 0.0430  504 VAL B CA  
5019  C C   . VAL B 203 ? 1.0177 0.7603 0.7524 -0.2381 -0.0595 0.0385  504 VAL B C   
5020  O O   . VAL B 203 ? 1.1653 0.8871 0.8822 -0.2511 -0.0635 0.0317  504 VAL B O   
5021  C CB  . VAL B 203 ? 1.0317 0.8259 0.7844 -0.2672 -0.0555 0.0515  504 VAL B CB  
5022  C CG1 . VAL B 203 ? 1.0681 0.8152 0.7863 -0.2937 -0.0578 0.0501  504 VAL B CG1 
5023  C CG2 . VAL B 203 ? 0.9452 0.8025 0.7244 -0.2791 -0.0544 0.0548  504 VAL B CG2 
5024  N N   . GLN B 204 ? 0.9466 0.6640 0.6773 -0.2143 -0.0564 0.0416  505 GLN B N   
5025  C CA  . GLN B 204 ? 1.0047 0.6681 0.7082 -0.2029 -0.0573 0.0374  505 GLN B CA  
5026  C C   . GLN B 204 ? 1.0235 0.6973 0.7341 -0.1909 -0.0600 0.0284  505 GLN B C   
5027  O O   . GLN B 204 ? 1.0474 0.6857 0.7339 -0.1951 -0.0627 0.0218  505 GLN B O   
5028  C CB  . GLN B 204 ? 1.0061 0.6455 0.7042 -0.1792 -0.0535 0.0432  505 GLN B CB  
5029  C CG  . GLN B 204 ? 1.1256 0.6983 0.7839 -0.1773 -0.0536 0.0427  505 GLN B CG  
5030  C CD  . GLN B 204 ? 1.2049 0.7564 0.8578 -0.1464 -0.0510 0.0448  505 GLN B CD  
5031  O OE1 . GLN B 204 ? 1.1940 0.7804 0.8732 -0.1270 -0.0495 0.0449  505 GLN B OE1 
5032  N NE2 . GLN B 204 ? 1.2368 0.7309 0.8542 -0.1418 -0.0504 0.0466  505 GLN B NE2 
5033  N N   . PHE B 205 ? 0.9627 0.6824 0.7039 -0.1760 -0.0591 0.0279  506 PHE B N   
5034  C CA  . PHE B 205 ? 0.8438 0.5752 0.5915 -0.1656 -0.0613 0.0202  506 PHE B CA  
5035  C C   . PHE B 205 ? 0.9769 0.7230 0.7213 -0.1884 -0.0663 0.0144  506 PHE B C   
5036  O O   . PHE B 205 ? 1.1217 0.8457 0.8491 -0.1901 -0.0694 0.0069  506 PHE B O   
5037  C CB  . PHE B 205 ? 0.6922 0.4668 0.4710 -0.1459 -0.0589 0.0219  506 PHE B CB  
5038  C CG  . PHE B 205 ? 0.8887 0.6701 0.6720 -0.1312 -0.0600 0.0154  506 PHE B CG  
5039  C CD1 . PHE B 205 ? 0.8756 0.6256 0.6459 -0.1133 -0.0586 0.0128  506 PHE B CD1 
5040  C CD2 . PHE B 205 ? 0.9495 0.7701 0.7495 -0.1344 -0.0623 0.0124  506 PHE B CD2 
5041  C CE1 . PHE B 205 ? 0.8974 0.6546 0.6712 -0.1004 -0.0591 0.0074  506 PHE B CE1 
5042  C CE2 . PHE B 205 ? 0.9352 0.7610 0.7377 -0.1207 -0.0631 0.0072  506 PHE B CE2 
5043  C CZ  . PHE B 205 ? 0.8541 0.6480 0.6436 -0.1045 -0.0613 0.0048  506 PHE B CZ  
5044  N N   . THR B 206 ? 0.8375 0.6226 0.5973 -0.2063 -0.0670 0.0176  507 THR B N   
5045  C CA  . THR B 206 ? 0.8130 0.6189 0.5710 -0.2301 -0.0719 0.0125  507 THR B CA  
5046  C C   . THR B 206 ? 0.9824 0.7381 0.7052 -0.2512 -0.0751 0.0079  507 THR B C   
5047  O O   . THR B 206 ? 0.9939 0.7559 0.7090 -0.2674 -0.0801 0.0007  507 THR B O   
5048  C CB  . THR B 206 ? 0.8000 0.6543 0.5779 -0.2463 -0.0714 0.0181  507 THR B CB  
5049  O OG1 . THR B 206 ? 0.8610 0.7583 0.6686 -0.2253 -0.0683 0.0216  507 THR B OG1 
5050  C CG2 . THR B 206 ? 0.6965 0.5807 0.4748 -0.2714 -0.0767 0.0130  507 THR B CG2 
5051  N N   . GLU B 207 ? 1.1860 0.8901 0.8847 -0.2510 -0.0724 0.0116  508 GLU B N   
5052  C CA  . GLU B 207 ? 1.2897 0.9381 0.9501 -0.2690 -0.0751 0.0066  508 GLU B CA  
5053  C C   . GLU B 207 ? 1.2825 0.8929 0.9244 -0.2494 -0.0762 -0.0013 508 GLU B C   
5054  O O   . GLU B 207 ? 1.3512 0.9349 0.9689 -0.2634 -0.0803 -0.0097 508 GLU B O   
5055  C CB  . GLU B 207 ? 1.3978 1.0032 1.0355 -0.2786 -0.0717 0.0143  508 GLU B CB  
5056  C CG  . GLU B 207 ? 1.5687 1.2030 1.2137 -0.3093 -0.0717 0.0199  508 GLU B CG  
5057  C CD  . GLU B 207 ? 1.7859 1.3846 1.4125 -0.3160 -0.0674 0.0296  508 GLU B CD  
5058  O OE1 . GLU B 207 ? 1.9040 1.4558 1.5123 -0.2950 -0.0647 0.0321  508 GLU B OE1 
5059  O OE2 . GLU B 207 ? 1.8031 1.4229 1.4334 -0.3417 -0.0666 0.0351  508 GLU B OE2 
5060  N N   . ILE B 208 ? 1.2269 0.8371 0.8799 -0.2177 -0.0726 0.0008  509 ILE B N   
5061  C CA  . ILE B 208 ? 1.1619 0.7410 0.7987 -0.1975 -0.0730 -0.0063 509 ILE B CA  
5062  C C   . ILE B 208 ? 1.1812 0.7910 0.8283 -0.2002 -0.0773 -0.0148 509 ILE B C   
5063  O O   . ILE B 208 ? 1.2692 0.8485 0.8920 -0.2021 -0.0802 -0.0235 509 ILE B O   
5064  C CB  . ILE B 208 ? 1.0073 0.5888 0.6572 -0.1646 -0.0681 -0.0017 509 ILE B CB  
5065  C CG1 . ILE B 208 ? 1.0892 0.6484 0.7319 -0.1615 -0.0643 0.0076  509 ILE B CG1 
5066  C CG2 . ILE B 208 ? 0.9485 0.4952 0.5781 -0.1444 -0.0679 -0.0084 509 ILE B CG2 
5067  C CD1 . ILE B 208 ? 1.0986 0.6665 0.7560 -0.1312 -0.0599 0.0123  509 ILE B CD1 
5068  N N   . CYS B 209 ? 1.0587 0.7284 0.7403 -0.1989 -0.0776 -0.0124 510 CYS B N   
5069  C CA  . CYS B 209 ? 0.9990 0.7042 0.6911 -0.2048 -0.0821 -0.0190 510 CYS B CA  
5070  C C   . CYS B 209 ? 1.1576 0.8471 0.8263 -0.2353 -0.0878 -0.0260 510 CYS B C   
5071  O O   . CYS B 209 ? 1.1919 0.8656 0.8435 -0.2368 -0.0916 -0.0351 510 CYS B O   
5072  C CB  . CYS B 209 ? 0.8802 0.6497 0.6090 -0.2032 -0.0814 -0.0137 510 CYS B CB  
5073  S SG  . CYS B 209 ? 0.9077 0.6977 0.6629 -0.1690 -0.0755 -0.0077 510 CYS B SG  
5074  N N   . ILE B 210 ? 1.1921 0.8872 0.8591 -0.2611 -0.0885 -0.0218 511 ILE B N   
5075  C CA  . ILE B 210 ? 1.2198 0.9006 0.8638 -0.2945 -0.0939 -0.0281 511 ILE B CA  
5076  C C   . ILE B 210 ? 1.3121 0.9201 0.9136 -0.2951 -0.0948 -0.0353 511 ILE B C   
5077  O O   . ILE B 210 ? 1.2841 0.8795 0.8669 -0.3063 -0.0999 -0.0455 511 ILE B O   
5078  C CB  . ILE B 210 ? 1.1077 0.7995 0.7538 -0.3217 -0.0930 -0.0211 511 ILE B CB  
5079  C CG1 . ILE B 210 ? 1.0575 0.8272 0.7417 -0.3271 -0.0939 -0.0170 511 ILE B CG1 
5080  C CG2 . ILE B 210 ? 1.1685 0.8242 0.7806 -0.3564 -0.0973 -0.0271 511 ILE B CG2 
5081  C CD1 . ILE B 210 ? 1.0340 0.8216 0.7275 -0.3440 -0.0906 -0.0075 511 ILE B CD1 
5082  N N   . GLN B 211 ? 1.3851 0.9445 0.9696 -0.2812 -0.0899 -0.0303 512 GLN B N   
5083  C CA  . GLN B 211 ? 1.4307 0.9170 0.9728 -0.2761 -0.0896 -0.0360 512 GLN B CA  
5084  C C   . GLN B 211 ? 1.3188 0.7995 0.8574 -0.2514 -0.0905 -0.0444 512 GLN B C   
5085  O O   . GLN B 211 ? 1.3665 0.7908 0.8685 -0.2480 -0.0913 -0.0517 512 GLN B O   
5086  C CB  . GLN B 211 ? 1.5355 0.9820 1.0660 -0.2611 -0.0837 -0.0268 512 GLN B CB  
5087  C CG  . GLN B 211 ? 1.6463 1.0121 1.1283 -0.2580 -0.0827 -0.0303 512 GLN B CG  
5088  C CD  . GLN B 211 ? 1.7000 1.0438 1.1760 -0.2200 -0.0797 -0.0326 512 GLN B CD  
5089  O OE1 . GLN B 211 ? 1.6888 1.0730 1.1972 -0.1953 -0.0767 -0.0279 512 GLN B OE1 
5090  N NE2 . GLN B 211 ? 1.7167 1.0054 1.1549 -0.2124 -0.0793 -0.0388 512 GLN B NE2 
5091  N N   . GLN B 212 ? 1.2283 0.7644 0.8019 -0.2343 -0.0903 -0.0436 513 GLN B N   
5092  C CA  . GLN B 212 ? 1.2716 0.8084 0.8438 -0.2124 -0.0909 -0.0509 513 GLN B CA  
5093  C C   . GLN B 212 ? 1.1505 0.7168 0.7249 -0.2281 -0.0973 -0.0599 513 GLN B C   
5094  O O   . GLN B 212 ? 1.0984 0.6689 0.6716 -0.2117 -0.0982 -0.0660 513 GLN B O   
5095  C CB  . GLN B 212 ? 1.3580 0.9323 0.9637 -0.1823 -0.0860 -0.0441 513 GLN B CB  
5096  C CG  . GLN B 212 ? 1.3826 0.9191 0.9769 -0.1568 -0.0803 -0.0404 513 GLN B CG  
5097  C CD  . GLN B 212 ? 1.4471 0.9310 1.0047 -0.1474 -0.0809 -0.0494 513 GLN B CD  
5098  O OE1 . GLN B 212 ? 1.5716 1.0002 1.0945 -0.1552 -0.0811 -0.0513 513 GLN B OE1 
5099  N NE2 . GLN B 212 ? 1.3684 0.8677 0.9313 -0.1304 -0.0810 -0.0550 513 GLN B NE2 
5100  N N   . GLY B 213 ? 1.1750 0.7641 0.7526 -0.2595 -0.1019 -0.0606 514 GLY B N   
5101  C CA  . GLY B 213 ? 1.1311 0.7564 0.7133 -0.2755 -0.1087 -0.0685 514 GLY B CA  
5102  C C   . GLY B 213 ? 1.0968 0.7977 0.7190 -0.2802 -0.1100 -0.0627 514 GLY B C   
5103  O O   . GLY B 213 ? 1.0518 0.7900 0.6800 -0.2929 -0.1160 -0.0685 514 GLY B O   
5104  N N   . TRP B 214 ? 1.0796 0.8059 0.7286 -0.2694 -0.1049 -0.0518 515 TRP B N   
5105  C CA  . TRP B 214 ? 1.0143 0.8109 0.6996 -0.2702 -0.1057 -0.0464 515 TRP B CA  
5106  C C   . TRP B 214 ? 1.1306 0.9538 0.8154 -0.3059 -0.1107 -0.0477 515 TRP B C   
5107  O O   . TRP B 214 ? 1.1381 0.9298 0.8044 -0.3284 -0.1102 -0.0464 515 TRP B O   
5108  C CB  . TRP B 214 ? 0.9498 0.7622 0.6600 -0.2513 -0.0989 -0.0353 515 TRP B CB  
5109  C CG  . TRP B 214 ? 0.9869 0.8671 0.7324 -0.2439 -0.0989 -0.0305 515 TRP B CG  
5110  C CD1 . TRP B 214 ? 0.9286 0.8436 0.6880 -0.2289 -0.1009 -0.0331 515 TRP B CD1 
5111  C CD2 . TRP B 214 ? 0.9651 0.8848 0.7338 -0.2497 -0.0965 -0.0222 515 TRP B CD2 
5112  N NE1 . TRP B 214 ? 0.9094 0.8808 0.6981 -0.2241 -0.0999 -0.0268 515 TRP B NE1 
5113  C CE2 . TRP B 214 ? 0.9264 0.9027 0.7216 -0.2365 -0.0972 -0.0205 515 TRP B CE2 
5114  C CE3 . TRP B 214 ? 1.0539 0.9660 0.8220 -0.2641 -0.0936 -0.0159 515 TRP B CE3 
5115  C CZ2 . TRP B 214 ? 0.9274 0.9523 0.7480 -0.2361 -0.0951 -0.0134 515 TRP B CZ2 
5116  C CZ3 . TRP B 214 ? 1.0147 0.9776 0.8094 -0.2648 -0.0915 -0.0087 515 TRP B CZ3 
5117  C CH2 . TRP B 214 ? 0.9856 1.0040 0.8060 -0.2504 -0.0923 -0.0079 515 TRP B CH2 
5118  N N   . LYS B 215 ? 1.1538 1.0357 0.8577 -0.3111 -0.1154 -0.0500 516 LYS B N   
5119  C CA  . LYS B 215 ? 1.1838 1.1077 0.8935 -0.3430 -0.1204 -0.0508 516 LYS B CA  
5120  C C   . LYS B 215 ? 1.1502 1.1270 0.8935 -0.3376 -0.1164 -0.0400 516 LYS B C   
5121  O O   . LYS B 215 ? 1.2157 1.2438 0.9858 -0.3182 -0.1162 -0.0371 516 LYS B O   
5122  C CB  . LYS B 215 ? 1.1638 1.1267 0.8756 -0.3492 -0.1281 -0.0594 516 LYS B CB  
5123  C CG  . LYS B 215 ? 1.1556 1.1478 0.8872 -0.3144 -0.1272 -0.0583 516 LYS B CG  
5124  C CD  . LYS B 215 ? 1.1970 1.1386 0.9057 -0.2966 -0.1269 -0.0653 516 LYS B CD  
5125  C CE  . LYS B 215 ? 1.2623 1.2297 0.9657 -0.2993 -0.1343 -0.0744 516 LYS B CE  
5126  N NZ  . LYS B 215 ? 1.2674 1.1814 0.9332 -0.3118 -0.1382 -0.0863 516 LYS B NZ  
5127  N N   . PRO B 216 ? 1.0701 1.0344 0.8112 -0.3526 -0.1128 -0.0336 517 PRO B N   
5128  C CA  . PRO B 216 ? 0.9814 0.9930 0.7527 -0.3449 -0.1084 -0.0236 517 PRO B CA  
5129  C C   . PRO B 216 ? 0.9838 1.0664 0.7738 -0.3649 -0.1128 -0.0237 517 PRO B C   
5130  O O   . PRO B 216 ? 1.0702 1.1541 0.8470 -0.3960 -0.1157 -0.0268 517 PRO B O   
5131  C CB  . PRO B 216 ? 1.0671 1.0359 0.8243 -0.3569 -0.1034 -0.0175 517 PRO B CB  
5132  C CG  . PRO B 216 ? 1.1323 1.0541 0.8540 -0.3875 -0.1077 -0.0247 517 PRO B CG  
5133  C CD  . PRO B 216 ? 1.1383 1.0439 0.8468 -0.3783 -0.1126 -0.0353 517 PRO B CD  
5134  N N   . PRO B 217 ? 0.8603 1.0025 0.6805 -0.3443 -0.1118 -0.0196 518 PRO B N   
5135  C CA  . PRO B 217 ? 0.8585 1.0743 0.6990 -0.3604 -0.1148 -0.0176 518 PRO B CA  
5136  C C   . PRO B 217 ? 0.8741 1.1039 0.7218 -0.3778 -0.1102 -0.0096 518 PRO B C   
5137  O O   . PRO B 217 ? 0.8854 1.1632 0.7442 -0.3902 -0.1083 -0.0068 518 PRO B O   
5138  C CB  . PRO B 217 ? 0.7889 1.0532 0.6557 -0.3266 -0.1138 -0.0147 518 PRO B CB  
5139  C CG  . PRO B 217 ? 0.7237 0.9406 0.5890 -0.2959 -0.1074 -0.0114 518 PRO B CG  
5140  C CD  . PRO B 217 ? 0.7232 0.8675 0.5584 -0.3055 -0.1080 -0.0167 518 PRO B CD  
5141  N N   . ARG B 218 ? 0.8604 1.0448 0.7021 -0.3687 -0.1037 -0.0039 519 ARG B N   
5142  C CA  . ARG B 218 ? 1.0178 1.2019 0.8594 -0.3873 -0.0992 0.0036  519 ARG B CA  
5143  C C   . ARG B 218 ? 1.1013 1.3613 0.9741 -0.3830 -0.0967 0.0103  519 ARG B C   
5144  O O   . ARG B 218 ? 1.0700 1.3585 0.9450 -0.4008 -0.0934 0.0142  519 ARG B O   
5145  C CB  . ARG B 218 ? 1.0466 1.2006 0.8621 -0.4187 -0.0988 0.0018  519 ARG B CB  
5146  C CG  . ARG B 218 ? 1.0784 1.1513 0.8593 -0.4227 -0.1006 -0.0043 519 ARG B CG  
5147  C CD  . ARG B 218 ? 1.1254 1.1568 0.8778 -0.4483 -0.0973 -0.0025 519 ARG B CD  
5148  N NE  . ARG B 218 ? 1.1705 1.1468 0.9071 -0.4453 -0.0924 0.0038  519 ARG B NE  
5149  C CZ  . ARG B 218 ? 1.2455 1.1460 0.9498 -0.4430 -0.0920 0.0010  519 ARG B CZ  
5150  N NH1 . ARG B 218 ? 1.2402 1.0964 0.9319 -0.4374 -0.0871 0.0079  519 ARG B NH1 
5151  N NH2 . ARG B 218 ? 1.2496 1.1194 0.9335 -0.4446 -0.0961 -0.0085 519 ARG B NH2 
5152  N N   . GLY B 219 ? 1.1438 1.4271 1.0373 -0.3477 -0.0937 0.0130  520 GLY B N   
5153  C CA  . GLY B 219 ? 1.1292 1.4718 1.0491 -0.3353 -0.0897 0.0197  520 GLY B CA  
5154  C C   . GLY B 219 ? 1.1378 1.4532 1.0617 -0.3144 -0.0819 0.0266  520 GLY B C   
5155  O O   . GLY B 219 ? 1.1369 1.3906 1.0428 -0.3154 -0.0795 0.0273  520 GLY B O   
5156  N N   . ARG B 220 ? 1.0942 1.4569 1.0408 -0.2943 -0.0780 0.0314  521 ARG B N   
5157  C CA  . ARG B 220 ? 1.0070 1.3472 0.9577 -0.2731 -0.0709 0.0370  521 ARG B CA  
5158  C C   . ARG B 220 ? 1.0538 1.3634 1.0045 -0.2410 -0.0700 0.0345  521 ARG B C   
5159  O O   . ARG B 220 ? 1.0526 1.3095 0.9922 -0.2327 -0.0671 0.0353  521 ARG B O   
5160  C CB  . ARG B 220 ? 0.9171 1.3170 0.8891 -0.2655 -0.0666 0.0428  521 ARG B CB  
5161  C CG  . ARG B 220 ? 0.9008 1.2807 0.8738 -0.2555 -0.0594 0.0490  521 ARG B CG  
5162  C CD  . ARG B 220 ? 1.0276 1.4486 1.0074 -0.2763 -0.0564 0.0547  521 ARG B CD  
5163  N NE  . ARG B 220 ? 1.0372 1.4318 1.0127 -0.2735 -0.0501 0.0608  521 ARG B NE  
5164  C CZ  . ARG B 220 ? 1.0079 1.4344 0.9971 -0.2577 -0.0445 0.0652  521 ARG B CZ  
5165  N NH1 . ARG B 220 ? 0.9380 1.4233 0.9456 -0.2422 -0.0441 0.0645  521 ARG B NH1 
5166  N NH2 . ARG B 220 ? 1.0419 1.4412 1.0250 -0.2564 -0.0394 0.0703  521 ARG B NH2 
5167  N N   . PHE B 221 ? 1.1077 1.4500 1.0693 -0.2234 -0.0724 0.0317  522 PHE B N   
5168  C CA  . PHE B 221 ? 1.0441 1.3633 1.0064 -0.1932 -0.0709 0.0302  522 PHE B CA  
5169  C C   . PHE B 221 ? 1.0226 1.3202 0.9727 -0.1950 -0.0767 0.0235  522 PHE B C   
5170  O O   . PHE B 221 ? 1.0422 1.3657 0.9983 -0.1809 -0.0793 0.0212  522 PHE B O   
5171  C CB  . PHE B 221 ? 0.9949 1.3615 0.9755 -0.1683 -0.0683 0.0330  522 PHE B CB  
5172  C CG  . PHE B 221 ? 0.9629 1.3481 0.9535 -0.1644 -0.0623 0.0388  522 PHE B CG  
5173  C CD1 . PHE B 221 ? 0.9398 1.3830 0.9460 -0.1538 -0.0607 0.0415  522 PHE B CD1 
5174  C CD2 . PHE B 221 ? 1.0439 1.3892 1.0271 -0.1703 -0.0583 0.0415  522 PHE B CD2 
5175  C CE1 . PHE B 221 ? 0.9803 1.4404 0.9943 -0.1498 -0.0549 0.0464  522 PHE B CE1 
5176  C CE2 . PHE B 221 ? 1.0749 1.4372 1.0661 -0.1670 -0.0528 0.0467  522 PHE B CE2 
5177  C CZ  . PHE B 221 ? 1.0426 1.4620 1.0492 -0.1570 -0.0510 0.0489  522 PHE B CZ  
5178  N N   . ASP B 222 ? 0.8783 1.1259 0.8091 -0.2113 -0.0783 0.0204  523 ASP B N   
5179  C CA  . ASP B 222 ? 0.6474 0.8643 0.5626 -0.2126 -0.0829 0.0135  523 ASP B CA  
5180  C C   . ASP B 222 ? 0.7087 0.8830 0.6195 -0.1871 -0.0791 0.0137  523 ASP B C   
5181  O O   . ASP B 222 ? 0.7766 0.9093 0.6785 -0.1867 -0.0755 0.0157  523 ASP B O   
5182  C CB  . ASP B 222 ? 0.6252 0.8063 0.5184 -0.2425 -0.0862 0.0099  523 ASP B CB  
5183  C CG  . ASP B 222 ? 0.8342 1.0567 0.7290 -0.2724 -0.0910 0.0084  523 ASP B CG  
5184  O OD1 . ASP B 222 ? 0.9137 1.1978 0.8281 -0.2683 -0.0923 0.0099  523 ASP B OD1 
5185  O OD2 . ASP B 222 ? 0.8455 1.0388 0.7206 -0.3001 -0.0935 0.0056  523 ASP B OD2 
5186  N N   . VAL B 223 ? 0.6449 0.8304 0.5612 -0.1659 -0.0797 0.0119  524 VAL B N   
5187  C CA  . VAL B 223 ? 0.5021 0.6487 0.4133 -0.1443 -0.0760 0.0118  524 VAL B CA  
5188  C C   . VAL B 223 ? 0.6039 0.7008 0.4933 -0.1544 -0.0782 0.0066  524 VAL B C   
5189  O O   . VAL B 223 ? 0.6999 0.7959 0.5782 -0.1660 -0.0837 0.0007  524 VAL B O   
5190  C CB  . VAL B 223 ? 0.4811 0.6475 0.3997 -0.1217 -0.0761 0.0114  524 VAL B CB  
5191  C CG1 . VAL B 223 ? 0.4098 0.5368 0.3228 -0.1026 -0.0718 0.0116  524 VAL B CG1 
5192  C CG2 . VAL B 223 ? 0.4011 0.6143 0.3381 -0.1095 -0.0738 0.0164  524 VAL B CG2 
5193  N N   . LEU B 224 ? 0.5960 0.6521 0.4779 -0.1497 -0.0741 0.0086  525 LEU B N   
5194  C CA  . LEU B 224 ? 0.7013 0.7079 0.5605 -0.1563 -0.0755 0.0042  525 LEU B CA  
5195  C C   . LEU B 224 ? 0.6790 0.6743 0.5319 -0.1413 -0.0768 -0.0009 525 LEU B C   
5196  O O   . LEU B 224 ? 0.7843 0.7997 0.6502 -0.1222 -0.0746 0.0010  525 LEU B O   
5197  C CB  . LEU B 224 ? 0.7258 0.6959 0.5796 -0.1497 -0.0705 0.0083  525 LEU B CB  
5198  C CG  . LEU B 224 ? 0.7719 0.7401 0.6242 -0.1668 -0.0693 0.0130  525 LEU B CG  
5199  C CD1 . LEU B 224 ? 0.6773 0.6318 0.5355 -0.1519 -0.0635 0.0189  525 LEU B CD1 
5200  C CD2 . LEU B 224 ? 0.9517 0.8800 0.7778 -0.1873 -0.0723 0.0095  525 LEU B CD2 
5201  N N   . PRO B 225 ? 0.5930 0.5554 0.4241 -0.1498 -0.0801 -0.0073 526 PRO B N   
5202  C CA  . PRO B 225 ? 0.5518 0.4983 0.3746 -0.1342 -0.0803 -0.0119 526 PRO B CA  
5203  C C   . PRO B 225 ? 0.6849 0.6059 0.5090 -0.1134 -0.0741 -0.0085 526 PRO B C   
5204  O O   . PRO B 225 ? 0.7829 0.6946 0.6116 -0.1122 -0.0704 -0.0034 526 PRO B O   
5205  C CB  . PRO B 225 ? 0.6200 0.5322 0.4159 -0.1506 -0.0849 -0.0197 526 PRO B CB  
5206  C CG  . PRO B 225 ? 0.7503 0.6395 0.5370 -0.1675 -0.0843 -0.0173 526 PRO B CG  
5207  C CD  . PRO B 225 ? 0.7350 0.6674 0.5449 -0.1736 -0.0831 -0.0105 526 PRO B CD  
5208  N N   . LEU B 226 ? 0.6920 0.6036 0.5115 -0.0974 -0.0730 -0.0113 527 LEU B N   
5209  C CA  . LEU B 226 ? 0.7108 0.5960 0.5275 -0.0797 -0.0677 -0.0095 527 LEU B CA  
5210  C C   . LEU B 226 ? 0.8395 0.6797 0.6303 -0.0831 -0.0688 -0.0148 527 LEU B C   
5211  O O   . LEU B 226 ? 1.0188 0.8482 0.7928 -0.0935 -0.0735 -0.0216 527 LEU B O   
5212  C CB  . LEU B 226 ? 0.5927 0.4924 0.4171 -0.0612 -0.0652 -0.0093 527 LEU B CB  
5213  C CG  . LEU B 226 ? 0.5930 0.5274 0.4398 -0.0527 -0.0624 -0.0031 527 LEU B CG  
5214  C CD1 . LEU B 226 ? 0.4461 0.3908 0.2955 -0.0371 -0.0604 -0.0029 527 LEU B CD1 
5215  C CD2 . LEU B 226 ? 0.4552 0.3836 0.3122 -0.0468 -0.0571 0.0027  527 LEU B CD2 
5216  N N   . LEU B 227 ? 0.8174 0.6310 0.6033 -0.0739 -0.0646 -0.0120 528 LEU B N   
5217  C CA  . LEU B 227 ? 0.8129 0.5816 0.5724 -0.0708 -0.0647 -0.0166 528 LEU B CA  
5218  C C   . LEU B 227 ? 0.8858 0.6501 0.6486 -0.0471 -0.0595 -0.0154 528 LEU B C   
5219  O O   . LEU B 227 ? 0.8393 0.5984 0.6080 -0.0377 -0.0555 -0.0103 528 LEU B O   
5220  C CB  . LEU B 227 ? 0.6926 0.4308 0.4386 -0.0805 -0.0645 -0.0142 528 LEU B CB  
5221  C CG  . LEU B 227 ? 0.7930 0.4951 0.5101 -0.0998 -0.0689 -0.0195 528 LEU B CG  
5222  C CD1 . LEU B 227 ? 0.8624 0.5271 0.5635 -0.1020 -0.0668 -0.0153 528 LEU B CD1 
5223  C CD2 . LEU B 227 ? 0.8450 0.5213 0.5389 -0.0952 -0.0710 -0.0285 528 LEU B CD2 
5224  N N   . LEU B 228 ? 0.9097 0.6776 0.6682 -0.0380 -0.0596 -0.0200 529 LEU B N   
5225  C CA  . LEU B 228 ? 0.8355 0.6082 0.6003 -0.0171 -0.0543 -0.0183 529 LEU B CA  
5226  C C   . LEU B 228 ? 0.8476 0.5845 0.5882 -0.0060 -0.0530 -0.0231 529 LEU B C   
5227  O O   . LEU B 228 ? 0.7344 0.4480 0.4525 -0.0120 -0.0567 -0.0303 529 LEU B O   
5228  C CB  . LEU B 228 ? 0.7135 0.5155 0.4893 -0.0126 -0.0543 -0.0189 529 LEU B CB  
5229  C CG  . LEU B 228 ? 0.6709 0.5056 0.4675 -0.0222 -0.0557 -0.0142 529 LEU B CG  
5230  C CD1 . LEU B 228 ? 0.4772 0.3398 0.2846 -0.0153 -0.0550 -0.0130 529 LEU B CD1 
5231  C CD2 . LEU B 228 ? 0.6140 0.4555 0.4266 -0.0192 -0.0518 -0.0072 529 LEU B CD2 
5232  N N   . GLN B 229 ? 0.8128 0.5454 0.5570 0.0100  -0.0479 -0.0193 530 GLN B N   
5233  C CA  . GLN B 229 ? 0.7896 0.4924 0.5124 0.0252  -0.0456 -0.0228 530 GLN B CA  
5234  C C   . GLN B 229 ? 0.8617 0.5853 0.5951 0.0442  -0.0401 -0.0213 530 GLN B C   
5235  O O   . GLN B 229 ? 0.8569 0.6057 0.6121 0.0491  -0.0364 -0.0149 530 GLN B O   
5236  C CB  . GLN B 229 ? 0.8299 0.5081 0.5438 0.0284  -0.0445 -0.0192 530 GLN B CB  
5237  C CG  . GLN B 229 ? 0.9518 0.6037 0.6451 0.0490  -0.0414 -0.0217 530 GLN B CG  
5238  C CD  . GLN B 229 ? 1.0498 0.6848 0.7379 0.0573  -0.0395 -0.0162 530 GLN B CD  
5239  O OE1 . GLN B 229 ? 0.9395 0.5747 0.6347 0.0452  -0.0410 -0.0113 530 GLN B OE1 
5240  N NE2 . GLN B 229 ? 1.1508 0.7730 0.8259 0.0792  -0.0360 -0.0170 530 GLN B NE2 
5241  N N   . ALA B 230 ? 0.7996 0.5121 0.5162 0.0540  -0.0394 -0.0274 531 ALA B N   
5242  C CA  . ALA B 230 ? 0.7201 0.4522 0.4436 0.0709  -0.0340 -0.0266 531 ALA B CA  
5243  C C   . ALA B 230 ? 0.8091 0.5170 0.5111 0.0892  -0.0312 -0.0302 531 ALA B C   
5244  O O   . ALA B 230 ? 0.9138 0.5846 0.5886 0.0887  -0.0342 -0.0363 531 ALA B O   
5245  C CB  . ALA B 230 ? 0.7080 0.4549 0.4315 0.0683  -0.0350 -0.0301 531 ALA B CB  
5246  N N   . ASN B 231 ? 0.8589 0.5883 0.5720 0.1054  -0.0252 -0.0265 532 ASN B N   
5247  C CA  . ASN B 231 ? 0.9726 0.6887 0.6694 0.1266  -0.0214 -0.0285 532 ASN B CA  
5248  C C   . ASN B 231 ? 0.9250 0.5952 0.5932 0.1300  -0.0244 -0.0323 532 ASN B C   
5249  O O   . ASN B 231 ? 0.9554 0.5968 0.5958 0.1395  -0.0247 -0.0395 532 ASN B O   
5250  C CB  . ASN B 231 ? 1.0460 0.7671 0.7319 0.1378  -0.0187 -0.0339 532 ASN B CB  
5251  C CG  . ASN B 231 ? 1.1477 0.8828 0.8330 0.1608  -0.0121 -0.0325 532 ASN B CG  
5252  O OD1 . ASN B 231 ? 1.1764 0.9385 0.8825 0.1648  -0.0086 -0.0256 532 ASN B OD1 
5253  N ND2 . ASN B 231 ? 1.1610 0.8796 0.8221 0.1762  -0.0104 -0.0392 532 ASN B ND2 
5254  N N   . GLY B 232 ? 0.8796 0.5405 0.5524 0.1221  -0.0265 -0.0275 533 GLY B N   
5255  C CA  . GLY B 232 ? 0.9677 0.5834 0.6126 0.1257  -0.0286 -0.0292 533 GLY B CA  
5256  C C   . GLY B 232 ? 1.0556 0.6296 0.6739 0.1092  -0.0342 -0.0360 533 GLY B C   
5257  O O   . GLY B 232 ? 1.0892 0.6241 0.6857 0.1060  -0.0363 -0.0359 533 GLY B O   
5258  N N   . ASN B 233 ? 0.9879 0.5697 0.6065 0.0978  -0.0367 -0.0416 534 ASN B N   
5259  C CA  . ASN B 233 ? 1.0909 0.6341 0.6809 0.0833  -0.0421 -0.0499 534 ASN B CA  
5260  C C   . ASN B 233 ? 1.0686 0.6048 0.6631 0.0573  -0.0470 -0.0471 534 ASN B C   
5261  O O   . ASN B 233 ? 0.9813 0.5431 0.6014 0.0517  -0.0461 -0.0389 534 ASN B O   
5262  C CB  . ASN B 233 ? 1.0604 0.6190 0.6498 0.0801  -0.0435 -0.0568 534 ASN B CB  
5263  C CG  . ASN B 233 ? 1.0408 0.5970 0.6170 0.1051  -0.0387 -0.0611 534 ASN B CG  
5264  O OD1 . ASN B 233 ? 1.2264 0.7413 0.7699 0.1172  -0.0382 -0.0670 534 ASN B OD1 
5265  N ND2 . ASN B 233 ? 0.9196 0.5188 0.5192 0.1134  -0.0348 -0.0581 534 ASN B ND2 
5266  N N   . ASP B 234 ? 1.1111 0.6120 0.6789 0.0406  -0.0521 -0.0543 535 ASP B N   
5267  C CA  . ASP B 234 ? 1.0454 0.5409 0.6154 0.0135  -0.0567 -0.0522 535 ASP B CA  
5268  C C   . ASP B 234 ? 0.9569 0.5060 0.5627 -0.0004 -0.0585 -0.0485 535 ASP B C   
5269  O O   . ASP B 234 ? 0.9158 0.4926 0.5327 0.0040  -0.0585 -0.0513 535 ASP B O   
5270  C CB  . ASP B 234 ? 1.1532 0.6041 0.6872 -0.0043 -0.0620 -0.0617 535 ASP B CB  
5271  C CG  . ASP B 234 ? 1.2566 0.6452 0.7500 0.0067  -0.0605 -0.0647 535 ASP B CG  
5272  O OD1 . ASP B 234 ? 1.2829 0.6273 0.7432 -0.0101 -0.0646 -0.0719 535 ASP B OD1 
5273  O OD2 . ASP B 234 ? 1.2907 0.6743 0.7838 0.0321  -0.0553 -0.0601 535 ASP B OD2 
5274  N N   . PRO B 235 ? 0.8896 0.4537 0.5126 -0.0158 -0.0597 -0.0418 536 PRO B N   
5275  C CA  . PRO B 235 ? 0.9131 0.5263 0.5677 -0.0276 -0.0613 -0.0384 536 PRO B CA  
5276  C C   . PRO B 235 ? 0.9547 0.5731 0.6016 -0.0472 -0.0674 -0.0456 536 PRO B C   
5277  O O   . PRO B 235 ? 1.0779 0.6599 0.6949 -0.0571 -0.0710 -0.0533 536 PRO B O   
5278  C CB  . PRO B 235 ? 0.8234 0.4441 0.4921 -0.0381 -0.0609 -0.0301 536 PRO B CB  
5279  C CG  . PRO B 235 ? 0.7859 0.3581 0.4267 -0.0379 -0.0604 -0.0300 536 PRO B CG  
5280  C CD  . PRO B 235 ? 0.8794 0.4223 0.4977 -0.0162 -0.0580 -0.0352 536 PRO B CD  
5281  N N   . GLU B 236 ? 0.8592 0.5240 0.5327 -0.0523 -0.0686 -0.0431 537 GLU B N   
5282  C CA  . GLU B 236 ? 0.9485 0.6299 0.6194 -0.0669 -0.0743 -0.0493 537 GLU B CA  
5283  C C   . GLU B 236 ? 0.8567 0.5832 0.5550 -0.0802 -0.0765 -0.0438 537 GLU B C   
5284  O O   . GLU B 236 ? 0.8705 0.6292 0.5944 -0.0685 -0.0728 -0.0370 537 GLU B O   
5285  C CB  . GLU B 236 ? 0.9873 0.6807 0.6576 -0.0504 -0.0731 -0.0533 537 GLU B CB  
5286  C CG  . GLU B 236 ? 0.9769 0.6276 0.6154 -0.0395 -0.0723 -0.0614 537 GLU B CG  
5287  C CD  . GLU B 236 ? 1.0006 0.6671 0.6402 -0.0222 -0.0701 -0.0643 537 GLU B CD  
5288  O OE1 . GLU B 236 ? 0.9915 0.6856 0.6377 -0.0290 -0.0738 -0.0667 537 GLU B OE1 
5289  O OE2 . GLU B 236 ? 1.0121 0.6650 0.6457 -0.0013 -0.0646 -0.0638 537 GLU B OE2 
5290  N N   . LEU B 237 ? 0.6952 0.4246 0.3870 -0.1047 -0.0822 -0.0469 538 LEU B N   
5291  C CA  . LEU B 237 ? 0.7481 0.5239 0.4649 -0.1170 -0.0844 -0.0421 538 LEU B CA  
5292  C C   . LEU B 237 ? 0.8147 0.6324 0.5480 -0.1076 -0.0856 -0.0424 538 LEU B C   
5293  O O   . LEU B 237 ? 0.8045 0.6168 0.5243 -0.1040 -0.0881 -0.0491 538 LEU B O   
5294  C CB  . LEU B 237 ? 0.6629 0.4349 0.3674 -0.1467 -0.0904 -0.0460 538 LEU B CB  
5295  C CG  . LEU B 237 ? 0.9227 0.6605 0.6153 -0.1586 -0.0887 -0.0426 538 LEU B CG  
5296  C CD1 . LEU B 237 ? 0.9614 0.6949 0.6401 -0.1910 -0.0943 -0.0463 538 LEU B CD1 
5297  C CD2 . LEU B 237 ? 0.7534 0.5118 0.4713 -0.1494 -0.0834 -0.0320 538 LEU B CD2 
5298  N N   . PHE B 238 ? 0.8195 0.6772 0.5802 -0.1022 -0.0835 -0.0348 539 PHE B N   
5299  C CA  . PHE B 238 ? 0.7422 0.6418 0.5181 -0.0949 -0.0849 -0.0337 539 PHE B CA  
5300  C C   . PHE B 238 ? 0.8507 0.7913 0.6487 -0.1025 -0.0858 -0.0277 539 PHE B C   
5301  O O   . PHE B 238 ? 0.8478 0.7875 0.6568 -0.1021 -0.0820 -0.0217 539 PHE B O   
5302  C CB  . PHE B 238 ? 0.6543 0.5564 0.4389 -0.0699 -0.0789 -0.0297 539 PHE B CB  
5303  C CG  . PHE B 238 ? 0.7808 0.6512 0.5460 -0.0594 -0.0774 -0.0350 539 PHE B CG  
5304  C CD1 . PHE B 238 ? 0.8522 0.6865 0.6071 -0.0531 -0.0733 -0.0351 539 PHE B CD1 
5305  C CD2 . PHE B 238 ? 0.7352 0.6134 0.4914 -0.0544 -0.0799 -0.0399 539 PHE B CD2 
5306  C CE1 . PHE B 238 ? 0.9227 0.7302 0.6592 -0.0413 -0.0715 -0.0401 539 PHE B CE1 
5307  C CE2 . PHE B 238 ? 0.7209 0.5712 0.4584 -0.0439 -0.0780 -0.0451 539 PHE B CE2 
5308  C CZ  . PHE B 238 ? 0.7733 0.5888 0.5011 -0.0369 -0.0736 -0.0453 539 PHE B CZ  
5309  N N   . GLN B 239 ? 0.8199 0.7986 0.6243 -0.1080 -0.0908 -0.0292 540 GLN B N   
5310  C CA  . GLN B 239 ? 0.8212 0.8446 0.6464 -0.1126 -0.0917 -0.0237 540 GLN B CA  
5311  C C   . GLN B 239 ? 0.6816 0.7320 0.5229 -0.0893 -0.0880 -0.0178 540 GLN B C   
5312  O O   . GLN B 239 ? 0.6724 0.7372 0.5107 -0.0808 -0.0903 -0.0197 540 GLN B O   
5313  C CB  . GLN B 239 ? 0.9121 0.9649 0.7340 -0.1338 -0.0996 -0.0287 540 GLN B CB  
5314  C CG  . GLN B 239 ? 1.0022 1.1100 0.8460 -0.1351 -0.1008 -0.0233 540 GLN B CG  
5315  C CD  . GLN B 239 ? 1.0548 1.2051 0.9034 -0.1274 -0.1055 -0.0246 540 GLN B CD  
5316  O OE1 . GLN B 239 ? 1.0123 1.1521 0.8528 -0.1128 -0.1054 -0.0267 540 GLN B OE1 
5317  N NE2 . GLN B 239 ? 0.9366 1.1372 0.7982 -0.1366 -0.1093 -0.0229 540 GLN B NE2 
5318  N N   . ILE B 240 ? 0.6454 0.7002 0.5017 -0.0791 -0.0823 -0.0106 541 ILE B N   
5319  C CA  . ILE B 240 ? 0.5382 0.6157 0.4073 -0.0583 -0.0786 -0.0048 541 ILE B CA  
5320  C C   . ILE B 240 ? 0.6201 0.7436 0.4959 -0.0597 -0.0837 -0.0046 541 ILE B C   
5321  O O   . ILE B 240 ? 0.6151 0.7639 0.4967 -0.0757 -0.0876 -0.0053 541 ILE B O   
5322  C CB  . ILE B 240 ? 0.5749 0.6524 0.4580 -0.0509 -0.0724 0.0020  541 ILE B CB  
5323  C CG1 . ILE B 240 ? 0.5570 0.5936 0.4343 -0.0503 -0.0680 0.0019  541 ILE B CG1 
5324  C CG2 . ILE B 240 ? 0.4764 0.5712 0.3686 -0.0302 -0.0684 0.0074  541 ILE B CG2 
5325  C CD1 . ILE B 240 ? 0.5892 0.6251 0.4761 -0.0549 -0.0649 0.0062  541 ILE B CD1 
5326  N N   . PRO B 241 ? 0.6050 0.7428 0.4796 -0.0440 -0.0840 -0.0034 542 PRO B N   
5327  C CA  . PRO B 241 ? 0.5911 0.7760 0.4726 -0.0419 -0.0886 -0.0022 542 PRO B CA  
5328  C C   . PRO B 241 ? 0.5695 0.7823 0.4680 -0.0378 -0.0859 0.0040  542 PRO B C   
5329  O O   . PRO B 241 ? 0.5132 0.7131 0.4173 -0.0227 -0.0791 0.0095  542 PRO B O   
5330  C CB  . PRO B 241 ? 0.6345 0.8200 0.5105 -0.0203 -0.0869 0.0003  542 PRO B CB  
5331  C CG  . PRO B 241 ? 0.5820 0.7234 0.4443 -0.0198 -0.0843 -0.0033 542 PRO B CG  
5332  C CD  . PRO B 241 ? 0.5764 0.6893 0.4422 -0.0275 -0.0801 -0.0029 542 PRO B CD  
5333  N N   . PRO B 242 ? 0.5127 0.7641 0.4187 -0.0521 -0.0909 0.0029  543 PRO B N   
5334  C CA  . PRO B 242 ? 0.4862 0.7690 0.4081 -0.0477 -0.0882 0.0086  543 PRO B CA  
5335  C C   . PRO B 242 ? 0.6160 0.9112 0.5431 -0.0194 -0.0836 0.0152  543 PRO B C   
5336  O O   . PRO B 242 ? 0.8148 1.1097 0.7503 -0.0102 -0.0780 0.0200  543 PRO B O   
5337  C CB  . PRO B 242 ? 0.5356 0.8677 0.4628 -0.0650 -0.0956 0.0058  543 PRO B CB  
5338  C CG  . PRO B 242 ? 0.4928 0.8044 0.4053 -0.0867 -0.1015 -0.0023 543 PRO B CG  
5339  C CD  . PRO B 242 ? 0.5311 0.8043 0.4309 -0.0716 -0.0994 -0.0037 543 PRO B CD  
5340  N N   . GLU B 243 ? 0.5605 0.8644 0.4807 -0.0052 -0.0857 0.0155  544 GLU B N   
5341  C CA  . GLU B 243 ? 0.5205 0.8317 0.4413 0.0224  -0.0812 0.0222  544 GLU B CA  
5342  C C   . GLU B 243 ? 0.5603 0.8255 0.4776 0.0338  -0.0727 0.0256  544 GLU B C   
5343  O O   . GLU B 243 ? 0.6336 0.8983 0.5508 0.0543  -0.0677 0.0313  544 GLU B O   
5344  C CB  . GLU B 243 ? 0.4074 0.7335 0.3185 0.0343  -0.0853 0.0221  544 GLU B CB  
5345  C CG  . GLU B 243 ? 0.3952 0.6814 0.2916 0.0326  -0.0850 0.0187  544 GLU B CG  
5346  C CD  . GLU B 243 ? 0.5679 0.8609 0.4582 0.0114  -0.0929 0.0104  544 GLU B CD  
5347  O OE1 . GLU B 243 ? 0.5223 0.8440 0.4203 -0.0066 -0.0980 0.0071  544 GLU B OE1 
5348  O OE2 . GLU B 243 ? 0.7178 0.9884 0.5945 0.0124  -0.0940 0.0070  544 GLU B OE2 
5349  N N   . LEU B 244 ? 0.4851 0.7120 0.3983 0.0210  -0.0710 0.0221  545 LEU B N   
5350  C CA  . LEU B 244 ? 0.4219 0.6103 0.3333 0.0292  -0.0634 0.0249  545 LEU B CA  
5351  C C   . LEU B 244 ? 0.5016 0.6858 0.4229 0.0220  -0.0602 0.0260  545 LEU B C   
5352  O O   . LEU B 244 ? 0.6185 0.7759 0.5395 0.0291  -0.0540 0.0284  545 LEU B O   
5353  C CB  . LEU B 244 ? 0.4696 0.6205 0.3705 0.0231  -0.0628 0.0211  545 LEU B CB  
5354  C CG  . LEU B 244 ? 0.4296 0.5747 0.3182 0.0310  -0.0643 0.0200  545 LEU B CG  
5355  C CD1 . LEU B 244 ? 0.4254 0.5384 0.3042 0.0211  -0.0646 0.0145  545 LEU B CD1 
5356  C CD2 . LEU B 244 ? 0.4341 0.5696 0.3186 0.0520  -0.0581 0.0265  545 LEU B CD2 
5357  N N   . VAL B 245 ? 0.5236 0.7346 0.4532 0.0073  -0.0641 0.0244  546 VAL B N   
5358  C CA  . VAL B 245 ? 0.5289 0.7370 0.4671 -0.0006 -0.0610 0.0257  546 VAL B CA  
5359  C C   . VAL B 245 ? 0.4203 0.6640 0.3683 0.0106  -0.0592 0.0300  546 VAL B C   
5360  O O   . VAL B 245 ? 0.4658 0.7496 0.4210 0.0025  -0.0632 0.0296  546 VAL B O   
5361  C CB  . VAL B 245 ? 0.5956 0.8053 0.5341 -0.0262 -0.0656 0.0216  546 VAL B CB  
5362  C CG1 . VAL B 245 ? 0.6221 0.8291 0.5681 -0.0336 -0.0621 0.0239  546 VAL B CG1 
5363  C CG2 . VAL B 245 ? 0.7546 0.9262 0.6803 -0.0348 -0.0672 0.0170  546 VAL B CG2 
5364  N N   . LEU B 246 ? 0.4756 0.7060 0.4230 0.0291  -0.0529 0.0338  547 LEU B N   
5365  C CA  . LEU B 246 ? 0.5261 0.7868 0.4799 0.0428  -0.0505 0.0375  547 LEU B CA  
5366  C C   . LEU B 246 ? 0.5109 0.7870 0.4752 0.0292  -0.0499 0.0374  547 LEU B C   
5367  O O   . LEU B 246 ? 0.4770 0.7264 0.4415 0.0160  -0.0483 0.0360  547 LEU B O   
5368  C CB  . LEU B 246 ? 0.4747 0.7103 0.4211 0.0650  -0.0438 0.0410  547 LEU B CB  
5369  C CG  . LEU B 246 ? 0.4567 0.7176 0.4052 0.0837  -0.0406 0.0446  547 LEU B CG  
5370  C CD1 . LEU B 246 ? 0.4220 0.7325 0.3750 0.0884  -0.0458 0.0455  547 LEU B CD1 
5371  C CD2 . LEU B 246 ? 0.4808 0.7110 0.4159 0.1056  -0.0348 0.0476  547 LEU B CD2 
5372  N N   . GLU B 247 ? 0.4481 0.7703 0.4209 0.0325  -0.0511 0.0391  548 GLU B N   
5373  C CA  . GLU B 247 ? 0.4005 0.7455 0.3835 0.0178  -0.0509 0.0394  548 GLU B CA  
5374  C C   . GLU B 247 ? 0.5077 0.8905 0.4971 0.0358  -0.0476 0.0429  548 GLU B C   
5375  O O   . GLU B 247 ? 0.4319 0.8419 0.4202 0.0535  -0.0488 0.0445  548 GLU B O   
5376  C CB  . GLU B 247 ? 0.3792 0.7519 0.3668 -0.0074 -0.0576 0.0368  548 GLU B CB  
5377  C CG  . GLU B 247 ? 0.3920 0.7264 0.3723 -0.0296 -0.0602 0.0330  548 GLU B CG  
5378  C CD  . GLU B 247 ? 0.5747 0.9358 0.5567 -0.0554 -0.0669 0.0300  548 GLU B CD  
5379  O OE1 . GLU B 247 ? 0.5688 0.9675 0.5532 -0.0539 -0.0717 0.0289  548 GLU B OE1 
5380  O OE2 . GLU B 247 ? 0.5595 0.9045 0.5392 -0.0776 -0.0674 0.0290  548 GLU B OE2 
5381  N N   . VAL B 248 ? 0.4941 0.8788 0.4887 0.0326  -0.0434 0.0441  549 VAL B N   
5382  C CA  . VAL B 248 ? 0.4638 0.8807 0.4628 0.0509  -0.0394 0.0469  549 VAL B CA  
5383  C C   . VAL B 248 ? 0.5732 1.0352 0.5849 0.0332  -0.0407 0.0477  549 VAL B C   
5384  O O   . VAL B 248 ? 0.7148 1.1610 0.7286 0.0133  -0.0399 0.0472  549 VAL B O   
5385  C CB  . VAL B 248 ? 0.4743 0.8538 0.4660 0.0660  -0.0322 0.0476  549 VAL B CB  
5386  C CG1 . VAL B 248 ? 0.5145 0.9253 0.5074 0.0882  -0.0279 0.0498  549 VAL B CG1 
5387  C CG2 . VAL B 248 ? 0.3917 0.7238 0.3702 0.0784  -0.0307 0.0469  549 VAL B CG2 
5388  N N   . PRO B 249 ? 0.6153 1.1351 0.6351 0.0393  -0.0428 0.0492  550 PRO B N   
5389  C CA  . PRO B 249 ? 0.5272 1.0946 0.5596 0.0226  -0.0430 0.0505  550 PRO B CA  
5390  C C   . PRO B 249 ? 0.6527 1.2264 0.6866 0.0382  -0.0357 0.0528  550 PRO B C   
5391  O O   . PRO B 249 ? 0.7197 1.2925 0.7479 0.0678  -0.0318 0.0539  550 PRO B O   
5392  C CB  . PRO B 249 ? 0.6799 1.3103 0.7201 0.0265  -0.0480 0.0512  550 PRO B CB  
5393  C CG  . PRO B 249 ? 0.6967 1.3151 0.7273 0.0583  -0.0476 0.0518  550 PRO B CG  
5394  C CD  . PRO B 249 ? 0.6433 1.1896 0.6609 0.0589  -0.0458 0.0500  550 PRO B CD  
5395  N N   . ILE B 250 ? 0.6272 1.2050 0.6667 0.0183  -0.0338 0.0537  551 ILE B N   
5396  C CA  . ILE B 250 ? 0.5125 1.0875 0.5516 0.0297  -0.0267 0.0552  551 ILE B CA  
5397  C C   . ILE B 250 ? 0.4936 1.1376 0.5436 0.0373  -0.0248 0.0579  551 ILE B C   
5398  O O   . ILE B 250 ? 0.4009 1.0867 0.4617 0.0141  -0.0271 0.0594  551 ILE B O   
5399  C CB  . ILE B 250 ? 0.4715 1.0135 0.5093 0.0068  -0.0250 0.0554  551 ILE B CB  
5400  C CG1 . ILE B 250 ? 0.4518 0.9336 0.4800 -0.0031 -0.0277 0.0529  551 ILE B CG1 
5401  C CG2 . ILE B 250 ? 0.3594 0.8892 0.3934 0.0229  -0.0178 0.0561  551 ILE B CG2 
5402  C CD1 . ILE B 250 ? 0.3082 0.7509 0.3264 0.0213  -0.0255 0.0511  551 ILE B CD1 
5403  N N   . ARG B 251 ? 0.5373 1.1928 0.5831 0.0699  -0.0205 0.0584  552 ARG B N   
5404  C CA  . ARG B 251 ? 0.4876 1.2035 0.5413 0.0836  -0.0169 0.0608  552 ARG B CA  
5405  C C   . ARG B 251 ? 0.5229 1.2142 0.5676 0.1032  -0.0089 0.0603  552 ARG B C   
5406  O O   . ARG B 251 ? 0.4356 1.0654 0.4673 0.1098  -0.0067 0.0580  552 ARG B O   
5407  C CB  . ARG B 251 ? 0.4285 1.1875 0.4833 0.1089  -0.0189 0.0618  552 ARG B CB  
5408  C CG  . ARG B 251 ? 0.6116 1.3237 0.6497 0.1376  -0.0179 0.0606  552 ARG B CG  
5409  C CD  . ARG B 251 ? 0.6120 1.3047 0.6479 0.1270  -0.0249 0.0595  552 ARG B CD  
5410  N NE  . ARG B 251 ? 0.5431 1.2015 0.5629 0.1564  -0.0237 0.0597  552 ARG B NE  
5411  C CZ  . ARG B 251 ? 0.5936 1.1974 0.6032 0.1518  -0.0257 0.0581  552 ARG B CZ  
5412  N NH1 . ARG B 251 ? 0.6152 1.1895 0.6089 0.1785  -0.0239 0.0591  552 ARG B NH1 
5413  N NH2 . ARG B 251 ? 0.5431 1.1210 0.5571 0.1212  -0.0291 0.0559  552 ARG B NH2 
5414  N N   . HIS B 252 ? 0.5384 1.2809 0.5899 0.1120  -0.0046 0.0623  553 HIS B N   
5415  C CA  . HIS B 252 ? 0.4383 1.1640 0.4813 0.1284  0.0031  0.0614  553 HIS B CA  
5416  C C   . HIS B 252 ? 0.4851 1.2391 0.5212 0.1676  0.0075  0.0614  553 HIS B C   
5417  O O   . HIS B 252 ? 0.5378 1.3479 0.5796 0.1736  0.0066  0.0634  553 HIS B O   
5418  C CB  . HIS B 252 ? 0.4054 1.1617 0.4589 0.1063  0.0058  0.0636  553 HIS B CB  
5419  C CG  . HIS B 252 ? 0.5343 1.2614 0.5775 0.1170  0.0127  0.0620  553 HIS B CG  
5420  N ND1 . HIS B 252 ? 0.5561 1.3106 0.5946 0.1452  0.0192  0.0615  553 HIS B ND1 
5421  C CD2 . HIS B 252 ? 0.4520 1.1258 0.4877 0.1038  0.0141  0.0604  553 HIS B CD2 
5422  C CE1 . HIS B 252 ? 0.4732 1.1909 0.5011 0.1478  0.0241  0.0592  553 HIS B CE1 
5423  N NE2 . HIS B 252 ? 0.5093 1.1792 0.5361 0.1228  0.0210  0.0587  553 HIS B NE2 
5424  N N   . PRO B 253 ? 0.4715 1.1784 0.4891 0.1926  0.0129  0.0586  554 PRO B N   
5425  C CA  . PRO B 253 ? 0.4590 1.1815 0.4644 0.2331  0.0173  0.0584  554 PRO B CA  
5426  C C   . PRO B 253 ? 0.5222 1.2903 0.5252 0.2408  0.0215  0.0593  554 PRO B C   
5427  O O   . PRO B 253 ? 0.5846 1.3541 0.5686 0.2697  0.0239  0.0590  554 PRO B O   
5428  C CB  . PRO B 253 ? 0.4352 1.0810 0.4164 0.2494  0.0218  0.0542  554 PRO B CB  
5429  C CG  . PRO B 253 ? 0.4650 1.0702 0.4494 0.2185  0.0209  0.0524  554 PRO B CG  
5430  C CD  . PRO B 253 ? 0.3731 1.0056 0.3778 0.1847  0.0143  0.0553  554 PRO B CD  
5431  N N   . LYS B 254 ? 0.6044 1.4042 0.6222 0.2155  0.0220  0.0608  555 LYS B N   
5432  C CA  . LYS B 254 ? 0.6198 1.4635 0.6341 0.2200  0.0244  0.0624  555 LYS B CA  
5433  C C   . LYS B 254 ? 0.6077 1.5033 0.6396 0.1863  0.0203  0.0661  555 LYS B C   
5434  O O   . LYS B 254 ? 0.5923 1.5343 0.6221 0.1894  0.0191  0.0681  555 LYS B O   
5435  C CB  . LYS B 254 ? 0.7135 1.5392 0.7218 0.2258  0.0306  0.0604  555 LYS B CB  
5436  C CG  . LYS B 254 ? 0.8019 1.5728 0.7877 0.2587  0.0355  0.0557  555 LYS B CG  
5437  C CD  . LYS B 254 ? 0.8863 1.6602 0.8509 0.2929  0.0352  0.0558  555 LYS B CD  
5438  C CE  . LYS B 254 ? 0.8931 1.6972 0.8474 0.3088  0.0376  0.0564  555 LYS B CE  
5439  N NZ  . LYS B 254 ? 0.8407 1.6004 0.7773 0.3267  0.0433  0.0517  555 LYS B NZ  
5440  N N   . PHE B 255 ? 0.6748 1.5607 0.7219 0.1536  0.0183  0.0670  556 PHE B N   
5441  C CA  . PHE B 255 ? 0.7018 1.6256 0.7621 0.1176  0.0143  0.0703  556 PHE B CA  
5442  C C   . PHE B 255 ? 0.6145 1.5519 0.6779 0.1110  0.0083  0.0702  556 PHE B C   
5443  O O   . PHE B 255 ? 0.6198 1.5268 0.6883 0.1011  0.0040  0.0690  556 PHE B O   
5444  C CB  . PHE B 255 ? 0.7611 1.6605 0.8320 0.0859  0.0141  0.0714  556 PHE B CB  
5445  C CG  . PHE B 255 ? 0.7302 1.6163 0.7973 0.0908  0.0208  0.0714  556 PHE B CG  
5446  C CD1 . PHE B 255 ? 0.6833 1.5252 0.7512 0.0758  0.0227  0.0710  556 PHE B CD1 
5447  C CD2 . PHE B 255 ? 0.6754 1.5877 0.7338 0.1101  0.0247  0.0716  556 PHE B CD2 
5448  C CE1 . PHE B 255 ? 0.6789 1.5041 0.7391 0.0798  0.0289  0.0705  556 PHE B CE1 
5449  C CE2 . PHE B 255 ? 0.6057 1.5048 0.6592 0.1147  0.0306  0.0710  556 PHE B CE2 
5450  C CZ  . PHE B 255 ? 0.6630 1.5232 0.7190 0.0997  0.0337  0.0706  556 PHE B CZ  
5451  N N   . GLU B 256 ? 0.6234 1.6074 0.6828 0.1174  0.0079  0.0714  557 GLU B N   
5452  C CA  . GLU B 256 ? 0.7091 1.7112 0.7712 0.1095  0.0030  0.0711  557 GLU B CA  
5453  C C   . GLU B 256 ? 0.7284 1.7394 0.8028 0.0657  -0.0018 0.0721  557 GLU B C   
5454  O O   . GLU B 256 ? 0.7910 1.7950 0.8689 0.0533  -0.0069 0.0707  557 GLU B O   
5455  C CB  . GLU B 256 ? 0.7329 1.7858 0.7867 0.1283  0.0045  0.0721  557 GLU B CB  
5456  C CG  . GLU B 256 ? 0.8095 1.8548 0.8474 0.1691  0.0096  0.0717  557 GLU B CG  
5457  C CD  . GLU B 256 ? 0.9540 2.0315 0.9798 0.1956  0.0102  0.0721  557 GLU B CD  
5458  O OE1 . GLU B 256 ? 0.9820 2.1112 1.0129 0.1810  0.0082  0.0737  557 GLU B OE1 
5459  O OE2 . GLU B 256 ? 1.0677 2.1171 1.0770 0.2307  0.0128  0.0709  557 GLU B OE2 
5460  N N   . TRP B 257 ? 0.6972 1.7192 0.7759 0.0419  -0.0003 0.0746  558 TRP B N   
5461  C CA  . TRP B 257 ? 0.5912 1.6132 0.6770 -0.0005 -0.0044 0.0758  558 TRP B CA  
5462  C C   . TRP B 257 ? 0.5765 1.5445 0.6664 -0.0152 -0.0080 0.0743  558 TRP B C   
5463  O O   . TRP B 257 ? 0.6445 1.6026 0.7368 -0.0502 -0.0118 0.0749  558 TRP B O   
5464  C CB  . TRP B 257 ? 0.5695 1.6114 0.6557 -0.0208 -0.0016 0.0795  558 TRP B CB  
5465  C CG  . TRP B 257 ? 0.5716 1.5872 0.6567 -0.0082 0.0035  0.0803  558 TRP B CG  
5466  C CD1 . TRP B 257 ? 0.6471 1.6802 0.7269 0.0186  0.0085  0.0807  558 TRP B CD1 
5467  C CD2 . TRP B 257 ? 0.5311 1.4983 0.6191 -0.0219 0.0041  0.0805  558 TRP B CD2 
5468  N NE1 . TRP B 257 ? 0.6066 1.6049 0.6860 0.0220  0.0126  0.0807  558 TRP B NE1 
5469  C CE2 . TRP B 257 ? 0.6033 1.5621 0.6880 -0.0025 0.0103  0.0808  558 TRP B CE2 
5470  C CE3 . TRP B 257 ? 0.5507 1.4802 0.6422 -0.0482 0.0000  0.0802  558 TRP B CE3 
5471  C CZ2 . TRP B 257 ? 0.6260 1.5428 0.7115 -0.0090 0.0135  0.0812  558 TRP B CZ2 
5472  C CZ3 . TRP B 257 ? 0.6167 1.5044 0.7089 -0.0539 0.0027  0.0811  558 TRP B CZ3 
5473  C CH2 . TRP B 257 ? 0.6090 1.4919 0.6986 -0.0348 0.0098  0.0816  558 TRP B CH2 
5474  N N   . PHE B 258 ? 0.5453 1.4764 0.6338 0.0103  -0.0070 0.0722  559 PHE B N   
5475  C CA  . PHE B 258 ? 0.5480 1.4295 0.6403 -0.0034 -0.0105 0.0712  559 PHE B CA  
5476  C C   . PHE B 258 ? 0.5947 1.4631 0.6878 -0.0173 -0.0186 0.0690  559 PHE B C   
5477  O O   . PHE B 258 ? 0.6859 1.5297 0.7807 -0.0475 -0.0232 0.0688  559 PHE B O   
5478  C CB  . PHE B 258 ? 0.4296 1.2676 0.5148 0.0270  -0.0068 0.0693  559 PHE B CB  
5479  C CG  . PHE B 258 ? 0.4649 1.2313 0.5399 0.0111  -0.0065 0.0681  559 PHE B CG  
5480  C CD1 . PHE B 258 ? 0.4690 1.2198 0.5403 0.0088  -0.0007 0.0694  559 PHE B CD1 
5481  C CD2 . PHE B 258 ? 0.5138 1.2317 0.5828 -0.0014 -0.0121 0.0658  559 PHE B CD2 
5482  C CE1 . PHE B 258 ? 0.4654 1.1548 0.5274 -0.0048 -0.0008 0.0686  559 PHE B CE1 
5483  C CE2 . PHE B 258 ? 0.4758 1.1320 0.5355 -0.0144 -0.0118 0.0650  559 PHE B CE2 
5484  C CZ  . PHE B 258 ? 0.4299 1.0728 0.4865 -0.0158 -0.0063 0.0665  559 PHE B CZ  
5485  N N   . LYS B 259 ? 0.5766 1.4574 0.6662 0.0051  -0.0204 0.0670  560 LYS B N   
5486  C CA  . LYS B 259 ? 0.5835 1.4511 0.6724 -0.0066 -0.0281 0.0645  560 LYS B CA  
5487  C C   . LYS B 259 ? 0.4843 1.3690 0.5755 -0.0465 -0.0315 0.0644  560 LYS B C   
5488  O O   . LYS B 259 ? 0.3106 1.1668 0.4002 -0.0680 -0.0381 0.0622  560 LYS B O   
5489  C CB  . LYS B 259 ? 0.6093 1.4945 0.6929 0.0231  -0.0280 0.0632  560 LYS B CB  
5490  C CG  . LYS B 259 ? 0.5653 1.5054 0.6471 0.0354  -0.0228 0.0647  560 LYS B CG  
5491  C CD  . LYS B 259 ? 0.5003 1.4392 0.5723 0.0785  -0.0193 0.0644  560 LYS B CD  
5492  C CE  . LYS B 259 ? 0.4568 1.4497 0.5252 0.0893  -0.0169 0.0651  560 LYS B CE  
5493  N NZ  . LYS B 259 ? 0.5279 1.5644 0.5997 0.0744  -0.0135 0.0673  560 LYS B NZ  
5494  N N   . ASP B 260 ? 0.5974 1.5241 0.6895 -0.0574 -0.0274 0.0669  561 ASP B N   
5495  C CA  . ASP B 260 ? 0.5975 1.5373 0.6884 -0.0963 -0.0301 0.0672  561 ASP B CA  
5496  C C   . ASP B 260 ? 0.5836 1.4782 0.6724 -0.1269 -0.0322 0.0680  561 ASP B C   
5497  O O   . ASP B 260 ? 0.6227 1.5113 0.7061 -0.1600 -0.0356 0.0674  561 ASP B O   
5498  C CB  . ASP B 260 ? 0.6509 1.6440 0.7412 -0.1004 -0.0253 0.0704  561 ASP B CB  
5499  C CG  . ASP B 260 ? 0.7327 1.7702 0.8228 -0.0663 -0.0222 0.0703  561 ASP B CG  
5500  O OD1 . ASP B 260 ? 0.7542 1.7868 0.8437 -0.0464 -0.0245 0.0676  561 ASP B OD1 
5501  O OD2 . ASP B 260 ? 0.7155 1.7919 0.8043 -0.0591 -0.0175 0.0731  561 ASP B OD2 
5502  N N   . LEU B 261 ? 0.5210 1.3818 0.6116 -0.1167 -0.0298 0.0692  562 LEU B N   
5503  C CA  . LEU B 261 ? 0.5798 1.3937 0.6666 -0.1440 -0.0320 0.0700  562 LEU B CA  
5504  C C   . LEU B 261 ? 0.7596 1.5385 0.8410 -0.1589 -0.0403 0.0658  562 LEU B C   
5505  O O   . LEU B 261 ? 0.8098 1.5461 0.8807 -0.1863 -0.0420 0.0657  562 LEU B O   
5506  C CB  . LEU B 261 ? 0.3783 1.1480 0.4611 -0.1252 -0.0268 0.0710  562 LEU B CB  
5507  C CG  . LEU B 261 ? 0.4840 1.2815 0.5718 -0.1167 -0.0189 0.0752  562 LEU B CG  
5508  C CD1 . LEU B 261 ? 0.4880 1.2325 0.5662 -0.0909 -0.0139 0.0741  562 LEU B CD1 
5509  C CD2 . LEU B 261 ? 0.5147 1.3178 0.6011 -0.1522 -0.0174 0.0798  562 LEU B CD2 
5510  N N   . GLY B 262 ? 0.7604 1.5470 0.8432 -0.1388 -0.0444 0.0622  563 GLY B N   
5511  C CA  . GLY B 262 ? 0.7995 1.5538 0.8736 -0.1506 -0.0516 0.0575  563 GLY B CA  
5512  C C   . GLY B 262 ? 0.7427 1.4160 0.8019 -0.1432 -0.0510 0.0552  563 GLY B C   
5513  O O   . GLY B 262 ? 0.6786 1.3126 0.7269 -0.1639 -0.0554 0.0522  563 GLY B O   
5514  N N   . LEU B 263 ? 0.7095 1.3573 0.7669 -0.1142 -0.0456 0.0561  564 LEU B N   
5515  C CA  . LEU B 263 ? 0.6456 1.2215 0.6903 -0.1072 -0.0443 0.0544  564 LEU B CA  
5516  C C   . LEU B 263 ? 0.6135 1.1717 0.6545 -0.0791 -0.0453 0.0516  564 LEU B C   
5517  O O   . LEU B 263 ? 0.5607 1.1548 0.6078 -0.0555 -0.0441 0.0523  564 LEU B O   
5518  C CB  . LEU B 263 ? 0.6245 1.1787 0.6677 -0.0994 -0.0372 0.0574  564 LEU B CB  
5519  C CG  . LEU B 263 ? 0.6555 1.2261 0.7010 -0.1242 -0.0347 0.0615  564 LEU B CG  
5520  C CD1 . LEU B 263 ? 0.6826 1.2531 0.7298 -0.1077 -0.0274 0.0645  564 LEU B CD1 
5521  C CD2 . LEU B 263 ? 0.6220 1.1433 0.6549 -0.1519 -0.0373 0.0614  564 LEU B CD2 
5522  N N   . LYS B 264 ? 0.6588 1.1607 0.6885 -0.0812 -0.0473 0.0487  565 LYS B N   
5523  C CA  . LYS B 264 ? 0.6097 1.0812 0.6331 -0.0560 -0.0467 0.0468  565 LYS B CA  
5524  C C   . LYS B 264 ? 0.5720 0.9791 0.5845 -0.0600 -0.0451 0.0455  565 LYS B C   
5525  O O   . LYS B 264 ? 0.6825 1.0686 0.6906 -0.0828 -0.0464 0.0453  565 LYS B O   
5526  C CB  . LYS B 264 ? 0.5495 1.0361 0.5715 -0.0536 -0.0529 0.0440  565 LYS B CB  
5527  C CG  . LYS B 264 ? 0.6178 1.0770 0.6313 -0.0783 -0.0587 0.0401  565 LYS B CG  
5528  C CD  . LYS B 264 ? 0.7006 1.1878 0.7140 -0.0786 -0.0653 0.0372  565 LYS B CD  
5529  C CE  . LYS B 264 ? 0.8224 1.2895 0.8267 -0.1072 -0.0713 0.0326  565 LYS B CE  
5530  N NZ  . LYS B 264 ? 0.8889 1.3815 0.8915 -0.1072 -0.0781 0.0290  565 LYS B NZ  
5531  N N   . TRP B 265 ? 0.4506 0.8267 0.4578 -0.0377 -0.0421 0.0448  566 TRP B N   
5532  C CA  . TRP B 265 ? 0.4119 0.7318 0.4093 -0.0398 -0.0412 0.0432  566 TRP B CA  
5533  C C   . TRP B 265 ? 0.5824 0.8828 0.5733 -0.0250 -0.0427 0.0409  566 TRP B C   
5534  O O   . TRP B 265 ? 0.5968 0.9230 0.5897 -0.0099 -0.0435 0.0413  566 TRP B O   
5535  C CB  . TRP B 265 ? 0.3973 0.6945 0.3937 -0.0312 -0.0352 0.0449  566 TRP B CB  
5536  C CG  . TRP B 265 ? 0.4261 0.6757 0.4146 -0.0413 -0.0349 0.0440  566 TRP B CG  
5537  C CD1 . TRP B 265 ? 0.4737 0.6847 0.4557 -0.0300 -0.0327 0.0426  566 TRP B CD1 
5538  C CD2 . TRP B 265 ? 0.3890 0.6252 0.3738 -0.0639 -0.0369 0.0447  566 TRP B CD2 
5539  N NE1 . TRP B 265 ? 0.4366 0.6152 0.4127 -0.0426 -0.0335 0.0423  566 TRP B NE1 
5540  C CE2 . TRP B 265 ? 0.4309 0.6215 0.4074 -0.0625 -0.0359 0.0438  566 TRP B CE2 
5541  C CE3 . TRP B 265 ? 0.4140 0.6720 0.4006 -0.0856 -0.0392 0.0464  566 TRP B CE3 
5542  C CZ2 . TRP B 265 ? 0.4650 0.6298 0.4336 -0.0791 -0.0371 0.0446  566 TRP B CZ2 
5543  C CZ3 . TRP B 265 ? 0.4848 0.7131 0.4623 -0.1043 -0.0403 0.0472  566 TRP B CZ3 
5544  C CH2 . TRP B 265 ? 0.5255 0.7068 0.4935 -0.0995 -0.0393 0.0464  566 TRP B CH2 
5545  N N   . TYR B 266 ? 0.4985 0.7544 0.4809 -0.0292 -0.0431 0.0389  567 TYR B N   
5546  C CA  . TYR B 266 ? 0.5139 0.7481 0.4893 -0.0158 -0.0435 0.0372  567 TYR B CA  
5547  C C   . TYR B 266 ? 0.6072 0.8202 0.5799 0.0042  -0.0375 0.0387  567 TYR B C   
5548  O O   . TYR B 266 ? 0.6560 0.8625 0.6308 0.0054  -0.0335 0.0399  567 TYR B O   
5549  C CB  . TYR B 266 ? 0.5112 0.7099 0.4779 -0.0283 -0.0462 0.0342  567 TYR B CB  
5550  C CG  . TYR B 266 ? 0.5896 0.7570 0.5532 -0.0385 -0.0441 0.0345  567 TYR B CG  
5551  C CD1 . TYR B 266 ? 0.6899 0.8241 0.6494 -0.0286 -0.0402 0.0346  567 TYR B CD1 
5552  C CD2 . TYR B 266 ? 0.4009 0.5723 0.3645 -0.0584 -0.0461 0.0350  567 TYR B CD2 
5553  C CE1 . TYR B 266 ? 0.7090 0.8180 0.6655 -0.0362 -0.0387 0.0351  567 TYR B CE1 
5554  C CE2 . TYR B 266 ? 0.4847 0.6261 0.4432 -0.0660 -0.0443 0.0359  567 TYR B CE2 
5555  C CZ  . TYR B 266 ? 0.7141 0.8259 0.6696 -0.0538 -0.0408 0.0359  567 TYR B CZ  
5556  O OH  . TYR B 266 ? 0.7952 0.8809 0.7457 -0.0597 -0.0393 0.0372  567 TYR B OH  
5557  N N   . GLY B 267 ? 0.5704 0.7713 0.5367 0.0191  -0.0369 0.0384  568 GLY B N   
5558  C CA  . GLY B 267 ? 0.4112 0.5935 0.3723 0.0378  -0.0312 0.0399  568 GLY B CA  
5559  C C   . GLY B 267 ? 0.5056 0.6451 0.4600 0.0370  -0.0284 0.0387  568 GLY B C   
5560  O O   . GLY B 267 ? 0.5289 0.6496 0.4785 0.0480  -0.0234 0.0395  568 GLY B O   
5561  N N   . LEU B 268 ? 0.4567 0.5806 0.4095 0.0239  -0.0315 0.0367  569 LEU B N   
5562  C CA  . LEU B 268 ? 0.3842 0.4729 0.3305 0.0248  -0.0292 0.0357  569 LEU B CA  
5563  C C   . LEU B 268 ? 0.5902 0.6629 0.5382 0.0113  -0.0295 0.0345  569 LEU B C   
5564  O O   . LEU B 268 ? 0.6060 0.6777 0.5530 -0.0012 -0.0336 0.0329  569 LEU B O   
5565  C CB  . LEU B 268 ? 0.3683 0.4504 0.3082 0.0263  -0.0318 0.0345  569 LEU B CB  
5566  C CG  . LEU B 268 ? 0.4391 0.4900 0.3721 0.0308  -0.0282 0.0343  569 LEU B CG  
5567  C CD1 . LEU B 268 ? 0.4262 0.4692 0.3556 0.0444  -0.0226 0.0368  569 LEU B CD1 
5568  C CD2 . LEU B 268 ? 0.4161 0.4606 0.3418 0.0313  -0.0306 0.0328  569 LEU B CD2 
5569  N N   . PRO B 269 ? 0.5249 0.5837 0.4738 0.0136  -0.0255 0.0352  570 PRO B N   
5570  C CA  . PRO B 269 ? 0.4553 0.4965 0.4039 0.0038  -0.0257 0.0345  570 PRO B CA  
5571  C C   . PRO B 269 ? 0.4812 0.4988 0.4240 0.0064  -0.0249 0.0331  570 PRO B C   
5572  O O   . PRO B 269 ? 0.5288 0.5375 0.4691 0.0154  -0.0213 0.0334  570 PRO B O   
5573  C CB  . PRO B 269 ? 0.3985 0.4391 0.3502 0.0069  -0.0218 0.0356  570 PRO B CB  
5574  C CG  . PRO B 269 ? 0.5222 0.5645 0.4715 0.0207  -0.0182 0.0358  570 PRO B CG  
5575  C CD  . PRO B 269 ? 0.6087 0.6661 0.5567 0.0258  -0.0207 0.0363  570 PRO B CD  
5576  N N   . ALA B 270 ? 0.3932 0.4003 0.3323 -0.0017 -0.0279 0.0317  571 ALA B N   
5577  C CA  . ALA B 270 ? 0.4877 0.4762 0.4206 0.0014  -0.0274 0.0301  571 ALA B CA  
5578  C C   . ALA B 270 ? 0.4555 0.4284 0.3848 -0.0054 -0.0287 0.0294  571 ALA B C   
5579  O O   . ALA B 270 ? 0.7100 0.6794 0.6340 -0.0138 -0.0325 0.0282  571 ALA B O   
5580  C CB  . ALA B 270 ? 0.4766 0.4690 0.4043 0.0025  -0.0303 0.0284  571 ALA B CB  
5581  N N   . VAL B 271 ? 0.3833 0.3465 0.3138 -0.0021 -0.0257 0.0302  572 VAL B N   
5582  C CA  . VAL B 271 ? 0.5341 0.4834 0.4601 -0.0058 -0.0268 0.0303  572 VAL B CA  
5583  C C   . VAL B 271 ? 0.5762 0.5103 0.4938 -0.0017 -0.0273 0.0281  572 VAL B C   
5584  O O   . VAL B 271 ? 0.6923 0.6268 0.6109 0.0055  -0.0246 0.0274  572 VAL B O   
5585  C CB  . VAL B 271 ? 0.5042 0.4540 0.4352 -0.0032 -0.0239 0.0321  572 VAL B CB  
5586  C CG1 . VAL B 271 ? 0.4854 0.4220 0.4105 -0.0052 -0.0253 0.0332  572 VAL B CG1 
5587  C CG2 . VAL B 271 ? 0.5278 0.4919 0.4655 -0.0059 -0.0230 0.0337  572 VAL B CG2 
5588  N N   . SER B 272 ? 0.4592 0.3784 0.3667 -0.0062 -0.0304 0.0270  573 SER B N   
5589  C CA  . SER B 272 ? 0.6758 0.5799 0.5728 -0.0012 -0.0309 0.0240  573 SER B CA  
5590  C C   . SER B 272 ? 0.7437 0.6256 0.6285 0.0001  -0.0319 0.0237  573 SER B C   
5591  O O   . SER B 272 ? 0.7181 0.5843 0.5905 0.0039  -0.0329 0.0205  573 SER B O   
5592  C CB  . SER B 272 ? 0.5304 0.4356 0.4213 -0.0062 -0.0343 0.0208  573 SER B CB  
5593  O OG  . SER B 272 ? 0.5309 0.4344 0.4174 -0.0188 -0.0383 0.0205  573 SER B OG  
5594  N N   . ASN B 273 ? 0.8203 0.6990 0.7061 -0.0016 -0.0316 0.0269  574 ASN B N   
5595  C CA  . ASN B 273 ? 0.6752 0.5316 0.5476 0.0025  -0.0322 0.0276  574 ASN B CA  
5596  C C   . ASN B 273 ? 0.6016 0.4642 0.4794 0.0145  -0.0290 0.0295  574 ASN B C   
5597  O O   . ASN B 273 ? 0.6982 0.5454 0.5653 0.0210  -0.0292 0.0308  574 ASN B O   
5598  C CB  . ASN B 273 ? 0.6141 0.4601 0.4800 -0.0080 -0.0343 0.0306  574 ASN B CB  
5599  C CG  . ASN B 273 ? 0.7103 0.5782 0.5913 -0.0125 -0.0330 0.0343  574 ASN B CG  
5600  O OD1 . ASN B 273 ? 0.7617 0.6484 0.6561 -0.0066 -0.0304 0.0345  574 ASN B OD1 
5601  N ND2 . ASN B 273 ? 0.6753 0.5403 0.5528 -0.0239 -0.0346 0.0371  574 ASN B ND2 
5602  N N   . MET B 274 ? 0.5243 0.4085 0.4167 0.0175  -0.0261 0.0297  575 MET B N   
5603  C CA  . MET B 274 ? 0.5644 0.4598 0.4637 0.0251  -0.0234 0.0314  575 MET B CA  
5604  C C   . MET B 274 ? 0.6159 0.5143 0.5138 0.0355  -0.0210 0.0294  575 MET B C   
5605  O O   . MET B 274 ? 0.6057 0.4986 0.4984 0.0369  -0.0209 0.0267  575 MET B O   
5606  C CB  . MET B 274 ? 0.5199 0.4354 0.4339 0.0202  -0.0215 0.0326  575 MET B CB  
5607  C CG  . MET B 274 ? 0.4837 0.3998 0.3991 0.0133  -0.0231 0.0354  575 MET B CG  
5608  S SD  . MET B 274 ? 0.6030 0.5398 0.5321 0.0102  -0.0206 0.0360  575 MET B SD  
5609  C CE  . MET B 274 ? 0.5202 0.4629 0.4501 0.0164  -0.0200 0.0377  575 MET B CE  
5610  N N   . LEU B 275 ? 0.4239 0.3336 0.3262 0.0427  -0.0190 0.0309  576 LEU B N   
5611  C CA  . LEU B 275 ? 0.4725 0.3898 0.3737 0.0533  -0.0164 0.0296  576 LEU B CA  
5612  C C   . LEU B 275 ? 0.5619 0.5046 0.4779 0.0506  -0.0128 0.0300  576 LEU B C   
5613  O O   . LEU B 275 ? 0.7136 0.6687 0.6377 0.0471  -0.0126 0.0317  576 LEU B O   
5614  C CB  . LEU B 275 ? 0.6275 0.5385 0.5192 0.0656  -0.0171 0.0310  576 LEU B CB  
5615  C CG  . LEU B 275 ? 0.6418 0.5630 0.5313 0.0789  -0.0142 0.0296  576 LEU B CG  
5616  C CD1 . LEU B 275 ? 0.5818 0.4801 0.4517 0.0928  -0.0157 0.0291  576 LEU B CD1 
5617  C CD2 . LEU B 275 ? 0.5942 0.5471 0.4978 0.0814  -0.0117 0.0315  576 LEU B CD2 
5618  N N   . LEU B 276 ? 0.4994 0.4489 0.4173 0.0513  -0.0098 0.0285  577 LEU B N   
5619  C CA  . LEU B 276 ? 0.4371 0.4076 0.3659 0.0473  -0.0057 0.0289  577 LEU B CA  
5620  C C   . LEU B 276 ? 0.5526 0.5407 0.4829 0.0564  -0.0033 0.0292  577 LEU B C   
5621  O O   . LEU B 276 ? 0.6636 0.6474 0.5858 0.0663  -0.0027 0.0280  577 LEU B O   
5622  C CB  . LEU B 276 ? 0.4305 0.3985 0.3590 0.0428  -0.0032 0.0281  577 LEU B CB  
5623  C CG  . LEU B 276 ? 0.5120 0.4962 0.4477 0.0373  0.0017  0.0290  577 LEU B CG  
5624  C CD1 . LEU B 276 ? 0.5181 0.5071 0.4608 0.0285  0.0017  0.0296  577 LEU B CD1 
5625  C CD2 . LEU B 276 ? 0.4506 0.4280 0.3821 0.0348  0.0044  0.0291  577 LEU B CD2 
5626  N N   . GLU B 277 ? 0.6242 0.6337 0.5641 0.0533  -0.0020 0.0303  578 GLU B N   
5627  C CA  . GLU B 277 ? 0.6135 0.6472 0.5568 0.0617  0.0000  0.0308  578 GLU B CA  
5628  C C   . GLU B 277 ? 0.6179 0.6755 0.5716 0.0512  0.0045  0.0307  578 GLU B C   
5629  O O   . GLU B 277 ? 0.5578 0.6184 0.5176 0.0388  0.0046  0.0306  578 GLU B O   
5630  C CB  . GLU B 277 ? 0.7755 0.8167 0.7196 0.0677  -0.0031 0.0324  578 GLU B CB  
5631  C CG  . GLU B 277 ? 0.8675 0.9349 0.8133 0.0807  -0.0018 0.0332  578 GLU B CG  
5632  C CD  . GLU B 277 ? 0.9887 1.0920 0.9487 0.0718  0.0002  0.0334  578 GLU B CD  
5633  O OE1 . GLU B 277 ? 1.0526 1.1551 1.0187 0.0570  -0.0003 0.0328  578 GLU B OE1 
5634  O OE2 . GLU B 277 ? 1.0028 1.1360 0.9673 0.0792  0.0025  0.0338  578 GLU B OE2 
5635  N N   . ILE B 278 ? 0.6397 0.7123 0.5936 0.0557  0.0085  0.0306  579 ILE B N   
5636  C CA  . ILE B 278 ? 0.5029 0.5980 0.4646 0.0446  0.0135  0.0310  579 ILE B CA  
5637  C C   . ILE B 278 ? 0.5360 0.6630 0.5012 0.0541  0.0164  0.0316  579 ILE B C   
5638  O O   . ILE B 278 ? 0.6098 0.7334 0.5678 0.0675  0.0175  0.0312  579 ILE B O   
5639  C CB  . ILE B 278 ? 0.4563 0.5350 0.4130 0.0372  0.0168  0.0312  579 ILE B CB  
5640  C CG1 . ILE B 278 ? 0.4377 0.4880 0.3905 0.0306  0.0140  0.0308  579 ILE B CG1 
5641  C CG2 . ILE B 278 ? 0.5345 0.6337 0.4968 0.0242  0.0224  0.0323  579 ILE B CG2 
5642  C CD1 . ILE B 278 ? 0.5133 0.5471 0.4598 0.0256  0.0167  0.0315  579 ILE B CD1 
5643  N N   . GLY B 279 ? 0.5020 0.6615 0.4778 0.0470  0.0178  0.0320  580 GLY B N   
5644  C CA  . GLY B 279 ? 0.4883 0.6864 0.4697 0.0550  0.0208  0.0328  580 GLY B CA  
5645  C C   . GLY B 279 ? 0.5472 0.7452 0.5214 0.0793  0.0189  0.0329  580 GLY B C   
5646  O O   . GLY B 279 ? 0.5595 0.7770 0.5325 0.0901  0.0226  0.0331  580 GLY B O   
5647  N N   . GLY B 280 ? 0.5317 0.7065 0.4991 0.0883  0.0135  0.0328  581 GLY B N   
5648  C CA  . GLY B 280 ? 0.6646 0.8316 0.6208 0.1115  0.0115  0.0331  581 GLY B CA  
5649  C C   . GLY B 280 ? 0.7145 0.8457 0.6552 0.1199  0.0116  0.0313  581 GLY B C   
5650  O O   . GLY B 280 ? 0.7385 0.8567 0.6659 0.1392  0.0102  0.0308  581 GLY B O   
5651  N N   . LEU B 281 ? 0.6533 0.7675 0.5937 0.1063  0.0133  0.0302  582 LEU B N   
5652  C CA  . LEU B 281 ? 0.6625 0.7425 0.5885 0.1111  0.0124  0.0281  582 LEU B CA  
5653  C C   . LEU B 281 ? 0.5473 0.5927 0.4675 0.1044  0.0071  0.0276  582 LEU B C   
5654  O O   . LEU B 281 ? 0.5386 0.5848 0.4678 0.0903  0.0058  0.0288  582 LEU B O   
5655  C CB  . LEU B 281 ? 0.6230 0.7059 0.5509 0.1012  0.0168  0.0277  582 LEU B CB  
5656  C CG  . LEU B 281 ? 0.4913 0.6119 0.4262 0.1037  0.0230  0.0288  582 LEU B CG  
5657  C CD1 . LEU B 281 ? 0.4265 0.5480 0.3621 0.0919  0.0278  0.0295  582 LEU B CD1 
5658  C CD2 . LEU B 281 ? 0.4540 0.5814 0.3793 0.1266  0.0238  0.0274  582 LEU B CD2 
5659  N N   . GLU B 282 ? 0.5719 0.5868 0.4758 0.1139  0.0042  0.0257  583 GLU B N   
5660  C CA  . GLU B 282 ? 0.6127 0.5968 0.5097 0.1079  -0.0008 0.0256  583 GLU B CA  
5661  C C   . GLU B 282 ? 0.7252 0.6853 0.6138 0.1015  -0.0018 0.0229  583 GLU B C   
5662  O O   . GLU B 282 ? 0.8225 0.7649 0.6958 0.1109  -0.0023 0.0200  583 GLU B O   
5663  C CB  . GLU B 282 ? 0.7587 0.7245 0.6412 0.1221  -0.0039 0.0260  583 GLU B CB  
5664  C CG  . GLU B 282 ? 0.7358 0.7271 0.6249 0.1316  -0.0034 0.0291  583 GLU B CG  
5665  C CD  . GLU B 282 ? 0.8246 0.7920 0.6966 0.1453  -0.0068 0.0306  583 GLU B CD  
5666  O OE1 . GLU B 282 ? 0.9407 0.9086 0.8163 0.1413  -0.0094 0.0338  583 GLU B OE1 
5667  O OE2 . GLU B 282 ? 0.8098 0.7557 0.6629 0.1602  -0.0066 0.0286  583 GLU B OE2 
5668  N N   . PHE B 283 ? 0.5806 0.5401 0.4779 0.0863  -0.0023 0.0236  584 PHE B N   
5669  C CA  . PHE B 283 ? 0.5038 0.4444 0.3946 0.0795  -0.0041 0.0216  584 PHE B CA  
5670  C C   . PHE B 283 ? 0.5804 0.4973 0.4641 0.0743  -0.0094 0.0211  584 PHE B C   
5671  O O   . PHE B 283 ? 0.6082 0.5266 0.5000 0.0637  -0.0110 0.0229  584 PHE B O   
5672  C CB  . PHE B 283 ? 0.4686 0.4221 0.3708 0.0683  -0.0015 0.0231  584 PHE B CB  
5673  C CG  . PHE B 283 ? 0.5988 0.5732 0.5057 0.0707  0.0042  0.0240  584 PHE B CG  
5674  C CD1 . PHE B 283 ? 0.6329 0.6310 0.5517 0.0671  0.0074  0.0262  584 PHE B CD1 
5675  C CD2 . PHE B 283 ? 0.6026 0.5744 0.5013 0.0754  0.0063  0.0224  584 PHE B CD2 
5676  C CE1 . PHE B 283 ? 0.6258 0.6451 0.5488 0.0667  0.0130  0.0274  584 PHE B CE1 
5677  C CE2 . PHE B 283 ? 0.6228 0.6153 0.5254 0.0766  0.0122  0.0239  584 PHE B CE2 
5678  C CZ  . PHE B 283 ? 0.7064 0.7231 0.6214 0.0716  0.0157  0.0266  584 PHE B CZ  
5679  N N   . SER B 284 ? 0.5766 0.4702 0.4431 0.0816  -0.0120 0.0186  585 SER B N   
5680  C CA  . SER B 284 ? 0.5577 0.4265 0.4142 0.0756  -0.0167 0.0184  585 SER B CA  
5681  C C   . SER B 284 ? 0.5545 0.4165 0.4115 0.0619  -0.0195 0.0168  585 SER B C   
5682  O O   . SER B 284 ? 0.6391 0.4851 0.4898 0.0537  -0.0232 0.0170  585 SER B O   
5683  C CB  . SER B 284 ? 0.6542 0.4954 0.4882 0.0866  -0.0182 0.0156  585 SER B CB  
5684  O OG  . SER B 284 ? 0.7946 0.6305 0.6188 0.0923  -0.0171 0.0112  585 SER B OG  
5685  N N   . ALA B 285 ? 0.5988 0.4732 0.4619 0.0592  -0.0178 0.0157  586 ALA B N   
5686  C CA  . ALA B 285 ? 0.5594 0.4330 0.4243 0.0481  -0.0205 0.0149  586 ALA B CA  
5687  C C   . ALA B 285 ? 0.5796 0.4748 0.4591 0.0457  -0.0171 0.0174  586 ALA B C   
5688  O O   . ALA B 285 ? 0.5895 0.4925 0.4689 0.0510  -0.0137 0.0170  586 ALA B O   
5689  C CB  . ALA B 285 ? 0.6982 0.5571 0.5478 0.0487  -0.0229 0.0101  586 ALA B CB  
5690  N N   . CYS B 286 ? 0.4590 0.3622 0.3490 0.0378  -0.0177 0.0200  587 CYS B N   
5691  C CA  . CYS B 286 ? 0.5545 0.4732 0.4557 0.0359  -0.0141 0.0226  587 CYS B CA  
5692  C C   . CYS B 286 ? 0.7974 0.7197 0.7042 0.0282  -0.0162 0.0239  587 CYS B C   
5693  O O   . CYS B 286 ? 0.9170 0.8463 0.8321 0.0254  -0.0147 0.0260  587 CYS B O   
5694  C CB  . CYS B 286 ? 0.6466 0.5755 0.5559 0.0380  -0.0106 0.0246  587 CYS B CB  
5695  S SG  . CYS B 286 ? 0.6028 0.5281 0.5140 0.0361  -0.0135 0.0258  587 CYS B SG  
5696  N N   . PRO B 287 ? 0.7609 0.6809 0.6632 0.0249  -0.0196 0.0225  588 PRO B N   
5697  C CA  . PRO B 287 ? 0.5603 0.4881 0.4683 0.0186  -0.0216 0.0239  588 PRO B CA  
5698  C C   . PRO B 287 ? 0.6350 0.5729 0.5501 0.0209  -0.0178 0.0265  588 PRO B C   
5699  O O   . PRO B 287 ? 0.6630 0.6018 0.5755 0.0254  -0.0152 0.0271  588 PRO B O   
5700  C CB  . PRO B 287 ? 0.5668 0.4945 0.4679 0.0154  -0.0259 0.0216  588 PRO B CB  
5701  C CG  . PRO B 287 ? 0.5421 0.4629 0.4346 0.0214  -0.0250 0.0193  588 PRO B CG  
5702  C CD  . PRO B 287 ? 0.5678 0.4803 0.4591 0.0266  -0.0220 0.0193  588 PRO B CD  
5703  N N   . PHE B 288 ? 0.5592 0.5024 0.4813 0.0179  -0.0171 0.0281  589 PHE B N   
5704  C CA  . PHE B 288 ? 0.4665 0.4149 0.3923 0.0199  -0.0136 0.0300  589 PHE B CA  
5705  C C   . PHE B 288 ? 0.3612 0.3191 0.2901 0.0183  -0.0156 0.0307  589 PHE B C   
5706  O O   . PHE B 288 ? 0.3364 0.2989 0.2667 0.0130  -0.0193 0.0302  589 PHE B O   
5707  C CB  . PHE B 288 ? 0.5288 0.4760 0.4588 0.0188  -0.0101 0.0305  589 PHE B CB  
5708  C CG  . PHE B 288 ? 0.6008 0.5493 0.5346 0.0150  -0.0122 0.0303  589 PHE B CG  
5709  C CD1 . PHE B 288 ? 0.6066 0.5606 0.5444 0.0118  -0.0130 0.0310  589 PHE B CD1 
5710  C CD2 . PHE B 288 ? 0.5414 0.4854 0.4732 0.0160  -0.0133 0.0297  589 PHE B CD2 
5711  C CE1 . PHE B 288 ? 0.4735 0.4282 0.4133 0.0083  -0.0148 0.0315  589 PHE B CE1 
5712  C CE2 . PHE B 288 ? 0.5836 0.5267 0.5164 0.0139  -0.0152 0.0303  589 PHE B CE2 
5713  C CZ  . PHE B 288 ? 0.5383 0.4865 0.4751 0.0094  -0.0160 0.0315  589 PHE B CZ  
5714  N N   . SER B 289 ? 0.3140 0.2747 0.2425 0.0230  -0.0127 0.0321  590 SER B N   
5715  C CA  . SER B 289 ? 0.3138 0.2868 0.2436 0.0253  -0.0142 0.0330  590 SER B CA  
5716  C C   . SER B 289 ? 0.3532 0.3225 0.2805 0.0317  -0.0096 0.0343  590 SER B C   
5717  O O   . SER B 289 ? 0.5007 0.4567 0.4223 0.0343  -0.0057 0.0349  590 SER B O   
5718  C CB  . SER B 289 ? 0.5269 0.5078 0.4529 0.0284  -0.0172 0.0331  590 SER B CB  
5719  O OG  . SER B 289 ? 0.5353 0.5186 0.4567 0.0382  -0.0147 0.0352  590 SER B OG  
5720  N N   . GLY B 290 ? 0.4255 0.4057 0.3555 0.0335  -0.0099 0.0347  591 GLY B N   
5721  C CA  . GLY B 290 ? 0.3350 0.3097 0.2596 0.0414  -0.0057 0.0353  591 GLY B CA  
5722  C C   . GLY B 290 ? 0.5785 0.5728 0.5049 0.0477  -0.0073 0.0362  591 GLY B C   
5723  O O   . GLY B 290 ? 0.7817 0.7898 0.7086 0.0510  -0.0102 0.0373  591 GLY B O   
5724  N N   . TRP B 291 ? 0.6143 0.6133 0.5421 0.0492  -0.0055 0.0356  592 TRP B N   
5725  C CA  . TRP B 291 ? 0.5753 0.5983 0.5062 0.0552  -0.0067 0.0365  592 TRP B CA  
5726  C C   . TRP B 291 ? 0.6055 0.6390 0.5434 0.0484  -0.0068 0.0355  592 TRP B C   
5727  O O   . TRP B 291 ? 0.6170 0.6364 0.5547 0.0424  -0.0053 0.0341  592 TRP B O   
5728  C CB  . TRP B 291 ? 0.5186 0.5372 0.4385 0.0720  -0.0030 0.0376  592 TRP B CB  
5729  C CG  . TRP B 291 ? 0.5937 0.5841 0.5028 0.0749  0.0022  0.0361  592 TRP B CG  
5730  C CD1 . TRP B 291 ? 0.5811 0.5677 0.4888 0.0743  0.0047  0.0338  592 TRP B CD1 
5731  C CD2 . TRP B 291 ? 0.6982 0.6596 0.5949 0.0773  0.0056  0.0365  592 TRP B CD2 
5732  N NE1 . TRP B 291 ? 0.6680 0.6241 0.5628 0.0754  0.0091  0.0321  592 TRP B NE1 
5733  C CE2 . TRP B 291 ? 0.6935 0.6338 0.5815 0.0765  0.0099  0.0340  592 TRP B CE2 
5734  C CE3 . TRP B 291 ? 0.7343 0.6859 0.6256 0.0790  0.0056  0.0388  592 TRP B CE3 
5735  C CZ2 . TRP B 291 ? 0.7649 0.6742 0.6388 0.0756  0.0143  0.0338  592 TRP B CZ2 
5736  C CZ3 . TRP B 291 ? 0.6642 0.5856 0.5418 0.0793  0.0104  0.0393  592 TRP B CZ3 
5737  C CH2 . TRP B 291 ? 0.7850 0.6854 0.6540 0.0768  0.0146  0.0368  592 TRP B CH2 
5738  N N   . TYR B 292 ? 0.4620 0.5232 0.4059 0.0491  -0.0087 0.0367  593 TYR B N   
5739  C CA  . TYR B 292 ? 0.3554 0.4310 0.3065 0.0406  -0.0093 0.0367  593 TYR B CA  
5740  C C   . TYR B 292 ? 0.5624 0.6361 0.5090 0.0491  -0.0049 0.0355  593 TYR B C   
5741  O O   . TYR B 292 ? 0.5305 0.6051 0.4699 0.0638  -0.0019 0.0352  593 TYR B O   
5742  C CB  . TYR B 292 ? 0.4286 0.5380 0.3873 0.0368  -0.0126 0.0386  593 TYR B CB  
5743  C CG  . TYR B 292 ? 0.4453 0.5586 0.4092 0.0205  -0.0174 0.0392  593 TYR B CG  
5744  C CD1 . TYR B 292 ? 0.5339 0.6650 0.4999 0.0175  -0.0214 0.0396  593 TYR B CD1 
5745  C CD2 . TYR B 292 ? 0.4929 0.5915 0.4574 0.0083  -0.0181 0.0392  593 TYR B CD2 
5746  C CE1 . TYR B 292 ? 0.5780 0.7090 0.5455 0.0012  -0.0258 0.0394  593 TYR B CE1 
5747  C CE2 . TYR B 292 ? 0.6160 0.7130 0.5813 -0.0060 -0.0221 0.0398  593 TYR B CE2 
5748  C CZ  . TYR B 292 ? 0.6700 0.7814 0.6361 -0.0102 -0.0259 0.0395  593 TYR B CZ  
5749  O OH  . TYR B 292 ? 0.7122 0.8173 0.6760 -0.0255 -0.0299 0.0393  593 TYR B OH  
5750  N N   . MET B 293 ? 0.5841 0.6541 0.5332 0.0406  -0.0043 0.0347  594 MET B N   
5751  C CA  . MET B 293 ? 0.4865 0.5656 0.4337 0.0457  -0.0012 0.0337  594 MET B CA  
5752  C C   . MET B 293 ? 0.3284 0.4420 0.2846 0.0413  -0.0029 0.0364  594 MET B C   
5753  O O   . MET B 293 ? 0.4564 0.5771 0.4195 0.0272  -0.0064 0.0385  594 MET B O   
5754  C CB  . MET B 293 ? 0.5069 0.5693 0.4522 0.0383  -0.0001 0.0318  594 MET B CB  
5755  C CG  . MET B 293 ? 0.5701 0.6331 0.5087 0.0460  0.0039  0.0291  594 MET B CG  
5756  S SD  . MET B 293 ? 0.5667 0.6097 0.5017 0.0373  0.0045  0.0261  594 MET B SD  
5757  C CE  . MET B 293 ? 0.5730 0.6341 0.5192 0.0232  0.0007  0.0305  594 MET B CE  
5758  N N   . GLY B 294 ? 0.3095 0.4447 0.2645 0.0537  -0.0004 0.0365  595 GLY B N   
5759  C CA  . GLY B 294 ? 0.3268 0.5016 0.2913 0.0498  -0.0019 0.0394  595 GLY B CA  
5760  C C   . GLY B 294 ? 0.5880 0.7719 0.5594 0.0318  -0.0034 0.0415  595 GLY B C   
5761  O O   . GLY B 294 ? 0.6093 0.8146 0.5881 0.0195  -0.0065 0.0444  595 GLY B O   
5762  N N   . THR B 295 ? 0.5384 0.7053 0.5057 0.0295  -0.0012 0.0403  596 THR B N   
5763  C CA  . THR B 295 ? 0.5878 0.7610 0.5590 0.0142  -0.0021 0.0431  596 THR B CA  
5764  C C   . THR B 295 ? 0.5389 0.7011 0.5128 -0.0019 -0.0067 0.0456  596 THR B C   
5765  O O   . THR B 295 ? 0.4747 0.6474 0.4511 -0.0158 -0.0080 0.0492  596 THR B O   
5766  C CB  . THR B 295 ? 0.5904 0.7436 0.5553 0.0151  0.0001  0.0411  596 THR B CB  
5767  O OG1 . THR B 295 ? 0.4472 0.5686 0.4086 0.0123  -0.0017 0.0393  596 THR B OG1 
5768  C CG2 . THR B 295 ? 0.6349 0.7903 0.5930 0.0313  0.0048  0.0373  596 THR B CG2 
5769  N N   . GLU B 296 ? 0.6787 0.8174 0.6500 -0.0004 -0.0088 0.0437  597 GLU B N   
5770  C CA  . GLU B 296 ? 0.6536 0.7794 0.6250 -0.0135 -0.0130 0.0452  597 GLU B CA  
5771  C C   . GLU B 296 ? 0.6572 0.8076 0.6332 -0.0237 -0.0158 0.0476  597 GLU B C   
5772  O O   . GLU B 296 ? 0.6564 0.8025 0.6309 -0.0391 -0.0182 0.0500  597 GLU B O   
5773  C CB  . GLU B 296 ? 0.6491 0.7509 0.6170 -0.0078 -0.0142 0.0425  597 GLU B CB  
5774  C CG  . GLU B 296 ? 0.6318 0.7103 0.5951 -0.0009 -0.0117 0.0401  597 GLU B CG  
5775  C CD  . GLU B 296 ? 0.6102 0.6681 0.5703 0.0028  -0.0125 0.0382  597 GLU B CD  
5776  O OE1 . GLU B 296 ? 0.5211 0.5658 0.4802 -0.0043 -0.0151 0.0387  597 GLU B OE1 
5777  O OE2 . GLU B 296 ? 0.5022 0.5565 0.4593 0.0134  -0.0102 0.0363  597 GLU B OE2 
5778  N N   . ILE B 297 ? 0.5649 0.7410 0.5451 -0.0154 -0.0154 0.0469  598 ILE B N   
5779  C CA  . ILE B 297 ? 0.5544 0.7613 0.5401 -0.0257 -0.0183 0.0488  598 ILE B CA  
5780  C C   . ILE B 297 ? 0.6313 0.8687 0.6218 -0.0330 -0.0161 0.0520  598 ILE B C   
5781  O O   . ILE B 297 ? 0.6788 0.9267 0.6705 -0.0517 -0.0183 0.0548  598 ILE B O   
5782  C CB  . ILE B 297 ? 0.4586 0.6862 0.4470 -0.0123 -0.0189 0.0472  598 ILE B CB  
5783  C CG1 . ILE B 297 ? 0.4298 0.6281 0.4125 -0.0054 -0.0206 0.0446  598 ILE B CG1 
5784  C CG2 . ILE B 297 ? 0.4056 0.6713 0.4008 -0.0236 -0.0221 0.0489  598 ILE B CG2 
5785  C CD1 . ILE B 297 ? 0.4281 0.6365 0.4093 0.0145  -0.0191 0.0436  598 ILE B CD1 
5786  N N   . GLY B 298 ? 0.7152 0.9675 0.7071 -0.0183 -0.0116 0.0516  599 GLY B N   
5787  C CA  . GLY B 298 ? 0.6838 0.9731 0.6809 -0.0214 -0.0089 0.0545  599 GLY B CA  
5788  C C   . GLY B 298 ? 0.6136 0.8931 0.6077 -0.0327 -0.0069 0.0572  599 GLY B C   
5789  O O   . GLY B 298 ? 0.5546 0.8619 0.5525 -0.0449 -0.0059 0.0612  599 GLY B O   
5790  N N   . VAL B 299 ? 0.5179 0.7602 0.5049 -0.0296 -0.0064 0.0557  600 VAL B N   
5791  C CA  . VAL B 299 ? 0.5943 0.8272 0.5774 -0.0399 -0.0051 0.0589  600 VAL B CA  
5792  C C   . VAL B 299 ? 0.6436 0.8531 0.6222 -0.0580 -0.0091 0.0619  600 VAL B C   
5793  O O   . VAL B 299 ? 0.6986 0.9188 0.6762 -0.0746 -0.0094 0.0667  600 VAL B O   
5794  C CB  . VAL B 299 ? 0.5947 0.8044 0.5718 -0.0275 -0.0025 0.0559  600 VAL B CB  
5795  C CG1 . VAL B 299 ? 0.7150 0.9165 0.6874 -0.0378 -0.0018 0.0597  600 VAL B CG1 
5796  C CG2 . VAL B 299 ? 0.4175 0.6460 0.3950 -0.0098 0.0017  0.0525  600 VAL B CG2 
5797  N N   . ARG B 300 ? 0.6086 0.7853 0.5829 -0.0549 -0.0118 0.0592  601 ARG B N   
5798  C CA  . ARG B 300 ? 0.6507 0.7996 0.6175 -0.0685 -0.0151 0.0615  601 ARG B CA  
5799  C C   . ARG B 300 ? 0.6917 0.8482 0.6586 -0.0828 -0.0186 0.0623  601 ARG B C   
5800  O O   . ARG B 300 ? 0.7336 0.8825 0.6937 -0.1000 -0.0200 0.0662  601 ARG B O   
5801  C CB  . ARG B 300 ? 0.5933 0.7084 0.5556 -0.0593 -0.0164 0.0581  601 ARG B CB  
5802  C CG  . ARG B 300 ? 0.5383 0.6449 0.4997 -0.0474 -0.0136 0.0564  601 ARG B CG  
5803  C CD  . ARG B 300 ? 0.6816 0.7881 0.6384 -0.0539 -0.0123 0.0609  601 ARG B CD  
5804  N NE  . ARG B 300 ? 0.5922 0.6772 0.5403 -0.0657 -0.0148 0.0652  601 ARG B NE  
5805  C CZ  . ARG B 300 ? 0.6036 0.6604 0.5452 -0.0621 -0.0167 0.0647  601 ARG B CZ  
5806  N NH1 . ARG B 300 ? 0.6002 0.6501 0.5449 -0.0496 -0.0163 0.0601  601 ARG B NH1 
5807  N NH2 . ARG B 300 ? 0.6091 0.6444 0.5400 -0.0710 -0.0187 0.0689  601 ARG B NH2 
5808  N N   . ASP B 301 ? 0.7593 0.9291 0.7319 -0.0764 -0.0202 0.0587  602 ASP B N   
5809  C CA  . ASP B 301 ? 0.7739 0.9483 0.7453 -0.0898 -0.0244 0.0582  602 ASP B CA  
5810  C C   . ASP B 301 ? 0.7421 0.9533 0.7180 -0.1058 -0.0243 0.0616  602 ASP B C   
5811  O O   . ASP B 301 ? 0.6179 0.8228 0.5872 -0.1263 -0.0270 0.0635  602 ASP B O   
5812  C CB  . ASP B 301 ? 0.7392 0.9195 0.7149 -0.0771 -0.0262 0.0537  602 ASP B CB  
5813  C CG  . ASP B 301 ? 0.7850 0.9264 0.7536 -0.0702 -0.0277 0.0507  602 ASP B CG  
5814  O OD1 . ASP B 301 ? 0.6601 0.7729 0.6194 -0.0803 -0.0294 0.0516  602 ASP B OD1 
5815  O OD2 . ASP B 301 ? 0.8792 1.0183 0.8501 -0.0544 -0.0268 0.0478  602 ASP B OD2 
5816  N N   . TYR B 302 ? 0.7375 0.9870 0.7233 -0.0971 -0.0211 0.0624  603 TYR B N   
5817  C CA  . TYR B 302 ? 0.6986 0.9905 0.6905 -0.1116 -0.0205 0.0658  603 TYR B CA  
5818  C C   . TYR B 302 ? 0.5971 0.8895 0.5849 -0.1244 -0.0172 0.0714  603 TYR B C   
5819  O O   . TYR B 302 ? 0.5345 0.8507 0.5230 -0.1447 -0.0174 0.0752  603 TYR B O   
5820  C CB  . TYR B 302 ? 0.7605 1.0976 0.7641 -0.0945 -0.0182 0.0644  603 TYR B CB  
5821  C CG  . TYR B 302 ? 0.7241 1.0755 0.7321 -0.0879 -0.0221 0.0608  603 TYR B CG  
5822  C CD1 . TYR B 302 ? 0.6681 1.0366 0.6810 -0.0633 -0.0203 0.0584  603 TYR B CD1 
5823  C CD2 . TYR B 302 ? 0.6686 1.0156 0.6737 -0.1060 -0.0275 0.0598  603 TYR B CD2 
5824  C CE1 . TYR B 302 ? 0.5594 0.9417 0.5750 -0.0559 -0.0238 0.0559  603 TYR B CE1 
5825  C CE2 . TYR B 302 ? 0.7232 1.0852 0.7316 -0.0996 -0.0312 0.0565  603 TYR B CE2 
5826  C CZ  . TYR B 302 ? 0.7138 1.0945 0.7280 -0.0740 -0.0293 0.0549  603 TYR B CZ  
5827  O OH  . TYR B 302 ? 0.8658 1.2618 0.8820 -0.0660 -0.0330 0.0524  603 TYR B OH  
5828  N N   . CYS B 303 ? 0.6640 0.9319 0.6468 -0.1144 -0.0142 0.0723  604 CYS B N   
5829  C CA  . CYS B 303 ? 0.7159 0.9935 0.6963 -0.1219 -0.0102 0.0777  604 CYS B CA  
5830  C C   . CYS B 303 ? 0.6559 0.8920 0.6221 -0.1324 -0.0106 0.0818  604 CYS B C   
5831  O O   . CYS B 303 ? 0.6628 0.9073 0.6245 -0.1463 -0.0082 0.0878  604 CYS B O   
5832  C CB  . CYS B 303 ? 0.7556 1.0502 0.7414 -0.1008 -0.0055 0.0760  604 CYS B CB  
5833  S SG  . CYS B 303 ? 0.7684 1.1196 0.7677 -0.0889 -0.0034 0.0738  604 CYS B SG  
5834  N N   . ASP B 304 ? 0.7037 0.8974 0.6623 -0.1253 -0.0131 0.0792  605 ASP B N   
5835  C CA  . ASP B 304 ? 0.7852 0.9388 0.7283 -0.1350 -0.0142 0.0833  605 ASP B CA  
5836  C C   . ASP B 304 ? 0.9527 1.1062 0.8870 -0.1607 -0.0152 0.0886  605 ASP B C   
5837  O O   . ASP B 304 ? 1.0604 1.2367 1.0002 -0.1718 -0.0170 0.0870  605 ASP B O   
5838  C CB  . ASP B 304 ? 0.7684 0.8824 0.7049 -0.1270 -0.0178 0.0792  605 ASP B CB  
5839  C CG  . ASP B 304 ? 0.7227 0.8201 0.6594 -0.1080 -0.0166 0.0771  605 ASP B CG  
5840  O OD1 . ASP B 304 ? 0.6893 0.8083 0.6341 -0.0971 -0.0135 0.0758  605 ASP B OD1 
5841  O OD2 . ASP B 304 ? 0.6415 0.7046 0.5693 -0.1040 -0.0188 0.0763  605 ASP B OD2 
5842  N N   . ASN B 305 ? 1.0161 1.1436 0.9352 -0.1710 -0.0141 0.0950  606 ASN B N   
5843  C CA  . ASN B 305 ? 1.0014 1.1262 0.9091 -0.1975 -0.0142 0.1008  606 ASN B CA  
5844  C C   . ASN B 305 ? 1.1334 1.2256 1.0289 -0.2093 -0.0190 0.0980  606 ASN B C   
5845  O O   . ASN B 305 ? 1.2226 1.3298 1.1173 -0.2300 -0.0205 0.0980  606 ASN B O   
5846  C CB  . ASN B 305 ? 0.9402 1.0434 0.8322 -0.2040 -0.0112 0.1093  606 ASN B CB  
5847  C CG  . ASN B 305 ? 0.8770 1.0213 0.7785 -0.2037 -0.0061 0.1135  606 ASN B CG  
5848  O OD1 . ASN B 305 ? 0.8871 1.0607 0.7905 -0.2226 -0.0040 0.1176  606 ASN B OD1 
5849  N ND2 . ASN B 305 ? 0.8358 0.9842 0.7429 -0.1829 -0.0041 0.1121  606 ASN B ND2 
5850  N N   . SER B 306 ? 1.0437 1.0930 0.9293 -0.1967 -0.0214 0.0952  607 SER B N   
5851  C CA  . SER B 306 ? 0.9633 0.9779 0.8352 -0.2045 -0.0257 0.0917  607 SER B CA  
5852  C C   . SER B 306 ? 0.9679 1.0012 0.8541 -0.1957 -0.0288 0.0833  607 SER B C   
5853  O O   . SER B 306 ? 0.9364 0.9396 0.8142 -0.1908 -0.0320 0.0786  607 SER B O   
5854  C CB  . SER B 306 ? 0.8517 0.8136 0.7049 -0.1935 -0.0265 0.0929  607 SER B CB  
5855  O OG  . SER B 306 ? 1.0303 0.9933 0.8856 -0.1796 -0.0233 0.0972  607 SER B OG  
5856  N N   . ARG B 307 ? 0.9308 1.0137 0.8374 -0.1920 -0.0275 0.0815  608 ARG B N   
5857  C CA  . ARG B 307 ? 0.8697 0.9750 0.7894 -0.1835 -0.0302 0.0746  608 ARG B CA  
5858  C C   . ARG B 307 ? 0.7559 0.9114 0.6871 -0.1978 -0.0304 0.0750  608 ARG B C   
5859  O O   . ARG B 307 ? 0.7921 0.9493 0.7146 -0.2227 -0.0313 0.0780  608 ARG B O   
5860  C CB  . ARG B 307 ? 0.8031 0.9159 0.7354 -0.1564 -0.0283 0.0714  608 ARG B CB  
5861  C CG  . ARG B 307 ? 0.6920 0.7608 0.6144 -0.1432 -0.0285 0.0705  608 ARG B CG  
5862  C CD  . ARG B 307 ? 0.7420 0.7793 0.6538 -0.1449 -0.0326 0.0662  608 ARG B CD  
5863  N NE  . ARG B 307 ? 0.7234 0.7821 0.6462 -0.1382 -0.0347 0.0605  608 ARG B NE  
5864  C CZ  . ARG B 307 ? 0.7258 0.7937 0.6594 -0.1182 -0.0334 0.0573  608 ARG B CZ  
5865  N NH1 . ARG B 307 ? 0.6993 0.7583 0.6350 -0.1044 -0.0303 0.0584  608 ARG B NH1 
5866  N NH2 . ARG B 307 ? 0.7322 0.8179 0.6733 -0.1126 -0.0352 0.0531  608 ARG B NH2 
5867  N N   . TYR B 308 ? 0.6468 0.8437 0.5962 -0.1829 -0.0295 0.0722  609 TYR B N   
5868  C CA  . TYR B 308 ? 0.7121 0.9595 0.6722 -0.1952 -0.0305 0.0721  609 TYR B CA  
5869  C C   . TYR B 308 ? 0.7561 1.0392 0.7216 -0.2060 -0.0261 0.0783  609 TYR B C   
5870  O O   . TYR B 308 ? 0.8626 1.1823 0.8322 -0.2256 -0.0270 0.0798  609 TYR B O   
5871  C CB  . TYR B 308 ? 0.7995 1.0782 0.7745 -0.1744 -0.0315 0.0671  609 TYR B CB  
5872  C CG  . TYR B 308 ? 0.8995 1.1661 0.8700 -0.1792 -0.0372 0.0619  609 TYR B CG  
5873  C CD1 . TYR B 308 ? 0.8292 1.0492 0.7901 -0.1687 -0.0391 0.0583  609 TYR B CD1 
5874  C CD2 . TYR B 308 ? 0.9558 1.2587 0.9306 -0.1955 -0.0409 0.0605  609 TYR B CD2 
5875  C CE1 . TYR B 308 ? 0.7387 0.9473 0.6940 -0.1729 -0.0442 0.0533  609 TYR B CE1 
5876  C CE2 . TYR B 308 ? 0.8666 1.1586 0.8359 -0.2006 -0.0465 0.0553  609 TYR B CE2 
5877  C CZ  . TYR B 308 ? 0.7887 1.0324 0.7478 -0.1888 -0.0480 0.0516  609 TYR B CZ  
5878  O OH  . TYR B 308 ? 0.7305 0.9639 0.6829 -0.1934 -0.0533 0.0461  609 TYR B OH  
5879  N N   . ASN B 309 ? 0.7281 1.0039 0.6934 -0.1942 -0.0214 0.0817  610 ASN B N   
5880  C CA  . ASN B 309 ? 0.6352 0.9305 0.5994 -0.2071 -0.0169 0.0888  610 ASN B CA  
5881  C C   . ASN B 309 ? 0.5598 0.9209 0.5394 -0.2132 -0.0150 0.0900  610 ASN B C   
5882  O O   . ASN B 309 ? 0.4353 0.8180 0.4128 -0.2364 -0.0133 0.0955  610 ASN B O   
5883  C CB  . ASN B 309 ? 0.6157 0.8745 0.5603 -0.2337 -0.0180 0.0939  610 ASN B CB  
5884  C CG  . ASN B 309 ? 0.6854 0.9503 0.6245 -0.2438 -0.0128 0.1022  610 ASN B CG  
5885  O OD1 . ASN B 309 ? 0.7162 0.9996 0.6634 -0.2268 -0.0086 0.1035  610 ASN B OD1 
5886  N ND2 . ASN B 309 ? 0.5509 0.7980 0.4739 -0.2718 -0.0129 0.1078  610 ASN B ND2 
5887  N N   . ILE B 310 ? 0.6840 1.0781 0.6783 -0.1920 -0.0152 0.0852  611 ILE B N   
5888  C CA  . ILE B 310 ? 0.7614 1.2214 0.7705 -0.1951 -0.0143 0.0858  611 ILE B CA  
5889  C C   . ILE B 310 ? 0.8002 1.2978 0.8170 -0.1852 -0.0076 0.0895  611 ILE B C   
5890  O O   . ILE B 310 ? 0.7969 1.3538 0.8266 -0.1834 -0.0059 0.0901  611 ILE B O   
5891  C CB  . ILE B 310 ? 0.7300 1.2112 0.7496 -0.1748 -0.0174 0.0795  611 ILE B CB  
5892  C CG1 . ILE B 310 ? 0.6314 1.0930 0.6519 -0.1420 -0.0147 0.0762  611 ILE B CG1 
5893  C CG2 . ILE B 310 ? 0.8041 1.2563 0.8166 -0.1861 -0.0241 0.0756  611 ILE B CG2 
5894  C CD1 . ILE B 310 ? 0.5831 1.0716 0.6126 -0.1199 -0.0160 0.0718  611 ILE B CD1 
5895  N N   . LEU B 311 ? 0.7765 1.2433 0.7850 -0.1785 -0.0038 0.0921  612 LEU B N   
5896  C CA  . LEU B 311 ? 0.6493 1.1463 0.6634 -0.1637 0.0025  0.0941  612 LEU B CA  
5897  C C   . LEU B 311 ? 0.6488 1.2018 0.6696 -0.1821 0.0061  0.1000  612 LEU B C   
5898  O O   . LEU B 311 ? 0.6906 1.2961 0.7234 -0.1680 0.0096  0.0993  612 LEU B O   
5899  C CB  . LEU B 311 ? 0.4981 0.9504 0.5001 -0.1580 0.0051  0.0960  612 LEU B CB  
5900  C CG  . LEU B 311 ? 0.3809 0.7989 0.3805 -0.1309 0.0046  0.0898  612 LEU B CG  
5901  C CD1 . LEU B 311 ? 0.3427 0.7150 0.3292 -0.1318 0.0053  0.0921  612 LEU B CD1 
5902  C CD2 . LEU B 311 ? 0.3300 0.7816 0.3377 -0.1061 0.0089  0.0864  612 LEU B CD2 
5903  N N   . GLU B 312 ? 0.5943 1.1369 0.6063 -0.2132 0.0057  0.1061  613 GLU B N   
5904  C CA  . GLU B 312 ? 0.7012 1.2983 0.7191 -0.2345 0.0094  0.1123  613 GLU B CA  
5905  C C   . GLU B 312 ? 0.7077 1.3686 0.7431 -0.2322 0.0078  0.1092  613 GLU B C   
5906  O O   . GLU B 312 ? 0.6259 1.3379 0.6696 -0.2222 0.0109  0.1097  613 GLU B O   
5907  C CB  . GLU B 312 ? 0.7848 1.3560 0.7879 -0.2719 0.0081  0.1187  613 GLU B CB  
5908  C CG  . GLU B 312 ? 0.9081 1.4055 0.8907 -0.2743 0.0072  0.1209  613 GLU B CG  
5909  C CD  . GLU B 312 ? 0.9949 1.4419 0.9699 -0.2718 0.0003  0.1148  613 GLU B CD  
5910  O OE1 . GLU B 312 ? 1.0478 1.4713 1.0107 -0.2980 -0.0032 0.1161  613 GLU B OE1 
5911  O OE2 . GLU B 312 ? 0.8989 1.3296 0.8788 -0.2441 -0.0014 0.1085  613 GLU B OE2 
5912  N N   . GLU B 313 ? 0.8150 1.4646 0.8515 -0.2356 0.0011  0.1041  614 GLU B N   
5913  C CA  . GLU B 313 ? 0.8461 1.5517 0.8957 -0.2344 -0.0020 0.1009  614 GLU B CA  
5914  C C   . GLU B 313 ? 0.7847 1.5305 0.8490 -0.1980 0.0011  0.0976  614 GLU B C   
5915  O O   . GLU B 313 ? 0.8216 1.6171 0.8909 -0.1890 0.0011  0.0966  614 GLU B O   
5916  C CB  . GLU B 313 ? 0.8809 1.5646 0.9280 -0.2473 -0.0096 0.0965  614 GLU B CB  
5917  C CG  . GLU B 313 ? 1.0578 1.7627 1.0983 -0.2713 -0.0143 0.0955  614 GLU B CG  
5918  C CD  . GLU B 313 ? 1.1561 1.8855 1.2043 -0.2628 -0.0198 0.0894  614 GLU B CD  
5919  O OE1 . GLU B 313 ? 1.1645 1.9114 1.2256 -0.2327 -0.0192 0.0866  614 GLU B OE1 
5920  O OE2 . GLU B 313 ? 1.1836 1.9128 1.2232 -0.2854 -0.0246 0.0873  614 GLU B OE2 
5921  N N   . VAL B 314 ? 0.7312 1.4324 0.7900 -0.1703 0.0015  0.0934  615 VAL B N   
5922  C CA  . VAL B 314 ? 0.6871 1.4138 0.7531 -0.1343 0.0049  0.0900  615 VAL B CA  
5923  C C   . VAL B 314 ? 0.6832 1.4429 0.7516 -0.1277 0.0127  0.0940  615 VAL B C   
5924  O O   . VAL B 314 ? 0.8181 1.6302 0.8958 -0.1074 0.0163  0.0933  615 VAL B O   
5925  C CB  . VAL B 314 ? 0.6854 1.3519 0.7423 -0.1096 0.0035  0.0845  615 VAL B CB  
5926  C CG1 . VAL B 314 ? 0.6783 1.3657 0.7387 -0.0731 0.0072  0.0809  615 VAL B CG1 
5927  C CG2 . VAL B 314 ? 0.5861 1.2220 0.6401 -0.1167 -0.0037 0.0810  615 VAL B CG2 
5928  N N   . ALA B 315 ? 0.6298 1.3605 0.6887 -0.1436 0.0156  0.0984  616 ALA B N   
5929  C CA  . ALA B 315 ? 0.6365 1.3997 0.6966 -0.1392 0.0231  0.1025  616 ALA B CA  
5930  C C   . ALA B 315 ? 0.5650 1.3805 0.6289 -0.1512 0.0211  0.1047  616 ALA B C   
5931  O O   . ALA B 315 ? 0.5626 1.4173 0.6295 -0.1316 0.0239  0.1038  616 ALA B O   
5932  C CB  . ALA B 315 ? 0.7219 1.4386 0.7680 -0.1545 0.0252  0.1072  616 ALA B CB  
5933  N N   . LYS B 316 ? 0.5701 1.3824 0.6304 -0.1822 0.0157  0.1068  617 LYS B N   
5934  C CA  . LYS B 316 ? 0.5669 1.4247 0.6269 -0.1961 0.0134  0.1086  617 LYS B CA  
5935  C C   . LYS B 316 ? 0.5782 1.4872 0.6475 -0.1724 0.0119  0.1043  617 LYS B C   
5936  O O   . LYS B 316 ? 0.6185 1.5742 0.6892 -0.1649 0.0134  0.1055  617 LYS B O   
5937  C CB  . LYS B 316 ? 0.5819 1.4207 0.6334 -0.2330 0.0079  0.1104  617 LYS B CB  
5938  C CG  . LYS B 316 ? 0.7251 1.6118 0.7750 -0.2497 0.0057  0.1120  617 LYS B CG  
5939  C CD  . LYS B 316 ? 0.8061 1.6764 0.8468 -0.2824 -0.0001 0.1115  617 LYS B CD  
5940  C CE  . LYS B 316 ? 0.8662 1.7915 0.9063 -0.2964 -0.0021 0.1122  617 LYS B CE  
5941  N NZ  . LYS B 316 ? 0.9108 1.8344 0.9465 -0.3147 -0.0080 0.1084  617 LYS B NZ  
5942  N N   . LYS B 317 ? 0.5374 1.4377 0.6116 -0.1594 0.0089  0.0997  618 LYS B N   
5943  C CA  . LYS B 317 ? 0.6163 1.5585 0.6966 -0.1324 0.0080  0.0959  618 LYS B CA  
5944  C C   . LYS B 317 ? 0.6809 1.6368 0.7625 -0.0958 0.0137  0.0945  618 LYS B C   
5945  O O   . LYS B 317 ? 0.7055 1.6997 0.7881 -0.0720 0.0138  0.0925  618 LYS B O   
5946  C CB  . LYS B 317 ? 0.6107 1.5334 0.6946 -0.1254 0.0035  0.0913  618 LYS B CB  
5947  C CG  . LYS B 317 ? 0.6477 1.5906 0.7308 -0.1455 -0.0028 0.0901  618 LYS B CG  
5948  C CD  . LYS B 317 ? 0.6157 1.6084 0.7017 -0.1206 -0.0032 0.0878  618 LYS B CD  
5949  C CE  . LYS B 317 ? 0.7341 1.7755 0.8172 -0.1404 -0.0049 0.0898  618 LYS B CE  
5950  N NZ  . LYS B 317 ? 0.8694 1.9017 0.9497 -0.1702 -0.0107 0.0882  618 LYS B NZ  
5951  N N   . MET B 318 ? 0.6511 1.5748 0.7302 -0.0904 0.0187  0.0954  619 MET B N   
5952  C CA  . MET B 318 ? 0.5586 1.4892 0.6357 -0.0571 0.0246  0.0934  619 MET B CA  
5953  C C   . MET B 318 ? 0.5680 1.5268 0.6419 -0.0610 0.0277  0.0970  619 MET B C   
5954  O O   . MET B 318 ? 0.6228 1.5915 0.6935 -0.0333 0.0321  0.0949  619 MET B O   
5955  C CB  . MET B 318 ? 0.5234 1.4026 0.5972 -0.0461 0.0291  0.0913  619 MET B CB  
5956  C CG  . MET B 318 ? 0.4354 1.2948 0.5117 -0.0244 0.0280  0.0862  619 MET B CG  
5957  S SD  . MET B 318 ? 0.5061 1.2839 0.5664 -0.0079 0.0295  0.0812  619 MET B SD  
5958  C CE  . MET B 318 ? 0.6464 1.4453 0.7004 0.0208  0.0387  0.0795  619 MET B CE  
5959  N N   . ASN B 319 ? 0.5891 1.5585 0.6621 -0.0944 0.0255  0.1021  620 ASN B N   
5960  C CA  . ASN B 319 ? 0.6280 1.6237 0.6982 -0.1024 0.0281  0.1064  620 ASN B CA  
5961  C C   . ASN B 319 ? 0.6117 1.5739 0.6766 -0.0951 0.0341  0.1073  620 ASN B C   
5962  O O   . ASN B 319 ? 0.5888 1.5661 0.6518 -0.0708 0.0384  0.1057  620 ASN B O   
5963  C CB  . ASN B 319 ? 0.6218 1.6752 0.6941 -0.0796 0.0283  0.1051  620 ASN B CB  
5964  C CG  . ASN B 319 ? 0.7688 1.8590 0.8441 -0.0881 0.0228  0.1047  620 ASN B CG  
5965  O OD1 . ASN B 319 ? 0.8875 1.9969 0.9621 -0.1187 0.0199  0.1084  620 ASN B OD1 
5966  N ND2 . ASN B 319 ? 0.7640 1.8632 0.8406 -0.0610 0.0216  0.1003  620 ASN B ND2 
5967  N N   . LEU B 320 ? 0.5237 1.4384 0.5839 -0.1169 0.0343  0.1099  621 LEU B N   
5968  C CA  . LEU B 320 ? 0.4652 1.3414 0.5180 -0.1106 0.0397  0.1107  621 LEU B CA  
5969  C C   . LEU B 320 ? 0.6952 1.5597 0.7404 -0.1393 0.0406  0.1178  621 LEU B C   
5970  O O   . LEU B 320 ? 0.7601 1.6231 0.8035 -0.1691 0.0364  0.1219  621 LEU B O   
5971  C CB  . LEU B 320 ? 0.4291 1.2547 0.4794 -0.1070 0.0400  0.1081  621 LEU B CB  
5972  C CG  . LEU B 320 ? 0.4179 1.2451 0.4717 -0.0720 0.0417  0.1007  621 LEU B CG  
5973  C CD1 . LEU B 320 ? 0.3850 1.1540 0.4330 -0.0683 0.0404  0.0974  621 LEU B CD1 
5974  C CD2 . LEU B 320 ? 0.4453 1.2868 0.4942 -0.0431 0.0472  0.0975  621 LEU B CD2 
5975  N N   . ASP B 321 ? 0.7684 1.6229 0.8070 -0.1292 0.0460  0.1191  622 ASP B N   
5976  C CA  . ASP B 321 ? 0.9126 1.7555 0.9424 -0.1516 0.0477  0.1262  622 ASP B CA  
5977  C C   . ASP B 321 ? 0.8943 1.6779 0.9135 -0.1716 0.0466  0.1299  622 ASP B C   
5978  O O   . ASP B 321 ? 1.0080 1.7550 1.0178 -0.1635 0.0500  0.1304  622 ASP B O   
5979  C CB  . ASP B 321 ? 1.0577 1.9087 1.0831 -0.1313 0.0537  0.1255  622 ASP B CB  
5980  C CG  . ASP B 321 ? 1.1911 2.0401 1.2083 -0.1523 0.0556  0.1331  622 ASP B CG  
5981  O OD1 . ASP B 321 ? 1.2225 2.0805 1.2357 -0.1381 0.0603  0.1331  622 ASP B OD1 
5982  O OD2 . ASP B 321 ? 1.2199 2.0573 1.2334 -0.1827 0.0525  0.1390  622 ASP B OD2 
5983  N N   . MET B 322 ? 0.8109 1.5836 0.8292 -0.1981 0.0414  0.1324  623 MET B N   
5984  C CA  . MET B 322 ? 0.7428 1.4569 0.7494 -0.2160 0.0394  0.1355  623 MET B CA  
5985  C C   . MET B 322 ? 0.7807 1.4664 0.7717 -0.2393 0.0404  0.1436  623 MET B C   
5986  O O   . MET B 322 ? 0.8236 1.4611 0.8021 -0.2581 0.0377  0.1470  623 MET B O   
5987  C CB  . MET B 322 ? 0.5938 1.3035 0.6041 -0.2319 0.0330  0.1333  623 MET B CB  
5988  C CG  . MET B 322 ? 0.7186 1.4564 0.7436 -0.2090 0.0317  0.1259  623 MET B CG  
5989  S SD  . MET B 322 ? 0.8689 1.6039 0.8970 -0.2288 0.0238  0.1232  623 MET B SD  
5990  C CE  . MET B 322 ? 0.9333 1.5912 0.9443 -0.2498 0.0221  0.1268  623 MET B CE  
5991  N N   . ARG B 323 ? 0.7118 1.4242 0.7019 -0.2372 0.0442  0.1468  624 ARG B N   
5992  C CA  . ARG B 323 ? 0.6188 1.3063 0.5935 -0.2591 0.0455  0.1550  624 ARG B CA  
5993  C C   . ARG B 323 ? 0.6653 1.3031 0.6256 -0.2511 0.0486  0.1582  624 ARG B C   
5994  O O   . ARG B 323 ? 0.7327 1.3291 0.6763 -0.2700 0.0480  0.1650  624 ARG B O   
5995  C CB  . ARG B 323 ? 0.7574 1.4931 0.7359 -0.2610 0.0485  0.1578  624 ARG B CB  
5996  C CG  . ARG B 323 ? 0.8440 1.6420 0.8388 -0.2550 0.0466  0.1532  624 ARG B CG  
5997  C CD  . ARG B 323 ? 0.9797 1.8236 0.9762 -0.2578 0.0498  0.1570  624 ARG B CD  
5998  N NE  . ARG B 323 ? 0.9965 1.8335 0.9878 -0.2415 0.0558  0.1589  624 ARG B NE  
5999  C CZ  . ARG B 323 ? 0.9817 1.7917 0.9590 -0.2561 0.0586  0.1662  624 ARG B CZ  
6000  N NH1 . ARG B 323 ? 1.0103 1.7933 0.9761 -0.2869 0.0564  0.1726  624 ARG B NH1 
6001  N NH2 . ARG B 323 ? 0.9457 1.7533 0.9184 -0.2392 0.0638  0.1671  624 ARG B NH2 
6002  N N   . LYS B 324 ? 0.7674 1.4076 0.7315 -0.2231 0.0518  0.1536  625 LYS B N   
6003  C CA  . LYS B 324 ? 0.8665 1.4620 0.8160 -0.2140 0.0539  0.1559  625 LYS B CA  
6004  C C   . LYS B 324 ? 0.8386 1.4229 0.7922 -0.1899 0.0540  0.1485  625 LYS B C   
6005  O O   . LYS B 324 ? 0.9284 1.5460 0.8964 -0.1745 0.0543  0.1414  625 LYS B O   
6006  C CB  . LYS B 324 ? 0.9102 1.5206 0.8539 -0.2056 0.0590  0.1587  625 LYS B CB  
6007  C CG  . LYS B 324 ? 1.0285 1.5921 0.9538 -0.2007 0.0602  0.1626  625 LYS B CG  
6008  C CD  . LYS B 324 ? 1.1325 1.7152 1.0535 -0.1871 0.0651  0.1631  625 LYS B CD  
6009  C CE  . LYS B 324 ? 1.1793 1.7181 1.0820 -0.1792 0.0654  0.1658  625 LYS B CE  
6010  N NZ  . LYS B 324 ? 1.1641 1.7211 1.0616 -0.1653 0.0698  0.1652  625 LYS B NZ  
6011  N N   . THR B 325 ? 0.6729 1.2092 0.6121 -0.1859 0.0535  0.1504  626 THR B N   
6012  C CA  . THR B 325 ? 0.6495 1.1600 0.5926 -0.1613 0.0493  0.1396  626 THR B CA  
6013  C C   . THR B 325 ? 0.6268 1.1650 0.5755 -0.1335 0.0531  0.1315  626 THR B C   
6014  O O   . THR B 325 ? 0.6547 1.1900 0.6112 -0.1138 0.0507  0.1217  626 THR B O   
6015  C CB  . THR B 325 ? 0.6304 1.0794 0.5586 -0.1590 0.0446  0.1401  626 THR B CB  
6016  O OG1 . THR B 325 ? 0.9143 1.3597 0.8296 -0.1567 0.0484  0.1453  626 THR B OG1 
6017  C CG2 . THR B 325 ? 0.6515 1.0656 0.5712 -0.1822 0.0405  0.1465  626 THR B CG2 
6018  N N   . SER B 326 ? 0.5775 1.1403 0.5203 -0.1312 0.0593  0.1354  627 SER B N   
6019  C CA  . SER B 326 ? 0.4995 1.0793 0.4421 -0.1042 0.0629  0.1273  627 SER B CA  
6020  C C   . SER B 326 ? 0.5493 1.1678 0.5060 -0.0867 0.0647  0.1194  627 SER B C   
6021  O O   . SER B 326 ? 0.5784 1.1951 0.5329 -0.0609 0.0660  0.1100  627 SER B O   
6022  C CB  . SER B 326 ? 0.4128 1.0174 0.3485 -0.1068 0.0686  0.1328  627 SER B CB  
6023  O OG  . SER B 326 ? 0.6885 1.2645 0.6126 -0.1284 0.0669  0.1428  627 SER B OG  
6024  N N   . SER B 327 ? 0.4460 1.0992 0.4156 -0.0996 0.0646  0.1228  628 SER B N   
6025  C CA  . SER B 327 ? 0.4986 1.1877 0.4816 -0.0811 0.0650  0.1155  628 SER B CA  
6026  C C   . SER B 327 ? 0.4613 1.1150 0.4453 -0.0647 0.0600  0.1066  628 SER B C   
6027  O O   . SER B 327 ? 0.5653 1.2407 0.5556 -0.0431 0.0611  0.0997  628 SER B O   
6028  C CB  . SER B 327 ? 0.4809 1.2055 0.4780 -0.0989 0.0614  0.1191  628 SER B CB  
6029  O OG  . SER B 327 ? 0.5436 1.2395 0.5399 -0.1221 0.0571  0.1234  628 SER B OG  
6030  N N   . LEU B 328 ? 0.4128 1.0109 0.3900 -0.0734 0.0541  0.1065  629 LEU B N   
6031  C CA  . LEU B 328 ? 0.4226 0.9821 0.4003 -0.0601 0.0485  0.0983  629 LEU B CA  
6032  C C   . LEU B 328 ? 0.5508 1.1322 0.5417 -0.0621 0.0457  0.0970  629 LEU B C   
6033  O O   . LEU B 328 ? 0.5395 1.1129 0.5332 -0.0426 0.0438  0.0895  629 LEU B O   
6034  C CB  . LEU B 328 ? 0.4602 1.0075 0.4310 -0.0310 0.0505  0.0885  629 LEU B CB  
6035  C CG  . LEU B 328 ? 0.4982 1.0227 0.4550 -0.0272 0.0524  0.0878  629 LEU B CG  
6036  C CD1 . LEU B 328 ? 0.3887 0.8809 0.3371 -0.0040 0.0513  0.0767  629 LEU B CD1 
6037  C CD2 . LEU B 328 ? 0.4666 0.9563 0.4171 -0.0486 0.0485  0.0949  629 LEU B CD2 
6038  N N   . TRP B 329 ? 0.4630 1.0722 0.4609 -0.0867 0.0454  0.1047  630 TRP B N   
6039  C CA  . TRP B 329 ? 0.4357 1.0752 0.4466 -0.0904 0.0428  0.1038  630 TRP B CA  
6040  C C   . TRP B 329 ? 0.4464 1.0401 0.4565 -0.0913 0.0354  0.0995  630 TRP B C   
6041  O O   . TRP B 329 ? 0.4664 1.0694 0.4836 -0.0766 0.0332  0.0940  630 TRP B O   
6042  C CB  . TRP B 329 ? 0.4861 1.1665 0.5031 -0.1202 0.0443  0.1128  630 TRP B CB  
6043  C CG  . TRP B 329 ? 0.6018 1.2436 0.6083 -0.1501 0.0416  0.1200  630 TRP B CG  
6044  C CD1 . TRP B 329 ? 0.6484 1.2804 0.6437 -0.1641 0.0453  0.1276  630 TRP B CD1 
6045  C CD2 . TRP B 329 ? 0.6382 1.2447 0.6419 -0.1686 0.0349  0.1205  630 TRP B CD2 
6046  N NE1 . TRP B 329 ? 0.7445 1.3349 0.7291 -0.1892 0.0414  0.1331  630 TRP B NE1 
6047  C CE2 . TRP B 329 ? 0.7710 1.3444 0.7603 -0.1923 0.0351  0.1284  630 TRP B CE2 
6048  C CE3 . TRP B 329 ? 0.5900 1.1887 0.6004 -0.1666 0.0290  0.1150  630 TRP B CE3 
6049  C CZ2 . TRP B 329 ? 0.6886 1.2192 0.6689 -0.2130 0.0296  0.1305  630 TRP B CZ2 
6050  C CZ3 . TRP B 329 ? 0.5684 1.1273 0.5710 -0.1881 0.0235  0.1168  630 TRP B CZ3 
6051  C CH2 . TRP B 329 ? 0.6021 1.1267 0.5894 -0.2107 0.0239  0.1242  630 TRP B CH2 
6052  N N   . LYS B 330 ? 0.3910 0.9353 0.3912 -0.1069 0.0319  0.1023  631 LYS B N   
6053  C CA  . LYS B 330 ? 0.4047 0.9005 0.4016 -0.1040 0.0256  0.0977  631 LYS B CA  
6054  C C   . LYS B 330 ? 0.5197 1.0014 0.5168 -0.0744 0.0256  0.0888  631 LYS B C   
6055  O O   . LYS B 330 ? 0.5528 1.0252 0.5541 -0.0661 0.0220  0.0840  631 LYS B O   
6056  C CB  . LYS B 330 ? 0.4274 0.8724 0.4108 -0.1170 0.0234  0.1016  631 LYS B CB  
6057  C CG  . LYS B 330 ? 0.5171 0.9585 0.4948 -0.1475 0.0226  0.1104  631 LYS B CG  
6058  C CD  . LYS B 330 ? 0.6107 0.9910 0.5741 -0.1538 0.0183  0.1118  631 LYS B CD  
6059  C CE  . LYS B 330 ? 0.5716 0.9343 0.5240 -0.1828 0.0169  0.1200  631 LYS B CE  
6060  N NZ  . LYS B 330 ? 0.7000 1.0031 0.6393 -0.1817 0.0122  0.1191  631 LYS B NZ  
6061  N N   . ASP B 331 ? 0.5098 0.9872 0.5003 -0.0591 0.0297  0.0865  632 ASP B N   
6062  C CA  . ASP B 331 ? 0.4927 0.9486 0.4792 -0.0336 0.0298  0.0778  632 ASP B CA  
6063  C C   . ASP B 331 ? 0.5405 1.0285 0.5345 -0.0155 0.0312  0.0735  632 ASP B C   
6064  O O   . ASP B 331 ? 0.4475 0.9129 0.4401 -0.0012 0.0288  0.0677  632 ASP B O   
6065  C CB  . ASP B 331 ? 0.3453 0.7945 0.3217 -0.0222 0.0341  0.0756  632 ASP B CB  
6066  C CG  . ASP B 331 ? 0.4244 0.8481 0.3928 -0.0385 0.0329  0.0809  632 ASP B CG  
6067  O OD1 . ASP B 331 ? 0.5013 0.9488 0.4698 -0.0535 0.0356  0.0885  632 ASP B OD1 
6068  O OD2 . ASP B 331 ? 0.4499 0.8311 0.4112 -0.0361 0.0296  0.0778  632 ASP B OD2 
6069  N N   . GLN B 332 ? 0.5849 1.1269 0.5863 -0.0154 0.0353  0.0768  633 GLN B N   
6070  C CA  . GLN B 332 ? 0.6122 1.1903 0.6196 0.0054  0.0373  0.0732  633 GLN B CA  
6071  C C   . GLN B 332 ? 0.5645 1.1459 0.5808 -0.0002 0.0317  0.0732  633 GLN B C   
6072  O O   . GLN B 332 ? 0.4969 1.0700 0.5119 0.0201  0.0306  0.0680  633 GLN B O   
6073  C CB  . GLN B 332 ? 0.5552 1.1962 0.5694 0.0057  0.0431  0.0773  633 GLN B CB  
6074  C CG  . GLN B 332 ? 0.5786 1.2334 0.5856 0.0363  0.0491  0.0718  633 GLN B CG  
6075  C CD  . GLN B 332 ? 0.7435 1.4607 0.7562 0.0372  0.0555  0.0760  633 GLN B CD  
6076  O OE1 . GLN B 332 ? 0.8181 1.5603 0.8372 0.0118  0.0563  0.0836  633 GLN B OE1 
6077  N NE2 . GLN B 332 ? 0.8022 1.5442 0.8108 0.0669  0.0606  0.0713  633 GLN B NE2 
6078  N N   . ALA B 333 ? 0.5999 1.1913 0.6231 -0.0280 0.0283  0.0790  634 ALA B N   
6079  C CA  . ALA B 333 ? 0.5169 1.1076 0.5466 -0.0361 0.0224  0.0785  634 ALA B CA  
6080  C C   . ALA B 333 ? 0.4540 0.9866 0.4759 -0.0273 0.0182  0.0733  634 ALA B C   
6081  O O   . ALA B 333 ? 0.4415 0.9730 0.4658 -0.0156 0.0154  0.0698  634 ALA B O   
6082  C CB  . ALA B 333 ? 0.4185 1.0185 0.4520 -0.0703 0.0195  0.0849  634 ALA B CB  
6083  N N   . LEU B 334 ? 0.4049 0.8909 0.4170 -0.0323 0.0180  0.0730  635 LEU B N   
6084  C CA  . LEU B 334 ? 0.3788 0.8128 0.3842 -0.0256 0.0143  0.0685  635 LEU B CA  
6085  C C   . LEU B 334 ? 0.5458 0.9751 0.5482 0.0025  0.0160  0.0621  635 LEU B C   
6086  O O   . LEU B 334 ? 0.6170 1.0254 0.6186 0.0085  0.0126  0.0591  635 LEU B O   
6087  C CB  . LEU B 334 ? 0.4044 0.7975 0.3999 -0.0317 0.0146  0.0690  635 LEU B CB  
6088  C CG  . LEU B 334 ? 0.3855 0.7286 0.3741 -0.0240 0.0115  0.0642  635 LEU B CG  
6089  C CD1 . LEU B 334 ? 0.4131 0.7396 0.4043 -0.0364 0.0060  0.0651  635 LEU B CD1 
6090  C CD2 . LEU B 334 ? 0.5755 0.8878 0.5552 -0.0271 0.0121  0.0645  635 LEU B CD2 
6091  N N   . VAL B 335 ? 0.5314 0.9791 0.5303 0.0202  0.0215  0.0601  636 VAL B N   
6092  C CA  . VAL B 335 ? 0.5545 0.9924 0.5462 0.0478  0.0236  0.0540  636 VAL B CA  
6093  C C   . VAL B 335 ? 0.5441 1.0126 0.5431 0.0572  0.0220  0.0545  636 VAL B C   
6094  O O   . VAL B 335 ? 0.5337 0.9784 0.5278 0.0700  0.0200  0.0512  636 VAL B O   
6095  C CB  . VAL B 335 ? 0.4594 0.9094 0.4429 0.0652  0.0301  0.0513  636 VAL B CB  
6096  C CG1 . VAL B 335 ? 0.4530 0.9125 0.4303 0.0943  0.0330  0.0470  636 VAL B CG1 
6097  C CG2 . VAL B 335 ? 0.5019 0.9058 0.4730 0.0648  0.0308  0.0475  636 VAL B CG2 
6098  N N   . GLU B 336 ? 0.4012 0.9246 0.4118 0.0501  0.0226  0.0589  637 GLU B N   
6099  C CA  . GLU B 336 ? 0.4495 1.0105 0.4678 0.0602  0.0209  0.0594  637 GLU B CA  
6100  C C   . GLU B 336 ? 0.5431 1.0823 0.5643 0.0485  0.0141  0.0593  637 GLU B C   
6101  O O   . GLU B 336 ? 0.6557 1.1947 0.6753 0.0651  0.0124  0.0572  637 GLU B O   
6102  C CB  . GLU B 336 ? 0.3904 1.0182 0.4219 0.0499  0.0225  0.0643  637 GLU B CB  
6103  C CG  . GLU B 336 ? 0.3986 1.0582 0.4277 0.0657  0.0298  0.0644  637 GLU B CG  
6104  C CD  . GLU B 336 ? 0.4825 1.1475 0.5027 0.1031  0.0337  0.0598  637 GLU B CD  
6105  O OE1 . GLU B 336 ? 0.5551 1.1973 0.5700 0.1181  0.0310  0.0569  637 GLU B OE1 
6106  O OE2 . GLU B 336 ? 0.5752 1.2664 0.5919 0.1185  0.0399  0.0591  637 GLU B OE2 
6107  N N   . ILE B 337 ? 0.5047 1.0239 0.5284 0.0210  0.0104  0.0617  638 ILE B N   
6108  C CA  . ILE B 337 ? 0.4935 0.9877 0.5178 0.0096  0.0042  0.0610  638 ILE B CA  
6109  C C   . ILE B 337 ? 0.5504 0.9970 0.5644 0.0280  0.0037  0.0564  638 ILE B C   
6110  O O   . ILE B 337 ? 0.5871 1.0290 0.6010 0.0343  0.0004  0.0550  638 ILE B O   
6111  C CB  . ILE B 337 ? 0.4125 0.8842 0.4364 -0.0202 0.0012  0.0640  638 ILE B CB  
6112  C CG1 . ILE B 337 ? 0.4556 0.9745 0.4883 -0.0416 0.0014  0.0691  638 ILE B CG1 
6113  C CG2 . ILE B 337 ? 0.4084 0.8471 0.4297 -0.0291 -0.0047 0.0622  638 ILE B CG2 
6114  C CD1 . ILE B 337 ? 0.6079 1.1022 0.6366 -0.0707 -0.0010 0.0726  638 ILE B CD1 
6115  N N   . ASN B 338 ? 0.5914 1.0033 0.5958 0.0362  0.0072  0.0539  639 ASN B N   
6116  C CA  . ASN B 338 ? 0.6061 0.9721 0.5999 0.0503  0.0070  0.0496  639 ASN B CA  
6117  C C   . ASN B 338 ? 0.5793 0.9545 0.5668 0.0783  0.0100  0.0471  639 ASN B C   
6118  O O   . ASN B 338 ? 0.6626 1.0092 0.6425 0.0889  0.0089  0.0449  639 ASN B O   
6119  C CB  . ASN B 338 ? 0.6321 0.9593 0.6172 0.0477  0.0092  0.0474  639 ASN B CB  
6120  C CG  . ASN B 338 ? 0.5638 0.8665 0.5509 0.0247  0.0052  0.0495  639 ASN B CG  
6121  O OD1 . ASN B 338 ? 0.5799 0.8465 0.5627 0.0232  0.0028  0.0475  639 ASN B OD1 
6122  N ND2 . ASN B 338 ? 0.5194 0.8421 0.5120 0.0071  0.0048  0.0538  639 ASN B ND2 
6123  N N   . ILE B 339 ? 0.4918 0.9061 0.4808 0.0912  0.0141  0.0478  640 ILE B N   
6124  C CA  . ILE B 339 ? 0.4253 0.8532 0.4076 0.1196  0.0166  0.0462  640 ILE B CA  
6125  C C   . ILE B 339 ? 0.5960 1.0505 0.5868 0.1193  0.0119  0.0488  640 ILE B C   
6126  O O   . ILE B 339 ? 0.6151 1.0612 0.5975 0.1403  0.0120  0.0477  640 ILE B O   
6127  C CB  . ILE B 339 ? 0.3352 0.8033 0.3172 0.1347  0.0223  0.0464  640 ILE B CB  
6128  C CG1 . ILE B 339 ? 0.4709 0.9045 0.4389 0.1416  0.0272  0.0423  640 ILE B CG1 
6129  C CG2 . ILE B 339 ? 0.3481 0.8428 0.3252 0.1643  0.0243  0.0462  640 ILE B CG2 
6130  C CD1 . ILE B 339 ? 0.3553 0.8248 0.3202 0.1589  0.0332  0.0417  640 ILE B CD1 
6131  N N   . ALA B 340 ? 0.6218 1.1060 0.6273 0.0951  0.0075  0.0521  641 ALA B N   
6132  C CA  . ALA B 340 ? 0.4773 0.9905 0.4909 0.0925  0.0024  0.0538  641 ALA B CA  
6133  C C   . ALA B 340 ? 0.5653 1.0331 0.5729 0.0878  -0.0019 0.0522  641 ALA B C   
6134  O O   . ALA B 340 ? 0.6388 1.1102 0.6434 0.1019  -0.0040 0.0520  641 ALA B O   
6135  C CB  . ALA B 340 ? 0.4583 1.0159 0.4871 0.0653  -0.0008 0.0573  641 ALA B CB  
6136  N N   . VAL B 341 ? 0.5293 0.9565 0.5349 0.0689  -0.0032 0.0512  642 VAL B N   
6137  C CA  . VAL B 341 ? 0.4597 0.8441 0.4595 0.0641  -0.0068 0.0496  642 VAL B CA  
6138  C C   . VAL B 341 ? 0.5680 0.9226 0.5545 0.0896  -0.0040 0.0474  642 VAL B C   
6139  O O   . VAL B 341 ? 0.4530 0.8027 0.4362 0.0976  -0.0065 0.0475  642 VAL B O   
6140  C CB  . VAL B 341 ? 0.2963 0.6430 0.2945 0.0440  -0.0074 0.0490  642 VAL B CB  
6141  C CG1 . VAL B 341 ? 0.2978 0.5959 0.2872 0.0463  -0.0087 0.0466  642 VAL B CG1 
6142  C CG2 . VAL B 341 ? 0.3268 0.6934 0.3341 0.0168  -0.0116 0.0516  642 VAL B CG2 
6143  N N   . LEU B 342 ? 0.5689 0.9018 0.5458 0.1021  0.0014  0.0454  643 LEU B N   
6144  C CA  . LEU B 342 ? 0.5424 0.8423 0.5031 0.1250  0.0048  0.0432  643 LEU B CA  
6145  C C   . LEU B 342 ? 0.5780 0.9061 0.5354 0.1480  0.0051  0.0449  643 LEU B C   
6146  O O   . LEU B 342 ? 0.5853 0.8911 0.5326 0.1599  0.0045  0.0451  643 LEU B O   
6147  C CB  . LEU B 342 ? 0.6016 0.8806 0.5514 0.1341  0.0106  0.0401  643 LEU B CB  
6148  C CG  . LEU B 342 ? 0.5853 0.8279 0.5338 0.1163  0.0105  0.0379  643 LEU B CG  
6149  C CD1 . LEU B 342 ? 0.4563 0.6890 0.3954 0.1241  0.0157  0.0347  643 LEU B CD1 
6150  C CD2 . LEU B 342 ? 0.5048 0.7029 0.4443 0.1157  0.0094  0.0364  643 LEU B CD2 
6151  N N   . TYR B 343 ? 0.6225 1.0016 0.5878 0.1553  0.0062  0.0466  644 TYR B N   
6152  C CA  . TYR B 343 ? 0.6102 1.0212 0.5719 0.1807  0.0068  0.0485  644 TYR B CA  
6153  C C   . TYR B 343 ? 0.7620 1.1907 0.7308 0.1751  0.0005  0.0509  644 TYR B C   
6154  O O   . TYR B 343 ? 0.7692 1.2029 0.7294 0.1974  0.0003  0.0524  644 TYR B O   
6155  C CB  . TYR B 343 ? 0.4138 0.8830 0.3851 0.1871  0.0092  0.0500  644 TYR B CB  
6156  C CG  . TYR B 343 ? 0.3873 0.9070 0.3607 0.2093  0.0085  0.0527  644 TYR B CG  
6157  C CD1 . TYR B 343 ? 0.4397 0.9491 0.3950 0.2444  0.0130  0.0524  644 TYR B CD1 
6158  C CD2 . TYR B 343 ? 0.4594 1.0386 0.4519 0.1954  0.0035  0.0556  644 TYR B CD2 
6159  C CE1 . TYR B 343 ? 0.5346 1.0932 0.4912 0.2675  0.0124  0.0554  644 TYR B CE1 
6160  C CE2 . TYR B 343 ? 0.5577 1.1898 0.5535 0.2159  0.0025  0.0582  644 TYR B CE2 
6161  C CZ  . TYR B 343 ? 0.6448 1.2678 0.6231 0.2532  0.0069  0.0584  644 TYR B CZ  
6162  O OH  . TYR B 343 ? 0.6977 1.3682 0.6749 0.2728  0.0065  0.0607  644 TYR B OH  
6163  N N   . SER B 344 ? 0.6989 1.1351 0.6813 0.1463  -0.0048 0.0512  645 SER B N   
6164  C CA  . SER B 344 ? 0.4943 0.9491 0.4826 0.1394  -0.0111 0.0525  645 SER B CA  
6165  C C   . SER B 344 ? 0.5901 0.9932 0.5657 0.1434  -0.0122 0.0515  645 SER B C   
6166  O O   . SER B 344 ? 0.7428 1.1524 0.7130 0.1579  -0.0143 0.0530  645 SER B O   
6167  C CB  . SER B 344 ? 0.4444 0.9225 0.4482 0.1068  -0.0160 0.0527  645 SER B CB  
6168  O OG  . SER B 344 ? 0.3956 0.9308 0.4113 0.1037  -0.0152 0.0545  645 SER B OG  
6169  N N   . PHE B 345 ? 0.5388 0.8922 0.5091 0.1316  -0.0105 0.0493  646 PHE B N   
6170  C CA  . PHE B 345 ? 0.5453 0.8503 0.5033 0.1351  -0.0106 0.0485  646 PHE B CA  
6171  C C   . PHE B 345 ? 0.6748 0.9603 0.6149 0.1644  -0.0060 0.0495  646 PHE B C   
6172  O O   . PHE B 345 ? 0.7988 1.0642 0.7291 0.1726  -0.0069 0.0508  646 PHE B O   
6173  C CB  . PHE B 345 ? 0.3749 0.6360 0.3309 0.1187  -0.0090 0.0461  646 PHE B CB  
6174  C CG  . PHE B 345 ? 0.4347 0.6938 0.4006 0.0927  -0.0141 0.0454  646 PHE B CG  
6175  C CD1 . PHE B 345 ? 0.4499 0.7446 0.4289 0.0754  -0.0174 0.0461  646 PHE B CD1 
6176  C CD2 . PHE B 345 ? 0.3658 0.5860 0.3259 0.0855  -0.0152 0.0442  646 PHE B CD2 
6177  C CE1 . PHE B 345 ? 0.4683 0.7549 0.4523 0.0517  -0.0218 0.0453  646 PHE B CE1 
6178  C CE2 . PHE B 345 ? 0.4484 0.6637 0.4149 0.0639  -0.0196 0.0433  646 PHE B CE2 
6179  C CZ  . PHE B 345 ? 0.4533 0.6993 0.4305 0.0473  -0.0230 0.0437  646 PHE B CZ  
6180  N N   . GLN B 346 ? 0.6939 0.9820 0.6272 0.1807  -0.0007 0.0490  647 GLN B N   
6181  C CA  . GLN B 346 ? 0.7190 0.9805 0.6308 0.2089  0.0042  0.0497  647 GLN B CA  
6182  C C   . GLN B 346 ? 0.7340 1.0333 0.6437 0.2312  0.0025  0.0534  647 GLN B C   
6183  O O   . GLN B 346 ? 0.7739 1.0483 0.6653 0.2517  0.0044  0.0555  647 GLN B O   
6184  C CB  . GLN B 346 ? 0.6482 0.8960 0.5497 0.2205  0.0106  0.0470  647 GLN B CB  
6185  C CG  . GLN B 346 ? 0.7098 0.9080 0.6050 0.2054  0.0132  0.0431  647 GLN B CG  
6186  C CD  . GLN B 346 ? 0.7044 0.9011 0.5945 0.2109  0.0181  0.0398  647 GLN B CD  
6187  O OE1 . GLN B 346 ? 0.7216 0.9595 0.6171 0.2220  0.0193  0.0406  647 GLN B OE1 
6188  N NE2 . GLN B 346 ? 0.6960 0.8479 0.5759 0.2028  0.0209  0.0360  647 GLN B NE2 
6189  N N   . SER B 347 ? 0.6712 1.0314 0.5988 0.2273  -0.0009 0.0546  648 SER B N   
6190  C CA  . SER B 347 ? 0.5530 0.9585 0.4812 0.2478  -0.0032 0.0582  648 SER B CA  
6191  C C   . SER B 347 ? 0.5928 0.9980 0.5223 0.2412  -0.0093 0.0600  648 SER B C   
6192  O O   . SER B 347 ? 0.6246 1.0492 0.5467 0.2633  -0.0106 0.0634  648 SER B O   
6193  C CB  . SER B 347 ? 0.5021 0.9775 0.4505 0.2419  -0.0053 0.0588  648 SER B CB  
6194  O OG  . SER B 347 ? 0.6477 1.1279 0.5921 0.2545  0.0010  0.0576  648 SER B OG  
6195  N N   . ASP B 348 ? 0.4624 0.8476 0.4003 0.2126  -0.0130 0.0579  649 ASP B N   
6196  C CA  . ASP B 348 ? 0.4709 0.8502 0.4084 0.2046  -0.0184 0.0587  649 ASP B CA  
6197  C C   . ASP B 348 ? 0.5305 0.8453 0.4502 0.2081  -0.0153 0.0587  649 ASP B C   
6198  O O   . ASP B 348 ? 0.5798 0.8781 0.5006 0.1934  -0.0188 0.0581  649 ASP B O   
6199  C CB  . ASP B 348 ? 0.3576 0.7571 0.3136 0.1716  -0.0246 0.0562  649 ASP B CB  
6200  C CG  . ASP B 348 ? 0.4466 0.9151 0.4192 0.1659  -0.0288 0.0568  649 ASP B CG  
6201  O OD1 . ASP B 348 ? 0.4300 0.9349 0.4016 0.1890  -0.0270 0.0593  649 ASP B OD1 
6202  O OD2 . ASP B 348 ? 0.6001 1.0864 0.5855 0.1383  -0.0340 0.0548  649 ASP B OD2 
6203  N N   . LYS B 349 ? 0.6213 0.8999 0.5233 0.2270  -0.0084 0.0593  650 LYS B N   
6204  C CA  . LYS B 349 ? 0.6076 0.8228 0.4916 0.2277  -0.0040 0.0589  650 LYS B CA  
6205  C C   . LYS B 349 ? 0.6923 0.8846 0.5849 0.1996  -0.0068 0.0564  650 LYS B C   
6206  O O   . LYS B 349 ? 0.7919 0.9529 0.6744 0.1987  -0.0067 0.0577  650 LYS B O   
6207  C CB  . LYS B 349 ? 0.5157 0.7127 0.3784 0.2525  -0.0024 0.0635  650 LYS B CB  
6208  C CG  . LYS B 349 ? 0.7655 0.9862 0.6174 0.2844  0.0003  0.0664  650 LYS B CG  
6209  C CD  . LYS B 349 ? 1.0199 1.2069 0.8435 0.3115  0.0037  0.0715  650 LYS B CD  
6210  C CE  . LYS B 349 ? 1.1858 1.3053 0.9841 0.3177  0.0117  0.0705  650 LYS B CE  
6211  N NZ  . LYS B 349 ? 1.2481 1.3665 1.0346 0.3390  0.0171  0.0690  650 LYS B NZ  
6212  N N   . VAL B 350 ? 0.4878 0.6949 0.3976 0.1775  -0.0090 0.0532  651 VAL B N   
6213  C CA  . VAL B 350 ? 0.5195 0.7031 0.4360 0.1528  -0.0110 0.0507  651 VAL B CA  
6214  C C   . VAL B 350 ? 0.6740 0.8220 0.5860 0.1472  -0.0060 0.0482  651 VAL B C   
6215  O O   . VAL B 350 ? 0.7323 0.8921 0.6475 0.1494  -0.0036 0.0469  651 VAL B O   
6216  C CB  . VAL B 350 ? 0.4577 0.6778 0.3932 0.1313  -0.0172 0.0492  651 VAL B CB  
6217  C CG1 . VAL B 350 ? 0.3920 0.5844 0.3313 0.1091  -0.0188 0.0467  651 VAL B CG1 
6218  C CG2 . VAL B 350 ? 0.4090 0.6655 0.3482 0.1349  -0.0228 0.0509  651 VAL B CG2 
6219  N N   . THR B 351 ? 0.5745 0.6815 0.4788 0.1400  -0.0043 0.0473  652 THR B N   
6220  C CA  . THR B 351 ? 0.5930 0.6670 0.4915 0.1351  0.0004  0.0447  652 THR B CA  
6221  C C   . THR B 351 ? 0.5849 0.6752 0.4984 0.1188  -0.0012 0.0422  652 THR B C   
6222  O O   . THR B 351 ? 0.6591 0.7670 0.5858 0.1030  -0.0059 0.0420  652 THR B O   
6223  C CB  . THR B 351 ? 0.5270 0.5624 0.4180 0.1265  0.0018  0.0443  652 THR B CB  
6224  O OG1 . THR B 351 ? 0.6220 0.6369 0.4952 0.1424  0.0047  0.0473  652 THR B OG1 
6225  C CG2 . THR B 351 ? 0.5122 0.5195 0.3991 0.1188  0.0058  0.0412  652 THR B CG2 
6226  N N   . ILE B 352 ? 0.5818 0.6647 0.4908 0.1232  0.0028  0.0403  653 ILE B N   
6227  C CA  . ILE B 352 ? 0.4701 0.5641 0.3903 0.1092  0.0022  0.0383  653 ILE B CA  
6228  C C   . ILE B 352 ? 0.4652 0.5352 0.3735 0.1161  0.0075  0.0354  653 ILE B C   
6229  O O   . ILE B 352 ? 0.4753 0.5315 0.3680 0.1342  0.0115  0.0352  653 ILE B O   
6230  C CB  . ILE B 352 ? 0.4662 0.6075 0.3996 0.1082  -0.0005 0.0399  653 ILE B CB  
6231  C CG1 . ILE B 352 ? 0.4202 0.5709 0.3657 0.0882  -0.0024 0.0392  653 ILE B CG1 
6232  C CG2 . ILE B 352 ? 0.3561 0.5127 0.2825 0.1286  0.0034  0.0400  653 ILE B CG2 
6233  C CD1 . ILE B 352 ? 0.4681 0.6649 0.4262 0.0827  -0.0050 0.0412  653 ILE B CD1 
6234  N N   . VAL B 353 ? 0.5333 0.5959 0.4467 0.1019  0.0076  0.0331  654 VAL B N   
6235  C CA  . VAL B 353 ? 0.5277 0.5688 0.4301 0.1053  0.0120  0.0294  654 VAL B CA  
6236  C C   . VAL B 353 ? 0.6439 0.7096 0.5564 0.0982  0.0115  0.0286  654 VAL B C   
6237  O O   . VAL B 353 ? 0.6554 0.7382 0.5821 0.0831  0.0077  0.0305  654 VAL B O   
6238  C CB  . VAL B 353 ? 0.5510 0.5551 0.4469 0.0946  0.0130  0.0271  654 VAL B CB  
6239  C CG1 . VAL B 353 ? 0.5255 0.5364 0.4364 0.0760  0.0085  0.0282  654 VAL B CG1 
6240  C CG2 . VAL B 353 ? 0.5995 0.5835 0.4841 0.0949  0.0168  0.0224  654 VAL B CG2 
6241  N N   . ASP B 354 ? 0.6309 0.6980 0.5343 0.1099  0.0156  0.0262  655 ASP B N   
6242  C CA  . ASP B 354 ? 0.5954 0.6853 0.5066 0.1038  0.0158  0.0256  655 ASP B CA  
6243  C C   . ASP B 354 ? 0.7366 0.8021 0.6448 0.0909  0.0161  0.0222  655 ASP B C   
6244  O O   . ASP B 354 ? 0.7768 0.8091 0.6756 0.0884  0.0169  0.0196  655 ASP B O   
6245  C CB  . ASP B 354 ? 0.6105 0.7174 0.5136 0.1226  0.0200  0.0242  655 ASP B CB  
6246  C CG  . ASP B 354 ? 0.6896 0.7595 0.5701 0.1357  0.0251  0.0189  655 ASP B CG  
6247  O OD1 . ASP B 354 ? 0.7964 0.8566 0.6627 0.1553  0.0279  0.0187  655 ASP B OD1 
6248  O OD2 . ASP B 354 ? 0.7170 0.7667 0.5920 0.1267  0.0261  0.0148  655 ASP B OD2 
6249  N N   . HIS B 355 ? 0.6698 0.7542 0.5858 0.0822  0.0155  0.0225  656 HIS B N   
6250  C CA  . HIS B 355 ? 0.6092 0.6758 0.5240 0.0697  0.0148  0.0201  656 HIS B CA  
6251  C C   . HIS B 355 ? 0.6517 0.6942 0.5493 0.0770  0.0188  0.0138  656 HIS B C   
6252  O O   . HIS B 355 ? 0.6282 0.6497 0.5219 0.0673  0.0182  0.0107  656 HIS B O   
6253  C CB  . HIS B 355 ? 0.6104 0.7020 0.5366 0.0580  0.0128  0.0232  656 HIS B CB  
6254  C CG  . HIS B 355 ? 0.6900 0.8122 0.6175 0.0658  0.0154  0.0243  656 HIS B CG  
6255  N ND1 . HIS B 355 ? 0.6647 0.8174 0.6004 0.0701  0.0150  0.0282  656 HIS B ND1 
6256  C CD2 . HIS B 355 ? 0.6872 0.8178 0.6093 0.0693  0.0184  0.0221  656 HIS B CD2 
6257  C CE1 . HIS B 355 ? 0.6953 0.8753 0.6312 0.0764  0.0180  0.0285  656 HIS B CE1 
6258  N NE2 . HIS B 355 ? 0.7231 0.8891 0.6502 0.0765  0.0203  0.0248  656 HIS B NE2 
6259  N N   . HIS B 356 ? 0.6122 0.6565 0.4981 0.0942  0.0229  0.0115  657 HIS B N   
6260  C CA  . HIS B 356 ? 0.6146 0.6298 0.4798 0.1017  0.0270  0.0046  657 HIS B CA  
6261  C C   . HIS B 356 ? 0.6851 0.6600 0.5365 0.1016  0.0280  0.0021  657 HIS B C   
6262  O O   . HIS B 356 ? 0.6916 0.6401 0.5334 0.0924  0.0285  -0.0028 657 HIS B O   
6263  C CB  . HIS B 356 ? 0.5509 0.5780 0.4052 0.1224  0.0315  0.0029  657 HIS B CB  
6264  C CG  . HIS B 356 ? 0.6325 0.7027 0.5004 0.1217  0.0312  0.0059  657 HIS B CG  
6265  N ND1 . HIS B 356 ? 0.6324 0.7087 0.4990 0.1154  0.0321  0.0031  657 HIS B ND1 
6266  C CD2 . HIS B 356 ? 0.6113 0.7218 0.4943 0.1245  0.0301  0.0117  657 HIS B CD2 
6267  C CE1 . HIS B 356 ? 0.6371 0.7543 0.5168 0.1148  0.0320  0.0076  657 HIS B CE1 
6268  N NE2 . HIS B 356 ? 0.5358 0.6749 0.4258 0.1195  0.0309  0.0127  657 HIS B NE2 
6269  N N   . SER B 357 ? 0.7499 0.7210 0.5999 0.1107  0.0282  0.0055  658 SER B N   
6270  C CA  . SER B 357 ? 0.7619 0.6943 0.5974 0.1102  0.0297  0.0041  658 SER B CA  
6271  C C   . SER B 357 ? 0.6680 0.5956 0.5161 0.0905  0.0259  0.0059  658 SER B C   
6272  O O   . SER B 357 ? 0.5987 0.4950 0.4354 0.0836  0.0273  0.0033  658 SER B O   
6273  C CB  . SER B 357 ? 0.8494 0.7785 0.6769 0.1282  0.0314  0.0077  658 SER B CB  
6274  O OG  . SER B 357 ? 0.8473 0.8129 0.6951 0.1279  0.0275  0.0137  658 SER B OG  
6275  N N   . ALA B 358 ? 0.4714 0.4287 0.3410 0.0810  0.0214  0.0101  659 ALA B N   
6276  C CA  . ALA B 358 ? 0.4974 0.4509 0.3777 0.0646  0.0180  0.0115  659 ALA B CA  
6277  C C   . ALA B 358 ? 0.6889 0.6321 0.5667 0.0524  0.0178  0.0071  659 ALA B C   
6278  O O   . ALA B 358 ? 0.6798 0.6035 0.5536 0.0433  0.0180  0.0054  659 ALA B O   
6279  C CB  . ALA B 358 ? 0.5016 0.4854 0.4017 0.0583  0.0135  0.0166  659 ALA B CB  
6280  N N   . THR B 359 ? 0.7142 0.6740 0.5954 0.0513  0.0174  0.0057  660 THR B N   
6281  C CA  . THR B 359 ? 0.5575 0.5111 0.4356 0.0409  0.0169  0.0014  660 THR B CA  
6282  C C   . THR B 359 ? 0.4903 0.4120 0.3474 0.0423  0.0206  -0.0055 660 THR B C   
6283  O O   . THR B 359 ? 0.5105 0.4184 0.3642 0.0301  0.0200  -0.0087 660 THR B O   
6284  C CB  . THR B 359 ? 0.5555 0.5324 0.4381 0.0420  0.0163  0.0015  660 THR B CB  
6285  O OG1 . THR B 359 ? 0.6733 0.6531 0.5463 0.0571  0.0201  0.0000  660 THR B OG1 
6286  C CG2 . THR B 359 ? 0.5086 0.5119 0.4094 0.0364  0.0126  0.0083  660 THR B CG2 
6287  N N   . GLU B 360 ? 0.5179 0.4274 0.3594 0.0571  0.0247  -0.0078 661 GLU B N   
6288  C CA  . GLU B 360 ? 0.6938 0.5658 0.5104 0.0592  0.0288  -0.0143 661 GLU B CA  
6289  C C   . GLU B 360 ? 0.8745 0.7217 0.6866 0.0490  0.0290  -0.0138 661 GLU B C   
6290  O O   . GLU B 360 ? 0.9410 0.7645 0.7402 0.0376  0.0302  -0.0193 661 GLU B O   
6291  C CB  . GLU B 360 ? 0.8184 0.6794 0.6182 0.0806  0.0333  -0.0149 661 GLU B CB  
6292  C CG  . GLU B 360 ? 1.0661 0.8807 0.8352 0.0847  0.0381  -0.0213 661 GLU B CG  
6293  C CD  . GLU B 360 ? 1.2336 1.0356 0.9844 0.1093  0.0426  -0.0208 661 GLU B CD  
6294  O OE1 . GLU B 360 ? 1.2354 1.0703 0.9995 0.1227  0.0418  -0.0157 661 GLU B OE1 
6295  O OE2 . GLU B 360 ? 1.2811 1.0402 1.0028 0.1153  0.0471  -0.0254 661 GLU B OE2 
6296  N N   . SER B 361 ? 0.7920 0.6456 0.6142 0.0520  0.0280  -0.0074 662 SER B N   
6297  C CA  A SER B 361 ? 0.7620 0.5952 0.5805 0.0429  0.0286  -0.0061 662 SER B CA  
6298  C CA  B SER B 361 ? 0.7577 0.5910 0.5763 0.0428  0.0286  -0.0061 662 SER B CA  
6299  C C   . SER B 361 ? 0.6515 0.4962 0.4837 0.0237  0.0252  -0.0069 662 SER B C   
6300  O O   . SER B 361 ? 0.7084 0.5336 0.5319 0.0116  0.0266  -0.0097 662 SER B O   
6301  C CB  A SER B 361 ? 0.8417 0.6827 0.6680 0.0516  0.0279  0.0009  662 SER B CB  
6302  C CB  B SER B 361 ? 0.8450 0.6863 0.6716 0.0514  0.0278  0.0009  662 SER B CB  
6303  O OG  A SER B 361 ? 0.8921 0.7242 0.7047 0.0709  0.0310  0.0019  662 SER B OG  
6304  O OG  B SER B 361 ? 0.8569 0.7300 0.7076 0.0451  0.0230  0.0051  662 SER B OG  
6305  N N   . PHE B 362 ? 0.5656 0.4424 0.4184 0.0206  0.0208  -0.0041 663 PHE B N   
6306  C CA  . PHE B 362 ? 0.6013 0.4910 0.4664 0.0056  0.0175  -0.0043 663 PHE B CA  
6307  C C   . PHE B 362 ? 0.7352 0.6150 0.5897 -0.0051 0.0182  -0.0114 663 PHE B C   
6308  O O   . PHE B 362 ? 0.8253 0.7064 0.6829 -0.0186 0.0170  -0.0128 663 PHE B O   
6309  C CB  . PHE B 362 ? 0.4684 0.3892 0.3527 0.0058  0.0131  0.0000  663 PHE B CB  
6310  C CG  . PHE B 362 ? 0.5686 0.5024 0.4641 -0.0061 0.0097  0.0006  663 PHE B CG  
6311  C CD1 . PHE B 362 ? 0.6369 0.5741 0.5414 -0.0093 0.0083  0.0044  663 PHE B CD1 
6312  C CD2 . PHE B 362 ? 0.7050 0.6480 0.6006 -0.0129 0.0080  -0.0028 663 PHE B CD2 
6313  C CE1 . PHE B 362 ? 0.5104 0.4610 0.4240 -0.0177 0.0055  0.0051  663 PHE B CE1 
6314  C CE2 . PHE B 362 ? 0.6908 0.6481 0.5959 -0.0216 0.0048  -0.0019 663 PHE B CE2 
6315  C CZ  . PHE B 362 ? 0.5644 0.5258 0.4786 -0.0234 0.0036  0.0021  663 PHE B CZ  
6316  N N   . ILE B 363 ? 0.7118 0.5842 0.5536 0.0004  0.0199  -0.0162 664 ILE B N   
6317  C CA  . ILE B 363 ? 0.7509 0.6098 0.5788 -0.0105 0.0207  -0.0241 664 ILE B CA  
6318  C C   . ILE B 363 ? 0.7876 0.6134 0.5983 -0.0188 0.0242  -0.0272 664 ILE B C   
6319  O O   . ILE B 363 ? 0.8217 0.6468 0.6321 -0.0356 0.0232  -0.0303 664 ILE B O   
6320  C CB  . ILE B 363 ? 0.6740 0.5280 0.4883 -0.0013 0.0225  -0.0293 664 ILE B CB  
6321  C CG1 . ILE B 363 ? 0.6782 0.5675 0.5096 0.0029  0.0190  -0.0260 664 ILE B CG1 
6322  C CG2 . ILE B 363 ? 0.5744 0.4066 0.3689 -0.0126 0.0237  -0.0388 664 ILE B CG2 
6323  C CD1 . ILE B 363 ? 0.5839 0.4927 0.4235 -0.0106 0.0148  -0.0281 664 ILE B CD1 
6324  N N   . LYS B 364 ? 0.8272 0.6271 0.6238 -0.0074 0.0284  -0.0255 665 LYS B N   
6325  C CA  . LYS B 364 ? 0.8380 0.6025 0.6157 -0.0149 0.0323  -0.0270 665 LYS B CA  
6326  C C   . LYS B 364 ? 0.7665 0.5437 0.5591 -0.0291 0.0307  -0.0228 665 LYS B C   
6327  O O   . LYS B 364 ? 0.7792 0.5398 0.5615 -0.0453 0.0325  -0.0259 665 LYS B O   
6328  C CB  . LYS B 364 ? 0.7933 0.5313 0.5544 0.0032  0.0367  -0.0238 665 LYS B CB  
6329  C CG  . LYS B 364 ? 1.0103 0.7099 0.7509 -0.0031 0.0412  -0.0232 665 LYS B CG  
6330  C CD  . LYS B 364 ? 1.2719 0.9240 0.9766 0.0014  0.0465  -0.0295 665 LYS B CD  
6331  C CE  . LYS B 364 ? 1.4422 1.0772 1.1334 -0.0212 0.0469  -0.0382 665 LYS B CE  
6332  N NZ  . LYS B 364 ? 1.4354 1.0578 1.1235 -0.0431 0.0483  -0.0370 665 LYS B NZ  
6333  N N   . HIS B 365 ? 0.5920 0.3992 0.4082 -0.0237 0.0273  -0.0160 666 HIS B N   
6334  C CA  . HIS B 365 ? 0.7026 0.5252 0.5334 -0.0351 0.0256  -0.0124 666 HIS B CA  
6335  C C   . HIS B 365 ? 0.7284 0.5687 0.5663 -0.0519 0.0229  -0.0167 666 HIS B C   
6336  O O   . HIS B 365 ? 0.7257 0.5611 0.5598 -0.0672 0.0243  -0.0184 666 HIS B O   
6337  C CB  . HIS B 365 ? 0.6231 0.4724 0.4752 -0.0251 0.0222  -0.0054 666 HIS B CB  
6338  C CG  . HIS B 365 ? 0.6335 0.4999 0.5002 -0.0336 0.0205  -0.0018 666 HIS B CG  
6339  N ND1 . HIS B 365 ? 0.6555 0.5079 0.5160 -0.0391 0.0237  0.0001  666 HIS B ND1 
6340  C CD2 . HIS B 365 ? 0.6307 0.5265 0.5163 -0.0358 0.0162  0.0004  666 HIS B CD2 
6341  C CE1 . HIS B 365 ? 0.5883 0.4635 0.4645 -0.0443 0.0216  0.0030  666 HIS B CE1 
6342  N NE2 . HIS B 365 ? 0.6032 0.5038 0.4942 -0.0417 0.0169  0.0031  666 HIS B NE2 
6343  N N   . MET B 366 ? 0.6325 0.4951 0.4799 -0.0496 0.0191  -0.0184 667 MET B N   
6344  C CA  . MET B 366 ? 0.4612 0.3430 0.3141 -0.0633 0.0160  -0.0227 667 MET B CA  
6345  C C   . MET B 366 ? 0.5374 0.3959 0.3705 -0.0792 0.0188  -0.0302 667 MET B C   
6346  O O   . MET B 366 ? 0.6052 0.4768 0.4429 -0.0953 0.0177  -0.0320 667 MET B O   
6347  C CB  . MET B 366 ? 0.5937 0.4929 0.4514 -0.0567 0.0127  -0.0242 667 MET B CB  
6348  C CG  . MET B 366 ? 0.6789 0.6095 0.5580 -0.0500 0.0084  -0.0176 667 MET B CG  
6349  S SD  . MET B 366 ? 0.6526 0.6039 0.5346 -0.0473 0.0048  -0.0196 667 MET B SD  
6350  C CE  . MET B 366 ? 0.5921 0.5638 0.4781 -0.0633 0.0012  -0.0236 667 MET B CE  
6351  N N   . GLU B 367 ? 0.5593 0.3837 0.3692 -0.0750 0.0226  -0.0350 668 GLU B N   
6352  C CA  A GLU B 367 ? 0.7239 0.5179 0.5099 -0.0908 0.0258  -0.0425 668 GLU B CA  
6353  C CA  B GLU B 367 ? 0.7184 0.5128 0.5046 -0.0910 0.0257  -0.0426 668 GLU B CA  
6354  C C   . GLU B 367 ? 0.8528 0.6407 0.6388 -0.1051 0.0281  -0.0397 668 GLU B C   
6355  O O   . GLU B 367 ? 0.8307 0.6297 0.6179 -0.1254 0.0271  -0.0434 668 GLU B O   
6356  C CB  A GLU B 367 ? 0.7996 0.5504 0.5579 -0.0790 0.0306  -0.0460 668 GLU B CB  
6357  C CB  B GLU B 367 ? 0.8053 0.5556 0.5627 -0.0804 0.0306  -0.0466 668 GLU B CB  
6358  C CG  A GLU B 367 ? 0.8215 0.5275 0.5490 -0.0934 0.0354  -0.0523 668 GLU B CG  
6359  C CG  B GLU B 367 ? 0.8458 0.6016 0.6040 -0.0592 0.0299  -0.0464 668 GLU B CG  
6360  C CD  A GLU B 367 ? 0.8589 0.5193 0.5569 -0.0770 0.0406  -0.0546 668 GLU B CD  
6361  C CD  B GLU B 367 ? 0.7903 0.5541 0.5428 -0.0626 0.0277  -0.0545 668 GLU B CD  
6362  O OE1 A GLU B 367 ? 0.8404 0.5084 0.5403 -0.0575 0.0398  -0.0547 668 GLU B OE1 
6363  O OE1 B GLU B 367 ? 0.6223 0.4230 0.3946 -0.0692 0.0227  -0.0539 668 GLU B OE1 
6364  O OE2 A GLU B 367 ? 0.9134 0.5302 0.5851 -0.0829 0.0457  -0.0558 668 GLU B OE2 
6365  O OE2 B GLU B 367 ? 0.6134 0.3458 0.3401 -0.0571 0.0310  -0.0611 668 GLU B OE2 
6366  N N   . ASN B 368 ? 0.8873 0.6609 0.6724 -0.0944 0.0312  -0.0329 669 ASN B N   
6367  C CA  . ASN B 368 ? 0.8529 0.6183 0.6360 -0.1059 0.0344  -0.0292 669 ASN B CA  
6368  C C   . ASN B 368 ? 0.7717 0.5797 0.5791 -0.1184 0.0308  -0.0272 669 ASN B C   
6369  O O   . ASN B 368 ? 0.7113 0.5207 0.5146 -0.1388 0.0323  -0.0294 669 ASN B O   
6370  C CB  . ASN B 368 ? 0.9190 0.6723 0.7023 -0.0886 0.0369  -0.0212 669 ASN B CB  
6371  C CG  . ASN B 368 ? 1.0145 0.7269 0.7726 -0.0737 0.0409  -0.0222 669 ASN B CG  
6372  O OD1 . ASN B 368 ? 1.0305 0.7084 0.7626 -0.0803 0.0441  -0.0285 669 ASN B OD1 
6373  N ND2 . ASN B 368 ? 0.9997 0.7158 0.7641 -0.0529 0.0407  -0.0160 669 ASN B ND2 
6374  N N   . GLU B 369 ? 0.5975 0.4407 0.4293 -0.1063 0.0262  -0.0227 670 GLU B N   
6375  C CA  . GLU B 369 ? 0.5687 0.4516 0.4223 -0.1136 0.0230  -0.0200 670 GLU B CA  
6376  C C   . GLU B 369 ? 0.8020 0.7035 0.6559 -0.1324 0.0207  -0.0266 670 GLU B C   
6377  O O   . GLU B 369 ? 0.8199 0.7394 0.6794 -0.1476 0.0213  -0.0265 670 GLU B O   
6378  C CB  . GLU B 369 ? 0.5269 0.4374 0.4013 -0.0966 0.0183  -0.0150 670 GLU B CB  
6379  C CG  . GLU B 369 ? 0.7052 0.6037 0.5814 -0.0800 0.0198  -0.0087 670 GLU B CG  
6380  C CD  . GLU B 369 ? 0.7597 0.6699 0.6461 -0.0802 0.0207  -0.0030 670 GLU B CD  
6381  O OE1 . GLU B 369 ? 0.6463 0.5762 0.5480 -0.0691 0.0176  0.0016  670 GLU B OE1 
6382  O OE2 . GLU B 369 ? 0.6323 0.5304 0.5096 -0.0919 0.0249  -0.0032 670 GLU B OE2 
6383  N N   . TYR B 370 ? 0.8059 0.7057 0.6536 -0.1321 0.0182  -0.0326 671 TYR B N   
6384  C CA  . TYR B 370 ? 0.6869 0.6060 0.5340 -0.1503 0.0155  -0.0394 671 TYR B CA  
6385  C C   . TYR B 370 ? 0.7632 0.6583 0.5909 -0.1729 0.0198  -0.0445 671 TYR B C   
6386  O O   . TYR B 370 ? 0.9202 0.8410 0.7541 -0.1918 0.0186  -0.0467 671 TYR B O   
6387  C CB  . TYR B 370 ? 0.7071 0.6252 0.5478 -0.1452 0.0123  -0.0452 671 TYR B CB  
6388  C CG  . TYR B 370 ? 0.6531 0.6103 0.5158 -0.1326 0.0066  -0.0410 671 TYR B CG  
6389  C CD1 . TYR B 370 ? 0.6448 0.6008 0.5154 -0.1123 0.0062  -0.0347 671 TYR B CD1 
6390  C CD2 . TYR B 370 ? 0.6988 0.6943 0.5731 -0.1416 0.0018  -0.0428 671 TYR B CD2 
6391  C CE1 . TYR B 370 ? 0.7007 0.6874 0.5881 -0.1021 0.0015  -0.0303 671 TYR B CE1 
6392  C CE2 . TYR B 370 ? 0.6095 0.6368 0.5008 -0.1289 -0.0030 -0.0381 671 TYR B CE2 
6393  C CZ  . TYR B 370 ? 0.6854 0.7057 0.5823 -0.1096 -0.0030 -0.0317 671 TYR B CZ  
6394  O OH  . TYR B 370 ? 0.6897 0.7368 0.6004 -0.0980 -0.0074 -0.0265 671 TYR B OH  
6395  N N   . ARG B 371 ? 0.6659 0.5119 0.4692 -0.1712 0.0252  -0.0459 672 ARG B N   
6396  C CA  . ARG B 371 ? 0.8272 0.6401 0.6054 -0.1933 0.0299  -0.0512 672 ARG B CA  
6397  C C   . ARG B 371 ? 0.8867 0.7122 0.6722 -0.2079 0.0327  -0.0461 672 ARG B C   
6398  O O   . ARG B 371 ? 0.8725 0.6986 0.6491 -0.2336 0.0342  -0.0505 672 ARG B O   
6399  C CB  . ARG B 371 ? 0.9425 0.6970 0.6910 -0.1831 0.0352  -0.0525 672 ARG B CB  
6400  C CG  . ARG B 371 ? 1.0262 0.7365 0.7485 -0.1974 0.0421  -0.0521 672 ARG B CG  
6401  C CD  . ARG B 371 ? 1.2223 0.8830 0.9219 -0.1763 0.0469  -0.0492 672 ARG B CD  
6402  N NE  . ARG B 371 ? 1.4405 1.0838 1.1269 -0.1624 0.0456  -0.0556 672 ARG B NE  
6403  C CZ  . ARG B 371 ? 1.5632 1.1723 1.2323 -0.1398 0.0488  -0.0541 672 ARG B CZ  
6404  N NH1 . ARG B 371 ? 1.6107 1.1980 1.2730 -0.1282 0.0530  -0.0462 672 ARG B NH1 
6405  N NH2 . ARG B 371 ? 1.5590 1.1580 1.2173 -0.1278 0.0477  -0.0604 672 ARG B NH2 
6406  N N   . CYS B 372 ? 0.8614 0.6988 0.6627 -0.1930 0.0336  -0.0369 673 CYS B N   
6407  C CA  . CYS B 372 ? 0.9949 0.8422 0.8009 -0.2054 0.0371  -0.0319 673 CYS B CA  
6408  C C   . CYS B 372 ? 1.0418 0.9452 0.8791 -0.2012 0.0333  -0.0269 673 CYS B C   
6409  O O   . CYS B 372 ? 1.1812 1.1033 1.0243 -0.2149 0.0358  -0.0242 673 CYS B O   
6410  C CB  . CYS B 372 ? 0.9769 0.7856 0.7693 -0.1939 0.0428  -0.0252 673 CYS B CB  
6411  S SG  . CYS B 372 ? 0.9123 0.7447 0.7291 -0.1649 0.0400  -0.0164 673 CYS B SG  
6412  N N   . ARG B 373 ? 0.9742 0.9039 0.8303 -0.1825 0.0278  -0.0253 674 ARG B N   
6413  C CA  . ARG B 373 ? 0.8349 0.8126 0.7173 -0.1753 0.0243  -0.0204 674 ARG B CA  
6414  C C   . ARG B 373 ? 0.8261 0.8440 0.7218 -0.1793 0.0183  -0.0245 674 ARG B C   
6415  O O   . ARG B 373 ? 0.7855 0.8456 0.7006 -0.1755 0.0155  -0.0211 674 ARG B O   
6416  C CB  . ARG B 373 ? 0.7333 0.7086 0.6258 -0.1494 0.0229  -0.0139 674 ARG B CB  
6417  C CG  . ARG B 373 ? 0.6005 0.6115 0.5136 -0.1406 0.0214  -0.0078 674 ARG B CG  
6418  C CD  . ARG B 373 ? 0.5597 0.5652 0.4799 -0.1172 0.0192  -0.0028 674 ARG B CD  
6419  N NE  . ARG B 373 ? 0.6641 0.6985 0.6005 -0.1077 0.0179  0.0023  674 ARG B NE  
6420  C CZ  . ARG B 373 ? 0.7189 0.7561 0.6633 -0.0892 0.0150  0.0062  674 ARG B CZ  
6421  N NH1 . ARG B 373 ? 0.7008 0.7182 0.6407 -0.0794 0.0130  0.0060  674 ARG B NH1 
6422  N NH2 . ARG B 373 ? 0.6715 0.7314 0.6272 -0.0807 0.0141  0.0101  674 ARG B NH2 
6423  N N   . GLY B 374 ? 0.9260 0.9320 0.8103 -0.1853 0.0161  -0.0316 675 GLY B N   
6424  C CA  . GLY B 374 ? 0.8471 0.8902 0.7420 -0.1881 0.0101  -0.0354 675 GLY B CA  
6425  C C   . GLY B 374 ? 0.7082 0.7651 0.6156 -0.1650 0.0052  -0.0318 675 GLY B C   
6426  O O   . GLY B 374 ? 0.6689 0.7637 0.5888 -0.1634 0.0000  -0.0322 675 GLY B O   
6427  N N   . GLY B 375 ? 0.5079 0.5369 0.4119 -0.1474 0.0068  -0.0279 676 GLY B N   
6428  C CA  . GLY B 375 ? 0.5385 0.5787 0.4526 -0.1280 0.0026  -0.0242 676 GLY B CA  
6429  C C   . GLY B 375 ? 0.6533 0.6744 0.5697 -0.1106 0.0046  -0.0176 676 GLY B C   
6430  O O   . GLY B 375 ? 0.7466 0.7490 0.6583 -0.1116 0.0088  -0.0153 676 GLY B O   
6431  N N   . CYS B 376 ? 0.6810 0.7081 0.6041 -0.0951 0.0013  -0.0144 677 CYS B N   
6432  C CA  . CYS B 376 ? 0.5496 0.5628 0.4756 -0.0795 0.0021  -0.0085 677 CYS B CA  
6433  C C   . CYS B 376 ? 0.5671 0.5975 0.5033 -0.0665 -0.0023 -0.0042 677 CYS B C   
6434  O O   . CYS B 376 ? 0.6634 0.6914 0.5956 -0.0634 -0.0039 -0.0058 677 CYS B O   
6435  C CB  . CYS B 376 ? 0.5725 0.5512 0.4833 -0.0762 0.0056  -0.0107 677 CYS B CB  
6436  S SG  . CYS B 376 ? 0.6400 0.6084 0.5551 -0.0577 0.0057  -0.0041 677 CYS B SG  
6437  N N   . PRO B 377 ? 0.5688 0.6138 0.5161 -0.0584 -0.0040 0.0015  678 PRO B N   
6438  C CA  . PRO B 377 ? 0.4131 0.4692 0.3667 -0.0467 -0.0079 0.0061  678 PRO B CA  
6439  C C   . PRO B 377 ? 0.5731 0.6095 0.5223 -0.0388 -0.0074 0.0081  678 PRO B C   
6440  O O   . PRO B 377 ? 0.6922 0.7120 0.6396 -0.0354 -0.0050 0.0097  678 PRO B O   
6441  C CB  . PRO B 377 ? 0.5577 0.6258 0.5198 -0.0399 -0.0087 0.0110  678 PRO B CB  
6442  C CG  . PRO B 377 ? 0.6014 0.6562 0.5614 -0.0444 -0.0044 0.0102  678 PRO B CG  
6443  C CD  . PRO B 377 ? 0.7169 0.7642 0.6688 -0.0587 -0.0017 0.0042  678 PRO B CD  
6444  N N   . ALA B 378 ? 0.5991 0.6403 0.5468 -0.0360 -0.0097 0.0084  679 ALA B N   
6445  C CA  . ALA B 378 ? 0.5632 0.5913 0.5070 -0.0300 -0.0090 0.0101  679 ALA B CA  
6446  C C   . ALA B 378 ? 0.5325 0.5722 0.4791 -0.0245 -0.0123 0.0147  679 ALA B C   
6447  O O   . ALA B 378 ? 0.6875 0.7425 0.6343 -0.0262 -0.0148 0.0141  679 ALA B O   
6448  C CB  . ALA B 378 ? 0.5435 0.5596 0.4770 -0.0340 -0.0063 0.0042  679 ALA B CB  
6449  N N   . ASP B 379 ? 0.5077 0.5402 0.4551 -0.0185 -0.0124 0.0195  680 ASP B N   
6450  C CA  . ASP B 379 ? 0.5030 0.5418 0.4506 -0.0144 -0.0151 0.0251  680 ASP B CA  
6451  C C   . ASP B 379 ? 0.6417 0.6784 0.5852 -0.0144 -0.0136 0.0249  680 ASP B C   
6452  O O   . ASP B 379 ? 0.6467 0.6759 0.5903 -0.0126 -0.0121 0.0264  680 ASP B O   
6453  C CB  . ASP B 379 ? 0.4337 0.4660 0.3837 -0.0097 -0.0164 0.0306  680 ASP B CB  
6454  C CG  . ASP B 379 ? 0.5137 0.5470 0.4606 -0.0064 -0.0189 0.0369  680 ASP B CG  
6455  O OD1 . ASP B 379 ? 0.6199 0.6504 0.5656 -0.0017 -0.0209 0.0408  680 ASP B OD1 
6456  O OD2 . ASP B 379 ? 0.6766 0.7122 0.6203 -0.0081 -0.0186 0.0384  680 ASP B OD2 
6457  N N   . TRP B 380 ? 0.6216 0.6679 0.5612 -0.0161 -0.0143 0.0231  681 TRP B N   
6458  C CA  . TRP B 380 ? 0.5313 0.5781 0.4658 -0.0156 -0.0122 0.0216  681 TRP B CA  
6459  C C   . TRP B 380 ? 0.4829 0.5303 0.4188 -0.0131 -0.0120 0.0283  681 TRP B C   
6460  O O   . TRP B 380 ? 0.3422 0.3891 0.2769 -0.0116 -0.0094 0.0276  681 TRP B O   
6461  C CB  . TRP B 380 ? 0.5345 0.5932 0.4640 -0.0176 -0.0135 0.0192  681 TRP B CB  
6462  C CG  . TRP B 380 ? 0.4001 0.4589 0.3223 -0.0168 -0.0107 0.0152  681 TRP B CG  
6463  C CD1 . TRP B 380 ? 0.4126 0.4640 0.3270 -0.0186 -0.0084 0.0067  681 TRP B CD1 
6464  C CD2 . TRP B 380 ? 0.4410 0.5068 0.3611 -0.0137 -0.0094 0.0193  681 TRP B CD2 
6465  N NE1 . TRP B 380 ? 0.5551 0.6084 0.4625 -0.0148 -0.0058 0.0050  681 TRP B NE1 
6466  C CE2 . TRP B 380 ? 0.5700 0.6349 0.4818 -0.0120 -0.0063 0.0128  681 TRP B CE2 
6467  C CE3 . TRP B 380 ? 0.5057 0.5778 0.4286 -0.0130 -0.0103 0.0279  681 TRP B CE3 
6468  C CZ2 . TRP B 380 ? 0.5417 0.6163 0.4500 -0.0084 -0.0040 0.0147  681 TRP B CZ2 
6469  C CZ3 . TRP B 380 ? 0.5527 0.6340 0.4722 -0.0118 -0.0080 0.0302  681 TRP B CZ3 
6470  C CH2 . TRP B 380 ? 0.4464 0.5310 0.3595 -0.0089 -0.0048 0.0237  681 TRP B CH2 
6471  N N   . VAL B 381 ? 0.5322 0.5810 0.4693 -0.0126 -0.0147 0.0349  682 VAL B N   
6472  C CA  . VAL B 381 ? 0.4950 0.5424 0.4311 -0.0133 -0.0148 0.0417  682 VAL B CA  
6473  C C   . VAL B 381 ? 0.6594 0.7000 0.5993 -0.0138 -0.0133 0.0415  682 VAL B C   
6474  O O   . VAL B 381 ? 0.7102 0.7553 0.6499 -0.0160 -0.0122 0.0447  682 VAL B O   
6475  C CB  . VAL B 381 ? 0.4725 0.5151 0.4057 -0.0122 -0.0179 0.0482  682 VAL B CB  
6476  C CG1 . VAL B 381 ? 0.4802 0.5132 0.4110 -0.0151 -0.0180 0.0543  682 VAL B CG1 
6477  C CG2 . VAL B 381 ? 0.3702 0.4228 0.2979 -0.0109 -0.0194 0.0505  682 VAL B CG2 
6478  N N   . TRP B 382 ? 0.5384 0.5707 0.4815 -0.0122 -0.0132 0.0382  683 TRP B N   
6479  C CA  . TRP B 382 ? 0.4861 0.5119 0.4322 -0.0117 -0.0125 0.0382  683 TRP B CA  
6480  C C   . TRP B 382 ? 0.5309 0.5562 0.4772 -0.0088 -0.0094 0.0329  683 TRP B C   
6481  O O   . TRP B 382 ? 0.5026 0.5279 0.4505 -0.0073 -0.0085 0.0335  683 TRP B O   
6482  C CB  . TRP B 382 ? 0.4549 0.4703 0.4024 -0.0106 -0.0143 0.0388  683 TRP B CB  
6483  C CG  . TRP B 382 ? 0.5961 0.6052 0.5405 -0.0116 -0.0170 0.0444  683 TRP B CG  
6484  C CD1 . TRP B 382 ? 0.6275 0.6369 0.5672 -0.0111 -0.0187 0.0483  683 TRP B CD1 
6485  C CD2 . TRP B 382 ? 0.7026 0.7010 0.6455 -0.0128 -0.0182 0.0466  683 TRP B CD2 
6486  N NE1 . TRP B 382 ? 0.6788 0.6751 0.6126 -0.0114 -0.0206 0.0531  683 TRP B NE1 
6487  C CE2 . TRP B 382 ? 0.7588 0.7480 0.6945 -0.0133 -0.0204 0.0516  683 TRP B CE2 
6488  C CE3 . TRP B 382 ? 0.6082 0.6031 0.5536 -0.0133 -0.0177 0.0447  683 TRP B CE3 
6489  C CZ2 . TRP B 382 ? 0.6741 0.6480 0.6038 -0.0153 -0.0221 0.0541  683 TRP B CZ2 
6490  C CZ3 . TRP B 382 ? 0.5607 0.5444 0.5019 -0.0156 -0.0198 0.0470  683 TRP B CZ3 
6491  C CH2 . TRP B 382 ? 0.6100 0.5821 0.5429 -0.0172 -0.0218 0.0513  683 TRP B CH2 
6492  N N   . ILE B 383 ? 0.5450 0.5688 0.4880 -0.0080 -0.0078 0.0277  684 ILE B N   
6493  C CA  . ILE B 383 ? 0.4657 0.4835 0.4043 -0.0044 -0.0044 0.0227  684 ILE B CA  
6494  C C   . ILE B 383 ? 0.5739 0.6013 0.5097 -0.0005 -0.0023 0.0227  684 ILE B C   
6495  O O   . ILE B 383 ? 0.6045 0.6302 0.5378 0.0055  0.0002  0.0213  684 ILE B O   
6496  C CB  . ILE B 383 ? 0.4324 0.4424 0.3654 -0.0069 -0.0033 0.0167  684 ILE B CB  
6497  C CG1 . ILE B 383 ? 0.3823 0.3881 0.3191 -0.0109 -0.0049 0.0169  684 ILE B CG1 
6498  C CG2 . ILE B 383 ? 0.4917 0.4888 0.4156 -0.0028 0.0006  0.0117  684 ILE B CG2 
6499  C CD1 . ILE B 383 ? 0.4291 0.4222 0.3652 -0.0091 -0.0030 0.0163  684 ILE B CD1 
6500  N N   . VAL B 384 ? 0.5888 0.6277 0.5239 -0.0028 -0.0030 0.0244  685 VAL B N   
6501  C CA  . VAL B 384 ? 0.4780 0.5290 0.4097 0.0009  -0.0005 0.0241  685 VAL B CA  
6502  C C   . VAL B 384 ? 0.5129 0.5762 0.4506 0.0014  -0.0004 0.0294  685 VAL B C   
6503  O O   . VAL B 384 ? 0.5542 0.6225 0.4962 -0.0051 -0.0028 0.0353  685 VAL B O   
6504  C CB  . VAL B 384 ? 0.4475 0.5086 0.3763 -0.0023 -0.0013 0.0252  685 VAL B CB  
6505  C CG1 . VAL B 384 ? 0.3281 0.4048 0.2537 0.0017  0.0019  0.0254  685 VAL B CG1 
6506  C CG2 . VAL B 384 ? 0.4474 0.5004 0.3701 -0.0037 -0.0018 0.0190  685 VAL B CG2 
6507  N N   . PRO B 385 ? 0.5015 0.5704 0.4382 0.0088  0.0024  0.0277  686 PRO B N   
6508  C CA  . PRO B 385 ? 0.5368 0.6214 0.4804 0.0080  0.0020  0.0325  686 PRO B CA  
6509  C C   . PRO B 385 ? 0.5847 0.6894 0.5310 0.0013  0.0018  0.0377  686 PRO B C   
6510  O O   . PRO B 385 ? 0.6456 0.7559 0.5875 0.0017  0.0034  0.0370  686 PRO B O   
6511  C CB  . PRO B 385 ? 0.4972 0.5871 0.4372 0.0203  0.0055  0.0291  686 PRO B CB  
6512  C CG  . PRO B 385 ? 0.4634 0.5307 0.3930 0.0262  0.0074  0.0226  686 PRO B CG  
6513  C CD  . PRO B 385 ? 0.4431 0.5044 0.3707 0.0185  0.0061  0.0214  686 PRO B CD  
6514  N N   . PRO B 386 ? 0.5356 0.6508 0.4879 -0.0060 0.0001  0.0431  687 PRO B N   
6515  C CA  . PRO B 386 ? 0.5029 0.6337 0.4560 -0.0156 0.0000  0.0491  687 PRO B CA  
6516  C C   . PRO B 386 ? 0.6335 0.7942 0.5884 -0.0126 0.0037  0.0500  687 PRO B C   
6517  O O   . PRO B 386 ? 0.6678 0.8448 0.6240 -0.0226 0.0040  0.0558  687 PRO B O   
6518  C CB  . PRO B 386 ? 0.4666 0.5933 0.4232 -0.0261 -0.0033 0.0535  687 PRO B CB  
6519  C CG  . PRO B 386 ? 0.3312 0.4580 0.2917 -0.0192 -0.0037 0.0498  687 PRO B CG  
6520  C CD  . PRO B 386 ? 0.3631 0.4720 0.3196 -0.0084 -0.0025 0.0440  687 PRO B CD  
6521  N N   . MET B 387 ? 0.6781 0.8464 0.6316 0.0008  0.0068  0.0449  688 MET B N   
6522  C CA  . MET B 387 ? 0.6670 0.8631 0.6197 0.0071  0.0110  0.0449  688 MET B CA  
6523  C C   . MET B 387 ? 0.7047 0.8889 0.6477 0.0221  0.0142  0.0374  688 MET B C   
6524  O O   . MET B 387 ? 0.7473 0.9076 0.6859 0.0287  0.0135  0.0326  688 MET B O   
6525  C CB  . MET B 387 ? 0.5673 0.7939 0.5276 0.0097  0.0121  0.0471  688 MET B CB  
6526  C CG  . MET B 387 ? 0.6380 0.8606 0.5969 0.0257  0.0130  0.0422  688 MET B CG  
6527  S SD  . MET B 387 ? 0.6790 0.9427 0.6475 0.0300  0.0133  0.0452  688 MET B SD  
6528  C CE  . MET B 387 ? 0.7137 1.0055 0.6769 0.0493  0.0198  0.0425  688 MET B CE  
6529  N N   . SER B 388 ? 0.5858 0.7848 0.5236 0.0262  0.0176  0.0365  689 SER B N   
6530  C CA  . SER B 388 ? 0.4563 0.6457 0.3820 0.0409  0.0212  0.0287  689 SER B CA  
6531  C C   . SER B 388 ? 0.4678 0.6223 0.3851 0.0391  0.0192  0.0232  689 SER B C   
6532  O O   . SER B 388 ? 0.5269 0.6621 0.4330 0.0495  0.0212  0.0160  689 SER B O   
6533  C CB  . SER B 388 ? 0.4795 0.6740 0.4029 0.0572  0.0240  0.0256  689 SER B CB  
6534  O OG  . SER B 388 ? 0.5641 0.7971 0.4966 0.0584  0.0256  0.0307  689 SER B OG  
6535  N N   . GLY B 389 ? 0.3590 0.5049 0.2802 0.0260  0.0154  0.0265  690 GLY B N   
6536  C CA  . GLY B 389 ? 0.4537 0.5724 0.3692 0.0232  0.0130  0.0218  690 GLY B CA  
6537  C C   . GLY B 389 ? 0.6207 0.7280 0.5221 0.0306  0.0157  0.0132  690 GLY B C   
6538  O O   . GLY B 389 ? 0.6378 0.7221 0.5314 0.0351  0.0163  0.0070  690 GLY B O   
6539  N N   . SER B 390 ? 0.5905 0.7127 0.4865 0.0317  0.0176  0.0128  691 SER B N   
6540  C CA  . SER B 390 ? 0.6086 0.7188 0.4892 0.0367  0.0194  0.0040  691 SER B CA  
6541  C C   . SER B 390 ? 0.5776 0.6731 0.4457 0.0508  0.0236  -0.0035 691 SER B C   
6542  O O   . SER B 390 ? 0.7159 0.7886 0.5685 0.0529  0.0246  -0.0122 691 SER B O   
6543  C CB  . SER B 390 ? 0.6343 0.7664 0.5111 0.0362  0.0209  0.0056  691 SER B CB  
6544  O OG  . SER B 390 ? 0.6833 0.8214 0.5480 0.0494  0.0261  -0.0002 691 SER B OG  
6545  N N   . ILE B 391 ? 0.5388 0.6456 0.4115 0.0604  0.0261  -0.0005 692 ILE B N   
6546  C CA  . ILE B 391 ? 0.6326 0.7233 0.4908 0.0767  0.0303  -0.0069 692 ILE B CA  
6547  C C   . ILE B 391 ? 0.6665 0.7294 0.5239 0.0762  0.0288  -0.0079 692 ILE B C   
6548  O O   . ILE B 391 ? 0.6789 0.7270 0.5247 0.0901  0.0320  -0.0112 692 ILE B O   
6549  C CB  . ILE B 391 ? 0.6478 0.7679 0.5088 0.0915  0.0344  -0.0038 692 ILE B CB  
6550  C CG1 . ILE B 391 ? 0.6954 0.8334 0.5741 0.0885  0.0322  0.0043  692 ILE B CG1 
6551  C CG2 . ILE B 391 ? 0.6407 0.7918 0.5031 0.0914  0.0365  -0.0018 692 ILE B CG2 
6552  C CD1 . ILE B 391 ? 0.7797 0.9512 0.6621 0.1025  0.0358  0.0073  692 ILE B CD1 
6553  N N   . THR B 392 ? 0.6379 0.6934 0.5061 0.0614  0.0242  -0.0047 693 THR B N   
6554  C CA  . THR B 392 ? 0.7136 0.7410 0.5788 0.0592  0.0230  -0.0065 693 THR B CA  
6555  C C   . THR B 392 ? 0.6945 0.6989 0.5513 0.0481  0.0213  -0.0124 693 THR B C   
6556  O O   . THR B 392 ? 0.5650 0.5802 0.4245 0.0396  0.0192  -0.0128 693 THR B O   
6557  C CB  . THR B 392 ? 0.7377 0.7742 0.6206 0.0520  0.0194  0.0011  693 THR B CB  
6558  O OG1 . THR B 392 ? 0.6832 0.7193 0.5745 0.0371  0.0152  0.0031  693 THR B OG1 
6559  C CG2 . THR B 392 ? 0.7366 0.8053 0.6319 0.0556  0.0194  0.0079  693 THR B CG2 
6560  N N   . PRO B 393 ? 0.5556 0.5293 0.4012 0.0474  0.0223  -0.0170 694 PRO B N   
6561  C CA  . PRO B 393 ? 0.6606 0.6146 0.4960 0.0358  0.0212  -0.0238 694 PRO B CA  
6562  C C   . PRO B 393 ? 0.6893 0.6565 0.5405 0.0206  0.0161  -0.0202 694 PRO B C   
6563  O O   . PRO B 393 ? 0.7278 0.6953 0.5749 0.0113  0.0141  -0.0246 694 PRO B O   
6564  C CB  . PRO B 393 ? 0.6217 0.5399 0.4416 0.0376  0.0239  -0.0279 694 PRO B CB  
6565  C CG  . PRO B 393 ? 0.7091 0.6331 0.5390 0.0467  0.0245  -0.0206 694 PRO B CG  
6566  C CD  . PRO B 393 ? 0.6425 0.5987 0.4828 0.0567  0.0247  -0.0160 694 PRO B CD  
6567  N N   . VAL B 394 ? 0.6482 0.6267 0.5160 0.0184  0.0137  -0.0126 695 VAL B N   
6568  C CA  . VAL B 394 ? 0.6108 0.5980 0.4907 0.0064  0.0092  -0.0095 695 VAL B CA  
6569  C C   . VAL B 394 ? 0.5622 0.5716 0.4475 0.0029  0.0066  -0.0073 695 VAL B C   
6570  O O   . VAL B 394 ? 0.4757 0.4909 0.3651 -0.0059 0.0031  -0.0071 695 VAL B O   
6571  C CB  . VAL B 394 ? 0.5389 0.5307 0.4328 0.0062  0.0074  -0.0023 695 VAL B CB  
6572  C CG1 . VAL B 394 ? 0.5126 0.4821 0.4010 0.0064  0.0093  -0.0044 695 VAL B CG1 
6573  C CG2 . VAL B 394 ? 0.5332 0.5398 0.4332 0.0145  0.0083  0.0030  695 VAL B CG2 
6574  N N   . PHE B 395 ? 0.4484 0.4721 0.3330 0.0100  0.0083  -0.0053 696 PHE B N   
6575  C CA  . PHE B 395 ? 0.6873 0.7310 0.5747 0.0067  0.0064  -0.0024 696 PHE B CA  
6576  C C   . PHE B 395 ? 0.6495 0.6890 0.5265 0.0012  0.0052  -0.0096 696 PHE B C   
6577  O O   . PHE B 395 ? 0.4500 0.5019 0.3315 -0.0052 0.0015  -0.0071 696 PHE B O   
6578  C CB  . PHE B 395 ? 0.6791 0.7390 0.5650 0.0150  0.0096  -0.0001 696 PHE B CB  
6579  C CG  . PHE B 395 ? 0.5873 0.6673 0.4743 0.0116  0.0083  0.0036  696 PHE B CG  
6580  C CD1 . PHE B 395 ? 0.6297 0.7266 0.5274 0.0083  0.0070  0.0133  696 PHE B CD1 
6581  C CD2 . PHE B 395 ? 0.6689 0.7496 0.5443 0.0112  0.0086  -0.0025 696 PHE B CD2 
6582  C CE1 . PHE B 395 ? 0.5886 0.7018 0.4850 0.0051  0.0064  0.0177  696 PHE B CE1 
6583  C CE2 . PHE B 395 ? 0.6252 0.7250 0.5006 0.0087  0.0076  0.0016  696 PHE B CE2 
6584  C CZ  . PHE B 395 ? 0.5528 0.6684 0.4385 0.0059  0.0066  0.0122  696 PHE B CZ  
6585  N N   . HIS B 396 ? 0.6068 0.6283 0.4682 0.0039  0.0081  -0.0187 697 HIS B N   
6586  C CA  . HIS B 396 ? 0.6038 0.6195 0.4527 -0.0029 0.0070  -0.0271 697 HIS B CA  
6587  C C   . HIS B 396 ? 0.6316 0.6335 0.4798 -0.0144 0.0046  -0.0311 697 HIS B C   
6588  O O   . HIS B 396 ? 0.7950 0.7876 0.6301 -0.0217 0.0042  -0.0398 697 HIS B O   
6589  C CB  . HIS B 396 ? 0.6270 0.6270 0.4556 0.0052  0.0116  -0.0358 697 HIS B CB  
6590  C CG  . HIS B 396 ? 0.7242 0.7390 0.5538 0.0184  0.0150  -0.0318 697 HIS B CG  
6591  N ND1 . HIS B 396 ? 0.7492 0.7888 0.5812 0.0195  0.0145  -0.0289 697 HIS B ND1 
6592  C CD2 . HIS B 396 ? 0.7397 0.7519 0.5691 0.0308  0.0190  -0.0294 697 HIS B CD2 
6593  C CE1 . HIS B 396 ? 0.7658 0.8181 0.5993 0.0310  0.0184  -0.0252 697 HIS B CE1 
6594  N NE2 . HIS B 396 ? 0.7921 0.8296 0.6246 0.0384  0.0209  -0.0256 697 HIS B NE2 
6595  N N   . GLN B 397 ? 0.6201 0.6216 0.4813 -0.0170 0.0033  -0.0254 698 GLN B N   
6596  C CA  . GLN B 397 ? 0.6568 0.6496 0.5189 -0.0282 0.0015  -0.0283 698 GLN B CA  
6597  C C   . GLN B 397 ? 0.6780 0.6947 0.5559 -0.0337 -0.0035 -0.0223 698 GLN B C   
6598  O O   . GLN B 397 ? 0.6616 0.6872 0.5524 -0.0289 -0.0046 -0.0138 698 GLN B O   
6599  C CB  . GLN B 397 ? 0.6254 0.5972 0.4871 -0.0260 0.0045  -0.0271 698 GLN B CB  
6600  C CG  . GLN B 397 ? 0.4929 0.4589 0.3570 -0.0381 0.0032  -0.0287 698 GLN B CG  
6601  C CD  . GLN B 397 ? 0.6541 0.5983 0.4992 -0.0484 0.0051  -0.0387 698 GLN B CD  
6602  O OE1 . GLN B 397 ? 0.6066 0.5235 0.4339 -0.0435 0.0094  -0.0436 698 GLN B OE1 
6603  N NE2 . GLN B 397 ? 0.7389 0.6948 0.5865 -0.0628 0.0019  -0.0420 698 GLN B NE2 
6604  N N   . GLU B 398 ? 0.5876 0.6141 0.4630 -0.0436 -0.0066 -0.0270 699 GLU B N   
6605  C CA  . GLU B 398 ? 0.6241 0.6732 0.5128 -0.0478 -0.0113 -0.0221 699 GLU B CA  
6606  C C   . GLU B 398 ? 0.6817 0.7251 0.5794 -0.0502 -0.0108 -0.0191 699 GLU B C   
6607  O O   . GLU B 398 ? 0.6936 0.7172 0.5845 -0.0554 -0.0077 -0.0238 699 GLU B O   
6608  C CB  . GLU B 398 ? 0.6113 0.6747 0.4947 -0.0584 -0.0147 -0.0288 699 GLU B CB  
6609  C CG  . GLU B 398 ? 0.7458 0.8170 0.6192 -0.0565 -0.0157 -0.0323 699 GLU B CG  
6610  C CD  . GLU B 398 ? 0.8803 0.9715 0.7501 -0.0669 -0.0202 -0.0381 699 GLU B CD  
6611  O OE1 . GLU B 398 ? 0.8055 0.9162 0.6747 -0.0630 -0.0232 -0.0359 699 GLU B OE1 
6612  O OE2 . GLU B 398 ? 0.9614 1.0502 0.8285 -0.0796 -0.0209 -0.0447 699 GLU B OE2 
6613  N N   . MET B 399 ? 0.5754 0.6349 0.4863 -0.0463 -0.0137 -0.0112 700 MET B N   
6614  C CA  . MET B 399 ? 0.6351 0.6919 0.5546 -0.0472 -0.0132 -0.0080 700 MET B CA  
6615  C C   . MET B 399 ? 0.7400 0.8218 0.6693 -0.0477 -0.0175 -0.0043 700 MET B C   
6616  O O   . MET B 399 ? 0.8980 0.9951 0.8296 -0.0420 -0.0207 0.0002  700 MET B O   
6617  C CB  . MET B 399 ? 0.7102 0.7550 0.6343 -0.0377 -0.0113 -0.0016 700 MET B CB  
6618  C CG  . MET B 399 ? 0.6441 0.6662 0.5593 -0.0352 -0.0068 -0.0048 700 MET B CG  
6619  S SD  . MET B 399 ? 0.5894 0.6083 0.5099 -0.0241 -0.0058 0.0027  700 MET B SD  
6620  C CE  . MET B 399 ? 0.4707 0.4713 0.3787 -0.0190 -0.0009 -0.0022 700 MET B CE  
6621  N N   . LEU B 400 ? 0.5651 0.6518 0.4992 -0.0538 -0.0173 -0.0057 701 LEU B N   
6622  C CA  . LEU B 400 ? 0.4603 0.5720 0.4044 -0.0517 -0.0206 -0.0016 701 LEU B CA  
6623  C C   . LEU B 400 ? 0.6108 0.7148 0.5618 -0.0428 -0.0195 0.0050  701 LEU B C   
6624  O O   . LEU B 400 ? 0.6845 0.7698 0.6344 -0.0447 -0.0159 0.0041  701 LEU B O   
6625  C CB  . LEU B 400 ? 0.3910 0.5185 0.3367 -0.0647 -0.0209 -0.0074 701 LEU B CB  
6626  C CG  . LEU B 400 ? 0.5642 0.7041 0.5031 -0.0763 -0.0230 -0.0150 701 LEU B CG  
6627  C CD1 . LEU B 400 ? 0.5528 0.7130 0.4958 -0.0899 -0.0234 -0.0191 701 LEU B CD1 
6628  C CD2 . LEU B 400 ? 0.5228 0.6844 0.4633 -0.0677 -0.0277 -0.0115 701 LEU B CD2 
6629  N N   . ASN B 401 ? 0.5814 0.6982 0.5375 -0.0326 -0.0225 0.0116  702 ASN B N   
6630  C CA  . ASN B 401 ? 0.6085 0.7168 0.5688 -0.0239 -0.0217 0.0173  702 ASN B CA  
6631  C C   . ASN B 401 ? 0.7307 0.8620 0.6976 -0.0200 -0.0235 0.0192  702 ASN B C   
6632  O O   . ASN B 401 ? 0.6460 0.7991 0.6138 -0.0155 -0.0271 0.0211  702 ASN B O   
6633  C CB  . ASN B 401 ? 0.5689 0.6648 0.5260 -0.0141 -0.0228 0.0238  702 ASN B CB  
6634  C CG  . ASN B 401 ? 0.4305 0.5083 0.3887 -0.0093 -0.0211 0.0271  702 ASN B CG  
6635  O OD1 . ASN B 401 ? 0.5331 0.6070 0.4941 -0.0124 -0.0187 0.0245  702 ASN B OD1 
6636  N ND2 . ASN B 401 ? 0.4309 0.4972 0.3854 -0.0027 -0.0221 0.0328  702 ASN B ND2 
6637  N N   . TYR B 402 ? 0.6655 0.7933 0.6364 -0.0205 -0.0210 0.0190  703 TYR B N   
6638  C CA  . TYR B 402 ? 0.5277 0.6779 0.5050 -0.0154 -0.0217 0.0209  703 TYR B CA  
6639  C C   . TYR B 402 ? 0.6120 0.7466 0.5904 -0.0123 -0.0185 0.0224  703 TYR B C   
6640  O O   . TYR B 402 ? 0.4090 0.5195 0.3841 -0.0169 -0.0157 0.0210  703 TYR B O   
6641  C CB  . TYR B 402 ? 0.4296 0.6087 0.4118 -0.0273 -0.0220 0.0158  703 TYR B CB  
6642  C CG  . TYR B 402 ? 0.5310 0.6964 0.5096 -0.0445 -0.0185 0.0092  703 TYR B CG  
6643  C CD1 . TYR B 402 ? 0.6092 0.7710 0.5896 -0.0519 -0.0144 0.0077  703 TYR B CD1 
6644  C CD2 . TYR B 402 ? 0.5137 0.6678 0.4849 -0.0525 -0.0188 0.0047  703 TYR B CD2 
6645  C CE1 . TYR B 402 ? 0.5552 0.6996 0.5289 -0.0671 -0.0109 0.0023  703 TYR B CE1 
6646  C CE2 . TYR B 402 ? 0.5765 0.7132 0.5407 -0.0668 -0.0154 -0.0014 703 TYR B CE2 
6647  C CZ  . TYR B 402 ? 0.5970 0.7274 0.5618 -0.0741 -0.0114 -0.0024 703 TYR B CZ  
6648  O OH  . TYR B 402 ? 0.6046 0.7128 0.5590 -0.0879 -0.0077 -0.0079 703 TYR B OH  
6649  N N   . ARG B 403 ? 0.6525 0.8024 0.6349 -0.0030 -0.0188 0.0253  704 ARG B N   
6650  C CA  . ARG B 403 ? 0.5530 0.6876 0.5344 0.0046  -0.0166 0.0278  704 ARG B CA  
6651  C C   . ARG B 403 ? 0.7263 0.8772 0.7135 -0.0014 -0.0132 0.0254  704 ARG B C   
6652  O O   . ARG B 403 ? 0.7589 0.9400 0.7518 0.0029  -0.0138 0.0261  704 ARG B O   
6653  C CB  . ARG B 403 ? 0.4790 0.6126 0.4564 0.0222  -0.0192 0.0332  704 ARG B CB  
6654  C CG  . ARG B 403 ? 0.5360 0.6451 0.5048 0.0268  -0.0216 0.0365  704 ARG B CG  
6655  C CD  . ARG B 403 ? 0.7196 0.8038 0.6807 0.0370  -0.0213 0.0399  704 ARG B CD  
6656  N NE  . ARG B 403 ? 0.7458 0.8314 0.6994 0.0529  -0.0238 0.0447  704 ARG B NE  
6657  C CZ  . ARG B 403 ? 0.7456 0.8190 0.6924 0.0646  -0.0232 0.0464  704 ARG B CZ  
6658  N NH1 . ARG B 403 ? 0.6221 0.6849 0.5703 0.0612  -0.0205 0.0438  704 ARG B NH1 
6659  N NH2 . ARG B 403 ? 0.7700 0.8409 0.7068 0.0806  -0.0252 0.0508  704 ARG B NH2 
6660  N N   . LEU B 404 ? 0.7712 0.9036 0.7566 -0.0106 -0.0095 0.0232  705 LEU B N   
6661  C CA  . LEU B 404 ? 0.6955 0.8382 0.6843 -0.0168 -0.0054 0.0220  705 LEU B CA  
6662  C C   . LEU B 404 ? 0.6552 0.7830 0.6415 -0.0059 -0.0036 0.0249  705 LEU B C   
6663  O O   . LEU B 404 ? 0.6635 0.7649 0.6440 0.0000  -0.0046 0.0263  705 LEU B O   
6664  C CB  . LEU B 404 ? 0.6146 0.7440 0.5998 -0.0342 -0.0019 0.0180  705 LEU B CB  
6665  C CG  . LEU B 404 ? 0.5148 0.6500 0.4984 -0.0468 -0.0033 0.0137  705 LEU B CG  
6666  C CD1 . LEU B 404 ? 0.4509 0.5618 0.4258 -0.0613 0.0007  0.0100  705 LEU B CD1 
6667  C CD2 . LEU B 404 ? 0.5539 0.7291 0.5453 -0.0525 -0.0048 0.0122  705 LEU B CD2 
6668  N N   . THR B 405 ? 0.6658 0.8130 0.6561 -0.0041 -0.0009 0.0255  706 THR B N   
6669  C CA  . THR B 405 ? 0.5385 0.6745 0.5257 0.0040  0.0017  0.0273  706 THR B CA  
6670  C C   . THR B 405 ? 0.5366 0.6683 0.5230 -0.0094 0.0069  0.0259  706 THR B C   
6671  O O   . THR B 405 ? 0.4570 0.6039 0.4466 -0.0241 0.0089  0.0239  706 THR B O   
6672  C CB  . THR B 405 ? 0.6411 0.8030 0.6316 0.0184  0.0015  0.0292  706 THR B CB  
6673  O OG1 . THR B 405 ? 0.8754 1.0240 0.8608 0.0270  0.0040  0.0303  706 THR B OG1 
6674  C CG2 . THR B 405 ? 0.5554 0.7581 0.5554 0.0097  0.0039  0.0281  706 THR B CG2 
6675  N N   . PRO B 406 ? 0.5988 0.7078 0.5792 -0.0061 0.0092  0.0271  707 PRO B N   
6676  C CA  . PRO B 406 ? 0.6144 0.7008 0.5887 0.0072  0.0071  0.0285  707 PRO B CA  
6677  C C   . PRO B 406 ? 0.6332 0.6984 0.6040 0.0078  0.0031  0.0283  707 PRO B C   
6678  O O   . PRO B 406 ? 0.6490 0.7102 0.6203 -0.0022 0.0030  0.0268  707 PRO B O   
6679  C CB  . PRO B 406 ? 0.5263 0.5969 0.4951 0.0040  0.0111  0.0290  707 PRO B CB  
6680  C CG  . PRO B 406 ? 0.5635 0.6542 0.5359 -0.0068 0.0159  0.0289  707 PRO B CG  
6681  C CD  . PRO B 406 ? 0.5358 0.6417 0.5136 -0.0176 0.0147  0.0269  707 PRO B CD  
6682  N N   . SER B 407 ? 0.6131 0.6641 0.5790 0.0190  0.0001  0.0297  708 SER B N   
6683  C CA  . SER B 407 ? 0.6363 0.6723 0.5994 0.0195  -0.0037 0.0302  708 SER B CA  
6684  C C   . SER B 407 ? 0.6158 0.6295 0.5711 0.0262  -0.0055 0.0311  708 SER B C   
6685  O O   . SER B 407 ? 0.6916 0.7025 0.6426 0.0340  -0.0049 0.0312  708 SER B O   
6686  C CB  . SER B 407 ? 0.7738 0.8234 0.7388 0.0247  -0.0068 0.0314  708 SER B CB  
6687  O OG  . SER B 407 ? 0.8675 0.9213 0.8289 0.0382  -0.0077 0.0331  708 SER B OG  
6688  N N   . PHE B 408 ? 0.6633 0.6626 0.6162 0.0227  -0.0078 0.0314  709 PHE B N   
6689  C CA  . PHE B 408 ? 0.5186 0.4994 0.4639 0.0268  -0.0108 0.0325  709 PHE B CA  
6690  C C   . PHE B 408 ? 0.5929 0.5716 0.5343 0.0317  -0.0139 0.0347  709 PHE B C   
6691  O O   . PHE B 408 ? 0.5974 0.5875 0.5432 0.0295  -0.0145 0.0356  709 PHE B O   
6692  C CB  . PHE B 408 ? 0.3280 0.2986 0.2730 0.0197  -0.0112 0.0321  709 PHE B CB  
6693  C CG  . PHE B 408 ? 0.4296 0.3977 0.3746 0.0177  -0.0085 0.0307  709 PHE B CG  
6694  C CD1 . PHE B 408 ? 0.5259 0.4983 0.4743 0.0121  -0.0054 0.0299  709 PHE B CD1 
6695  C CD2 . PHE B 408 ? 0.4319 0.3914 0.3712 0.0218  -0.0089 0.0303  709 PHE B CD2 
6696  C CE1 . PHE B 408 ? 0.4708 0.4378 0.4164 0.0113  -0.0026 0.0296  709 PHE B CE1 
6697  C CE2 . PHE B 408 ? 0.4236 0.3811 0.3617 0.0208  -0.0064 0.0297  709 PHE B CE2 
6698  C CZ  . PHE B 408 ? 0.4310 0.3919 0.3720 0.0160  -0.0031 0.0298  709 PHE B CZ  
6699  N N   . GLU B 409 ? 0.3284 0.2910 0.2596 0.0386  -0.0159 0.0357  710 GLU B N   
6700  C CA  . GLU B 409 ? 0.4655 0.4206 0.3885 0.0455  -0.0185 0.0385  710 GLU B CA  
6701  C C   . GLU B 409 ? 0.4539 0.3821 0.3642 0.0435  -0.0210 0.0394  710 GLU B C   
6702  O O   . GLU B 409 ? 0.6966 0.6138 0.6029 0.0414  -0.0210 0.0370  710 GLU B O   
6703  C CB  . GLU B 409 ? 0.3508 0.3123 0.2694 0.0596  -0.0178 0.0389  710 GLU B CB  
6704  C CG  . GLU B 409 ? 0.7987 0.7917 0.7298 0.0607  -0.0153 0.0381  710 GLU B CG  
6705  C CD  . GLU B 409 ? 0.8998 0.9098 0.8379 0.0565  -0.0166 0.0397  710 GLU B CD  
6706  O OE1 . GLU B 409 ? 0.8211 0.8194 0.7528 0.0575  -0.0193 0.0426  710 GLU B OE1 
6707  O OE2 . GLU B 409 ? 0.8660 0.9009 0.8152 0.0512  -0.0148 0.0381  710 GLU B OE2 
6708  N N   . TYR B 410 ? 0.5856 0.5036 0.4887 0.0433  -0.0232 0.0428  711 TYR B N   
6709  C CA  . TYR B 410 ? 0.6829 0.5727 0.5705 0.0409  -0.0254 0.0438  711 TYR B CA  
6710  C C   . TYR B 410 ? 0.7086 0.5808 0.5812 0.0539  -0.0256 0.0430  711 TYR B C   
6711  O O   . TYR B 410 ? 0.5997 0.4845 0.4742 0.0665  -0.0241 0.0429  711 TYR B O   
6712  C CB  . TYR B 410 ? 0.7550 0.6360 0.6364 0.0359  -0.0271 0.0484  711 TYR B CB  
6713  C CG  . TYR B 410 ? 0.8139 0.7127 0.7087 0.0244  -0.0266 0.0487  711 TYR B CG  
6714  C CD1 . TYR B 410 ? 0.7873 0.7052 0.6907 0.0256  -0.0260 0.0503  711 TYR B CD1 
6715  C CD2 . TYR B 410 ? 0.8799 0.7783 0.7785 0.0133  -0.0268 0.0468  711 TYR B CD2 
6716  C CE1 . TYR B 410 ? 0.7725 0.7048 0.6860 0.0165  -0.0252 0.0499  711 TYR B CE1 
6717  C CE2 . TYR B 410 ? 0.8197 0.7351 0.7294 0.0055  -0.0259 0.0469  711 TYR B CE2 
6718  C CZ  . TYR B 410 ? 0.8132 0.7437 0.7295 0.0074  -0.0249 0.0483  711 TYR B CZ  
6719  O OH  . TYR B 410 ? 0.8964 0.8416 0.8214 0.0009  -0.0237 0.0478  711 TYR B OH  
6720  N N   . GLN B 411 ? 0.6966 0.5400 0.5531 0.0506  -0.0274 0.0421  712 GLN B N   
6721  C CA  . GLN B 411 ? 0.6614 0.4798 0.4982 0.0625  -0.0277 0.0408  712 GLN B CA  
6722  C C   . GLN B 411 ? 0.6459 0.4284 0.4620 0.0542  -0.0303 0.0419  712 GLN B C   
6723  O O   . GLN B 411 ? 0.6677 0.4509 0.4884 0.0377  -0.0317 0.0426  712 GLN B O   
6724  C CB  . GLN B 411 ? 0.6999 0.5230 0.5388 0.0665  -0.0263 0.0354  712 GLN B CB  
6725  C CG  . GLN B 411 ? 0.6883 0.5069 0.5291 0.0522  -0.0275 0.0318  712 GLN B CG  
6726  C CD  . GLN B 411 ? 0.6933 0.5214 0.5378 0.0571  -0.0257 0.0272  712 GLN B CD  
6727  O OE1 . GLN B 411 ? 0.5895 0.4084 0.4227 0.0701  -0.0245 0.0250  712 GLN B OE1 
6728  N NE2 . GLN B 411 ? 0.6480 0.4947 0.5072 0.0478  -0.0250 0.0261  712 GLN B NE2 
6729  N N   . PRO B 412 ? 0.6633 0.4140 0.4553 0.0650  -0.0309 0.0423  713 PRO B N   
6730  C CA  . PRO B 412 ? 0.7114 0.4228 0.4800 0.0550  -0.0332 0.0434  713 PRO B CA  
6731  C C   . PRO B 412 ? 0.7783 0.4820 0.5453 0.0390  -0.0349 0.0379  713 PRO B C   
6732  O O   . PRO B 412 ? 1.0104 0.7277 0.7857 0.0419  -0.0343 0.0328  713 PRO B O   
6733  C CB  . PRO B 412 ? 0.8025 0.4803 0.5437 0.0738  -0.0328 0.0437  713 PRO B CB  
6734  C CG  . PRO B 412 ? 0.6998 0.4074 0.4539 0.0944  -0.0305 0.0447  713 PRO B CG  
6735  C CD  . PRO B 412 ? 0.6892 0.4383 0.4728 0.0872  -0.0292 0.0417  713 PRO B CD  
6736  N N   . ASP B 413 ? 0.8497 0.5336 0.6058 0.0214  -0.0371 0.0394  714 ASP B N   
6737  C CA  . ASP B 413 ? 0.9074 0.5812 0.6574 0.0056  -0.0394 0.0340  714 ASP B CA  
6738  C C   . ASP B 413 ? 1.0690 0.7075 0.7932 0.0155  -0.0400 0.0287  714 ASP B C   
6739  O O   . ASP B 413 ? 1.1441 0.7475 0.8437 0.0255  -0.0396 0.0308  714 ASP B O   
6740  C CB  . ASP B 413 ? 0.9273 0.5871 0.6685 -0.0165 -0.0415 0.0370  714 ASP B CB  
6741  C CG  . ASP B 413 ? 1.0357 0.7337 0.8027 -0.0268 -0.0408 0.0413  714 ASP B CG  
6742  O OD1 . ASP B 413 ? 0.9876 0.7211 0.7785 -0.0244 -0.0399 0.0390  714 ASP B OD1 
6743  O OD2 . ASP B 413 ? 1.1006 0.7916 0.8622 -0.0370 -0.0408 0.0469  714 ASP B OD2 
6744  N N   . PRO B 414 ? 1.1181 0.7636 0.8452 0.0145  -0.0408 0.0219  715 PRO B N   
6745  C CA  . PRO B 414 ? 0.9102 0.5268 0.6142 0.0283  -0.0405 0.0163  715 PRO B CA  
6746  C C   . PRO B 414 ? 1.0122 0.5754 0.6799 0.0217  -0.0427 0.0145  715 PRO B C   
6747  O O   . PRO B 414 ? 1.2064 0.7373 0.8494 0.0390  -0.0416 0.0126  715 PRO B O   
6748  C CB  . PRO B 414 ? 0.8192 0.4576 0.5352 0.0237  -0.0414 0.0099  715 PRO B CB  
6749  C CG  . PRO B 414 ? 0.8729 0.5356 0.6072 0.0026  -0.0435 0.0114  715 PRO B CG  
6750  C CD  . PRO B 414 ? 1.0022 0.6805 0.7510 0.0016  -0.0419 0.0190  715 PRO B CD  
6751  N N   . TRP B 415 ? 0.9856 0.5380 0.6477 -0.0026 -0.0456 0.0151  716 TRP B N   
6752  C CA  . TRP B 415 ? 0.9874 0.4860 0.6125 -0.0131 -0.0477 0.0129  716 TRP B CA  
6753  C C   . TRP B 415 ? 1.1512 0.6132 0.7534 -0.0024 -0.0458 0.0196  716 TRP B C   
6754  O O   . TRP B 415 ? 1.2675 0.6759 0.8328 -0.0058 -0.0468 0.0179  716 TRP B O   
6755  C CB  . TRP B 415 ? 0.9779 0.4806 0.6050 -0.0444 -0.0511 0.0123  716 TRP B CB  
6756  C CG  . TRP B 415 ? 1.0691 0.6004 0.7178 -0.0551 -0.0502 0.0206  716 TRP B CG  
6757  C CD1 . TRP B 415 ? 1.1613 0.6707 0.7972 -0.0591 -0.0490 0.0282  716 TRP B CD1 
6758  C CD2 . TRP B 415 ? 1.0306 0.6165 0.7154 -0.0623 -0.0502 0.0223  716 TRP B CD2 
6759  N NE1 . TRP B 415 ? 1.1535 0.7026 0.8163 -0.0688 -0.0482 0.0341  716 TRP B NE1 
6760  C CE2 . TRP B 415 ? 1.0580 0.6536 0.7507 -0.0703 -0.0489 0.0303  716 TRP B CE2 
6761  C CE3 . TRP B 415 ? 1.0161 0.6418 0.7253 -0.0616 -0.0509 0.0179  716 TRP B CE3 
6762  C CZ2 . TRP B 415 ? 0.9469 0.5904 0.6706 -0.0769 -0.0483 0.0334  716 TRP B CZ2 
6763  C CZ3 . TRP B 415 ? 0.8613 0.5322 0.6003 -0.0677 -0.0502 0.0215  716 TRP B CZ3 
6764  C CH2 . TRP B 415 ? 0.8398 0.5190 0.5856 -0.0751 -0.0489 0.0287  716 TRP B CH2 
6765  N N   . ASN B 416 ? 1.1741 0.6618 0.7950 0.0101  -0.0433 0.0271  717 ASN B N   
6766  C CA  . ASN B 416 ? 1.2248 0.6807 0.8234 0.0271  -0.0414 0.0334  717 ASN B CA  
6767  C C   . ASN B 416 ? 1.3039 0.7438 0.8868 0.0564  -0.0396 0.0297  717 ASN B C   
6768  O O   . ASN B 416 ? 1.3676 0.7664 0.9201 0.0720  -0.0385 0.0328  717 ASN B O   
6769  C CB  . ASN B 416 ? 1.1349 0.6267 0.7582 0.0317  -0.0398 0.0421  717 ASN B CB  
6770  C CG  . ASN B 416 ? 1.1576 0.6648 0.7941 0.0049  -0.0410 0.0464  717 ASN B CG  
6771  O OD1 . ASN B 416 ? 1.1896 0.6677 0.8072 -0.0164 -0.0427 0.0458  717 ASN B OD1 
6772  N ND2 . ASN B 416 ? 1.0857 0.6394 0.7537 0.0055  -0.0398 0.0505  717 ASN B ND2 
6773  N N   . THR B 417 ? 1.3110 0.7812 0.9120 0.0643  -0.0390 0.0233  718 THR B N   
6774  C CA  . THR B 417 ? 1.3741 0.8423 0.9669 0.0928  -0.0365 0.0200  718 THR B CA  
6775  C C   . THR B 417 ? 1.3860 0.8261 0.9565 0.0942  -0.0373 0.0101  718 THR B C   
6776  O O   . THR B 417 ? 1.4808 0.8944 1.0268 0.1174  -0.0355 0.0075  718 THR B O   
6777  C CB  . THR B 417 ? 1.3102 0.8392 0.9414 0.1030  -0.0342 0.0210  718 THR B CB  
6778  O OG1 . THR B 417 ? 1.2300 0.7883 0.8844 0.0962  -0.0341 0.0287  718 THR B OG1 
6779  C CG2 . THR B 417 ? 1.3469 0.8806 0.9715 0.1343  -0.0309 0.0204  718 THR B CG2 
6780  N N   . HIS B 418 ? 1.3532 0.7996 0.9304 0.0714  -0.0401 0.0045  719 HIS B N   
6781  C CA  . HIS B 418 ? 1.3787 0.8141 0.9433 0.0739  -0.0409 -0.0054 719 HIS B CA  
6782  C C   . HIS B 418 ? 1.4932 0.8613 1.0101 0.0744  -0.0423 -0.0107 719 HIS B C   
6783  O O   . HIS B 418 ? 1.4672 0.8010 0.9651 0.0537  -0.0449 -0.0095 719 HIS B O   
6784  C CB  . HIS B 418 ? 1.2939 0.7599 0.8807 0.0495  -0.0439 -0.0092 719 HIS B CB  
6785  C CG  . HIS B 418 ? 1.2574 0.7167 0.8329 0.0506  -0.0451 -0.0191 719 HIS B CG  
6786  N ND1 . HIS B 418 ? 1.3482 0.7694 0.8956 0.0334  -0.0491 -0.0265 719 HIS B ND1 
6787  C CD2 . HIS B 418 ? 1.2673 0.7531 0.8544 0.0661  -0.0429 -0.0230 719 HIS B CD2 
6788  C CE1 . HIS B 418 ? 1.3848 0.8097 0.9271 0.0393  -0.0495 -0.0348 719 HIS B CE1 
6789  N NE2 . HIS B 418 ? 1.3349 0.7988 0.9011 0.0594  -0.0456 -0.0325 719 HIS B NE2 
6790  N N   . VAL B 419 ? 1.6337 0.9823 1.1297 0.0976  -0.0403 -0.0166 720 VAL B N   
6791  C CA  . VAL B 419 ? 1.7580 1.0404 1.2056 0.1003  -0.0413 -0.0238 720 VAL B CA  
6792  C C   . VAL B 419 ? 1.7554 1.0373 1.1987 0.0844  -0.0445 -0.0347 720 VAL B C   
6793  O O   . VAL B 419 ? 1.7733 1.0866 1.2312 0.0969  -0.0430 -0.0393 720 VAL B O   
6794  C CB  . VAL B 419 ? 1.7851 1.0477 1.2103 0.1371  -0.0370 -0.0242 720 VAL B CB  
6795  C CG1 . VAL B 419 ? 1.7994 1.0376 1.2065 0.1435  -0.0353 -0.0162 720 VAL B CG1 
6796  C CG2 . VAL B 419 ? 1.6953 1.0193 1.1567 0.1594  -0.0333 -0.0211 720 VAL B CG2 
6797  N N   . TRP B 420 ? 1.7654 1.0121 1.1874 0.0563  -0.0489 -0.0388 721 TRP B N   
6798  C CA  . TRP B 420 ? 1.7547 1.0062 1.1750 0.0360  -0.0530 -0.0488 721 TRP B CA  
6799  C C   . TRP B 420 ? 1.8058 1.0146 1.1878 0.0513  -0.0526 -0.0599 721 TRP B C   
6800  O O   . TRP B 420 ? 1.8419 1.0308 1.2056 0.0757  -0.0485 -0.0574 721 TRP B O   
6801  C CB  . TRP B 420 ? 1.7827 1.0153 1.1938 -0.0009 -0.0579 -0.0491 721 TRP B CB  
6802  C CG  . TRP B 420 ? 1.7449 1.0299 1.1973 -0.0183 -0.0587 -0.0404 721 TRP B CG  
6803  C CD1 . TRP B 420 ? 1.7018 0.9986 1.1696 -0.0143 -0.0561 -0.0293 721 TRP B CD1 
6804  C CD2 . TRP B 420 ? 1.6624 0.9952 1.1445 -0.0411 -0.0624 -0.0422 721 TRP B CD2 
6805  N NE1 . TRP B 420 ? 1.6081 0.9559 1.1129 -0.0333 -0.0576 -0.0245 721 TRP B NE1 
6806  C CE2 . TRP B 420 ? 1.5884 0.9592 1.1025 -0.0492 -0.0614 -0.0320 721 TRP B CE2 
6807  C CE3 . TRP B 420 ? 1.6549 1.0030 1.1386 -0.0543 -0.0664 -0.0513 721 TRP B CE3 
6808  C CZ2 . TRP B 420 ? 1.5486 0.9706 1.0953 -0.0685 -0.0640 -0.0308 721 TRP B CZ2 
6809  C CZ3 . TRP B 420 ? 1.6055 1.0061 1.1222 -0.0735 -0.0693 -0.0496 721 TRP B CZ3 
6810  C CH2 . TRP B 420 ? 1.5703 1.0069 1.1179 -0.0798 -0.0679 -0.0394 721 TRP B CH2 
6811  N N   . LYS B 421 ? 1.8050 1.0196 1.1841 0.0360  -0.0564 -0.0697 722 LYS B N   
6812  C CA  . LYS B 421 ? 1.7964 0.9858 1.1468 0.0468  -0.0560 -0.0791 722 LYS B CA  
6813  C C   . LYS B 421 ? 1.7138 0.9027 1.0568 0.0200  -0.0619 -0.0895 722 LYS B C   
6814  O O   . LYS B 421 ? 1.7092 0.8769 1.0385 -0.0079 -0.0657 -0.0904 722 LYS B O   
6815  C CB  . LYS B 421 ? 1.7655 0.9793 1.1254 0.0813  -0.0512 -0.0809 722 LYS B CB  
6816  C CG  . LYS B 421 ? 1.6730 0.9564 1.0818 0.0822  -0.0501 -0.0758 722 LYS B CG  
6817  C CD  . LYS B 421 ? 1.6310 0.9428 1.0531 0.1165  -0.0436 -0.0729 722 LYS B CD  
6818  C CE  . LYS B 421 ? 1.5744 0.9546 1.0404 0.1148  -0.0424 -0.0699 722 LYS B CE  
6819  N NZ  . LYS B 421 ? 1.5046 0.9188 0.9887 0.1441  -0.0358 -0.0647 722 LYS B NZ  
6820  N N   . PRO C 2   ? 1.2639 1.7983 1.2256 0.1801  0.0487  -0.0576 303 PRO C N   
6821  C CA  . PRO C 2   ? 1.2942 1.8404 1.2722 0.1579  0.0463  -0.0469 303 PRO C CA  
6822  C C   . PRO C 2   ? 1.3229 1.8508 1.3051 0.1673  0.0393  -0.0466 303 PRO C C   
6823  O O   . PRO C 2   ? 1.2129 1.7365 1.2047 0.1489  0.0361  -0.0385 303 PRO C O   
6824  C CB  . PRO C 2   ? 1.2216 1.8372 1.2143 0.1525  0.0528  -0.0445 303 PRO C CB  
6825  C CG  . PRO C 2   ? 1.1519 1.7851 1.1349 0.1614  0.0597  -0.0509 303 PRO C CG  
6826  C CD  . PRO C 2   ? 1.1706 1.7479 1.1331 0.1770  0.0567  -0.0589 303 PRO C CD  
6827  N N   . ARG C 3   ? 1.4095 1.9241 1.3818 0.1964  0.0370  -0.0553 304 ARG C N   
6828  C CA  . ARG C 3   ? 1.3183 1.8194 1.2916 0.2111  0.0307  -0.0558 304 ARG C CA  
6829  C C   . ARG C 3   ? 1.1325 1.5645 1.0904 0.2107  0.0244  -0.0563 304 ARG C C   
6830  O O   . ARG C 3   ? 1.1604 1.5705 1.1121 0.2274  0.0193  -0.0583 304 ARG C O   
6831  C CB  . ARG C 3   ? 1.3908 1.9179 1.3598 0.2452  0.0321  -0.0646 304 ARG C CB  
6832  C CG  . ARG C 3   ? 1.4660 2.0260 1.4476 0.2576  0.0286  -0.0623 304 ARG C CG  
6833  C CD  . ARG C 3   ? 1.5158 2.1233 1.4979 0.2888  0.0325  -0.0701 304 ARG C CD  
6834  N NE  . ARG C 3   ? 1.5488 2.1959 1.5441 0.3024  0.0290  -0.0677 304 ARG C NE  
6835  C CZ  . ARG C 3   ? 1.4948 2.1321 1.4799 0.3362  0.0252  -0.0727 304 ARG C CZ  
6836  N NH1 . ARG C 3   ? 1.5211 2.1069 1.4807 0.3593  0.0248  -0.0810 304 ARG C NH1 
6837  N NH2 . ARG C 3   ? 1.3753 2.0540 1.3739 0.3469  0.0216  -0.0695 304 ARG C NH2 
6838  N N   . PHE C 4   ? 0.9500 1.3496 0.9015 0.1914  0.0247  -0.0539 305 PHE C N   
6839  C CA  . PHE C 4   ? 0.8326 1.1709 0.7666 0.1915  0.0203  -0.0564 305 PHE C CA  
6840  C C   . PHE C 4   ? 0.6659 0.9893 0.5971 0.1696  0.0223  -0.0532 305 PHE C C   
6841  O O   . PHE C 4   ? 0.6896 1.0427 0.6236 0.1645  0.0278  -0.0534 305 PHE C O   
6842  C CB  . PHE C 4   ? 0.9977 1.3126 0.9108 0.2189  0.0200  -0.0677 305 PHE C CB  
6843  C CG  . PHE C 4   ? 1.1974 1.5236 1.1010 0.2233  0.0259  -0.0747 305 PHE C CG  
6844  C CD1 . PHE C 4   ? 1.2379 1.5206 1.1218 0.2205  0.0250  -0.0801 305 PHE C CD1 
6845  C CD2 . PHE C 4   ? 1.2115 1.5947 1.1261 0.2285  0.0323  -0.0757 305 PHE C CD2 
6846  C CE1 . PHE C 4   ? 1.2562 1.5499 1.1305 0.2239  0.0302  -0.0866 305 PHE C CE1 
6847  C CE2 . PHE C 4   ? 1.1427 1.5377 1.0482 0.2322  0.0379  -0.0819 305 PHE C CE2 
6848  C CZ  . PHE C 4   ? 1.2267 1.5761 1.1116 0.2303  0.0368  -0.0875 305 PHE C CZ  
6849  N N   . LEU C 5   ? 0.4965 0.7769 0.4221 0.1568  0.0179  -0.0500 306 LEU C N   
6850  C CA  . LEU C 5   ? 0.4891 0.7531 0.4102 0.1391  0.0189  -0.0472 306 LEU C CA  
6851  C C   . LEU C 5   ? 0.6355 0.8484 0.5394 0.1414  0.0142  -0.0518 306 LEU C C   
6852  O O   . LEU C 5   ? 0.7620 0.9481 0.6647 0.1410  0.0094  -0.0500 306 LEU C O   
6853  C CB  . LEU C 5   ? 0.4868 0.7576 0.4218 0.1155  0.0187  -0.0360 306 LEU C CB  
6854  C CG  . LEU C 5   ? 0.5318 0.8495 0.4825 0.1072  0.0229  -0.0302 306 LEU C CG  
6855  C CD1 . LEU C 5   ? 0.5696 0.8815 0.5295 0.0857  0.0215  -0.0200 306 LEU C CD1 
6856  C CD2 . LEU C 5   ? 0.4299 0.7750 0.3785 0.1047  0.0290  -0.0311 306 LEU C CD2 
6857  N N   . LYS C 6   ? 0.5955 0.7960 0.4852 0.1427  0.0156  -0.0579 307 LYS C N   
6858  C CA  . LYS C 6   ? 0.6282 0.7825 0.4991 0.1435  0.0115  -0.0635 307 LYS C CA  
6859  C C   . LYS C 6   ? 0.6970 0.8381 0.5702 0.1219  0.0097  -0.0572 307 LYS C C   
6860  O O   . LYS C 6   ? 0.7334 0.8989 0.6153 0.1107  0.0128  -0.0517 307 LYS C O   
6861  C CB  . LYS C 6   ? 0.6987 0.8462 0.5499 0.1582  0.0138  -0.0752 307 LYS C CB  
6862  C CG  . LYS C 6   ? 0.7466 0.8961 0.5898 0.1842  0.0148  -0.0830 307 LYS C CG  
6863  C CD  . LYS C 6   ? 0.7083 0.8470 0.5289 0.1993  0.0174  -0.0954 307 LYS C CD  
6864  C CE  . LYS C 6   ? 0.7864 0.9301 0.5983 0.2285  0.0191  -0.1032 307 LYS C CE  
6865  N NZ  . LYS C 6   ? 0.8943 0.9846 0.6838 0.2411  0.0139  -0.1087 307 LYS C NZ  
6866  N N   . VAL C 7   ? 0.7019 0.8056 0.5669 0.1161  0.0046  -0.0575 308 VAL C N   
6867  C CA  . VAL C 7   ? 0.6293 0.7196 0.4934 0.0985  0.0025  -0.0535 308 VAL C CA  
6868  C C   . VAL C 7   ? 0.7518 0.8085 0.5937 0.0996  -0.0004 -0.0626 308 VAL C C   
6869  O O   . VAL C 7   ? 0.8431 0.8731 0.6707 0.1105  -0.0024 -0.0695 308 VAL C O   
6870  C CB  . VAL C 7   ? 0.6751 0.7563 0.5511 0.0865  -0.0006 -0.0445 308 VAL C CB  
6871  C CG1 . VAL C 7   ? 0.6961 0.8036 0.5898 0.0877  0.0015  -0.0377 308 VAL C CG1 
6872  C CG2 . VAL C 7   ? 0.7509 0.7946 0.6155 0.0881  -0.0054 -0.0479 308 VAL C CG2 
6873  N N   . LYS C 8   ? 0.7012 0.7588 0.5387 0.0880  -0.0008 -0.0626 309 LYS C N   
6874  C CA  . LYS C 8   ? 0.5493 0.5800 0.3648 0.0859  -0.0033 -0.0719 309 LYS C CA  
6875  C C   . LYS C 8   ? 0.6060 0.6260 0.4227 0.0676  -0.0074 -0.0672 309 LYS C C   
6876  O O   . LYS C 8   ? 0.7165 0.7580 0.5488 0.0581  -0.0069 -0.0580 309 LYS C O   
6877  C CB  . LYS C 8   ? 0.7456 0.7926 0.5515 0.0906  0.0002  -0.0784 309 LYS C CB  
6878  C CG  . LYS C 8   ? 0.8185 0.8404 0.6007 0.0855  -0.0025 -0.0882 309 LYS C CG  
6879  C CD  . LYS C 8   ? 0.8680 0.9113 0.6427 0.0885  0.0011  -0.0933 309 LYS C CD  
6880  C CE  . LYS C 8   ? 0.9747 0.9961 0.7264 0.0798  -0.0022 -0.1024 309 LYS C CE  
6881  N NZ  . LYS C 8   ? 0.9732 1.0176 0.7177 0.0819  0.0012  -0.1069 309 LYS C NZ  
6882  N N   . ASN C 9   ? 0.5795 0.5662 0.3784 0.0630  -0.0113 -0.0738 310 ASN C N   
6883  C CA  . ASN C 9   ? 0.5853 0.5635 0.3821 0.0452  -0.0153 -0.0715 310 ASN C CA  
6884  C C   . ASN C 9   ? 0.8415 0.8223 0.6232 0.0396  -0.0159 -0.0788 310 ASN C C   
6885  O O   . ASN C 9   ? 0.8959 0.8551 0.6554 0.0455  -0.0159 -0.0900 310 ASN C O   
6886  C CB  . ASN C 9   ? 0.7875 0.7289 0.5722 0.0407  -0.0192 -0.0744 310 ASN C CB  
6887  C CG  . ASN C 9   ? 0.9223 0.8602 0.7075 0.0215  -0.0230 -0.0713 310 ASN C CG  
6888  O OD1 . ASN C 9   ? 0.9824 0.9198 0.7560 0.0117  -0.0249 -0.0763 310 ASN C OD1 
6889  N ND2 . ASN C 9   ? 0.8968 0.8342 0.6952 0.0158  -0.0243 -0.0632 310 ASN C ND2 
6890  N N   . TRP C 10  ? 0.8337 0.8400 0.6256 0.0291  -0.0165 -0.0726 311 TRP C N   
6891  C CA  . TRP C 10  ? 0.8152 0.8306 0.5944 0.0242  -0.0171 -0.0784 311 TRP C CA  
6892  C C   . TRP C 10  ? 0.8771 0.8732 0.6402 0.0091  -0.0224 -0.0844 311 TRP C C   
6893  O O   . TRP C 10  ? 0.9299 0.9360 0.6831 0.0019  -0.0239 -0.0885 311 TRP C O   
6894  C CB  . TRP C 10  ? 0.5734 0.6257 0.3686 0.0214  -0.0154 -0.0685 311 TRP C CB  
6895  C CG  . TRP C 10  ? 0.5670 0.6382 0.3714 0.0338  -0.0098 -0.0652 311 TRP C CG  
6896  C CD1 . TRP C 10  ? 0.5976 0.6779 0.4199 0.0384  -0.0073 -0.0565 311 TRP C CD1 
6897  C CD2 . TRP C 10  ? 0.6518 0.7371 0.4474 0.0422  -0.0058 -0.0708 311 TRP C CD2 
6898  N NE1 . TRP C 10  ? 0.6068 0.7075 0.4326 0.0478  -0.0020 -0.0561 311 TRP C NE1 
6899  C CE2 . TRP C 10  ? 0.7113 0.8164 0.5214 0.0509  -0.0008 -0.0646 311 TRP C CE2 
6900  C CE3 . TRP C 10  ? 0.6994 0.7841 0.4758 0.0423  -0.0059 -0.0806 311 TRP C CE3 
6901  C CZ2 . TRP C 10  ? 0.6562 0.7824 0.4630 0.0599  0.0045  -0.0676 311 TRP C CZ2 
6902  C CZ3 . TRP C 10  ? 0.7377 0.8414 0.5101 0.0526  -0.0006 -0.0840 311 TRP C CZ3 
6903  C CH2 . TRP C 10  ? 0.7490 0.8744 0.5371 0.0613  0.0047  -0.0772 311 TRP C CH2 
6904  N N   . GLU C 11  ? 0.8790 0.8487 0.6382 0.0031  -0.0252 -0.0849 312 GLU C N   
6905  C CA  . GLU C 11  ? 0.8390 0.7854 0.5791 -0.0127 -0.0298 -0.0918 312 GLU C CA  
6906  C C   . GLU C 11  ? 0.9648 0.8676 0.6767 -0.0072 -0.0299 -0.1041 312 GLU C C   
6907  O O   . GLU C 11  ? 1.1846 1.0715 0.8725 -0.0135 -0.0315 -0.1147 312 GLU C O   
6908  C CB  . GLU C 11  ? 0.8273 0.7732 0.5800 -0.0250 -0.0327 -0.0837 312 GLU C CB  
6909  C CG  . GLU C 11  ? 0.9816 0.9264 0.7246 -0.0461 -0.0375 -0.0865 312 GLU C CG  
6910  C CD  . GLU C 11  ? 1.1393 1.0931 0.8987 -0.0565 -0.0393 -0.0772 312 GLU C CD  
6911  O OE1 . GLU C 11  ? 1.0776 1.0386 0.8560 -0.0470 -0.0369 -0.0685 312 GLU C OE1 
6912  O OE2 . GLU C 11  ? 1.2525 1.2074 1.0051 -0.0748 -0.0431 -0.0790 312 GLU C OE2 
6913  N N   . THR C 12  ? 0.9178 0.8005 0.6306 0.0058  -0.0281 -0.1029 313 THR C N   
6914  C CA  . THR C 12  ? 0.8996 0.7366 0.5844 0.0139  -0.0283 -0.1131 313 THR C CA  
6915  C C   . THR C 12  ? 0.8907 0.7279 0.5687 0.0372  -0.0238 -0.1194 313 THR C C   
6916  O O   . THR C 12  ? 1.0327 0.8317 0.6839 0.0471  -0.0237 -0.1292 313 THR C O   
6917  C CB  . THR C 12  ? 0.9792 0.7923 0.6666 0.0148  -0.0296 -0.1076 313 THR C CB  
6918  O OG1 . THR C 12  ? 0.9488 0.7806 0.6570 0.0330  -0.0263 -0.1007 313 THR C OG1 
6919  C CG2 . THR C 12  ? 0.9070 0.7316 0.6085 -0.0062 -0.0328 -0.0991 313 THR C CG2 
6920  N N   . GLU C 13  ? 0.8441 0.7231 0.5445 0.0464  -0.0200 -0.1138 314 GLU C N   
6921  C CA  . GLU C 13  ? 0.8583 0.7489 0.5576 0.0682  -0.0151 -0.1182 314 GLU C CA  
6922  C C   . GLU C 13  ? 0.8938 0.7697 0.5943 0.0868  -0.0136 -0.1173 314 GLU C C   
6923  O O   . GLU C 13  ? 0.9227 0.7977 0.6140 0.1069  -0.0101 -0.1241 314 GLU C O   
6924  C CB  . GLU C 13  ? 0.9404 0.8140 0.6106 0.0727  -0.0141 -0.1323 314 GLU C CB  
6925  C CG  . GLU C 13  ? 1.0323 0.9454 0.7108 0.0705  -0.0114 -0.1320 314 GLU C CG  
6926  C CD  . GLU C 13  ? 1.1314 1.0275 0.7798 0.0711  -0.0111 -0.1463 314 GLU C CD  
6927  O OE1 . GLU C 13  ? 1.2032 1.1133 0.8467 0.0876  -0.0062 -0.1521 314 GLU C OE1 
6928  O OE2 . GLU C 13  ? 1.1419 1.0117 0.7709 0.0545  -0.0157 -0.1521 314 GLU C OE2 
6929  N N   . VAL C 14  ? 0.8573 0.7250 0.5693 0.0816  -0.0161 -0.1091 315 VAL C N   
6930  C CA  . VAL C 14  ? 0.8848 0.7434 0.5999 0.0989  -0.0152 -0.1069 315 VAL C CA  
6931  C C   . VAL C 14  ? 0.8801 0.7859 0.6242 0.1082  -0.0112 -0.0989 315 VAL C C   
6932  O O   . VAL C 14  ? 0.8990 0.8355 0.6653 0.0958  -0.0107 -0.0901 315 VAL C O   
6933  C CB  . VAL C 14  ? 0.9206 0.7526 0.6355 0.0884  -0.0195 -0.1010 315 VAL C CB  
6934  C CG1 . VAL C 14  ? 0.8680 0.7040 0.5947 0.1038  -0.0189 -0.0951 315 VAL C CG1 
6935  C CG2 . VAL C 14  ? 0.9629 0.7424 0.6434 0.0823  -0.0228 -0.1099 315 VAL C CG2 
6936  N N   . VAL C 15  ? 0.8297 0.7417 0.5726 0.1302  -0.0084 -0.1021 316 VAL C N   
6937  C CA  . VAL C 15  ? 0.8571 0.8144 0.6261 0.1383  -0.0046 -0.0949 316 VAL C CA  
6938  C C   . VAL C 15  ? 0.9586 0.9099 0.7342 0.1493  -0.0062 -0.0905 316 VAL C C   
6939  O O   . VAL C 15  ? 1.0591 0.9803 0.8150 0.1654  -0.0076 -0.0968 316 VAL C O   
6940  C CB  . VAL C 15  ? 0.8242 0.8075 0.5899 0.1544  0.0007  -0.1019 316 VAL C CB  
6941  C CG1 . VAL C 15  ? 0.7671 0.7996 0.5596 0.1595  0.0047  -0.0941 316 VAL C CG1 
6942  C CG2 . VAL C 15  ? 0.6275 0.6163 0.3854 0.1433  0.0020  -0.1060 316 VAL C CG2 
6943  N N   . LEU C 16  ? 0.8706 0.8491 0.6718 0.1411  -0.0062 -0.0797 317 LEU C N   
6944  C CA  . LEU C 16  ? 0.7979 0.7798 0.6089 0.1499  -0.0076 -0.0745 317 LEU C CA  
6945  C C   . LEU C 16  ? 0.8239 0.8557 0.6563 0.1577  -0.0034 -0.0707 317 LEU C C   
6946  O O   . LEU C 16  ? 0.8170 0.8796 0.6623 0.1477  0.0000  -0.0675 317 LEU C O   
6947  C CB  . LEU C 16  ? 0.6553 0.6264 0.4768 0.1323  -0.0113 -0.0654 317 LEU C CB  
6948  C CG  . LEU C 16  ? 0.6511 0.5813 0.4553 0.1185  -0.0150 -0.0676 317 LEU C CG  
6949  C CD1 . LEU C 16  ? 0.5937 0.5225 0.4113 0.1009  -0.0175 -0.0584 317 LEU C CD1 
6950  C CD2 . LEU C 16  ? 0.6587 0.5449 0.4349 0.1311  -0.0176 -0.0752 317 LEU C CD2 
6951  N N   . THR C 17  ? 0.8443 0.8847 0.6792 0.1752  -0.0038 -0.0708 318 THR C N   
6952  C CA  . THR C 17  ? 0.7732 0.8637 0.6258 0.1847  0.0002  -0.0689 318 THR C CA  
6953  C C   . THR C 17  ? 0.6336 0.7433 0.5063 0.1783  -0.0017 -0.0594 318 THR C C   
6954  O O   . THR C 17  ? 0.6795 0.7738 0.5479 0.1888  -0.0055 -0.0588 318 THR C O   
6955  C CB  . THR C 17  ? 0.8214 0.9147 0.6603 0.2130  0.0019  -0.0779 318 THR C CB  
6956  O OG1 . THR C 17  ? 0.8478 0.9031 0.6602 0.2186  0.0019  -0.0877 318 THR C OG1 
6957  C CG2 . THR C 17  ? 0.7899 0.9402 0.6447 0.2199  0.0078  -0.0783 318 THR C CG2 
6958  N N   . ASP C 18  ? 0.5144 0.6569 0.4070 0.1615  0.0008  -0.0522 319 ASP C N   
6959  C CA  . ASP C 18  ? 0.5877 0.7441 0.4976 0.1500  -0.0010 -0.0433 319 ASP C CA  
6960  C C   . ASP C 18  ? 0.7249 0.9278 0.6491 0.1596  0.0011  -0.0420 319 ASP C C   
6961  O O   . ASP C 18  ? 0.6819 0.9227 0.6152 0.1566  0.0060  -0.0417 319 ASP C O   
6962  C CB  . ASP C 18  ? 0.6654 0.8271 0.5856 0.1260  0.0006  -0.0362 319 ASP C CB  
6963  C CG  . ASP C 18  ? 0.5665 0.7263 0.4983 0.1127  -0.0020 -0.0280 319 ASP C CG  
6964  O OD1 . ASP C 18  ? 0.5013 0.6880 0.4445 0.1150  -0.0020 -0.0252 319 ASP C OD1 
6965  O OD2 . ASP C 18  ? 0.6124 0.7453 0.5414 0.1000  -0.0041 -0.0248 319 ASP C OD2 
6966  N N   . THR C 19  ? 0.7939 0.9958 0.7197 0.1701  -0.0027 -0.0408 320 THR C N   
6967  C CA  . THR C 19  ? 0.7491 0.9982 0.6909 0.1756  -0.0019 -0.0381 320 THR C CA  
6968  C C   . THR C 19  ? 0.6638 0.9181 0.6186 0.1591  -0.0050 -0.0299 320 THR C C   
6969  O O   . THR C 19  ? 0.6156 0.9132 0.5861 0.1536  -0.0035 -0.0264 320 THR C O   
6970  C CB  . THR C 19  ? 0.7931 1.0457 0.7263 0.2050  -0.0040 -0.0437 320 THR C CB  
6971  O OG1 . THR C 19  ? 0.9843 1.1807 0.8954 0.2147  -0.0081 -0.0472 320 THR C OG1 
6972  C CG2 . THR C 19  ? 0.6702 0.9555 0.6022 0.2215  0.0013  -0.0505 320 THR C CG2 
6973  N N   . LEU C 20  ? 0.6617 0.8739 0.6095 0.1499  -0.0089 -0.0270 321 LEU C N   
6974  C CA  . LEU C 20  ? 0.6373 0.8509 0.5950 0.1356  -0.0118 -0.0200 321 LEU C CA  
6975  C C   . LEU C 20  ? 0.6022 0.8442 0.5747 0.1136  -0.0081 -0.0147 321 LEU C C   
6976  O O   . LEU C 20  ? 0.4866 0.7482 0.4697 0.1040  -0.0093 -0.0101 321 LEU C O   
6977  C CB  . LEU C 20  ? 0.5551 0.7192 0.5017 0.1284  -0.0155 -0.0184 321 LEU C CB  
6978  C CG  . LEU C 20  ? 0.5525 0.7082 0.5063 0.1098  -0.0175 -0.0116 321 LEU C CG  
6979  C CD1 . LEU C 20  ? 0.5516 0.7202 0.5101 0.1157  -0.0216 -0.0091 321 LEU C CD1 
6980  C CD2 . LEU C 20  ? 0.4774 0.5876 0.4195 0.1022  -0.0193 -0.0112 321 LEU C CD2 
6981  N N   . HIS C 21  ? 0.5367 0.7813 0.5084 0.1055  -0.0036 -0.0152 322 HIS C N   
6982  C CA  . HIS C 21  ? 0.5440 0.8088 0.5255 0.0844  0.0001  -0.0095 322 HIS C CA  
6983  C C   . HIS C 21  ? 0.5182 0.8330 0.5127 0.0816  0.0023  -0.0078 322 HIS C C   
6984  O O   . HIS C 21  ? 0.6118 0.9411 0.6128 0.0616  0.0049  -0.0023 322 HIS C O   
6985  C CB  . HIS C 21  ? 0.6011 0.8627 0.5773 0.0797  0.0045  -0.0105 322 HIS C CB  
6986  C CG  . HIS C 21  ? 0.4487 0.7450 0.4261 0.0914  0.0087  -0.0152 322 HIS C CG  
6987  N ND1 . HIS C 21  ? 0.4356 0.7760 0.4236 0.0826  0.0131  -0.0123 322 HIS C ND1 
6988  C CD2 . HIS C 21  ? 0.4130 0.7074 0.3814 0.1116  0.0092  -0.0231 322 HIS C CD2 
6989  C CE1 . HIS C 21  ? 0.5101 0.8775 0.4971 0.0974  0.0164  -0.0180 322 HIS C CE1 
6990  N NE2 . HIS C 21  ? 0.5308 0.8698 0.5054 0.1160  0.0142  -0.0249 322 HIS C NE2 
6991  N N   . LEU C 22  ? 0.4518 0.7937 0.4491 0.1007  0.0015  -0.0122 323 LEU C N   
6992  C CA  . LEU C 22  ? 0.4235 0.8191 0.4346 0.0969  0.0033  -0.0105 323 LEU C CA  
6993  C C   . LEU C 22  ? 0.4608 0.8620 0.4792 0.0872  -0.0011 -0.0061 323 LEU C C   
6994  O O   . LEU C 22  ? 0.4678 0.9126 0.4977 0.0776  0.0000  -0.0038 323 LEU C O   
6995  C CB  . LEU C 22  ? 0.3910 0.8202 0.4033 0.1227  0.0043  -0.0169 323 LEU C CB  
6996  C CG  . LEU C 22  ? 0.5769 1.0117 0.5829 0.1313  0.0098  -0.0219 323 LEU C CG  
6997  C CD1 . LEU C 22  ? 0.5731 1.0013 0.5686 0.1629  0.0086  -0.0302 323 LEU C CD1 
6998  C CD2 . LEU C 22  ? 0.7145 1.2057 0.7328 0.1205  0.0157  -0.0201 323 LEU C CD2 
6999  N N   . LYS C 23  ? 0.5803 0.9396 0.5916 0.0879  -0.0060 -0.0049 324 LYS C N   
7000  C CA  . LYS C 23  ? 0.5519 0.9100 0.5678 0.0760  -0.0099 -0.0006 324 LYS C CA  
7001  C C   . LYS C 23  ? 0.6115 0.9479 0.6263 0.0500  -0.0081 0.0045  324 LYS C C   
7002  O O   . LYS C 23  ? 0.7342 1.0513 0.7475 0.0411  -0.0115 0.0072  324 LYS C O   
7003  C CB  . LYS C 23  ? 0.6449 0.9695 0.6521 0.0911  -0.0160 -0.0018 324 LYS C CB  
7004  C CG  . LYS C 23  ? 0.7797 1.1212 0.7850 0.1186  -0.0187 -0.0060 324 LYS C CG  
7005  C CD  . LYS C 23  ? 0.8689 1.2279 0.8790 0.1225  -0.0244 -0.0035 324 LYS C CD  
7006  C CE  . LYS C 23  ? 0.8739 1.2970 0.8999 0.1198  -0.0232 -0.0030 324 LYS C CE  
7007  N NZ  . LYS C 23  ? 0.8037 1.2494 0.8337 0.1294  -0.0294 -0.0015 324 LYS C NZ  
7008  N N   . SER C 24  ? 0.6236 0.9602 0.6372 0.0389  -0.0029 0.0058  325 SER C N   
7009  C CA  . SER C 24  ? 0.6678 0.9784 0.6772 0.0174  -0.0011 0.0109  325 SER C CA  
7010  C C   . SER C 24  ? 0.7336 1.0688 0.7486 -0.0034 0.0000  0.0149  325 SER C C   
7011  O O   . SER C 24  ? 0.6802 1.0589 0.7027 -0.0073 0.0025  0.0148  325 SER C O   
7012  C CB  . SER C 24  ? 0.7112 1.0124 0.7151 0.0141  0.0037  0.0116  325 SER C CB  
7013  O OG  . SER C 24  ? 0.7478 1.0318 0.7473 -0.0064 0.0061  0.0174  325 SER C OG  
7014  N N   . THR C 25  ? 0.9322 1.2400 0.9426 -0.0175 -0.0016 0.0183  326 THR C N   
7015  C CA  . THR C 25  ? 1.0186 1.3434 1.0312 -0.0378 -0.0015 0.0212  326 THR C CA  
7016  C C   . THR C 25  ? 1.0495 1.3627 1.0545 -0.0605 0.0035  0.0260  326 THR C C   
7017  O O   . THR C 25  ? 1.1420 1.4848 1.1492 -0.0773 0.0059  0.0280  326 THR C O   
7018  C CB  . THR C 25  ? 1.0099 1.3123 1.0198 -0.0393 -0.0066 0.0212  326 THR C CB  
7019  O OG1 . THR C 25  ? 1.0461 1.3014 1.0473 -0.0341 -0.0072 0.0216  326 THR C OG1 
7020  C CG2 . THR C 25  ? 0.8965 1.2231 0.9140 -0.0217 -0.0118 0.0177  326 THR C CG2 
7021  N N   . LEU C 26  ? 0.9551 1.2271 0.9501 -0.0614 0.0050  0.0284  327 LEU C N   
7022  C CA  . LEU C 26  ? 0.9319 1.1838 0.9159 -0.0812 0.0091  0.0338  327 LEU C CA  
7023  C C   . LEU C 26  ? 0.8857 1.1325 0.8649 -0.0789 0.0135  0.0363  327 LEU C C   
7024  O O   . LEU C 26  ? 0.7538 1.0027 0.7364 -0.0616 0.0131  0.0333  327 LEU C O   
7025  C CB  . LEU C 26  ? 1.0144 1.2215 0.9886 -0.0850 0.0072  0.0353  327 LEU C CB  
7026  C CG  . LEU C 26  ? 1.0316 1.2413 1.0086 -0.0882 0.0029  0.0329  327 LEU C CG  
7027  C CD1 . LEU C 26  ? 1.0019 1.1680 0.9687 -0.0900 0.0016  0.0338  327 LEU C CD1 
7028  C CD2 . LEU C 26  ? 1.0305 1.2688 1.0081 -0.1085 0.0039  0.0339  327 LEU C CD2 
7029  N N   . GLU C 27  ? 0.7878 1.0259 0.7565 -0.0976 0.0176  0.0419  328 GLU C N   
7030  C CA  . GLU C 27  ? 0.7031 0.9334 0.6643 -0.0977 0.0218  0.0457  328 GLU C CA  
7031  C C   . GLU C 27  ? 0.7386 0.9284 0.6927 -0.0860 0.0204  0.0467  328 GLU C C   
7032  O O   . GLU C 27  ? 0.5467 0.7060 0.4958 -0.0866 0.0181  0.0472  328 GLU C O   
7033  C CB  . GLU C 27  ? 0.6123 0.8384 0.5606 -0.1217 0.0264  0.0526  328 GLU C CB  
7034  C CG  . GLU C 27  ? 0.6164 0.8900 0.5712 -0.1353 0.0292  0.0525  328 GLU C CG  
7035  C CD  . GLU C 27  ? 0.7306 0.9963 0.6696 -0.1623 0.0338  0.0596  328 GLU C CD  
7036  O OE1 . GLU C 27  ? 0.8181 1.0376 0.7397 -0.1685 0.0347  0.0646  328 GLU C OE1 
7037  O OE2 . GLU C 27  ? 0.7844 1.0902 0.7274 -0.1771 0.0367  0.0602  328 GLU C OE2 
7038  N N   . THR C 28  ? 0.8009 0.9933 0.7545 -0.0755 0.0218  0.0466  329 THR C N   
7039  C CA  . THR C 28  ? 0.6874 0.8473 0.6341 -0.0665 0.0207  0.0481  329 THR C CA  
7040  C C   . THR C 28  ? 0.5401 0.6764 0.4713 -0.0774 0.0240  0.0563  329 THR C C   
7041  O O   . THR C 28  ? 0.5910 0.6980 0.5152 -0.0714 0.0228  0.0586  329 THR C O   
7042  C CB  . THR C 28  ? 0.6726 0.8446 0.6238 -0.0507 0.0202  0.0439  329 THR C CB  
7043  O OG1 . THR C 28  ? 0.7139 0.9144 0.6648 -0.0551 0.0244  0.0451  329 THR C OG1 
7044  C CG2 . THR C 28  ? 0.6086 0.7907 0.5704 -0.0367 0.0162  0.0360  329 THR C CG2 
7045  N N   . GLY C 29  ? 0.4751 0.6238 0.3999 -0.0931 0.0282  0.0609  330 GLY C N   
7046  C CA  . GLY C 29  ? 0.6675 0.7943 0.5749 -0.1028 0.0317  0.0694  330 GLY C CA  
7047  C C   . GLY C 29  ? 0.7642 0.9103 0.6696 -0.1003 0.0349  0.0717  330 GLY C C   
7048  O O   . GLY C 29  ? 0.7111 0.8497 0.6019 -0.1129 0.0388  0.0795  330 GLY C O   
7049  N N   . CYS C 30  ? 0.7094 0.8783 0.6272 -0.0849 0.0333  0.0652  331 CYS C N   
7050  C CA  . CYS C 30  ? 0.5375 0.7277 0.4538 -0.0812 0.0362  0.0658  331 CYS C CA  
7051  C C   . CYS C 30  ? 0.6233 0.8514 0.5429 -0.0936 0.0407  0.0661  331 CYS C C   
7052  O O   . CYS C 30  ? 0.6444 0.8912 0.5727 -0.1004 0.0404  0.0632  331 CYS C O   
7053  C CB  . CYS C 30  ? 0.4231 0.6237 0.3494 -0.0613 0.0330  0.0573  331 CYS C CB  
7054  S SG  . CYS C 30  ? 0.5495 0.7136 0.4729 -0.0482 0.0279  0.0564  331 CYS C SG  
7055  N N   . THR C 31  ? 0.4780 0.7203 0.3904 -0.0971 0.0449  0.0699  332 THR C N   
7056  C CA  . THR C 31  ? 0.5103 0.7968 0.4278 -0.1053 0.0495  0.0688  332 THR C CA  
7057  C C   . THR C 31  ? 0.5745 0.8830 0.4945 -0.0906 0.0511  0.0645  332 THR C C   
7058  O O   . THR C 31  ? 0.7495 1.0377 0.6666 -0.0764 0.0481  0.0624  332 THR C O   
7059  C CB  . THR C 31  ? 0.6054 0.8897 0.5080 -0.1300 0.0547  0.0789  332 THR C CB  
7060  O OG1 . THR C 31  ? 0.6089 0.8762 0.4954 -0.1304 0.0571  0.0861  332 THR C OG1 
7061  C CG2 . THR C 31  ? 0.5542 0.8039 0.4484 -0.1439 0.0529  0.0834  332 THR C CG2 
7062  N N   . GLU C 32  ? 0.5889 0.9408 0.5136 -0.0946 0.0558  0.0627  333 GLU C N   
7063  C CA  . GLU C 32  ? 0.6666 1.0377 0.5894 -0.0828 0.0583  0.0593  333 GLU C CA  
7064  C C   . GLU C 32  ? 0.6110 0.9562 0.5159 -0.0880 0.0597  0.0679  333 GLU C C   
7065  O O   . GLU C 32  ? 0.6096 0.9569 0.5111 -0.0752 0.0594  0.0646  333 GLU C O   
7066  C CB  . GLU C 32  ? 0.8565 1.2812 0.7859 -0.0880 0.0643  0.0570  333 GLU C CB  
7067  C CG  . GLU C 32  ? 1.0228 1.4794 0.9680 -0.0675 0.0631  0.0449  333 GLU C CG  
7068  C CD  . GLU C 32  ? 1.2211 1.7016 1.1802 -0.0720 0.0620  0.0425  333 GLU C CD  
7069  O OE1 . GLU C 32  ? 1.3327 1.8591 1.3031 -0.0628 0.0643  0.0359  333 GLU C OE1 
7070  O OE2 . GLU C 32  ? 1.1664 1.6213 1.1246 -0.0840 0.0588  0.0471  333 GLU C OE2 
7071  N N   . TYR C 33  ? 0.5525 0.8707 0.4440 -0.1057 0.0607  0.0787  334 TYR C N   
7072  C CA  . TYR C 33  ? 0.5759 0.8711 0.4475 -0.1119 0.0625  0.0888  334 TYR C CA  
7073  C C   . TYR C 33  ? 0.6039 0.8503 0.4660 -0.1057 0.0576  0.0935  334 TYR C C   
7074  O O   . TYR C 33  ? 0.7369 0.9662 0.5842 -0.1036 0.0577  0.1003  334 TYR C O   
7075  C CB  . TYR C 33  ? 0.6309 0.9304 0.4890 -0.1372 0.0684  0.0992  334 TYR C CB  
7076  C CG  . TYR C 33  ? 0.7238 1.0766 0.5900 -0.1442 0.0741  0.0958  334 TYR C CG  
7077  C CD1 . TYR C 33  ? 0.7490 1.1225 0.6059 -0.1462 0.0790  0.0992  334 TYR C CD1 
7078  C CD2 . TYR C 33  ? 0.6684 1.0545 0.5521 -0.1472 0.0745  0.0888  334 TYR C CD2 
7079  C CE1 . TYR C 33  ? 0.7950 1.2210 0.6597 -0.1515 0.0848  0.0957  334 TYR C CE1 
7080  C CE2 . TYR C 33  ? 0.6854 1.1257 0.5777 -0.1516 0.0798  0.0854  334 TYR C CE2 
7081  C CZ  . TYR C 33  ? 0.8112 1.2712 0.6939 -0.1538 0.0852  0.0888  334 TYR C CZ  
7082  O OH  . TYR C 33  ? 0.9875 1.5044 0.8788 -0.1576 0.0912  0.0852  334 TYR C OH  
7083  N N   . ILE C 34  ? 0.6314 0.8570 0.5008 -0.1022 0.0533  0.0903  335 ILE C N   
7084  C CA  . ILE C 34  ? 0.6571 0.8406 0.5187 -0.0949 0.0489  0.0939  335 ILE C CA  
7085  C C   . ILE C 34  ? 0.5838 0.7643 0.4619 -0.0808 0.0436  0.0841  335 ILE C C   
7086  O O   . ILE C 34  ? 0.6399 0.8379 0.5311 -0.0826 0.0433  0.0777  335 ILE C O   
7087  C CB  . ILE C 34  ? 0.7255 0.8747 0.5702 -0.1106 0.0504  0.1040  335 ILE C CB  
7088  C CG1 . ILE C 34  ? 0.8064 0.9146 0.6390 -0.1005 0.0469  0.1094  335 ILE C CG1 
7089  C CG2 . ILE C 34  ? 0.7854 0.9348 0.6393 -0.1192 0.0497  0.0997  335 ILE C CG2 
7090  C CD1 . ILE C 34  ? 0.9192 0.9901 0.7275 -0.1138 0.0495  0.1212  335 ILE C CD1 
7091  N N   . CYS C 35  ? 0.4894 0.6503 0.3666 -0.0671 0.0393  0.0830  336 CYS C N   
7092  C CA  . CYS C 35  ? 0.5092 0.6645 0.3994 -0.0546 0.0343  0.0744  336 CYS C CA  
7093  C C   . CYS C 35  ? 0.6090 0.7287 0.4929 -0.0527 0.0314  0.0791  336 CYS C C   
7094  O O   . CYS C 35  ? 0.4565 0.5592 0.3278 -0.0504 0.0312  0.0863  336 CYS C O   
7095  C CB  . CYS C 35  ? 0.4262 0.5944 0.3217 -0.0400 0.0317  0.0669  336 CYS C CB  
7096  S SG  . CYS C 35  ? 0.5325 0.6803 0.4359 -0.0276 0.0253  0.0606  336 CYS C SG  
7097  N N   . MET C 36  ? 0.5607 0.6706 0.4529 -0.0521 0.0290  0.0749  337 MET C N   
7098  C CA  . MET C 36  ? 0.4833 0.5607 0.3693 -0.0515 0.0272  0.0788  337 MET C CA  
7099  C C   . MET C 36  ? 0.5040 0.5762 0.4007 -0.0390 0.0224  0.0721  337 MET C C   
7100  O O   . MET C 36  ? 0.4805 0.5313 0.3759 -0.0384 0.0210  0.0729  337 MET C O   
7101  C CB  . MET C 36  ? 0.4519 0.5183 0.3339 -0.0657 0.0293  0.0812  337 MET C CB  
7102  C CG  . MET C 36  ? 0.6796 0.7475 0.5480 -0.0814 0.0342  0.0888  337 MET C CG  
7103  S SD  . MET C 36  ? 0.8545 0.8872 0.7068 -0.0973 0.0361  0.0946  337 MET C SD  
7104  C CE  . MET C 36  ? 0.8915 0.9388 0.7319 -0.1199 0.0419  0.1009  337 MET C CE  
7105  N N   . GLY C 37  ? 0.5905 0.6802 0.4954 -0.0297 0.0202  0.0655  338 GLY C N   
7106  C CA  . GLY C 37  ? 0.5330 0.6195 0.4471 -0.0204 0.0159  0.0583  338 GLY C CA  
7107  C C   . GLY C 37  ? 0.5270 0.5935 0.4375 -0.0149 0.0133  0.0613  338 GLY C C   
7108  O O   . GLY C 37  ? 0.5906 0.6539 0.5082 -0.0095 0.0100  0.0559  338 GLY C O   
7109  N N   . SER C 38  ? 0.5126 0.5665 0.4115 -0.0154 0.0148  0.0699  339 SER C N   
7110  C CA  . SER C 38  ? 0.5325 0.5698 0.4271 -0.0083 0.0128  0.0737  339 SER C CA  
7111  C C   . SER C 38  ? 0.5897 0.6008 0.4735 -0.0120 0.0152  0.0805  339 SER C C   
7112  O O   . SER C 38  ? 0.5936 0.5894 0.4715 -0.0043 0.0143  0.0844  339 SER C O   
7113  C CB  . SER C 38  ? 0.5131 0.5573 0.4008 -0.0016 0.0117  0.0782  339 SER C CB  
7114  O OG  . SER C 38  ? 0.5951 0.6315 0.4682 -0.0056 0.0150  0.0873  339 SER C OG  
7115  N N   . ILE C 39  ? 0.5289 0.5348 0.4085 -0.0235 0.0184  0.0820  340 ILE C N   
7116  C CA  . ILE C 39  ? 0.6706 0.6491 0.5397 -0.0291 0.0203  0.0858  340 ILE C CA  
7117  C C   . ILE C 39  ? 0.6367 0.6113 0.5163 -0.0264 0.0180  0.0791  340 ILE C C   
7118  O O   . ILE C 39  ? 0.6804 0.6736 0.5743 -0.0272 0.0161  0.0717  340 ILE C O   
7119  C CB  . ILE C 39  ? 0.6771 0.6548 0.5387 -0.0453 0.0240  0.0886  340 ILE C CB  
7120  C CG1 . ILE C 39  ? 0.6688 0.6494 0.5181 -0.0482 0.0266  0.0961  340 ILE C CG1 
7121  C CG2 . ILE C 39  ? 0.7548 0.7012 0.6030 -0.0532 0.0259  0.0916  340 ILE C CG2 
7122  C CD1 . ILE C 39  ? 0.7785 0.7266 0.6068 -0.0434 0.0277  0.1057  340 ILE C CD1 
7123  N N   . MET C 40  ? 0.5583 0.5076 0.4292 -0.0220 0.0182  0.0817  341 MET C N   
7124  C CA  . MET C 40  ? 0.6986 0.6436 0.5777 -0.0190 0.0164  0.0758  341 MET C CA  
7125  C C   . MET C 40  ? 0.7636 0.7060 0.6443 -0.0317 0.0173  0.0722  341 MET C C   
7126  O O   . MET C 40  ? 0.6346 0.5908 0.5287 -0.0320 0.0150  0.0656  341 MET C O   
7127  C CB  . MET C 40  ? 0.8029 0.7236 0.6711 -0.0095 0.0170  0.0795  341 MET C CB  
7128  C CG  . MET C 40  ? 1.0194 0.9293 0.8906 -0.0091 0.0166  0.0745  341 MET C CG  
7129  S SD  . MET C 40  ? 1.0835 1.0150 0.9735 -0.0002 0.0128  0.0676  341 MET C SD  
7130  C CE  . MET C 40  ? 1.0854 1.0242 0.9730 0.0144  0.0119  0.0726  341 MET C CE  
7131  N N   . HIS C 41  ? 0.8293 0.7538 0.6951 -0.0430 0.0205  0.0767  342 HIS C N   
7132  C CA  . HIS C 41  ? 0.7131 0.6381 0.5787 -0.0580 0.0214  0.0738  342 HIS C CA  
7133  C C   . HIS C 41  ? 0.7164 0.6556 0.5788 -0.0710 0.0238  0.0770  342 HIS C C   
7134  O O   . HIS C 41  ? 0.7554 0.6746 0.5998 -0.0831 0.0270  0.0825  342 HIS C O   
7135  C CB  . HIS C 41  ? 0.7645 0.6546 0.6129 -0.0633 0.0232  0.0754  342 HIS C CB  
7136  C CG  . HIS C 41  ? 0.9206 0.7955 0.7688 -0.0492 0.0220  0.0735  342 HIS C CG  
7137  N ND1 . HIS C 41  ? 0.9331 0.8256 0.7986 -0.0417 0.0188  0.0673  342 HIS C ND1 
7138  C CD2 . HIS C 41  ? 1.0174 0.8618 0.8492 -0.0406 0.0237  0.0772  342 HIS C CD2 
7139  C CE1 . HIS C 41  ? 0.9896 0.8663 0.8508 -0.0306 0.0189  0.0671  342 HIS C CE1 
7140  N NE2 . HIS C 41  ? 1.0444 0.8929 0.8857 -0.0285 0.0218  0.0729  342 HIS C NE2 
7141  N N   . PRO C 42  ? 0.7409 0.7137 0.6186 -0.0694 0.0226  0.0737  343 PRO C N   
7142  C CA  . PRO C 42  ? 0.7669 0.7569 0.6413 -0.0795 0.0255  0.0772  343 PRO C CA  
7143  C C   . PRO C 42  ? 0.8216 0.8225 0.6953 -0.0979 0.0273  0.0762  343 PRO C C   
7144  O O   . PRO C 42  ? 0.8761 0.8846 0.7417 -0.1105 0.0308  0.0808  343 PRO C O   
7145  C CB  . PRO C 42  ? 0.8254 0.8475 0.7162 -0.0687 0.0236  0.0724  343 PRO C CB  
7146  C CG  . PRO C 42  ? 0.7943 0.8202 0.6988 -0.0594 0.0196  0.0650  343 PRO C CG  
7147  C CD  . PRO C 42  ? 0.7235 0.7177 0.6195 -0.0574 0.0189  0.0668  343 PRO C CD  
7148  N N   . SER C 43  ? 0.9050 0.9082 0.7860 -0.1009 0.0251  0.0708  344 SER C N   
7149  C CA  . SER C 43  ? 0.8740 0.8974 0.7581 -0.1175 0.0258  0.0687  344 SER C CA  
7150  C C   . SER C 43  ? 0.8603 0.8582 0.7347 -0.1272 0.0251  0.0675  344 SER C C   
7151  O O   . SER C 43  ? 0.8140 0.7895 0.6872 -0.1167 0.0230  0.0654  344 SER C O   
7152  C CB  . SER C 43  ? 0.7277 0.7924 0.6341 -0.1099 0.0229  0.0617  344 SER C CB  
7153  O OG  . SER C 43  ? 0.6409 0.7378 0.5517 -0.1242 0.0245  0.0611  344 SER C OG  
7154  N N   . GLN C 44  ? 0.9482 0.9504 0.8144 -0.1483 0.0270  0.0687  345 GLN C N   
7155  C CA  . GLN C 44  ? 1.0154 1.0017 0.8739 -0.1605 0.0259  0.0659  345 GLN C CA  
7156  C C   . GLN C 44  ? 1.0734 1.1013 0.9471 -0.1705 0.0236  0.0607  345 GLN C C   
7157  O O   . GLN C 44  ? 1.1683 1.1895 1.0351 -0.1851 0.0227  0.0584  345 GLN C O   
7158  C CB  . GLN C 44  ? 1.0242 0.9723 0.8544 -0.1792 0.0298  0.0715  345 GLN C CB  
7159  C CG  . GLN C 44  ? 1.0988 1.0047 0.9113 -0.1678 0.0320  0.0773  345 GLN C CG  
7160  C CD  . GLN C 44  ? 1.2378 1.1079 1.0201 -0.1865 0.0364  0.0843  345 GLN C CD  
7161  O OE1 . GLN C 44  ? 1.3301 1.2059 1.1058 -0.1929 0.0393  0.0906  345 GLN C OE1 
7162  N NE2 . GLN C 44  ? 1.2096 1.0409 0.9712 -0.1960 0.0370  0.0831  345 GLN C NE2 
7163  N N   . HIS C 45  ? 1.0426 1.1137 0.9358 -0.1625 0.0227  0.0587  346 HIS C N   
7164  C CA  . HIS C 45  ? 1.0606 1.1766 0.9704 -0.1667 0.0201  0.0539  346 HIS C CA  
7165  C C   . HIS C 45  ? 1.0483 1.1601 0.9658 -0.1568 0.0150  0.0483  346 HIS C C   
7166  O O   . HIS C 45  ? 0.9073 1.0140 0.8336 -0.1362 0.0126  0.0460  346 HIS C O   
7167  C CB  . HIS C 45  ? 0.9657 1.1238 0.8930 -0.1541 0.0203  0.0524  346 HIS C CB  
7168  C CG  . HIS C 45  ? 0.9012 1.1109 0.8421 -0.1617 0.0195  0.0494  346 HIS C CG  
7169  N ND1 . HIS C 45  ? 0.8915 1.1401 0.8508 -0.1441 0.0176  0.0451  346 HIS C ND1 
7170  C CD2 . HIS C 45  ? 0.9017 1.1317 0.8395 -0.1847 0.0203  0.0499  346 HIS C CD2 
7171  C CE1 . HIS C 45  ? 0.8596 1.1532 0.8281 -0.1540 0.0172  0.0434  346 HIS C CE1 
7172  N NE2 . HIS C 45  ? 0.8770 1.1621 0.8335 -0.1797 0.0188  0.0462  346 HIS C NE2 
7173  N N   . ALA C 46  ? 1.1081 1.2220 1.0212 -0.1726 0.0135  0.0463  347 ALA C N   
7174  C CA  . ALA C 46  ? 1.0112 1.1236 0.9298 -0.1662 0.0086  0.0413  347 ALA C CA  
7175  C C   . ALA C 46  ? 0.9950 1.1569 0.9280 -0.1718 0.0053  0.0379  347 ALA C C   
7176  O O   . ALA C 46  ? 0.9396 1.1324 0.8744 -0.1872 0.0072  0.0393  347 ALA C O   
7177  C CB  . ALA C 46  ? 0.9570 1.0266 0.8556 -0.1786 0.0092  0.0412  347 ALA C CB  
7178  N N   . ARG C 47  ? 1.1302 1.3008 1.0730 -0.1591 0.0002  0.0338  348 ARG C N   
7179  C CA  . ARG C 47  ? 1.1720 1.3918 1.1296 -0.1588 -0.0038 0.0308  348 ARG C CA  
7180  C C   . ARG C 47  ? 1.1792 1.4088 1.1301 -0.1821 -0.0057 0.0293  348 ARG C C   
7181  O O   . ARG C 47  ? 1.0866 1.3643 1.0480 -0.1890 -0.0079 0.0280  348 ARG C O   
7182  C CB  . ARG C 47  ? 1.1276 1.3518 1.0966 -0.1339 -0.0088 0.0279  348 ARG C CB  
7183  C CG  . ARG C 47  ? 1.0468 1.2809 1.0257 -0.1127 -0.0078 0.0280  348 ARG C CG  
7184  C CD  . ARG C 47  ? 1.0810 1.3011 1.0639 -0.0903 -0.0119 0.0258  348 ARG C CD  
7185  N NE  . ARG C 47  ? 1.1093 1.3540 1.0991 -0.0847 -0.0175 0.0233  348 ARG C NE  
7186  C CZ  . ARG C 47  ? 1.0601 1.3471 1.0617 -0.0741 -0.0199 0.0218  348 ARG C CZ  
7187  N NH1 . ARG C 47  ? 0.9470 1.2570 0.9550 -0.0687 -0.0166 0.0219  348 ARG C NH1 
7188  N NH2 . ARG C 47  ? 1.0604 1.3678 1.0667 -0.0680 -0.0254 0.0203  348 ARG C NH2 
7189  N N   . ARG C 48  ? 1.1916 1.3782 1.1243 -0.1943 -0.0049 0.0292  349 ARG C N   
7190  C CA  . ARG C 48  ? 1.0929 1.2829 1.0149 -0.2191 -0.0063 0.0271  349 ARG C CA  
7191  C C   . ARG C 48  ? 1.0400 1.1808 0.9362 -0.2385 -0.0013 0.0293  349 ARG C C   
7192  O O   . ARG C 48  ? 1.1091 1.2048 0.9950 -0.2274 0.0013  0.0310  349 ARG C O   
7193  C CB  . ARG C 48  ? 1.0191 1.2066 0.9427 -0.2123 -0.0120 0.0229  349 ARG C CB  
7194  C CG  . ARG C 48  ? 0.9467 1.1020 0.8716 -0.1875 -0.0129 0.0226  349 ARG C CG  
7195  C CD  . ARG C 48  ? 1.0268 1.1336 0.9320 -0.1941 -0.0119 0.0209  349 ARG C CD  
7196  N NE  . ARG C 48  ? 1.1224 1.2391 1.0208 -0.2113 -0.0155 0.0171  349 ARG C NE  
7197  C CZ  . ARG C 48  ? 1.2650 1.3709 1.1462 -0.2378 -0.0135 0.0160  349 ARG C CZ  
7198  N NH1 . ARG C 48  ? 1.3578 1.4403 1.2259 -0.2495 -0.0079 0.0191  349 ARG C NH1 
7199  N NH2 . ARG C 48  ? 1.3024 1.4193 1.1774 -0.2535 -0.0174 0.0118  349 ARG C NH2 
7200  N N   . PRO C 49  ? 1.0206 1.1692 0.9049 -0.2673 0.0000  0.0293  350 PRO C N   
7201  C CA  . PRO C 49  ? 1.1510 1.2508 1.0071 -0.2871 0.0053  0.0322  350 PRO C CA  
7202  C C   . PRO C 49  ? 1.4308 1.4691 1.2646 -0.2845 0.0060  0.0302  350 PRO C C   
7203  O O   . PRO C 49  ? 1.3881 1.4149 1.2288 -0.2630 0.0035  0.0277  350 PRO C O   
7204  C CB  . PRO C 49  ? 1.0851 1.2114 0.9335 -0.3208 0.0052  0.0311  350 PRO C CB  
7205  C CG  . PRO C 49  ? 1.1045 1.3025 0.9813 -0.3159 0.0011  0.0295  350 PRO C CG  
7206  C CD  . PRO C 49  ? 1.0548 1.2653 0.9535 -0.2807 -0.0021 0.0284  350 PRO C CD  
7207  N N   . GLU C 50  ? 1.7251 1.7227 1.5299 -0.3072 0.0098  0.0314  351 GLU C N   
7208  C CA  . GLU C 50  ? 1.7710 1.7035 1.5491 -0.3046 0.0122  0.0303  351 GLU C CA  
7209  C C   . GLU C 50  ? 1.6954 1.6203 1.4729 -0.2991 0.0080  0.0233  351 GLU C C   
7210  O O   . GLU C 50  ? 1.6595 1.5668 1.4421 -0.2747 0.0075  0.0223  351 GLU C O   
7211  C CB  . GLU C 50  ? 1.8914 1.7843 1.6354 -0.3340 0.0165  0.0321  351 GLU C CB  
7212  C CG  . GLU C 50  ? 1.9444 1.8128 1.6765 -0.3331 0.0221  0.0402  351 GLU C CG  
7213  C CD  . GLU C 50  ? 1.9868 1.7811 1.6851 -0.3288 0.0262  0.0419  351 GLU C CD  
7214  O OE1 . GLU C 50  ? 2.0154 1.7770 1.6963 -0.3321 0.0253  0.0361  351 GLU C OE1 
7215  O OE2 . GLU C 50  ? 1.9668 1.7364 1.6552 -0.3210 0.0303  0.0490  351 GLU C OE2 
7216  N N   . ASP C 51  ? 1.6803 1.6193 1.4506 -0.3228 0.0052  0.0186  352 ASP C N   
7217  C CA  . ASP C 51  ? 1.5881 1.5185 1.3538 -0.3213 0.0013  0.0118  352 ASP C CA  
7218  C C   . ASP C 51  ? 1.4988 1.4932 1.2915 -0.3203 -0.0054 0.0090  352 ASP C C   
7219  O O   . ASP C 51  ? 1.3765 1.4167 1.1952 -0.3085 -0.0070 0.0123  352 ASP C O   
7220  C CB  . ASP C 51  ? 1.5509 1.4372 1.2807 -0.3491 0.0034  0.0078  352 ASP C CB  
7221  C CG  . ASP C 51  ? 1.5014 1.3165 1.2035 -0.3380 0.0084  0.0077  352 ASP C CG  
7222  O OD1 . ASP C 51  ? 1.3997 1.2027 1.1093 -0.3117 0.0080  0.0063  352 ASP C OD1 
7223  O OD2 . ASP C 51  ? 1.5033 1.2750 1.1752 -0.3558 0.0129  0.0093  352 ASP C OD2 
7224  N N   . VAL C 52  ? 1.5285 1.5252 1.3134 -0.3317 -0.0095 0.0029  353 VAL C N   
7225  C CA  . VAL C 52  ? 1.4610 1.5127 1.2692 -0.3256 -0.0166 0.0004  353 VAL C CA  
7226  C C   . VAL C 52  ? 1.4476 1.5606 1.2733 -0.3394 -0.0187 0.0026  353 VAL C C   
7227  O O   . VAL C 52  ? 1.4926 1.6122 1.3047 -0.3701 -0.0177 0.0016  353 VAL C O   
7228  C CB  . VAL C 52  ? 1.3267 1.3661 1.1190 -0.3380 -0.0203 -0.0066 353 VAL C CB  
7229  C CG1 . VAL C 52  ? 1.3527 1.3568 1.1123 -0.3713 -0.0172 -0.0099 353 VAL C CG1 
7230  C CG2 . VAL C 52  ? 1.2215 1.3240 1.0350 -0.3384 -0.0282 -0.0085 353 VAL C CG2 
7231  N N   . ALA C 53  ? 1.2555 1.4135 1.1101 -0.3169 -0.0214 0.0055  354 ALA C N   
7232  C CA  . ALA C 53  ? 1.0225 1.2386 0.8955 -0.3234 -0.0219 0.0082  354 ALA C CA  
7233  C C   . ALA C 53  ? 0.9502 1.2221 0.8312 -0.3402 -0.0282 0.0048  354 ALA C C   
7234  O O   . ALA C 53  ? 1.0316 1.3064 0.9113 -0.3375 -0.0337 0.0008  354 ALA C O   
7235  C CB  . ALA C 53  ? 0.9585 1.2001 0.8572 -0.2909 -0.0225 0.0117  354 ALA C CB  
7236  N N   . THR C 54  ? 0.8428 1.1616 0.7317 -0.3582 -0.0274 0.0065  355 THR C N   
7237  C CA  . THR C 54  ? 0.7890 1.1759 0.6916 -0.3705 -0.0335 0.0040  355 THR C CA  
7238  C C   . THR C 54  ? 0.7254 1.1583 0.6565 -0.3361 -0.0390 0.0049  355 THR C C   
7239  O O   . THR C 54  ? 0.6984 1.1078 0.6368 -0.3059 -0.0379 0.0071  355 THR C O   
7240  C CB  . THR C 54  ? 0.7868 1.2149 0.6912 -0.3983 -0.0304 0.0060  355 THR C CB  
7241  O OG1 . THR C 54  ? 0.8389 1.2854 0.7602 -0.3797 -0.0261 0.0109  355 THR C OG1 
7242  C CG2 . THR C 54  ? 0.6414 1.0178 0.5132 -0.4336 -0.0249 0.0056  355 THR C CG2 
7243  N N   . LYS C 55  ? 0.7436 1.2431 0.6896 -0.3408 -0.0453 0.0034  356 LYS C N   
7244  C CA  . LYS C 55  ? 0.6629 1.2049 0.6327 -0.3073 -0.0509 0.0044  356 LYS C CA  
7245  C C   . LYS C 55  ? 0.6117 1.1865 0.6011 -0.2882 -0.0475 0.0081  356 LYS C C   
7246  O O   . LYS C 55  ? 0.5621 1.1334 0.5631 -0.2543 -0.0486 0.0097  356 LYS C O   
7247  C CB  . LYS C 55  ? 0.6960 1.3005 0.6749 -0.3158 -0.0592 0.0019  356 LYS C CB  
7248  C CG  . LYS C 55  ? 0.7590 1.3846 0.7525 -0.2809 -0.0663 0.0026  356 LYS C CG  
7249  C CD  . LYS C 55  ? 0.8684 1.5332 0.8615 -0.2923 -0.0749 -0.0003 356 LYS C CD  
7250  C CE  . LYS C 55  ? 0.8671 1.6195 0.8836 -0.2842 -0.0800 0.0010  356 LYS C CE  
7251  N NZ  . LYS C 55  ? 0.8256 1.5901 0.8574 -0.2402 -0.0837 0.0042  356 LYS C NZ  
7252  N N   . ASP C 56  ? 0.7236 1.3307 0.7155 -0.3101 -0.0431 0.0093  357 ASP C N   
7253  C CA  . ASP C 56  ? 0.7156 1.3553 0.7249 -0.2927 -0.0392 0.0124  357 ASP C CA  
7254  C C   . ASP C 56  ? 0.6404 1.2195 0.6420 -0.2778 -0.0327 0.0151  357 ASP C C   
7255  O O   . ASP C 56  ? 0.5740 1.1712 0.5891 -0.2568 -0.0300 0.0170  357 ASP C O   
7256  C CB  . ASP C 56  ? 0.7400 1.4339 0.7538 -0.3215 -0.0357 0.0133  357 ASP C CB  
7257  C CG  . ASP C 56  ? 0.8190 1.4677 0.8079 -0.3588 -0.0293 0.0144  357 ASP C CG  
7258  O OD1 . ASP C 56  ? 0.8394 1.4153 0.8104 -0.3558 -0.0254 0.0156  357 ASP C OD1 
7259  O OD2 . ASP C 56  ? 0.7909 1.4684 0.7721 -0.3860 -0.0273 0.0144  357 ASP C OD2 
7260  N N   . GLN C 57  ? 0.6231 1.1324 0.6028 -0.2874 -0.0304 0.0148  358 GLN C N   
7261  C CA  . GLN C 57  ? 0.6763 1.1285 0.6491 -0.2702 -0.0255 0.0173  358 GLN C CA  
7262  C C   . GLN C 57  ? 0.6780 1.1103 0.6577 -0.2367 -0.0295 0.0164  358 GLN C C   
7263  O O   . GLN C 57  ? 0.7881 1.2170 0.7775 -0.2115 -0.0279 0.0181  358 GLN C O   
7264  C CB  . GLN C 57  ? 0.7663 1.1540 0.7118 -0.2930 -0.0210 0.0177  358 GLN C CB  
7265  C CG  . GLN C 57  ? 0.8676 1.2547 0.8027 -0.3187 -0.0144 0.0209  358 GLN C CG  
7266  C CD  . GLN C 57  ? 0.9327 1.2622 0.8370 -0.3466 -0.0111 0.0207  358 GLN C CD  
7267  O OE1 . GLN C 57  ? 0.9162 1.1932 0.8063 -0.3399 -0.0119 0.0187  358 GLN C OE1 
7268  N NE2 . GLN C 57  ? 0.9011 1.2395 0.7933 -0.3783 -0.0072 0.0226  358 GLN C NE2 
7269  N N   . LEU C 58  ? 0.7503 1.1693 0.7237 -0.2372 -0.0348 0.0137  359 LEU C N   
7270  C CA  . LEU C 58  ? 0.7299 1.1206 0.7052 -0.2090 -0.0377 0.0135  359 LEU C CA  
7271  C C   . LEU C 58  ? 0.6813 1.1186 0.6760 -0.1828 -0.0435 0.0137  359 LEU C C   
7272  O O   . LEU C 58  ? 0.5159 0.9345 0.5148 -0.1558 -0.0441 0.0148  359 LEU C O   
7273  C CB  . LEU C 58  ? 0.6248 0.9781 0.5835 -0.2186 -0.0403 0.0108  359 LEU C CB  
7274  C CG  . LEU C 58  ? 0.6295 0.9454 0.5871 -0.1923 -0.0416 0.0112  359 LEU C CG  
7275  C CD1 . LEU C 58  ? 0.6418 0.9061 0.5906 -0.1875 -0.0348 0.0131  359 LEU C CD1 
7276  C CD2 . LEU C 58  ? 0.6037 0.9034 0.5506 -0.1960 -0.0463 0.0084  359 LEU C CD2 
7277  N N   . PHE C 59  ? 0.5991 1.0963 0.6044 -0.1896 -0.0481 0.0127  360 PHE C N   
7278  C CA  . PHE C 59  ? 0.5374 1.0755 0.5585 -0.1615 -0.0541 0.0131  360 PHE C CA  
7279  C C   . PHE C 59  ? 0.5286 1.0774 0.5617 -0.1353 -0.0511 0.0148  360 PHE C C   
7280  O O   . PHE C 59  ? 0.4816 1.0207 0.5178 -0.1062 -0.0543 0.0155  360 PHE C O   
7281  C CB  . PHE C 59  ? 0.4997 1.1074 0.5313 -0.1718 -0.0597 0.0120  360 PHE C CB  
7282  C CG  . PHE C 59  ? 0.6147 1.2626 0.6604 -0.1397 -0.0662 0.0129  360 PHE C CG  
7283  C CD1 . PHE C 59  ? 0.6974 1.3277 0.7375 -0.1247 -0.0728 0.0133  360 PHE C CD1 
7284  C CD2 . PHE C 59  ? 0.6864 1.3863 0.7488 -0.1229 -0.0655 0.0137  360 PHE C CD2 
7285  C CE1 . PHE C 59  ? 0.6980 1.3596 0.7477 -0.0940 -0.0789 0.0149  360 PHE C CE1 
7286  C CE2 . PHE C 59  ? 0.6844 1.4165 0.7568 -0.0906 -0.0714 0.0146  360 PHE C CE2 
7287  C CZ  . PHE C 59  ? 0.6992 1.4104 0.7645 -0.0761 -0.0783 0.0155  360 PHE C CZ  
7288  N N   . PRO C 60  ? 0.5722 1.1396 0.6105 -0.1439 -0.0451 0.0155  361 PRO C N   
7289  C CA  . PRO C 60  ? 0.3913 0.9727 0.4406 -0.1172 -0.0426 0.0162  361 PRO C CA  
7290  C C   . PRO C 60  ? 0.3928 0.9146 0.4342 -0.0973 -0.0408 0.0169  361 PRO C C   
7291  O O   . PRO C 60  ? 0.3853 0.9105 0.4324 -0.0684 -0.0423 0.0166  361 PRO C O   
7292  C CB  . PRO C 60  ? 0.5000 1.1058 0.5524 -0.1370 -0.0358 0.0170  361 PRO C CB  
7293  C CG  . PRO C 60  ? 0.6153 1.2490 0.6647 -0.1705 -0.0373 0.0164  361 PRO C CG  
7294  C CD  . PRO C 60  ? 0.6131 1.1962 0.6473 -0.1781 -0.0407 0.0156  361 PRO C CD  
7295  N N   . LEU C 61  ? 0.4878 0.9551 0.5148 -0.1123 -0.0376 0.0175  362 LEU C N   
7296  C CA  . LEU C 61  ? 0.5329 0.9449 0.5519 -0.0959 -0.0366 0.0181  362 LEU C CA  
7297  C C   . LEU C 61  ? 0.5938 0.9991 0.6126 -0.0755 -0.0433 0.0176  362 LEU C C   
7298  O O   . LEU C 61  ? 0.4695 0.8640 0.4903 -0.0505 -0.0443 0.0178  362 LEU C O   
7299  C CB  . LEU C 61  ? 0.5776 0.9389 0.5810 -0.1162 -0.0328 0.0187  362 LEU C CB  
7300  C CG  . LEU C 61  ? 0.5990 0.9558 0.5963 -0.1397 -0.0264 0.0201  362 LEU C CG  
7301  C CD1 . LEU C 61  ? 0.6097 0.9109 0.5885 -0.1548 -0.0236 0.0207  362 LEU C CD1 
7302  C CD2 . LEU C 61  ? 0.5786 0.9383 0.5818 -0.1273 -0.0218 0.0217  362 LEU C CD2 
7303  N N   . ALA C 62  ? 0.6549 1.0649 0.6694 -0.0868 -0.0479 0.0170  363 ALA C N   
7304  C CA  . ALA C 62  ? 0.5979 1.0019 0.6103 -0.0694 -0.0545 0.0173  363 ALA C CA  
7305  C C   . ALA C 62  ? 0.5572 0.9990 0.5806 -0.0425 -0.0585 0.0179  363 ALA C C   
7306  O O   . ALA C 62  ? 0.5518 0.9717 0.5712 -0.0192 -0.0612 0.0189  363 ALA C O   
7307  C CB  . ALA C 62  ? 0.6286 1.0445 0.6359 -0.0876 -0.0590 0.0163  363 ALA C CB  
7308  N N   . LYS C 63  ? 0.4795 0.9780 0.5155 -0.0451 -0.0587 0.0172  364 LYS C N   
7309  C CA  . LYS C 63  ? 0.5619 1.0991 0.6079 -0.0170 -0.0620 0.0174  364 LYS C CA  
7310  C C   . LYS C 63  ? 0.5478 1.0557 0.5917 0.0054  -0.0582 0.0171  364 LYS C C   
7311  O O   . LYS C 63  ? 0.5894 1.0937 0.6315 0.0335  -0.0617 0.0175  364 LYS C O   
7312  C CB  . LYS C 63  ? 0.6299 1.2372 0.6907 -0.0251 -0.0617 0.0164  364 LYS C CB  
7313  C CG  . LYS C 63  ? 0.6845 1.3359 0.7556 0.0070  -0.0649 0.0163  364 LYS C CG  
7314  C CD  . LYS C 63  ? 0.6985 1.4290 0.7853 -0.0002 -0.0663 0.0156  364 LYS C CD  
7315  C CE  . LYS C 63  ? 0.6430 1.4145 0.7386 0.0364  -0.0694 0.0153  364 LYS C CE  
7316  N NZ  . LYS C 63  ? 0.4918 1.2288 0.5828 0.0593  -0.0643 0.0140  364 LYS C NZ  
7317  N N   . GLU C 64  ? 0.3804 0.8653 0.4225 -0.0068 -0.0511 0.0166  365 GLU C N   
7318  C CA  . GLU C 64  ? 0.4918 0.9490 0.5310 0.0121  -0.0474 0.0158  365 GLU C CA  
7319  C C   . GLU C 64  ? 0.5085 0.9115 0.5350 0.0261  -0.0500 0.0166  365 GLU C C   
7320  O O   . GLU C 64  ? 0.4575 0.8492 0.4804 0.0510  -0.0514 0.0159  365 GLU C O   
7321  C CB  . GLU C 64  ? 0.6736 1.1161 0.7120 -0.0061 -0.0398 0.0157  365 GLU C CB  
7322  C CG  . GLU C 64  ? 0.7933 1.2017 0.8266 0.0088  -0.0360 0.0148  365 GLU C CG  
7323  C CD  . GLU C 64  ? 1.0495 1.4398 1.0799 -0.0108 -0.0292 0.0158  365 GLU C CD  
7324  O OE1 . GLU C 64  ? 1.1260 1.5234 1.1588 -0.0043 -0.0248 0.0148  365 GLU C OE1 
7325  O OE2 . GLU C 64  ? 1.0727 1.4412 1.0970 -0.0322 -0.0283 0.0175  365 GLU C OE2 
7326  N N   . PHE C 65  ? 0.6097 0.9780 0.6276 0.0102  -0.0505 0.0178  366 PHE C N   
7327  C CA  . PHE C 65  ? 0.6012 0.9191 0.6072 0.0206  -0.0519 0.0188  366 PHE C CA  
7328  C C   . PHE C 65  ? 0.6768 0.9989 0.6786 0.0408  -0.0590 0.0201  366 PHE C C   
7329  O O   . PHE C 65  ? 0.7357 1.0291 0.7289 0.0599  -0.0601 0.0204  366 PHE C O   
7330  C CB  . PHE C 65  ? 0.5641 0.8473 0.5619 -0.0003 -0.0503 0.0196  366 PHE C CB  
7331  C CG  . PHE C 65  ? 0.5751 0.8154 0.5614 0.0086  -0.0523 0.0208  366 PHE C CG  
7332  C CD1 . PHE C 65  ? 0.5082 0.7162 0.4892 0.0199  -0.0498 0.0206  366 PHE C CD1 
7333  C CD2 . PHE C 65  ? 0.5580 0.7919 0.5379 0.0049  -0.0568 0.0220  366 PHE C CD2 
7334  C CE1 . PHE C 65  ? 0.5122 0.6824 0.4819 0.0260  -0.0514 0.0219  366 PHE C CE1 
7335  C CE2 . PHE C 65  ? 0.4108 0.6066 0.3793 0.0121  -0.0583 0.0236  366 PHE C CE2 
7336  C CZ  . PHE C 65  ? 0.5390 0.7032 0.5025 0.0221  -0.0555 0.0236  366 PHE C CZ  
7337  N N   . ILE C 66  ? 0.5690 0.9243 0.5747 0.0360  -0.0639 0.0210  367 ILE C N   
7338  C CA  . ILE C 66  ? 0.5557 0.9201 0.5572 0.0569  -0.0712 0.0230  367 ILE C CA  
7339  C C   . ILE C 66  ? 0.6253 1.0076 0.6296 0.0850  -0.0719 0.0223  367 ILE C C   
7340  O O   . ILE C 66  ? 0.5959 0.9525 0.5889 0.1076  -0.0751 0.0237  367 ILE C O   
7341  C CB  . ILE C 66  ? 0.6136 1.0217 0.6211 0.0465  -0.0765 0.0238  367 ILE C CB  
7342  C CG1 . ILE C 66  ? 0.4320 0.8236 0.4353 0.0164  -0.0749 0.0231  367 ILE C CG1 
7343  C CG2 . ILE C 66  ? 0.7073 1.1213 0.7083 0.0691  -0.0845 0.0269  367 ILE C CG2 
7344  C CD1 . ILE C 66  ? 0.4078 0.7457 0.3964 0.0151  -0.0752 0.0246  367 ILE C CD1 
7345  N N   . ASP C 67  ? 0.6661 1.0921 0.6840 0.0837  -0.0687 0.0200  368 ASP C N   
7346  C CA  . ASP C 67  ? 0.5668 1.0123 0.5876 0.1104  -0.0681 0.0182  368 ASP C CA  
7347  C C   . ASP C 67  ? 0.5142 0.9057 0.5221 0.1235  -0.0649 0.0169  368 ASP C C   
7348  O O   . ASP C 67  ? 0.5562 0.9353 0.5547 0.1507  -0.0674 0.0166  368 ASP C O   
7349  C CB  . ASP C 67  ? 0.4950 0.9923 0.5319 0.1013  -0.0634 0.0157  368 ASP C CB  
7350  C CG  . ASP C 67  ? 0.5616 1.1261 0.6116 0.0995  -0.0676 0.0163  368 ASP C CG  
7351  O OD1 . ASP C 67  ? 0.6886 1.2597 0.7356 0.1031  -0.0746 0.0188  368 ASP C OD1 
7352  O OD2 . ASP C 67  ? 0.5808 1.1940 0.6441 0.0941  -0.0640 0.0145  368 ASP C OD2 
7353  N N   . GLN C 68  ? 0.4045 0.7625 0.4101 0.1043  -0.0595 0.0162  369 GLN C N   
7354  C CA  . GLN C 68  ? 0.4644 0.7718 0.4574 0.1131  -0.0569 0.0149  369 GLN C CA  
7355  C C   . GLN C 68  ? 0.5359 0.8007 0.5124 0.1237  -0.0617 0.0175  369 GLN C C   
7356  O O   . GLN C 68  ? 0.5115 0.7475 0.4751 0.1432  -0.0625 0.0165  369 GLN C O   
7357  C CB  . GLN C 68  ? 0.6570 0.9408 0.6511 0.0897  -0.0509 0.0145  369 GLN C CB  
7358  C CG  . GLN C 68  ? 0.7247 0.9594 0.7066 0.0952  -0.0484 0.0132  369 GLN C CG  
7359  C CD  . GLN C 68  ? 0.7417 0.9584 0.7256 0.0735  -0.0430 0.0133  369 GLN C CD  
7360  O OE1 . GLN C 68  ? 0.8004 1.0429 0.7942 0.0606  -0.0392 0.0130  369 GLN C OE1 
7361  N NE2 . GLN C 68  ? 0.6678 0.8409 0.6414 0.0690  -0.0428 0.0142  369 GLN C NE2 
7362  N N   . TYR C 69  ? 0.7208 0.9797 0.6956 0.1101  -0.0649 0.0206  370 TYR C N   
7363  C CA  . TYR C 69  ? 0.6345 0.8512 0.5926 0.1161  -0.0688 0.0236  370 TYR C CA  
7364  C C   . TYR C 69  ? 0.6026 0.8253 0.5518 0.1434  -0.0751 0.0256  370 TYR C C   
7365  O O   . TYR C 69  ? 0.5656 0.7461 0.4966 0.1568  -0.0770 0.0271  370 TYR C O   
7366  C CB  . TYR C 69  ? 0.5628 0.7749 0.5209 0.0953  -0.0704 0.0261  370 TYR C CB  
7367  C CG  . TYR C 69  ? 0.6218 0.8014 0.5632 0.1036  -0.0753 0.0300  370 TYR C CG  
7368  C CD1 . TYR C 69  ? 0.6756 0.8050 0.6027 0.1036  -0.0734 0.0307  370 TYR C CD1 
7369  C CD2 . TYR C 69  ? 0.7910 0.9919 0.7302 0.1117  -0.0820 0.0331  370 TYR C CD2 
7370  C CE1 . TYR C 69  ? 0.6915 0.7909 0.6016 0.1101  -0.0776 0.0348  370 TYR C CE1 
7371  C CE2 . TYR C 69  ? 0.8274 0.9975 0.7493 0.1196  -0.0865 0.0374  370 TYR C CE2 
7372  C CZ  . TYR C 69  ? 0.7498 0.8685 0.6569 0.1183  -0.0840 0.0384  370 TYR C CZ  
7373  O OH  . TYR C 69  ? 0.8395 0.9281 0.7280 0.1245  -0.0883 0.0432  370 TYR C OH  
7374  N N   . TYR C 70  ? 0.5216 0.7959 0.4816 0.1516  -0.0787 0.0260  371 TYR C N   
7375  C CA  . TYR C 70  ? 0.5104 0.7922 0.4612 0.1809  -0.0848 0.0282  371 TYR C CA  
7376  C C   . TYR C 70  ? 0.6169 0.8924 0.5624 0.2052  -0.0824 0.0248  371 TYR C C   
7377  O O   . TYR C 70  ? 0.6558 0.9045 0.5831 0.2301  -0.0860 0.0263  371 TYR C O   
7378  C CB  . TYR C 70  ? 0.6248 0.9675 0.5888 0.1831  -0.0900 0.0299  371 TYR C CB  
7379  C CG  . TYR C 70  ? 0.6821 1.0165 0.6401 0.1709  -0.0953 0.0343  371 TYR C CG  
7380  C CD1 . TYR C 70  ? 0.6508 0.9958 0.6181 0.1401  -0.0935 0.0336  371 TYR C CD1 
7381  C CD2 . TYR C 70  ? 0.7170 1.0278 0.6571 0.1900  -0.1017 0.0392  371 TYR C CD2 
7382  C CE1 . TYR C 70  ? 0.5979 0.9335 0.5581 0.1290  -0.0979 0.0368  371 TYR C CE1 
7383  C CE2 . TYR C 70  ? 0.7190 1.0219 0.6526 0.1784  -0.1063 0.0433  371 TYR C CE2 
7384  C CZ  . TYR C 70  ? 0.7187 1.0349 0.6628 0.1480  -0.1042 0.0417  371 TYR C CZ  
7385  O OH  . TYR C 70  ? 0.8374 1.1453 0.7736 0.1369  -0.1084 0.0450  371 TYR C OH  
7386  N N   . SER C 71  ? 0.7226 1.0178 0.6809 0.1980  -0.0762 0.0201  372 SER C N   
7387  C CA  . SER C 71  ? 0.7457 1.0280 0.6966 0.2188  -0.0730 0.0159  372 SER C CA  
7388  C C   . SER C 71  ? 0.6091 0.8221 0.5381 0.2197  -0.0718 0.0156  372 SER C C   
7389  O O   . SER C 71  ? 0.7445 0.9294 0.6553 0.2439  -0.0732 0.0142  372 SER C O   
7390  C CB  . SER C 71  ? 0.9025 1.2190 0.8708 0.2075  -0.0662 0.0114  372 SER C CB  
7391  O OG  . SER C 71  ? 1.0093 1.3930 0.9959 0.2091  -0.0672 0.0114  372 SER C OG  
7392  N N   . SER C 72  ? 0.5163 0.7008 0.4454 0.1938  -0.0693 0.0167  373 SER C N   
7393  C CA  . SER C 72  ? 0.5874 0.7111 0.4970 0.1916  -0.0681 0.0165  373 SER C CA  
7394  C C   . SER C 72  ? 0.7364 0.8242 0.6228 0.2092  -0.0740 0.0203  373 SER C C   
7395  O O   . SER C 72  ? 0.7028 0.7447 0.5681 0.2191  -0.0736 0.0189  373 SER C O   
7396  C CB  . SER C 72  ? 0.4822 0.5884 0.3967 0.1621  -0.0652 0.0180  373 SER C CB  
7397  O OG  . SER C 72  ? 0.9240 1.0132 0.8304 0.1567  -0.0695 0.0230  373 SER C OG  
7398  N N   . ILE C 73  ? 0.9136 1.0204 0.8015 0.2126  -0.0795 0.0252  374 ILE C N   
7399  C CA  . ILE C 73  ? 0.8672 0.9389 0.7318 0.2270  -0.0855 0.0304  374 ILE C CA  
7400  C C   . ILE C 73  ? 0.8209 0.9087 0.6771 0.2611  -0.0902 0.0310  374 ILE C C   
7401  O O   . ILE C 73  ? 0.9787 1.0535 0.8194 0.2751  -0.0963 0.0365  374 ILE C O   
7402  C CB  . ILE C 73  ? 0.7868 0.8631 0.6540 0.2104  -0.0890 0.0360  374 ILE C CB  
7403  C CG1 . ILE C 73  ? 0.8064 0.9448 0.6924 0.2135  -0.0928 0.0372  374 ILE C CG1 
7404  C CG2 . ILE C 73  ? 0.7715 0.8334 0.6467 0.1795  -0.0838 0.0348  374 ILE C CG2 
7405  C CD1 . ILE C 73  ? 0.5362 0.6835 0.4243 0.1976  -0.0967 0.0419  374 ILE C CD1 
7406  N N   . LYS C 74  ? 0.8206 0.9364 0.6854 0.2759  -0.0873 0.0256  375 LYS C N   
7407  C CA  . LYS C 74  ? 0.9562 1.0851 0.8113 0.3120  -0.0907 0.0249  375 LYS C CA  
7408  C C   . LYS C 74  ? 0.9187 1.0987 0.7841 0.3240  -0.0972 0.0298  375 LYS C C   
7409  O O   . LYS C 74  ? 0.9466 1.1273 0.7977 0.3554  -0.1022 0.0321  375 LYS C O   
7410  C CB  . LYS C 74  ? 1.0634 1.1237 0.8827 0.3317  -0.0929 0.0261  375 LYS C CB  
7411  C CG  . LYS C 74  ? 1.0433 1.0547 0.8498 0.3223  -0.0869 0.0204  375 LYS C CG  
7412  C CD  . LYS C 74  ? 1.0334 1.0620 0.8419 0.3425  -0.0829 0.0126  375 LYS C CD  
7413  C CE  . LYS C 74  ? 0.9082 0.9004 0.7100 0.3274  -0.0767 0.0063  375 LYS C CE  
7414  N NZ  . LYS C 74  ? 0.8329 0.8482 0.6603 0.2928  -0.0723 0.0060  375 LYS C NZ  
7415  N N   . ARG C 75  ? 0.8308 1.0530 0.7192 0.2994  -0.0974 0.0314  376 ARG C N   
7416  C CA  . ARG C 75  ? 0.7950 1.0787 0.6979 0.3070  -0.1030 0.0344  376 ARG C CA  
7417  C C   . ARG C 75  ? 0.9081 1.2575 0.8379 0.3030  -0.0988 0.0292  376 ARG C C   
7418  O O   . ARG C 75  ? 1.0067 1.3622 0.9359 0.3216  -0.0951 0.0244  376 ARG C O   
7419  C CB  . ARG C 75  ? 0.6648 0.9515 0.5722 0.2817  -0.1065 0.0393  376 ARG C CB  
7420  C CG  . ARG C 75  ? 0.7602 0.9857 0.6403 0.2857  -0.1107 0.0452  376 ARG C CG  
7421  C CD  . ARG C 75  ? 1.0057 1.2384 0.8705 0.3196  -0.1188 0.0506  376 ARG C CD  
7422  N NE  . ARG C 75  ? 1.1670 1.3330 0.9996 0.3295  -0.1222 0.0563  376 ARG C NE  
7423  C CZ  . ARG C 75  ? 1.2699 1.3830 1.0776 0.3491  -0.1208 0.0554  376 ARG C CZ  
7424  N NH1 . ARG C 75  ? 1.2357 1.2878 1.0124 0.3551  -0.1240 0.0613  376 ARG C NH1 
7425  N NH2 . ARG C 75  ? 1.4073 1.5271 1.2196 0.3616  -0.1160 0.0486  376 ARG C NH2 
7426  N N   . PHE C 76  ? 0.8503 1.2462 0.8018 0.2772  -0.0989 0.0298  377 PHE C N   
7427  C CA  . PHE C 76  ? 0.8580 1.3198 0.8351 0.2665  -0.0951 0.0258  377 PHE C CA  
7428  C C   . PHE C 76  ? 0.8828 1.4117 0.8700 0.2893  -0.1007 0.0272  377 PHE C C   
7429  O O   . PHE C 76  ? 0.8677 1.3995 0.8456 0.3247  -0.1026 0.0267  377 PHE C O   
7430  C CB  . PHE C 76  ? 0.8652 1.3204 0.8457 0.2687  -0.0869 0.0198  377 PHE C CB  
7431  C CG  . PHE C 76  ? 0.7859 1.3102 0.7910 0.2584  -0.0828 0.0164  377 PHE C CG  
7432  C CD1 . PHE C 76  ? 0.7266 1.2617 0.7455 0.2223  -0.0781 0.0155  377 PHE C CD1 
7433  C CD2 . PHE C 76  ? 0.7498 1.3286 0.7630 0.2849  -0.0835 0.0144  377 PHE C CD2 
7434  C CE1 . PHE C 76  ? 0.6571 1.2538 0.6963 0.2103  -0.0741 0.0131  377 PHE C CE1 
7435  C CE2 . PHE C 76  ? 0.7188 1.3648 0.7547 0.2734  -0.0794 0.0116  377 PHE C CE2 
7436  C CZ  . PHE C 76  ? 0.6823 1.3361 0.7305 0.2349  -0.0747 0.0112  377 PHE C CZ  
7437  N N   . GLY C 77  ? 0.8299 1.4142 0.8354 0.2691  -0.1032 0.0285  378 GLY C N   
7438  C CA  . GLY C 77  ? 0.8160 1.4667 0.8310 0.2872  -0.1099 0.0307  378 GLY C CA  
7439  C C   . GLY C 77  ? 0.7940 1.4259 0.7926 0.3038  -0.1191 0.0371  378 GLY C C   
7440  O O   . GLY C 77  ? 0.9361 1.6096 0.9393 0.3120  -0.1211 0.0380  378 GLY C O   
7441  N N   . SER C 78  ? 0.7764 1.3331 0.7530 0.3009  -0.1196 0.0398  379 SER C N   
7442  C CA  . SER C 78  ? 0.5565 1.0861 0.5138 0.3146  -0.1278 0.0466  379 SER C CA  
7443  C C   . SER C 78  ? 0.7033 1.2737 0.6719 0.2913  -0.1332 0.0495  379 SER C C   
7444  O O   . SER C 78  ? 0.6892 1.2920 0.6766 0.2597  -0.1298 0.0459  379 SER C O   
7445  C CB  . SER C 78  ? 0.5691 1.0113 0.5022 0.3084  -0.1255 0.0484  379 SER C CB  
7446  O OG  . SER C 78  ? 0.5437 0.9692 0.4836 0.2696  -0.1217 0.0472  379 SER C OG  
7447  N N   . LYS C 79  ? 0.6563 1.2206 0.6108 0.3060  -0.1412 0.0557  380 LYS C N   
7448  C CA  . LYS C 79  ? 0.6208 1.2186 0.5830 0.2832  -0.1462 0.0579  380 LYS C CA  
7449  C C   . LYS C 79  ? 0.6191 1.1821 0.5811 0.2447  -0.1425 0.0562  380 LYS C C   
7450  O O   . LYS C 79  ? 0.6748 1.2752 0.6520 0.2152  -0.1421 0.0535  380 LYS C O   
7451  C CB  . LYS C 79  ? 0.6758 1.2564 0.6195 0.3023  -0.1522 0.0643  380 LYS C CB  
7452  C CG  . LYS C 79  ? 0.7743 1.4040 0.7283 0.2847  -0.1568 0.0655  380 LYS C CG  
7453  C CD  . LYS C 79  ? 0.8528 1.4974 0.7986 0.3113  -0.1602 0.0694  380 LYS C CD  
7454  C CE  . LYS C 79  ? 0.8996 1.6002 0.8615 0.3280  -0.1552 0.0647  380 LYS C CE  
7455  N NZ  . LYS C 79  ? 0.8216 1.5929 0.8107 0.3002  -0.1523 0.0594  380 LYS C NZ  
7456  N N   . ALA C 80  ? 0.5514 1.0401 0.4956 0.2425  -0.1381 0.0568  381 ALA C N   
7457  C CA  . ALA C 80  ? 0.6869 1.1390 0.6299 0.2076  -0.1331 0.0548  381 ALA C CA  
7458  C C   . ALA C 80  ? 0.7496 1.2209 0.7123 0.1825  -0.1250 0.0479  381 ALA C C   
7459  O O   . ALA C 80  ? 0.7236 1.1964 0.6922 0.1512  -0.1226 0.0456  381 ALA C O   
7460  C CB  . ALA C 80  ? 0.7648 1.1384 0.6847 0.2124  -0.1304 0.0572  381 ALA C CB  
7461  N N   . HIS C 81  ? 0.8280 1.3118 0.7988 0.1964  -0.1206 0.0446  382 HIS C N   
7462  C CA  . HIS C 81  ? 0.7362 1.2389 0.7243 0.1744  -0.1128 0.0389  382 HIS C CA  
7463  C C   . HIS C 81  ? 0.7353 1.3086 0.7430 0.1558  -0.1147 0.0372  382 HIS C C   
7464  O O   . HIS C 81  ? 0.6847 1.2610 0.6997 0.1235  -0.1105 0.0342  382 HIS C O   
7465  C CB  . HIS C 81  ? 0.7379 1.2401 0.7282 0.1966  -0.1082 0.0360  382 HIS C CB  
7466  C CG  . HIS C 81  ? 0.8262 1.3460 0.8323 0.1764  -0.1000 0.0308  382 HIS C CG  
7467  N ND1 . HIS C 81  ? 0.8699 1.3972 0.8802 0.1922  -0.0951 0.0274  382 HIS C ND1 
7468  C CD2 . HIS C 81  ? 0.8410 1.3694 0.8572 0.1421  -0.0958 0.0287  382 HIS C CD2 
7469  C CE1 . HIS C 81  ? 0.8518 1.3936 0.8750 0.1680  -0.0883 0.0239  382 HIS C CE1 
7470  N NE2 . HIS C 81  ? 0.8475 1.3886 0.8737 0.1375  -0.0886 0.0248  382 HIS C NE2 
7471  N N   . MET C 82  ? 0.7695 1.4001 0.7843 0.1757  -0.1212 0.0390  383 MET C N   
7472  C CA  . MET C 82  ? 0.6775 1.3810 0.7110 0.1570  -0.1234 0.0372  383 MET C CA  
7473  C C   . MET C 82  ? 0.6520 1.3506 0.6811 0.1280  -0.1272 0.0381  383 MET C C   
7474  O O   . MET C 82  ? 0.6370 1.3638 0.6764 0.0960  -0.1249 0.0347  383 MET C O   
7475  C CB  . MET C 82  ? 0.6520 1.4205 0.6937 0.1869  -0.1302 0.0393  383 MET C CB  
7476  C CG  . MET C 82  ? 0.5671 1.3498 0.6151 0.2111  -0.1235 0.0363  383 MET C CG  
7477  S SD  . MET C 82  ? 0.7247 1.5117 0.7870 0.1836  -0.1141 0.0307  383 MET C SD  
7478  C CE  . MET C 82  ? 0.8551 1.6717 0.9240 0.2168  -0.1081 0.0274  383 MET C CE  
7479  N N   . GLU C 83  ? 0.6191 1.2805 0.6308 0.1382  -0.1328 0.0426  384 GLU C N   
7480  C CA  . GLU C 83  ? 0.5629 1.2124 0.5674 0.1117  -0.1357 0.0429  384 GLU C CA  
7481  C C   . GLU C 83  ? 0.5461 1.1523 0.5487 0.0795  -0.1272 0.0386  384 GLU C C   
7482  O O   . GLU C 83  ? 0.5699 1.1898 0.5751 0.0489  -0.1268 0.0356  384 GLU C O   
7483  C CB  . GLU C 83  ? 0.6286 1.2376 0.6125 0.1298  -0.1418 0.0489  384 GLU C CB  
7484  C CG  . GLU C 83  ? 0.6436 1.3001 0.6265 0.1394  -0.1526 0.0530  384 GLU C CG  
7485  C CD  . GLU C 83  ? 0.7178 1.3550 0.6847 0.1784  -0.1589 0.0603  384 GLU C CD  
7486  O OE1 . GLU C 83  ? 0.6662 1.2404 0.6181 0.1917  -0.1550 0.0621  384 GLU C OE1 
7487  O OE2 . GLU C 83  ? 0.8480 1.5238 0.8161 0.1930  -0.1649 0.0633  384 GLU C OE2 
7488  N N   . ARG C 84  ? 0.5130 1.0670 0.5098 0.0864  -0.1204 0.0380  385 ARG C N   
7489  C CA  . ARG C 84  ? 0.5466 1.0567 0.5401 0.0599  -0.1125 0.0346  385 ARG C CA  
7490  C C   . ARG C 84  ? 0.6782 1.2230 0.6866 0.0349  -0.1073 0.0300  385 ARG C C   
7491  O O   . ARG C 84  ? 0.7386 1.2687 0.7440 0.0056  -0.1041 0.0272  385 ARG C O   
7492  C CB  . ARG C 84  ? 0.4495 0.9035 0.4345 0.0745  -0.1070 0.0353  385 ARG C CB  
7493  C CG  . ARG C 84  ? 0.4526 0.8593 0.4325 0.0511  -0.0997 0.0327  385 ARG C CG  
7494  C CD  . ARG C 84  ? 0.5393 0.9081 0.5039 0.0424  -0.1017 0.0346  385 ARG C CD  
7495  N NE  . ARG C 84  ? 0.7023 1.0289 0.6625 0.0225  -0.0943 0.0319  385 ARG C NE  
7496  C CZ  . ARG C 84  ? 0.7151 1.0406 0.6743 -0.0038 -0.0920 0.0288  385 ARG C CZ  
7497  N NH1 . ARG C 84  ? 0.6572 1.0211 0.6192 -0.0162 -0.0967 0.0276  385 ARG C NH1 
7498  N NH2 . ARG C 84  ? 0.5285 0.8139 0.4825 -0.0175 -0.0851 0.0267  385 ARG C NH2 
7499  N N   . LEU C 85  ? 0.6730 1.2624 0.6958 0.0462  -0.1062 0.0290  386 LEU C N   
7500  C CA  . LEU C 85  ? 0.5393 1.1674 0.5755 0.0214  -0.1016 0.0253  386 LEU C CA  
7501  C C   . LEU C 85  ? 0.5420 1.2071 0.5802 -0.0054 -0.1061 0.0240  386 LEU C C   
7502  O O   . LEU C 85  ? 0.5192 1.1738 0.5550 -0.0374 -0.1018 0.0210  386 LEU C O   
7503  C CB  . LEU C 85  ? 0.4549 1.1353 0.5064 0.0406  -0.1008 0.0249  386 LEU C CB  
7504  C CG  . LEU C 85  ? 0.4857 1.1429 0.5397 0.0482  -0.0925 0.0232  386 LEU C CG  
7505  C CD1 . LEU C 85  ? 0.5187 1.1003 0.5569 0.0581  -0.0900 0.0243  386 LEU C CD1 
7506  C CD2 . LEU C 85  ? 0.4776 1.1814 0.5423 0.0777  -0.0935 0.0231  386 LEU C CD2 
7507  N N   . GLU C 86  ? 0.5270 1.2335 0.5673 0.0074  -0.1150 0.0263  387 GLU C N   
7508  C CA  . GLU C 86  ? 0.6410 1.3858 0.6825 -0.0185 -0.1200 0.0247  387 GLU C CA  
7509  C C   . GLU C 86  ? 0.6360 1.3263 0.6595 -0.0391 -0.1198 0.0235  387 GLU C C   
7510  O O   . GLU C 86  ? 0.6699 1.3711 0.6906 -0.0711 -0.1198 0.0199  387 GLU C O   
7511  C CB  . GLU C 86  ? 0.7470 1.5513 0.7949 0.0025  -0.1301 0.0278  387 GLU C CB  
7512  C CG  . GLU C 86  ? 0.9332 1.7868 0.9847 -0.0248 -0.1339 0.0254  387 GLU C CG  
7513  C CD  . GLU C 86  ? 1.0359 1.9159 1.0968 -0.0581 -0.1261 0.0207  387 GLU C CD  
7514  O OE1 . GLU C 86  ? 1.0463 1.9572 1.1207 -0.0492 -0.1204 0.0204  387 GLU C OE1 
7515  O OE2 . GLU C 86  ? 1.0432 1.9099 1.0954 -0.0933 -0.1253 0.0172  387 GLU C OE2 
7516  N N   . GLU C 87  ? 0.5918 1.2231 0.6019 -0.0224 -0.1193 0.0262  388 GLU C N   
7517  C CA  . GLU C 87  ? 0.5651 1.1448 0.5585 -0.0412 -0.1179 0.0248  388 GLU C CA  
7518  C C   . GLU C 87  ? 0.6041 1.1501 0.5950 -0.0676 -0.1085 0.0203  388 GLU C C   
7519  O O   . GLU C 87  ? 0.4490 0.9819 0.4305 -0.0950 -0.1074 0.0167  388 GLU C O   
7520  C CB  . GLU C 87  ? 0.5378 1.0652 0.5179 -0.0176 -0.1188 0.0290  388 GLU C CB  
7521  C CG  . GLU C 87  ? 0.6487 1.1275 0.6117 -0.0342 -0.1174 0.0278  388 GLU C CG  
7522  C CD  . GLU C 87  ? 0.7354 1.1643 0.6855 -0.0133 -0.1174 0.0322  388 GLU C CD  
7523  O OE1 . GLU C 87  ? 0.7681 1.1862 0.7212 0.0098  -0.1161 0.0351  388 GLU C OE1 
7524  O OE2 . GLU C 87  ? 0.8622 1.2625 0.7978 -0.0208 -0.1186 0.0326  388 GLU C OE2 
7525  N N   . VAL C 88  ? 0.4815 1.0123 0.4790 -0.0592 -0.1018 0.0205  389 VAL C N   
7526  C CA  . VAL C 88  ? 0.4755 0.9780 0.4706 -0.0826 -0.0933 0.0172  389 VAL C CA  
7527  C C   . VAL C 88  ? 0.5355 1.0836 0.5371 -0.1105 -0.0929 0.0140  389 VAL C C   
7528  O O   . VAL C 88  ? 0.6235 1.1493 0.6152 -0.1389 -0.0889 0.0107  389 VAL C O   
7529  C CB  . VAL C 88  ? 0.4679 0.9478 0.4683 -0.0662 -0.0869 0.0185  389 VAL C CB  
7530  C CG1 . VAL C 88  ? 0.4959 0.9490 0.4932 -0.0894 -0.0784 0.0159  389 VAL C CG1 
7531  C CG2 . VAL C 88  ? 0.4744 0.9061 0.4656 -0.0432 -0.0872 0.0212  389 VAL C CG2 
7532  N N   . ASN C 89  ? 0.4529 1.0657 0.4698 -0.1031 -0.0970 0.0149  390 ASN C N   
7533  C CA  . ASN C 89  ? 0.5332 1.1968 0.5571 -0.1312 -0.0969 0.0121  390 ASN C CA  
7534  C C   . ASN C 89  ? 0.6464 1.3079 0.6573 -0.1597 -0.1008 0.0088  390 ASN C C   
7535  O O   . ASN C 89  ? 0.6297 1.2741 0.6311 -0.1915 -0.0962 0.0053  390 ASN C O   
7536  C CB  . ASN C 89  ? 0.5960 1.3356 0.6390 -0.1142 -0.1019 0.0138  390 ASN C CB  
7537  C CG  . ASN C 89  ? 0.8222 1.6132 0.8762 -0.1387 -0.0985 0.0116  390 ASN C CG  
7538  O OD1 . ASN C 89  ? 0.7671 1.5631 0.8140 -0.1740 -0.0979 0.0086  390 ASN C OD1 
7539  N ND2 . ASN C 89  ? 1.0244 1.8526 1.0942 -0.1208 -0.0959 0.0130  390 ASN C ND2 
7540  N N   . LYS C 90  ? 0.5812 1.2573 0.5891 -0.1485 -0.1093 0.0100  391 LYS C N   
7541  C CA  . LYS C 90  ? 0.7086 1.3825 0.7028 -0.1744 -0.1134 0.0064  391 LYS C CA  
7542  C C   . LYS C 90  ? 0.6332 1.2321 0.6068 -0.1900 -0.1072 0.0034  391 LYS C C   
7543  O O   . LYS C 90  ? 0.6725 1.2608 0.6325 -0.2210 -0.1064 -0.0015 391 LYS C O   
7544  C CB  . LYS C 90  ? 0.8809 1.5772 0.8739 -0.1552 -0.1235 0.0092  391 LYS C CB  
7545  C CG  . LYS C 90  ? 1.0795 1.8605 1.0898 -0.1459 -0.1317 0.0112  391 LYS C CG  
7546  C CD  . LYS C 90  ? 1.1034 1.8963 1.1113 -0.1176 -0.1406 0.0159  391 LYS C CD  
7547  C CE  . LYS C 90  ? 1.0407 1.8955 1.0653 -0.0983 -0.1410 0.0187  391 LYS C CE  
7548  N NZ  . LYS C 90  ? 0.9543 1.8102 0.9776 -0.0592 -0.1478 0.0249  391 LYS C NZ  
7549  N N   . GLU C 91  ? 0.5894 1.1361 0.5595 -0.1687 -0.1027 0.0060  392 GLU C N   
7550  C CA  . GLU C 91  ? 0.6885 1.1668 0.6404 -0.1794 -0.0966 0.0035  392 GLU C CA  
7551  C C   . GLU C 91  ? 0.8292 1.2890 0.7753 -0.2064 -0.0888 0.0000  392 GLU C C   
7552  O O   . GLU C 91  ? 0.8435 1.2730 0.7716 -0.2307 -0.0866 -0.0046 392 GLU C O   
7553  C CB  . GLU C 91  ? 0.4519 0.8871 0.4037 -0.1508 -0.0936 0.0075  392 GLU C CB  
7554  C CG  . GLU C 91  ? 0.7087 1.0819 0.6422 -0.1549 -0.0897 0.0058  392 GLU C CG  
7555  C CD  . GLU C 91  ? 0.6822 1.0266 0.6153 -0.1267 -0.0899 0.0102  392 GLU C CD  
7556  O OE1 . GLU C 91  ? 0.6927 0.9878 0.6132 -0.1272 -0.0855 0.0094  392 GLU C OE1 
7557  O OE2 . GLU C 91  ? 0.6121 0.9834 0.5563 -0.1040 -0.0942 0.0145  392 GLU C OE2 
7558  N N   . ILE C 92  ? 0.7870 1.2635 0.7464 -0.2026 -0.0844 0.0020  393 ILE C N   
7559  C CA  . ILE C 92  ? 0.7302 1.1910 0.6832 -0.2284 -0.0772 -0.0002 393 ILE C CA  
7560  C C   . ILE C 92  ? 0.6859 1.1805 0.6327 -0.2624 -0.0799 -0.0043 393 ILE C C   
7561  O O   . ILE C 92  ? 0.7446 1.2052 0.6730 -0.2898 -0.0754 -0.0078 393 ILE C O   
7562  C CB  . ILE C 92  ? 0.7799 1.2588 0.7488 -0.2170 -0.0725 0.0031  393 ILE C CB  
7563  C CG1 . ILE C 92  ? 0.6242 1.0650 0.5962 -0.1866 -0.0695 0.0064  393 ILE C CG1 
7564  C CG2 . ILE C 92  ? 0.8046 1.2679 0.7650 -0.2447 -0.0651 0.0018  393 ILE C CG2 
7565  C CD1 . ILE C 92  ? 0.5140 0.9891 0.5047 -0.1663 -0.0685 0.0094  393 ILE C CD1 
7566  N N   . ASP C 93  ? 0.6603 1.2221 0.6209 -0.2611 -0.0875 -0.0039 394 ASP C N   
7567  C CA  . ASP C 93  ? 0.6886 1.2911 0.6447 -0.2948 -0.0909 -0.0079 394 ASP C CA  
7568  C C   . ASP C 93  ? 0.8268 1.3896 0.7579 -0.3172 -0.0924 -0.0133 394 ASP C C   
7569  O O   . ASP C 93  ? 0.9751 1.5426 0.8931 -0.3525 -0.0917 -0.0178 394 ASP C O   
7570  C CB  . ASP C 93  ? 0.5845 1.2675 0.5600 -0.2846 -0.1000 -0.0063 394 ASP C CB  
7571  C CG  . ASP C 93  ? 0.7418 1.4809 0.7378 -0.2808 -0.0972 -0.0035 394 ASP C CG  
7572  O OD1 . ASP C 93  ? 0.7981 1.5609 0.8117 -0.2479 -0.0994 0.0004  394 ASP C OD1 
7573  O OD2 . ASP C 93  ? 0.8583 1.6102 0.8497 -0.3075 -0.0905 -0.0047 394 ASP C OD2 
7574  N N   . THR C 94  ? 0.7149 1.2391 0.6376 -0.2984 -0.0943 -0.0132 395 THR C N   
7575  C CA  . THR C 94  ? 0.8195 1.3105 0.7185 -0.3169 -0.0960 -0.0187 395 THR C CA  
7576  C C   . THR C 94  ? 0.9418 1.3517 0.8198 -0.3172 -0.0881 -0.0209 395 THR C C   
7577  O O   . THR C 94  ? 1.0035 1.3805 0.8579 -0.3382 -0.0874 -0.0269 395 THR C O   
7578  C CB  . THR C 94  ? 0.7742 1.2905 0.6766 -0.2994 -0.1052 -0.0176 395 THR C CB  
7579  O OG1 . THR C 94  ? 0.8144 1.2961 0.7199 -0.2660 -0.1039 -0.0130 395 THR C OG1 
7580  C CG2 . THR C 94  ? 0.6509 1.2494 0.5756 -0.2928 -0.1132 -0.0145 395 THR C CG2 
7581  N N   . THR C 95  ? 0.9326 1.3103 0.8174 -0.2946 -0.0822 -0.0167 396 THR C N   
7582  C CA  . THR C 95  ? 0.9653 1.2715 0.8318 -0.2925 -0.0748 -0.0183 396 THR C CA  
7583  C C   . THR C 95  ? 0.9645 1.2424 0.8306 -0.2951 -0.0662 -0.0164 396 THR C C   
7584  O O   . THR C 95  ? 1.0664 1.2863 0.9149 -0.2969 -0.0599 -0.0181 396 THR C O   
7585  C CB  . THR C 95  ? 0.9534 1.2368 0.8239 -0.2611 -0.0756 -0.0151 396 THR C CB  
7586  O OG1 . THR C 95  ? 0.9911 1.2868 0.8818 -0.2365 -0.0741 -0.0090 396 THR C OG1 
7587  C CG2 . THR C 95  ? 0.9354 1.2489 0.8072 -0.2546 -0.0844 -0.0153 396 THR C CG2 
7588  N N   . SER C 96  ? 0.7801 1.0979 0.6645 -0.2939 -0.0658 -0.0127 397 SER C N   
7589  C CA  . SER C 96  ? 0.8356 1.1352 0.7220 -0.2949 -0.0583 -0.0098 397 SER C CA  
7590  C C   . SER C 96  ? 0.7434 1.0145 0.6385 -0.2637 -0.0548 -0.0056 397 SER C C   
7591  O O   . SER C 96  ? 0.7950 1.0481 0.6909 -0.2624 -0.0487 -0.0030 397 SER C O   
7592  C CB  . SER C 96  ? 0.9730 1.2233 0.8329 -0.3223 -0.0519 -0.0132 397 SER C CB  
7593  O OG  . SER C 96  ? 1.1029 1.3773 0.9523 -0.3546 -0.0550 -0.0176 397 SER C OG  
7594  N N   . THR C 97  ? 0.7329 0.9991 0.6330 -0.2402 -0.0584 -0.0045 398 THR C N   
7595  C CA  . THR C 97  ? 0.7244 0.9700 0.6338 -0.2118 -0.0558 -0.0004 398 THR C CA  
7596  C C   . THR C 97  ? 0.6503 0.9291 0.5741 -0.1885 -0.0629 0.0022  398 THR C C   
7597  O O   . THR C 97  ? 0.5871 0.9145 0.5190 -0.1920 -0.0691 0.0019  398 THR C O   
7598  C CB  . THR C 97  ? 0.7810 0.9644 0.6731 -0.2087 -0.0506 -0.0018 398 THR C CB  
7599  O OG1 . THR C 97  ? 0.7514 0.9170 0.6524 -0.1848 -0.0476 0.0021  398 THR C OG1 
7600  C CG2 . THR C 97  ? 0.7128 0.8842 0.5936 -0.2085 -0.0545 -0.0049 398 THR C CG2 
7601  N N   . TYR C 98  ? 0.6169 0.8711 0.5435 -0.1643 -0.0620 0.0050  399 TYR C N   
7602  C CA  . TYR C 98  ? 0.4626 0.7341 0.3959 -0.1426 -0.0685 0.0077  399 TYR C CA  
7603  C C   . TYR C 98  ? 0.6791 0.9068 0.6076 -0.1242 -0.0657 0.0099  399 TYR C C   
7604  O O   . TYR C 98  ? 0.7579 0.9504 0.6819 -0.1258 -0.0590 0.0095  399 TYR C O   
7605  C CB  . TYR C 98  ? 0.4295 0.7508 0.3810 -0.1278 -0.0725 0.0107  399 TYR C CB  
7606  C CG  . TYR C 98  ? 0.5012 0.8126 0.4619 -0.1110 -0.0679 0.0132  399 TYR C CG  
7607  C CD1 . TYR C 98  ? 0.5477 0.8461 0.5109 -0.0847 -0.0695 0.0163  399 TYR C CD1 
7608  C CD2 . TYR C 98  ? 0.4905 0.8039 0.4552 -0.1225 -0.0620 0.0125  399 TYR C CD2 
7609  C CE1 . TYR C 98  ? 0.5449 0.8328 0.5144 -0.0708 -0.0654 0.0178  399 TYR C CE1 
7610  C CE2 . TYR C 98  ? 0.4943 0.7987 0.4661 -0.1077 -0.0579 0.0145  399 TYR C CE2 
7611  C CZ  . TYR C 98  ? 0.5278 0.8204 0.5023 -0.0820 -0.0598 0.0167  399 TYR C CZ  
7612  O OH  . TYR C 98  ? 0.6592 0.9428 0.6393 -0.0685 -0.0559 0.0179  399 TYR C OH  
7613  N N   . GLN C 99  ? 0.6918 0.9231 0.6203 -0.1069 -0.0710 0.0125  400 GLN C N   
7614  C CA  . GLN C 99  ? 0.6537 0.8450 0.5744 -0.0935 -0.0692 0.0145  400 GLN C CA  
7615  C C   . GLN C 99  ? 0.5500 0.7465 0.4786 -0.0684 -0.0717 0.0191  400 GLN C C   
7616  O O   . GLN C 99  ? 0.5564 0.7861 0.4911 -0.0573 -0.0780 0.0214  400 GLN C O   
7617  C CB  . GLN C 99  ? 0.4443 0.6248 0.3513 -0.0982 -0.0726 0.0135  400 GLN C CB  
7618  C CG  . GLN C 99  ? 0.6313 0.8029 0.5268 -0.1228 -0.0702 0.0078  400 GLN C CG  
7619  C CD  . GLN C 99  ? 0.7636 0.8909 0.6502 -0.1294 -0.0616 0.0053  400 GLN C CD  
7620  O OE1 . GLN C 99  ? 0.7596 0.8583 0.6439 -0.1171 -0.0582 0.0072  400 GLN C OE1 
7621  N NE2 . GLN C 99  ? 0.7862 0.9081 0.6666 -0.1493 -0.0580 0.0011  400 GLN C NE2 
7622  N N   . LEU C 100 ? 0.6004 0.7633 0.5273 -0.0593 -0.0670 0.0204  401 LEU C N   
7623  C CA  . LEU C 100 ? 0.6404 0.8018 0.5718 -0.0374 -0.0686 0.0241  401 LEU C CA  
7624  C C   . LEU C 100 ? 0.5173 0.6647 0.4383 -0.0256 -0.0732 0.0275  401 LEU C C   
7625  O O   . LEU C 100 ? 0.4655 0.5856 0.3757 -0.0321 -0.0714 0.0273  401 LEU C O   
7626  C CB  . LEU C 100 ? 0.6220 0.7544 0.5548 -0.0344 -0.0619 0.0238  401 LEU C CB  
7627  C CG  . LEU C 100 ? 0.4856 0.6273 0.4268 -0.0446 -0.0568 0.0215  401 LEU C CG  
7628  C CD1 . LEU C 100 ? 0.5866 0.6962 0.5262 -0.0432 -0.0505 0.0214  401 LEU C CD1 
7629  C CD2 . LEU C 100 ? 0.4044 0.5833 0.3575 -0.0357 -0.0593 0.0220  401 LEU C CD2 
7630  N N   . LYS C 101 ? 0.4527 0.6187 0.3756 -0.0076 -0.0791 0.0309  402 LYS C N   
7631  C CA  . LYS C 101 ? 0.4401 0.5847 0.3506 0.0071  -0.0829 0.0355  402 LYS C CA  
7632  C C   . LYS C 101 ? 0.5582 0.6592 0.4615 0.0084  -0.0774 0.0361  402 LYS C C   
7633  O O   . LYS C 101 ? 0.5862 0.6788 0.4964 0.0046  -0.0717 0.0336  402 LYS C O   
7634  C CB  . LYS C 101 ? 0.4740 0.6392 0.3866 0.0298  -0.0888 0.0389  402 LYS C CB  
7635  C CG  . LYS C 101 ? 0.5861 0.8002 0.5059 0.0307  -0.0952 0.0389  402 LYS C CG  
7636  C CD  . LYS C 101 ? 0.7047 0.9218 0.6148 0.0203  -0.0996 0.0400  402 LYS C CD  
7637  C CE  . LYS C 101 ? 0.7768 1.0472 0.6959 0.0139  -0.1052 0.0385  402 LYS C CE  
7638  N NZ  . LYS C 101 ? 0.8719 1.1450 0.7810 -0.0003 -0.1089 0.0382  402 LYS C NZ  
7639  N N   . ASP C 102 ? 0.6577 0.7326 0.5467 0.0130  -0.0791 0.0398  403 ASP C N   
7640  C CA  . ASP C 102 ? 0.6280 0.6654 0.5099 0.0121  -0.0739 0.0404  403 ASP C CA  
7641  C C   . ASP C 102 ? 0.6294 0.6574 0.5139 0.0255  -0.0729 0.0410  403 ASP C C   
7642  O O   . ASP C 102 ? 0.5795 0.5893 0.4661 0.0210  -0.0673 0.0391  403 ASP C O   
7643  C CB  . ASP C 102 ? 0.7606 0.7744 0.6253 0.0139  -0.0762 0.0449  403 ASP C CB  
7644  C CG  . ASP C 102 ? 0.9152 0.9261 0.7751 -0.0022 -0.0740 0.0431  403 ASP C CG  
7645  O OD1 . ASP C 102 ? 0.9116 0.9391 0.7800 -0.0141 -0.0718 0.0383  403 ASP C OD1 
7646  O OD2 . ASP C 102 ? 0.9198 0.9103 0.7658 -0.0033 -0.0742 0.0464  403 ASP C OD2 
7647  N N   . THR C 103 ? 0.6124 0.6520 0.4951 0.0430  -0.0783 0.0434  404 THR C N   
7648  C CA  . THR C 103 ? 0.6624 0.6918 0.5451 0.0571  -0.0773 0.0431  404 THR C CA  
7649  C C   . THR C 103 ? 0.6809 0.7310 0.5807 0.0520  -0.0728 0.0382  404 THR C C   
7650  O O   . THR C 103 ? 0.6413 0.6750 0.5420 0.0535  -0.0686 0.0363  404 THR C O   
7651  C CB  . THR C 103 ? 0.6894 0.7284 0.5652 0.0794  -0.0841 0.0464  404 THR C CB  
7652  O OG1 . THR C 103 ? 0.5524 0.6349 0.4385 0.0802  -0.0884 0.0462  404 THR C OG1 
7653  C CG2 . THR C 103 ? 0.8148 0.8208 0.6688 0.0862  -0.0878 0.0521  404 THR C CG2 
7654  N N   . GLU C 104 ? 0.6997 0.7857 0.6120 0.0441  -0.0734 0.0362  405 GLU C N   
7655  C CA  . GLU C 104 ? 0.6493 0.7556 0.5763 0.0366  -0.0689 0.0322  405 GLU C CA  
7656  C C   . GLU C 104 ? 0.7571 0.8385 0.6844 0.0217  -0.0621 0.0302  405 GLU C C   
7657  O O   . GLU C 104 ? 0.7621 0.8398 0.6948 0.0224  -0.0579 0.0284  405 GLU C O   
7658  C CB  . GLU C 104 ? 0.5191 0.6662 0.4559 0.0269  -0.0712 0.0309  405 GLU C CB  
7659  C CG  . GLU C 104 ? 0.4291 0.6090 0.3678 0.0433  -0.0781 0.0329  405 GLU C CG  
7660  C CD  . GLU C 104 ? 0.5535 0.7774 0.5015 0.0314  -0.0810 0.0316  405 GLU C CD  
7661  O OE1 . GLU C 104 ? 0.5854 0.8442 0.5370 0.0441  -0.0870 0.0332  405 GLU C OE1 
7662  O OE2 . GLU C 104 ? 0.6233 0.8465 0.5735 0.0094  -0.0775 0.0290  405 GLU C OE2 
7663  N N   . LEU C 105 ? 0.7819 0.8471 0.7027 0.0092  -0.0609 0.0305  406 LEU C N   
7664  C CA  . LEU C 105 ? 0.6587 0.7025 0.5792 -0.0029 -0.0545 0.0287  406 LEU C CA  
7665  C C   . LEU C 105 ? 0.6480 0.6657 0.5643 0.0045  -0.0521 0.0296  406 LEU C C   
7666  O O   . LEU C 105 ? 0.6449 0.6561 0.5660 0.0002  -0.0472 0.0279  406 LEU C O   
7667  C CB  . LEU C 105 ? 0.6232 0.6544 0.5353 -0.0145 -0.0538 0.0287  406 LEU C CB  
7668  C CG  . LEU C 105 ? 0.6427 0.6539 0.5528 -0.0261 -0.0473 0.0266  406 LEU C CG  
7669  C CD1 . LEU C 105 ? 0.7107 0.7341 0.6254 -0.0390 -0.0446 0.0234  406 LEU C CD1 
7670  C CD2 . LEU C 105 ? 0.4801 0.4718 0.3786 -0.0299 -0.0466 0.0275  406 LEU C CD2 
7671  N N   . ILE C 106 ? 0.5442 0.5459 0.4498 0.0148  -0.0555 0.0324  407 ILE C N   
7672  C CA  . ILE C 106 ? 0.5716 0.5471 0.4709 0.0190  -0.0533 0.0328  407 ILE C CA  
7673  C C   . ILE C 106 ? 0.7283 0.7118 0.6341 0.0285  -0.0526 0.0307  407 ILE C C   
7674  O O   . ILE C 106 ? 0.6122 0.5845 0.5196 0.0259  -0.0487 0.0289  407 ILE C O   
7675  C CB  . ILE C 106 ? 0.5198 0.4722 0.4025 0.0260  -0.0571 0.0367  407 ILE C CB  
7676  C CG1 . ILE C 106 ? 0.4476 0.3909 0.3235 0.0147  -0.0564 0.0386  407 ILE C CG1 
7677  C CG2 . ILE C 106 ? 0.5643 0.4898 0.4383 0.0296  -0.0555 0.0367  407 ILE C CG2 
7678  C CD1 . ILE C 106 ? 0.5206 0.4594 0.3834 0.0216  -0.0622 0.0430  407 ILE C CD1 
7679  N N   . TYR C 107 ? 0.7408 0.7470 0.6506 0.0397  -0.0564 0.0306  408 TYR C N   
7680  C CA  . TYR C 107 ? 0.6475 0.6654 0.5632 0.0502  -0.0555 0.0281  408 TYR C CA  
7681  C C   . TYR C 107 ? 0.7024 0.7334 0.6308 0.0387  -0.0500 0.0253  408 TYR C C   
7682  O O   . TYR C 107 ? 0.6586 0.6809 0.5879 0.0406  -0.0469 0.0234  408 TYR C O   
7683  C CB  . TYR C 107 ? 0.6164 0.6643 0.5360 0.0638  -0.0602 0.0285  408 TYR C CB  
7684  C CG  . TYR C 107 ? 0.6728 0.7396 0.5998 0.0751  -0.0588 0.0254  408 TYR C CG  
7685  C CD1 . TYR C 107 ? 0.5992 0.6452 0.5157 0.0909  -0.0592 0.0241  408 TYR C CD1 
7686  C CD2 . TYR C 107 ? 0.6484 0.7531 0.5911 0.0690  -0.0567 0.0235  408 TYR C CD2 
7687  C CE1 . TYR C 107 ? 0.7194 0.7833 0.6416 0.1022  -0.0574 0.0206  408 TYR C CE1 
7688  C CE2 . TYR C 107 ? 0.6491 0.7742 0.5985 0.0790  -0.0549 0.0207  408 TYR C CE2 
7689  C CZ  . TYR C 107 ? 0.7655 0.8709 0.7051 0.0966  -0.0552 0.0190  408 TYR C CZ  
7690  O OH  . TYR C 107 ? 0.9042 1.0302 0.8494 0.1074  -0.0530 0.0156  408 TYR C OH  
7691  N N   . GLY C 108 ? 0.6630 0.7130 0.5995 0.0261  -0.0490 0.0252  409 GLY C N   
7692  C CA  . GLY C 108 ? 0.5693 0.6282 0.5147 0.0147  -0.0439 0.0234  409 GLY C CA  
7693  C C   . GLY C 108 ? 0.6074 0.6390 0.5490 0.0079  -0.0394 0.0233  409 GLY C C   
7694  O O   . GLY C 108 ? 0.7520 0.7839 0.6979 0.0067  -0.0357 0.0222  409 GLY C O   
7695  N N   . ALA C 109 ? 0.5698 0.5802 0.5033 0.0039  -0.0397 0.0247  410 ALA C N   
7696  C CA  . ALA C 109 ? 0.5151 0.5052 0.4461 -0.0022 -0.0354 0.0246  410 ALA C CA  
7697  C C   . ALA C 109 ? 0.5234 0.5023 0.4522 0.0055  -0.0349 0.0239  410 ALA C C   
7698  O O   . ALA C 109 ? 0.5371 0.5124 0.4689 0.0021  -0.0312 0.0231  410 ALA C O   
7699  C CB  . ALA C 109 ? 0.4014 0.3752 0.3242 -0.0075 -0.0355 0.0260  410 ALA C CB  
7700  N N   . LYS C 110 ? 0.5482 0.5207 0.4700 0.0162  -0.0388 0.0241  411 LYS C N   
7701  C CA  . LYS C 110 ? 0.5323 0.4896 0.4484 0.0221  -0.0384 0.0227  411 LYS C CA  
7702  C C   . LYS C 110 ? 0.7137 0.6872 0.6380 0.0269  -0.0365 0.0200  411 LYS C C   
7703  O O   . LYS C 110 ? 0.6710 0.6365 0.5943 0.0261  -0.0342 0.0183  411 LYS C O   
7704  C CB  . LYS C 110 ? 0.4495 0.3896 0.3518 0.0328  -0.0429 0.0236  411 LYS C CB  
7705  C CG  . LYS C 110 ? 0.5456 0.4647 0.4368 0.0263  -0.0440 0.0267  411 LYS C CG  
7706  C CD  . LYS C 110 ? 0.5745 0.4721 0.4484 0.0366  -0.0486 0.0286  411 LYS C CD  
7707  C CE  . LYS C 110 ? 0.6150 0.4879 0.4755 0.0272  -0.0486 0.0318  411 LYS C CE  
7708  N NZ  . LYS C 110 ? 0.6205 0.4683 0.4607 0.0364  -0.0532 0.0348  411 LYS C NZ  
7709  N N   . HIS C 111 ? 0.7235 0.7224 0.6559 0.0306  -0.0374 0.0197  412 HIS C N   
7710  C CA  . HIS C 111 ? 0.6428 0.6600 0.5822 0.0355  -0.0354 0.0172  412 HIS C CA  
7711  C C   . HIS C 111 ? 0.7499 0.7747 0.6974 0.0233  -0.0306 0.0176  412 HIS C C   
7712  O O   . HIS C 111 ? 0.8001 0.8298 0.7500 0.0252  -0.0281 0.0159  412 HIS C O   
7713  C CB  . HIS C 111 ? 0.5721 0.6179 0.5172 0.0441  -0.0380 0.0169  412 HIS C CB  
7714  C CG  . HIS C 111 ? 0.5396 0.5796 0.4759 0.0625  -0.0418 0.0156  412 HIS C CG  
7715  N ND1 . HIS C 111 ? 0.6273 0.6349 0.5487 0.0676  -0.0445 0.0165  412 HIS C ND1 
7716  C CD2 . HIS C 111 ? 0.6145 0.6754 0.5528 0.0777  -0.0431 0.0135  412 HIS C CD2 
7717  C CE1 . HIS C 111 ? 0.6374 0.6418 0.5502 0.0856  -0.0475 0.0151  412 HIS C CE1 
7718  N NE2 . HIS C 111 ? 0.6744 0.7122 0.5979 0.0933  -0.0467 0.0131  412 HIS C NE2 
7719  N N   . ALA C 112 ? 0.6544 0.6782 0.6040 0.0114  -0.0292 0.0196  413 ALA C N   
7720  C CA  . ALA C 112 ? 0.6696 0.6936 0.6228 0.0015  -0.0247 0.0205  413 ALA C CA  
7721  C C   . ALA C 112 ? 0.6212 0.6267 0.5706 0.0020  -0.0228 0.0203  413 ALA C C   
7722  O O   . ALA C 112 ? 0.5876 0.5963 0.5395 -0.0003 -0.0196 0.0206  413 ALA C O   
7723  C CB  . ALA C 112 ? 0.6031 0.6243 0.5556 -0.0099 -0.0236 0.0222  413 ALA C CB  
7724  N N   . TRP C 113 ? 0.6419 0.6295 0.5844 0.0043  -0.0247 0.0202  414 TRP C N   
7725  C CA  . TRP C 113 ? 0.6212 0.5953 0.5597 0.0043  -0.0236 0.0194  414 TRP C CA  
7726  C C   . TRP C 113 ? 0.5958 0.5729 0.5328 0.0123  -0.0243 0.0165  414 TRP C C   
7727  O O   . TRP C 113 ? 0.8181 0.7983 0.7569 0.0111  -0.0220 0.0157  414 TRP C O   
7728  C CB  . TRP C 113 ? 0.4769 0.4325 0.4069 0.0028  -0.0255 0.0200  414 TRP C CB  
7729  C CG  . TRP C 113 ? 0.5920 0.5367 0.5178 -0.0003 -0.0244 0.0193  414 TRP C CG  
7730  C CD1 . TRP C 113 ? 0.5274 0.4781 0.4568 -0.0012 -0.0221 0.0183  414 TRP C CD1 
7731  C CD2 . TRP C 113 ? 0.5973 0.5255 0.5138 -0.0041 -0.0256 0.0196  414 TRP C CD2 
7732  N NE1 . TRP C 113 ? 0.4769 0.4181 0.4007 -0.0054 -0.0222 0.0176  414 TRP C NE1 
7733  C CE2 . TRP C 113 ? 0.5326 0.4598 0.4484 -0.0080 -0.0241 0.0183  414 TRP C CE2 
7734  C CE3 . TRP C 113 ? 0.5975 0.5125 0.5054 -0.0055 -0.0278 0.0211  414 TRP C CE3 
7735  C CZ2 . TRP C 113 ? 0.5995 0.5147 0.5068 -0.0148 -0.0247 0.0183  414 TRP C CZ2 
7736  C CZ3 . TRP C 113 ? 0.4811 0.3816 0.3795 -0.0119 -0.0281 0.0214  414 TRP C CZ3 
7737  C CH2 . TRP C 113 ? 0.6217 0.5231 0.5202 -0.0172 -0.0265 0.0199  414 TRP C CH2 
7738  N N   . ARG C 114 ? 0.4730 0.4494 0.4056 0.0217  -0.0275 0.0148  415 ARG C N   
7739  C CA  . ARG C 114 ? 0.4573 0.4340 0.3857 0.0315  -0.0280 0.0112  415 ARG C CA  
7740  C C   . ARG C 114 ? 0.6738 0.6738 0.6115 0.0319  -0.0249 0.0103  415 ARG C C   
7741  O O   . ARG C 114 ? 0.8029 0.8030 0.7376 0.0365  -0.0239 0.0072  415 ARG C O   
7742  C CB  . ARG C 114 ? 0.4522 0.4264 0.3740 0.0441  -0.0319 0.0101  415 ARG C CB  
7743  C CG  . ARG C 114 ? 0.4230 0.3981 0.3391 0.0574  -0.0323 0.0057  415 ARG C CG  
7744  C CD  . ARG C 114 ? 0.4412 0.4195 0.3523 0.0727  -0.0359 0.0052  415 ARG C CD  
7745  N NE  . ARG C 114 ? 0.5526 0.5153 0.4499 0.0869  -0.0368 0.0005  415 ARG C NE  
7746  C CZ  . ARG C 114 ? 0.5856 0.5456 0.4742 0.1044  -0.0399 -0.0006 415 ARG C CZ  
7747  N NH1 . ARG C 114 ? 0.5452 0.4862 0.4182 0.1180  -0.0403 -0.0055 415 ARG C NH1 
7748  N NH2 . ARG C 114 ? 0.5563 0.5319 0.4502 0.1089  -0.0427 0.0030  415 ARG C NH2 
7749  N N   . ASN C 115 ? 0.5988 0.6173 0.5459 0.0258  -0.0233 0.0129  416 ASN C N   
7750  C CA  . ASN C 115 ? 0.4951 0.5354 0.4496 0.0236  -0.0200 0.0130  416 ASN C CA  
7751  C C   . ASN C 115 ? 0.5625 0.5982 0.5184 0.0136  -0.0165 0.0156  416 ASN C C   
7752  O O   . ASN C 115 ? 0.6953 0.7463 0.6554 0.0098  -0.0135 0.0169  416 ASN C O   
7753  C CB  . ASN C 115 ? 0.5051 0.5690 0.4671 0.0206  -0.0200 0.0146  416 ASN C CB  
7754  C CG  . ASN C 115 ? 0.6187 0.6951 0.5807 0.0330  -0.0235 0.0123  416 ASN C CG  
7755  O OD1 . ASN C 115 ? 0.5943 0.6658 0.5509 0.0460  -0.0247 0.0090  416 ASN C OD1 
7756  N ND2 . ASN C 115 ? 0.5414 0.6337 0.5082 0.0297  -0.0253 0.0140  416 ASN C ND2 
7757  N N   . ALA C 116 ? 0.4151 0.4317 0.3671 0.0092  -0.0167 0.0169  417 ALA C N   
7758  C CA  . ALA C 116 ? 0.5516 0.5648 0.5044 0.0021  -0.0135 0.0199  417 ALA C CA  
7759  C C   . ALA C 116 ? 0.6668 0.6822 0.6178 0.0052  -0.0126 0.0185  417 ALA C C   
7760  O O   . ALA C 116 ? 0.4905 0.4953 0.4369 0.0069  -0.0140 0.0164  417 ALA C O   
7761  C CB  . ALA C 116 ? 0.3493 0.3464 0.2992 -0.0020 -0.0139 0.0215  417 ALA C CB  
7762  N N   . SER C 117 ? 0.5548 0.5850 0.5086 0.0045  -0.0100 0.0195  418 SER C N   
7763  C CA  A SER C 117 ? 0.5961 0.6315 0.5475 0.0084  -0.0093 0.0174  418 SER C CA  
7764  C CA  B SER C 117 ? 0.5878 0.6236 0.5393 0.0083  -0.0092 0.0175  418 SER C CA  
7765  C C   . SER C 117 ? 0.5731 0.5993 0.5213 0.0058  -0.0091 0.0189  418 SER C C   
7766  O O   . SER C 117 ? 0.7112 0.7379 0.6556 0.0086  -0.0099 0.0159  418 SER C O   
7767  C CB  A SER C 117 ? 0.5718 0.6265 0.5262 0.0070  -0.0062 0.0190  418 SER C CB  
7768  C CB  B SER C 117 ? 0.5744 0.6289 0.5289 0.0062  -0.0059 0.0195  418 SER C CB  
7769  O OG  A SER C 117 ? 0.5893 0.6424 0.5438 -0.0014 -0.0035 0.0248  418 SER C OG  
7770  O OG  B SER C 117 ? 0.5673 0.6380 0.5251 0.0106  -0.0061 0.0168  418 SER C OG  
7771  N N   . ARG C 118 ? 0.5086 0.5276 0.4576 0.0009  -0.0081 0.0232  419 ARG C N   
7772  C CA  . ARG C 118 ? 0.4335 0.4488 0.3806 -0.0001 -0.0078 0.0253  419 ARG C CA  
7773  C C   . ARG C 118 ? 0.5421 0.5484 0.4873 -0.0006 -0.0104 0.0227  419 ARG C C   
7774  O O   . ARG C 118 ? 0.5796 0.5877 0.5241 -0.0016 -0.0105 0.0239  419 ARG C O   
7775  C CB  . ARG C 118 ? 0.3705 0.3820 0.3174 -0.0029 -0.0051 0.0311  419 ARG C CB  
7776  C CG  . ARG C 118 ? 0.3623 0.3800 0.3080 -0.0052 -0.0023 0.0344  419 ARG C CG  
7777  C CD  . ARG C 118 ? 0.4317 0.4385 0.3726 -0.0080 0.0004  0.0402  419 ARG C CD  
7778  N NE  . ARG C 118 ? 0.4587 0.4681 0.3945 -0.0106 0.0032  0.0448  419 ARG C NE  
7779  C CZ  . ARG C 118 ? 0.6406 0.6373 0.5688 -0.0153 0.0060  0.0497  419 ARG C CZ  
7780  N NH1 . ARG C 118 ? 0.7340 0.7162 0.6598 -0.0173 0.0063  0.0495  419 ARG C NH1 
7781  N NH2 . ARG C 118 ? 0.5933 0.5901 0.5144 -0.0188 0.0086  0.0546  419 ARG C NH2 
7782  N N   . CYS C 119 ? 0.5222 0.5205 0.4660 -0.0001 -0.0125 0.0196  420 CYS C N   
7783  C CA  . CYS C 119 ? 0.5922 0.5799 0.5327 -0.0030 -0.0144 0.0184  420 CYS C CA  
7784  C C   . CYS C 119 ? 0.6228 0.6051 0.5561 -0.0028 -0.0169 0.0136  420 CYS C C   
7785  O O   . CYS C 119 ? 0.6030 0.5791 0.5315 0.0016  -0.0185 0.0099  420 CYS C O   
7786  C CB  . CYS C 119 ? 0.5666 0.5452 0.5065 -0.0033 -0.0154 0.0185  420 CYS C CB  
7787  S SG  . CYS C 119 ? 0.5506 0.5161 0.4846 -0.0084 -0.0173 0.0178  420 CYS C SG  
7788  N N   . VAL C 120 ? 0.6199 0.6043 0.5513 -0.0076 -0.0174 0.0133  421 VAL C N   
7789  C CA  . VAL C 120 ? 0.6106 0.5877 0.5326 -0.0106 -0.0199 0.0083  421 VAL C CA  
7790  C C   . VAL C 120 ? 0.5900 0.5478 0.5031 -0.0147 -0.0221 0.0063  421 VAL C C   
7791  O O   . VAL C 120 ? 0.6624 0.6066 0.5635 -0.0171 -0.0244 0.0016  421 VAL C O   
7792  C CB  . VAL C 120 ? 0.5640 0.5543 0.4869 -0.0160 -0.0200 0.0088  421 VAL C CB  
7793  C CG1 . VAL C 120 ? 0.4526 0.4477 0.3793 -0.0220 -0.0196 0.0120  421 VAL C CG1 
7794  C CG2 . VAL C 120 ? 0.6040 0.5882 0.5158 -0.0201 -0.0226 0.0027  421 VAL C CG2 
7795  N N   . GLY C 121 ? 0.6682 0.6222 0.5845 -0.0157 -0.0216 0.0096  422 GLY C N   
7796  C CA  . GLY C 121 ? 0.5793 0.5159 0.4866 -0.0208 -0.0234 0.0091  422 GLY C CA  
7797  C C   . GLY C 121 ? 0.6661 0.5866 0.5670 -0.0141 -0.0252 0.0084  422 GLY C C   
7798  O O   . GLY C 121 ? 0.7616 0.6662 0.6539 -0.0177 -0.0267 0.0091  422 GLY C O   
7799  N N   . ARG C 122 ? 0.6071 0.5331 0.5115 -0.0042 -0.0251 0.0072  423 ARG C N   
7800  C CA  . ARG C 122 ? 0.5546 0.4727 0.4556 0.0042  -0.0268 0.0071  423 ARG C CA  
7801  C C   . ARG C 122 ? 0.5730 0.4659 0.4563 0.0083  -0.0299 0.0037  423 ARG C C   
7802  O O   . ARG C 122 ? 0.6322 0.5192 0.5115 0.0182  -0.0317 0.0037  423 ARG C O   
7803  C CB  . ARG C 122 ? 0.5024 0.4380 0.4120 0.0132  -0.0256 0.0065  423 ARG C CB  
7804  C CG  . ARG C 122 ? 0.5102 0.4663 0.4337 0.0098  -0.0226 0.0101  423 ARG C CG  
7805  C CD  . ARG C 122 ? 0.5802 0.5534 0.5095 0.0166  -0.0213 0.0090  423 ARG C CD  
7806  N NE  . ARG C 122 ? 0.5508 0.5316 0.4803 0.0166  -0.0195 0.0072  423 ARG C NE  
7807  C CZ  . ARG C 122 ? 0.6875 0.6845 0.6207 0.0215  -0.0178 0.0061  423 ARG C CZ  
7808  N NH1 . ARG C 122 ? 0.5689 0.5784 0.5070 0.0263  -0.0176 0.0065  423 ARG C NH1 
7809  N NH2 . ARG C 122 ? 0.6927 0.6961 0.6248 0.0209  -0.0162 0.0047  423 ARG C NH2 
7810  N N   . ILE C 123 ? 0.6287 0.5061 0.4999 0.0014  -0.0308 0.0007  424 ILE C N   
7811  C CA  . ILE C 123 ? 0.6584 0.5049 0.5085 0.0045  -0.0337 -0.0022 424 ILE C CA  
7812  C C   . ILE C 123 ? 0.7275 0.5583 0.5707 0.0020  -0.0354 0.0021  424 ILE C C   
7813  O O   . ILE C 123 ? 0.6263 0.4311 0.4521 0.0087  -0.0381 0.0014  424 ILE C O   
7814  C CB  . ILE C 123 ? 0.6462 0.4768 0.4818 -0.0059 -0.0343 -0.0066 424 ILE C CB  
7815  C CG1 . ILE C 123 ? 0.6877 0.4826 0.4981 0.0006  -0.0370 -0.0112 424 ILE C CG1 
7816  C CG2 . ILE C 123 ? 0.5183 0.3485 0.3535 -0.0233 -0.0340 -0.0035 424 ILE C CG2 
7817  C CD1 . ILE C 123 ? 0.7296 0.4980 0.5195 -0.0151 -0.0384 -0.0137 424 ILE C CD1 
7818  N N   . GLN C 124 ? 0.8193 0.6649 0.6746 -0.0063 -0.0338 0.0066  425 GLN C N   
7819  C CA  . GLN C 124 ? 0.7912 0.6269 0.6417 -0.0106 -0.0347 0.0110  425 GLN C CA  
7820  C C   . GLN C 124 ? 0.8557 0.7025 0.7152 -0.0007 -0.0353 0.0139  425 GLN C C   
7821  O O   . GLN C 124 ? 0.8579 0.6997 0.7145 -0.0038 -0.0360 0.0177  425 GLN C O   
7822  C CB  . GLN C 124 ? 0.7808 0.6296 0.6394 -0.0248 -0.0320 0.0136  425 GLN C CB  
7823  C CG  . GLN C 124 ? 0.8183 0.6592 0.6673 -0.0379 -0.0319 0.0115  425 GLN C CG  
7824  C CD  . GLN C 124 ? 1.0307 0.8417 0.8582 -0.0460 -0.0340 0.0127  425 GLN C CD  
7825  O OE1 . GLN C 124 ? 1.1464 0.9595 0.9730 -0.0565 -0.0329 0.0162  425 GLN C OE1 
7826  N NE2 . GLN C 124 ? 1.0802 0.8619 0.8884 -0.0407 -0.0369 0.0098  425 GLN C NE2 
7827  N N   . TRP C 125 ? 0.8409 0.7042 0.7103 0.0101  -0.0350 0.0122  426 TRP C N   
7828  C CA  . TRP C 125 ? 0.8089 0.6927 0.6915 0.0148  -0.0347 0.0147  426 TRP C CA  
7829  C C   . TRP C 125 ? 0.7923 0.6657 0.6666 0.0202  -0.0381 0.0175  426 TRP C C   
7830  O O   . TRP C 125 ? 0.7566 0.6411 0.6380 0.0171  -0.0379 0.0205  426 TRP C O   
7831  C CB  . TRP C 125 ? 0.7520 0.6553 0.6441 0.0244  -0.0339 0.0121  426 TRP C CB  
7832  C CG  . TRP C 125 ? 0.6483 0.5423 0.5298 0.0387  -0.0368 0.0096  426 TRP C CG  
7833  C CD1 . TRP C 125 ? 0.6559 0.5338 0.5252 0.0443  -0.0374 0.0053  426 TRP C CD1 
7834  C CD2 . TRP C 125 ? 0.6595 0.5598 0.5405 0.0504  -0.0397 0.0110  426 TRP C CD2 
7835  N NE1 . TRP C 125 ? 0.7755 0.6469 0.6355 0.0607  -0.0401 0.0038  426 TRP C NE1 
7836  C CE2 . TRP C 125 ? 0.7534 0.6408 0.6215 0.0651  -0.0417 0.0076  426 TRP C CE2 
7837  C CE3 . TRP C 125 ? 0.5962 0.5127 0.4855 0.0502  -0.0409 0.0145  426 TRP C CE3 
7838  C CZ2 . TRP C 125 ? 0.6755 0.5679 0.5398 0.0814  -0.0449 0.0081  426 TRP C CZ2 
7839  C CZ3 . TRP C 125 ? 0.7082 0.6316 0.5946 0.0643  -0.0444 0.0151  426 TRP C CZ3 
7840  C CH2 . TRP C 125 ? 0.6764 0.5889 0.5509 0.0806  -0.0464 0.0122  426 TRP C CH2 
7841  N N   . SER C 126 ? 0.7395 0.5904 0.5969 0.0290  -0.0413 0.0166  427 SER C N   
7842  C CA  . SER C 126 ? 0.6509 0.4916 0.4986 0.0366  -0.0451 0.0200  427 SER C CA  
7843  C C   . SER C 126 ? 0.8141 0.6369 0.6517 0.0249  -0.0455 0.0242  427 SER C C   
7844  O O   . SER C 126 ? 0.9194 0.7333 0.7479 0.0295  -0.0487 0.0279  427 SER C O   
7845  C CB  . SER C 126 ? 0.7258 0.5448 0.5557 0.0521  -0.0484 0.0181  427 SER C CB  
7846  O OG  . SER C 126 ? 0.7861 0.5679 0.5938 0.0456  -0.0493 0.0182  427 SER C OG  
7847  N N   . LYS C 127 ? 0.8057 0.6254 0.6444 0.0101  -0.0424 0.0238  428 LYS C N   
7848  C CA  . LYS C 127 ? 0.7635 0.5688 0.5923 -0.0025 -0.0420 0.0274  428 LYS C CA  
7849  C C   . LYS C 127 ? 0.7922 0.6226 0.6384 -0.0118 -0.0382 0.0285  428 LYS C C   
7850  O O   . LYS C 127 ? 1.0268 0.8630 0.8774 -0.0226 -0.0350 0.0277  428 LYS C O   
7851  C CB  . LYS C 127 ? 0.7272 0.5096 0.5409 -0.0125 -0.0415 0.0256  428 LYS C CB  
7852  C CG  . LYS C 127 ? 1.0375 0.8008 0.8357 -0.0257 -0.0415 0.0296  428 LYS C CG  
7853  C CD  . LYS C 127 ? 1.1519 0.9183 0.9503 -0.0430 -0.0385 0.0280  428 LYS C CD  
7854  C CE  . LYS C 127 ? 1.2076 0.9678 0.9968 -0.0583 -0.0371 0.0325  428 LYS C CE  
7855  N NZ  . LYS C 127 ? 1.1743 0.8972 0.9362 -0.0591 -0.0405 0.0362  428 LYS C NZ  
7856  N N   . LEU C 128 ? 0.6660 0.5121 0.5215 -0.0067 -0.0387 0.0300  429 LEU C N   
7857  C CA  . LEU C 128 ? 0.6345 0.5014 0.5042 -0.0130 -0.0352 0.0303  429 LEU C CA  
7858  C C   . LEU C 128 ? 0.7777 0.6434 0.6426 -0.0143 -0.0367 0.0335  429 LEU C C   
7859  O O   . LEU C 128 ? 0.8813 0.7430 0.7400 -0.0059 -0.0409 0.0351  429 LEU C O   
7860  C CB  . LEU C 128 ? 0.4251 0.3133 0.3102 -0.0073 -0.0342 0.0279  429 LEU C CB  
7861  C CG  . LEU C 128 ? 0.4091 0.3142 0.3051 -0.0115 -0.0315 0.0282  429 LEU C CG  
7862  C CD1 . LEU C 128 ? 0.4288 0.3381 0.3302 -0.0190 -0.0268 0.0277  429 LEU C CD1 
7863  C CD2 . LEU C 128 ? 0.4871 0.4093 0.3932 -0.0060 -0.0319 0.0267  429 LEU C CD2 
7864  N N   . GLN C 129 ? 0.6907 0.5614 0.5576 -0.0237 -0.0333 0.0345  430 GLN C N   
7865  C CA  . GLN C 129 ? 0.6446 0.5142 0.5055 -0.0264 -0.0342 0.0372  430 GLN C CA  
7866  C C   . GLN C 129 ? 0.7287 0.6171 0.6013 -0.0257 -0.0326 0.0354  430 GLN C C   
7867  O O   . GLN C 129 ? 0.9053 0.8037 0.7875 -0.0290 -0.0283 0.0331  430 GLN C O   
7868  C CB  . GLN C 129 ? 0.6647 0.5279 0.5183 -0.0376 -0.0309 0.0390  430 GLN C CB  
7869  C CG  . GLN C 129 ? 0.7785 0.6408 0.6244 -0.0414 -0.0310 0.0416  430 GLN C CG  
7870  C CD  . GLN C 129 ? 0.8364 0.6839 0.6684 -0.0357 -0.0368 0.0453  430 GLN C CD  
7871  O OE1 . GLN C 129 ? 0.9114 0.7396 0.7314 -0.0332 -0.0397 0.0473  430 GLN C OE1 
7872  N NE2 . GLN C 129 ? 0.9312 0.7869 0.7631 -0.0330 -0.0387 0.0462  430 GLN C NE2 
7873  N N   . VAL C 130 ? 0.7241 0.6166 0.5943 -0.0214 -0.0363 0.0364  431 VAL C N   
7874  C CA  . VAL C 130 ? 0.5620 0.4714 0.4411 -0.0224 -0.0357 0.0342  431 VAL C CA  
7875  C C   . VAL C 130 ? 0.6269 0.5356 0.4988 -0.0283 -0.0353 0.0351  431 VAL C C   
7876  O O   . VAL C 130 ? 0.7691 0.6723 0.6307 -0.0264 -0.0394 0.0382  431 VAL C O   
7877  C CB  . VAL C 130 ? 0.5243 0.4459 0.4078 -0.0143 -0.0403 0.0339  431 VAL C CB  
7878  C CG1 . VAL C 130 ? 0.4531 0.3927 0.3453 -0.0190 -0.0391 0.0313  431 VAL C CG1 
7879  C CG2 . VAL C 130 ? 0.6458 0.5671 0.5340 -0.0071 -0.0406 0.0329  431 VAL C CG2 
7880  N N   . PHE C 131 ? 0.5294 0.4427 0.4051 -0.0346 -0.0305 0.0324  432 PHE C N   
7881  C CA  . PHE C 131 ? 0.4627 0.3762 0.3314 -0.0401 -0.0292 0.0317  432 PHE C CA  
7882  C C   . PHE C 131 ? 0.6452 0.5694 0.5176 -0.0420 -0.0303 0.0286  432 PHE C C   
7883  O O   . PHE C 131 ? 0.6634 0.5900 0.5421 -0.0440 -0.0267 0.0255  432 PHE C O   
7884  C CB  . PHE C 131 ? 0.5153 0.4251 0.3828 -0.0447 -0.0227 0.0302  432 PHE C CB  
7885  C CG  . PHE C 131 ? 0.6245 0.5277 0.4885 -0.0459 -0.0216 0.0332  432 PHE C CG  
7886  C CD1 . PHE C 131 ? 0.4470 0.3414 0.2994 -0.0475 -0.0249 0.0372  432 PHE C CD1 
7887  C CD2 . PHE C 131 ? 0.5721 0.4777 0.4431 -0.0461 -0.0176 0.0322  432 PHE C CD2 
7888  C CE1 . PHE C 131 ? 0.5280 0.4139 0.3746 -0.0513 -0.0239 0.0400  432 PHE C CE1 
7889  C CE2 . PHE C 131 ? 0.5583 0.4596 0.4252 -0.0499 -0.0168 0.0347  432 PHE C CE2 
7890  C CZ  . PHE C 131 ? 0.5418 0.4322 0.3960 -0.0534 -0.0198 0.0384  432 PHE C CZ  
7891  N N   . ASP C 132 ? 0.5704 0.5006 0.4375 -0.0418 -0.0355 0.0296  433 ASP C N   
7892  C CA  . ASP C 132 ? 0.6337 0.5768 0.5025 -0.0461 -0.0374 0.0267  433 ASP C CA  
7893  C C   . ASP C 132 ? 0.6064 0.5432 0.4673 -0.0546 -0.0332 0.0230  433 ASP C C   
7894  O O   . ASP C 132 ? 0.8359 0.7691 0.6865 -0.0568 -0.0341 0.0238  433 ASP C O   
7895  C CB  . ASP C 132 ? 0.4399 0.3947 0.3052 -0.0423 -0.0448 0.0294  433 ASP C CB  
7896  C CG  . ASP C 132 ? 0.7128 0.6880 0.5830 -0.0467 -0.0478 0.0266  433 ASP C CG  
7897  O OD1 . ASP C 132 ? 0.7366 0.7281 0.6090 -0.0403 -0.0540 0.0291  433 ASP C OD1 
7898  O OD2 . ASP C 132 ? 0.5080 0.4831 0.3788 -0.0564 -0.0441 0.0222  433 ASP C OD2 
7899  N N   . ALA C 133 ? 0.5773 0.5105 0.4410 -0.0587 -0.0284 0.0191  434 ALA C N   
7900  C CA  . ALA C 133 ? 0.5756 0.4991 0.4295 -0.0652 -0.0239 0.0147  434 ALA C CA  
7901  C C   . ALA C 133 ? 0.5485 0.4763 0.3986 -0.0741 -0.0255 0.0107  434 ALA C C   
7902  O O   . ALA C 133 ? 0.4977 0.4129 0.3398 -0.0795 -0.0209 0.0061  434 ALA C O   
7903  C CB  . ALA C 133 ? 0.6031 0.5146 0.4586 -0.0623 -0.0167 0.0133  434 ALA C CB  
7904  N N   . ARG C 134 ? 0.4521 0.3979 0.3070 -0.0755 -0.0319 0.0122  435 ARG C N   
7905  C CA  . ARG C 134 ? 0.5634 0.5182 0.4162 -0.0863 -0.0337 0.0085  435 ARG C CA  
7906  C C   . ARG C 134 ? 0.6425 0.5933 0.4804 -0.0958 -0.0345 0.0043  435 ARG C C   
7907  O O   . ARG C 134 ? 0.8139 0.7660 0.6457 -0.1078 -0.0347 -0.0001 435 ARG C O   
7908  C CB  . ARG C 134 ? 0.5789 0.5603 0.4424 -0.0842 -0.0404 0.0114  435 ARG C CB  
7909  C CG  . ARG C 134 ? 0.5573 0.5440 0.4340 -0.0780 -0.0391 0.0136  435 ARG C CG  
7910  C CD  . ARG C 134 ? 0.4490 0.4651 0.3355 -0.0744 -0.0455 0.0158  435 ARG C CD  
7911  N NE  . ARG C 134 ? 0.4625 0.4826 0.3495 -0.0613 -0.0501 0.0201  435 ARG C NE  
7912  C CZ  . ARG C 134 ? 0.5092 0.5536 0.4015 -0.0541 -0.0565 0.0225  435 ARG C CZ  
7913  N NH1 . ARG C 134 ? 0.4522 0.5240 0.3517 -0.0604 -0.0587 0.0207  435 ARG C NH1 
7914  N NH2 . ARG C 134 ? 0.5435 0.5851 0.4326 -0.0409 -0.0605 0.0268  435 ARG C NH2 
7915  N N   . ASP C 135 ? 0.5781 0.5239 0.4084 -0.0919 -0.0349 0.0055  436 ASP C N   
7916  C CA  . ASP C 135 ? 0.5669 0.5082 0.3815 -0.1006 -0.0351 0.0010  436 ASP C CA  
7917  C C   . ASP C 135 ? 0.7178 0.6341 0.5209 -0.1036 -0.0270 -0.0046 436 ASP C C   
7918  O O   . ASP C 135 ? 0.8134 0.7215 0.6007 -0.1107 -0.0259 -0.0098 436 ASP C O   
7919  C CB  . ASP C 135 ? 0.6378 0.5841 0.4473 -0.0954 -0.0385 0.0049  436 ASP C CB  
7920  C CG  . ASP C 135 ? 0.7414 0.6734 0.5505 -0.0870 -0.0332 0.0077  436 ASP C CG  
7921  O OD1 . ASP C 135 ? 0.7254 0.6567 0.5267 -0.0849 -0.0342 0.0105  436 ASP C OD1 
7922  O OD2 . ASP C 135 ? 0.8599 0.7828 0.6762 -0.0832 -0.0280 0.0073  436 ASP C OD2 
7923  N N   . CYS C 136 ? 0.5859 0.4903 0.3953 -0.0974 -0.0215 -0.0039 437 CYS C N   
7924  C CA  . CYS C 136 ? 0.6446 0.5257 0.4433 -0.0960 -0.0136 -0.0085 437 CYS C CA  
7925  C C   . CYS C 136 ? 0.6983 0.5644 0.4824 -0.1076 -0.0121 -0.0151 437 CYS C C   
7926  O O   . CYS C 136 ? 0.6864 0.5614 0.4733 -0.1173 -0.0161 -0.0154 437 CYS C O   
7927  C CB  . CYS C 136 ? 0.5950 0.4706 0.4046 -0.0860 -0.0091 -0.0053 437 CYS C CB  
7928  S SG  . CYS C 136 ? 0.7679 0.6209 0.5665 -0.0783 0.0004  -0.0092 437 CYS C SG  
7929  N N   . THR C 137 ? 0.7049 0.5483 0.4715 -0.1073 -0.0061 -0.0209 438 THR C N   
7930  C CA  . THR C 137 ? 0.6183 0.4404 0.3653 -0.1191 -0.0042 -0.0282 438 THR C CA  
7931  C C   . THR C 137 ? 0.6317 0.4212 0.3633 -0.1121 0.0044  -0.0327 438 THR C C   
7932  O O   . THR C 137 ? 0.6353 0.4013 0.3505 -0.1211 0.0063  -0.0375 438 THR C O   
7933  C CB  . THR C 137 ? 0.7260 0.5514 0.4581 -0.1296 -0.0076 -0.0334 438 THR C CB  
7934  O OG1 . THR C 137 ? 0.7098 0.5237 0.4301 -0.1215 -0.0024 -0.0366 438 THR C OG1 
7935  C CG2 . THR C 137 ? 0.6143 0.4734 0.3600 -0.1328 -0.0164 -0.0282 438 THR C CG2 
7936  N N   . THR C 138 ? 0.7073 0.4945 0.4420 -0.0968 0.0097  -0.0313 439 THR C N   
7937  C CA  . THR C 138 ? 0.7501 0.5095 0.4704 -0.0867 0.0179  -0.0354 439 THR C CA  
7938  C C   . THR C 138 ? 0.8301 0.5966 0.5663 -0.0709 0.0214  -0.0296 439 THR C C   
7939  O O   . THR C 138 ? 0.7104 0.5026 0.4669 -0.0670 0.0185  -0.0234 439 THR C O   
7940  C CB  . THR C 138 ? 0.8755 0.6256 0.5787 -0.0817 0.0226  -0.0416 439 THR C CB  
7941  O OG1 . THR C 138 ? 1.0053 0.7831 0.7229 -0.0760 0.0214  -0.0373 439 THR C OG1 
7942  C CG2 . THR C 138 ? 0.8746 0.6112 0.5563 -0.0970 0.0204  -0.0492 439 THR C CG2 
7943  N N   . ALA C 139 ? 0.8757 0.6172 0.5999 -0.0614 0.0278  -0.0320 440 ALA C N   
7944  C CA  . ALA C 139 ? 0.7987 0.5469 0.5346 -0.0446 0.0319  -0.0275 440 ALA C CA  
7945  C C   . ALA C 139 ? 0.8053 0.5776 0.5511 -0.0356 0.0338  -0.0263 440 ALA C C   
7946  O O   . ALA C 139 ? 0.8606 0.6528 0.6242 -0.0272 0.0342  -0.0207 440 ALA C O   
7947  C CB  . ALA C 139 ? 0.8691 0.5843 0.5852 -0.0338 0.0387  -0.0312 440 ALA C CB  
7948  N N   . HIS C 140 ? 0.7816 0.5528 0.5148 -0.0382 0.0353  -0.0315 441 HIS C N   
7949  C CA  . HIS C 140 ? 0.6680 0.4638 0.4095 -0.0327 0.0371  -0.0298 441 HIS C CA  
7950  C C   . HIS C 140 ? 0.5953 0.4162 0.3549 -0.0417 0.0300  -0.0231 441 HIS C C   
7951  O O   . HIS C 140 ? 0.6343 0.4762 0.4079 -0.0371 0.0304  -0.0181 441 HIS C O   
7952  C CB  . HIS C 140 ? 0.7666 0.5542 0.4880 -0.0337 0.0407  -0.0371 441 HIS C CB  
7953  C CG  . HIS C 140 ? 0.7834 0.5528 0.4881 -0.0188 0.0495  -0.0434 441 HIS C CG  
7954  N ND1 . HIS C 140 ? 0.7258 0.5134 0.4356 -0.0044 0.0557  -0.0428 441 HIS C ND1 
7955  C CD2 . HIS C 140 ? 0.7800 0.5141 0.4610 -0.0156 0.0532  -0.0505 441 HIS C CD2 
7956  C CE1 . HIS C 140 ? 0.7046 0.4711 0.3959 0.0094  0.0629  -0.0493 441 HIS C CE1 
7957  N NE2 . HIS C 140 ? 0.8027 0.5334 0.4749 0.0031  0.0616  -0.0541 441 HIS C NE2 
7958  N N   . GLY C 141 ? 0.6909 0.5102 0.4495 -0.0546 0.0233  -0.0230 442 GLY C N   
7959  C CA  . GLY C 141 ? 0.6840 0.5245 0.4589 -0.0602 0.0163  -0.0162 442 GLY C CA  
7960  C C   . GLY C 141 ? 0.7941 0.6436 0.5874 -0.0543 0.0155  -0.0103 442 GLY C C   
7961  O O   . GLY C 141 ? 0.8736 0.7398 0.6791 -0.0526 0.0135  -0.0049 442 GLY C O   
7962  N N   . MET C 142 ? 0.7735 0.6100 0.5669 -0.0518 0.0172  -0.0112 443 MET C N   
7963  C CA  . MET C 142 ? 0.6596 0.5045 0.4693 -0.0463 0.0164  -0.0058 443 MET C CA  
7964  C C   . MET C 142 ? 0.6434 0.5006 0.4608 -0.0357 0.0207  -0.0034 443 MET C C   
7965  O O   . MET C 142 ? 0.7691 0.6420 0.6011 -0.0348 0.0182  0.0017  443 MET C O   
7966  C CB  . MET C 142 ? 0.5906 0.4170 0.3951 -0.0454 0.0183  -0.0072 443 MET C CB  
7967  C CG  . MET C 142 ? 0.5459 0.3685 0.3488 -0.0581 0.0132  -0.0076 443 MET C CG  
7968  S SD  . MET C 142 ? 0.7745 0.5674 0.5625 -0.0601 0.0169  -0.0100 443 MET C SD  
7969  C CE  . MET C 142 ? 0.7046 0.5081 0.5106 -0.0511 0.0170  -0.0031 443 MET C CE  
7970  N N   . PHE C 143 ? 0.6905 0.5419 0.4973 -0.0280 0.0272  -0.0073 444 PHE C N   
7971  C CA  . PHE C 143 ? 0.5053 0.3745 0.3199 -0.0187 0.0315  -0.0053 444 PHE C CA  
7972  C C   . PHE C 143 ? 0.6249 0.5144 0.4474 -0.0255 0.0286  -0.0015 444 PHE C C   
7973  O O   . PHE C 143 ? 0.6613 0.5679 0.4965 -0.0242 0.0281  0.0030  444 PHE C O   
7974  C CB  . PHE C 143 ? 0.8246 0.6854 0.6245 -0.0085 0.0391  -0.0109 444 PHE C CB  
7975  C CG  . PHE C 143 ? 0.7802 0.6650 0.5872 0.0010  0.0441  -0.0096 444 PHE C CG  
7976  C CD1 . PHE C 143 ? 0.7598 0.6554 0.5600 0.0006  0.0478  -0.0122 444 PHE C CD1 
7977  C CD2 . PHE C 143 ? 0.6572 0.5563 0.4774 0.0095  0.0453  -0.0057 444 PHE C CD2 
7978  C CE1 . PHE C 143 ? 0.7630 0.6851 0.5702 0.0079  0.0528  -0.0109 444 PHE C CE1 
7979  C CE2 . PHE C 143 ? 0.7261 0.6521 0.5534 0.0169  0.0498  -0.0046 444 PHE C CE2 
7980  C CZ  . PHE C 143 ? 0.7576 0.6960 0.5788 0.0157  0.0537  -0.0071 444 PHE C CZ  
7981  N N   . ASN C 144 ? 0.6651 0.5518 0.4783 -0.0337 0.0263  -0.0031 445 ASN C N   
7982  C CA  . ASN C 144 ? 0.7064 0.6077 0.5229 -0.0405 0.0234  0.0011  445 ASN C CA  
7983  C C   . ASN C 144 ? 0.6560 0.5621 0.4851 -0.0448 0.0167  0.0070  445 ASN C C   
7984  O O   . ASN C 144 ? 0.6827 0.6006 0.5189 -0.0463 0.0160  0.0116  445 ASN C O   
7985  C CB  . ASN C 144 ? 0.7055 0.6004 0.5073 -0.0475 0.0217  -0.0019 445 ASN C CB  
7986  C CG  . ASN C 144 ? 0.7602 0.6663 0.5611 -0.0547 0.0183  0.0032  445 ASN C CG  
7987  O OD1 . ASN C 144 ? 0.7615 0.6646 0.5593 -0.0612 0.0117  0.0053  445 ASN C OD1 
7988  N ND2 . ASN C 144 ? 0.7920 0.7115 0.5940 -0.0536 0.0229  0.0052  445 ASN C ND2 
7989  N N   . TYR C 145 ? 0.6931 0.5901 0.5240 -0.0472 0.0119  0.0067  446 TYR C N   
7990  C CA  . TYR C 145 ? 0.8112 0.7127 0.6532 -0.0492 0.0059  0.0115  446 TYR C CA  
7991  C C   . TYR C 145 ? 0.7637 0.6714 0.6177 -0.0437 0.0078  0.0139  446 TYR C C   
7992  O O   . TYR C 145 ? 0.6161 0.5296 0.4774 -0.0452 0.0043  0.0180  446 TYR C O   
7993  C CB  . TYR C 145 ? 0.7479 0.6428 0.5897 -0.0524 0.0015  0.0100  446 TYR C CB  
7994  C CG  . TYR C 145 ? 0.6245 0.5223 0.4614 -0.0586 -0.0047 0.0110  446 TYR C CG  
7995  C CD1 . TYR C 145 ? 0.6469 0.5396 0.4728 -0.0643 -0.0056 0.0067  446 TYR C CD1 
7996  C CD2 . TYR C 145 ? 0.4727 0.3775 0.3143 -0.0585 -0.0101 0.0163  446 TYR C CD2 
7997  C CE1 . TYR C 145 ? 0.5282 0.4275 0.3502 -0.0694 -0.0119 0.0079  446 TYR C CE1 
7998  C CE2 . TYR C 145 ? 0.5213 0.4297 0.3577 -0.0617 -0.0162 0.0179  446 TYR C CE2 
7999  C CZ  . TYR C 145 ? 0.5856 0.4936 0.4133 -0.0671 -0.0173 0.0139  446 TYR C CZ  
8000  O OH  . TYR C 145 ? 0.8300 0.7454 0.6530 -0.0697 -0.0239 0.0158  446 TYR C OH  
8001  N N   . ILE C 146 ? 0.6887 0.5940 0.5431 -0.0370 0.0131  0.0113  447 ILE C N   
8002  C CA  . ILE C 146 ? 0.6106 0.5238 0.4757 -0.0311 0.0148  0.0135  447 ILE C CA  
8003  C C   . ILE C 146 ? 0.6765 0.6065 0.5455 -0.0303 0.0177  0.0155  447 ILE C C   
8004  O O   . ILE C 146 ? 0.6219 0.5620 0.5002 -0.0312 0.0161  0.0187  447 ILE C O   
8005  C CB  . ILE C 146 ? 0.5244 0.4277 0.3861 -0.0229 0.0191  0.0107  447 ILE C CB  
8006  C CG1 . ILE C 146 ? 0.5272 0.4176 0.3888 -0.0262 0.0156  0.0107  447 ILE C CG1 
8007  C CG2 . ILE C 146 ? 0.4571 0.3730 0.3273 -0.0145 0.0223  0.0127  447 ILE C CG2 
8008  C CD1 . ILE C 146 ? 0.5309 0.4053 0.3851 -0.0201 0.0195  0.0086  447 ILE C CD1 
8009  N N   . CYS C 147 ? 0.6471 0.5813 0.5080 -0.0298 0.0221  0.0133  448 CYS C N   
8010  C CA  . CYS C 147 ? 0.4886 0.4425 0.3525 -0.0314 0.0252  0.0152  448 CYS C CA  
8011  C C   . CYS C 147 ? 0.5742 0.5306 0.4394 -0.0425 0.0202  0.0198  448 CYS C C   
8012  O O   . CYS C 147 ? 0.6515 0.6214 0.5226 -0.0462 0.0205  0.0227  448 CYS C O   
8013  C CB  . CYS C 147 ? 0.6110 0.5691 0.4644 -0.0294 0.0309  0.0117  448 CYS C CB  
8014  S SG  . CYS C 147 ? 0.7008 0.6628 0.5513 -0.0131 0.0391  0.0066  448 CYS C SG  
8015  N N   . ASN C 148 ? 0.7636 0.7065 0.6214 -0.0480 0.0155  0.0206  449 ASN C N   
8016  C CA  . ASN C 148 ? 0.6457 0.5859 0.5016 -0.0563 0.0105  0.0255  449 ASN C CA  
8017  C C   . ASN C 148 ? 0.5590 0.4969 0.4243 -0.0553 0.0065  0.0275  449 ASN C C   
8018  O O   . ASN C 148 ? 0.5534 0.4932 0.4188 -0.0610 0.0049  0.0309  449 ASN C O   
8019  C CB  . ASN C 148 ? 0.5456 0.4732 0.3913 -0.0596 0.0057  0.0262  449 ASN C CB  
8020  C CG  . ASN C 148 ? 0.6084 0.5378 0.4432 -0.0611 0.0095  0.0235  449 ASN C CG  
8021  O OD1 . ASN C 148 ? 0.6023 0.5430 0.4347 -0.0623 0.0151  0.0231  449 ASN C OD1 
8022  N ND2 . ASN C 148 ? 0.5797 0.4998 0.4073 -0.0613 0.0063  0.0215  449 ASN C ND2 
8023  N N   . HIS C 149 ? 0.5834 0.5168 0.4551 -0.0489 0.0053  0.0254  450 HIS C N   
8024  C CA  . HIS C 149 ? 0.5467 0.4801 0.4273 -0.0471 0.0025  0.0268  450 HIS C CA  
8025  C C   . HIS C 149 ? 0.5357 0.4831 0.4224 -0.0479 0.0056  0.0277  450 HIS C C   
8026  O O   . HIS C 149 ? 0.4781 0.4259 0.3653 -0.0533 0.0030  0.0301  450 HIS C O   
8027  C CB  . HIS C 149 ? 0.5795 0.5086 0.4652 -0.0408 0.0022  0.0244  450 HIS C CB  
8028  C CG  . HIS C 149 ? 0.5246 0.4547 0.4189 -0.0386 -0.0005 0.0256  450 HIS C CG  
8029  N ND1 . HIS C 149 ? 0.5067 0.4318 0.4039 -0.0362 -0.0032 0.0249  450 HIS C ND1 
8030  C CD2 . HIS C 149 ? 0.5104 0.4474 0.4101 -0.0392 -0.0008 0.0271  450 HIS C CD2 
8031  C CE1 . HIS C 149 ? 0.5640 0.4925 0.4682 -0.0343 -0.0047 0.0260  450 HIS C CE1 
8032  N NE2 . HIS C 149 ? 0.5280 0.4626 0.4333 -0.0361 -0.0036 0.0271  450 HIS C NE2 
8033  N N   . VAL C 150 ? 0.4089 0.3679 0.2991 -0.0421 0.0111  0.0256  451 VAL C N   
8034  C CA  . VAL C 150 ? 0.4047 0.3832 0.3019 -0.0418 0.0141  0.0264  451 VAL C CA  
8035  C C   . VAL C 150 ? 0.6311 0.6176 0.5244 -0.0536 0.0137  0.0289  451 VAL C C   
8036  O O   . VAL C 150 ? 0.6446 0.6388 0.5417 -0.0593 0.0121  0.0306  451 VAL C O   
8037  C CB  . VAL C 150 ? 0.4071 0.3982 0.3056 -0.0320 0.0205  0.0239  451 VAL C CB  
8038  C CG1 . VAL C 150 ? 0.4042 0.4225 0.3096 -0.0326 0.0237  0.0249  451 VAL C CG1 
8039  C CG2 . VAL C 150 ? 0.4052 0.3866 0.3063 -0.0213 0.0208  0.0224  451 VAL C CG2 
8040  N N   . LYS C 151 ? 0.6131 0.5967 0.4969 -0.0586 0.0150  0.0294  452 LYS C N   
8041  C CA  . LYS C 151 ? 0.4980 0.4902 0.3760 -0.0709 0.0159  0.0323  452 LYS C CA  
8042  C C   . LYS C 151 ? 0.4939 0.4673 0.3649 -0.0802 0.0097  0.0357  452 LYS C C   
8043  O O   . LYS C 151 ? 0.5339 0.5124 0.4023 -0.0909 0.0094  0.0379  452 LYS C O   
8044  C CB  . LYS C 151 ? 0.4379 0.4319 0.3062 -0.0734 0.0193  0.0320  452 LYS C CB  
8045  C CG  . LYS C 151 ? 0.5095 0.5147 0.3705 -0.0876 0.0213  0.0355  452 LYS C CG  
8046  C CD  . LYS C 151 ? 0.5229 0.5315 0.3736 -0.0891 0.0254  0.0350  452 LYS C CD  
8047  C CE  . LYS C 151 ? 0.4707 0.4971 0.3148 -0.1033 0.0292  0.0383  452 LYS C CE  
8048  N NZ  . LYS C 151 ? 0.6358 0.6678 0.4691 -0.1047 0.0337  0.0378  452 LYS C NZ  
8049  N N   . TYR C 152 ? 0.5432 0.4948 0.4097 -0.0762 0.0048  0.0360  453 TYR C N   
8050  C CA  . TYR C 152 ? 0.5953 0.5274 0.4544 -0.0810 -0.0011 0.0389  453 TYR C CA  
8051  C C   . TYR C 152 ? 0.6615 0.5960 0.5286 -0.0802 -0.0026 0.0378  453 TYR C C   
8052  O O   . TYR C 152 ? 0.6875 0.6138 0.5475 -0.0889 -0.0048 0.0396  453 TYR C O   
8053  C CB  . TYR C 152 ? 0.5005 0.4149 0.3551 -0.0741 -0.0060 0.0392  453 TYR C CB  
8054  C CG  . TYR C 152 ? 0.6745 0.5695 0.5225 -0.0739 -0.0120 0.0414  453 TYR C CG  
8055  C CD1 . TYR C 152 ? 0.7062 0.5830 0.5376 -0.0795 -0.0153 0.0457  453 TYR C CD1 
8056  C CD2 . TYR C 152 ? 0.6737 0.5674 0.5303 -0.0675 -0.0143 0.0393  453 TYR C CD2 
8057  C CE1 . TYR C 152 ? 0.7185 0.5743 0.5409 -0.0771 -0.0206 0.0476  453 TYR C CE1 
8058  C CE2 . TYR C 152 ? 0.6952 0.5706 0.5441 -0.0656 -0.0193 0.0407  453 TYR C CE2 
8059  C CZ  . TYR C 152 ? 0.7453 0.6009 0.5766 -0.0698 -0.0225 0.0447  453 TYR C CZ  
8060  O OH  . TYR C 152 ? 0.8430 0.6768 0.6635 -0.0658 -0.0274 0.0460  453 TYR C OH  
8061  N N   . ALA C 153 ? 0.5907 0.5339 0.4704 -0.0703 -0.0016 0.0349  454 ALA C N   
8062  C CA  . ALA C 153 ? 0.5613 0.5072 0.4483 -0.0683 -0.0033 0.0338  454 ALA C CA  
8063  C C   . ALA C 153 ? 0.5154 0.4802 0.4057 -0.0762 -0.0006 0.0339  454 ALA C C   
8064  O O   . ALA C 153 ? 0.6222 0.5841 0.5111 -0.0818 -0.0032 0.0338  454 ALA C O   
8065  C CB  . ALA C 153 ? 0.4197 0.3708 0.3176 -0.0566 -0.0024 0.0314  454 ALA C CB  
8066  N N   . THR C 154 ? 0.4685 0.4544 0.3626 -0.0768 0.0045  0.0337  455 THR C N   
8067  C CA  . THR C 154 ? 0.4475 0.4587 0.3465 -0.0840 0.0072  0.0338  455 THR C CA  
8068  C C   . THR C 154 ? 0.5651 0.5704 0.4519 -0.1019 0.0058  0.0362  455 THR C C   
8069  O O   . THR C 154 ? 0.5580 0.5716 0.4449 -0.1116 0.0046  0.0361  455 THR C O   
8070  C CB  . THR C 154 ? 0.5235 0.5607 0.4293 -0.0773 0.0135  0.0328  455 THR C CB  
8071  O OG1 . THR C 154 ? 0.4834 0.5191 0.3965 -0.0611 0.0146  0.0308  455 THR C OG1 
8072  C CG2 . THR C 154 ? 0.4063 0.4767 0.3189 -0.0835 0.0163  0.0331  455 THR C CG2 
8073  N N   . ASN C 155 ? 0.6729 0.6625 0.5472 -0.1074 0.0056  0.0386  456 ASN C N   
8074  C CA  . ASN C 155 ? 0.6633 0.6366 0.5207 -0.1242 0.0036  0.0419  456 ASN C CA  
8075  C C   . ASN C 155 ? 0.6451 0.6416 0.5028 -0.1402 0.0060  0.0423  456 ASN C C   
8076  O O   . ASN C 155 ? 0.6360 0.6177 0.4821 -0.1540 0.0030  0.0433  456 ASN C O   
8077  C CB  . ASN C 155 ? 0.6165 0.5546 0.4630 -0.1232 -0.0029 0.0425  456 ASN C CB  
8078  C CG  . ASN C 155 ? 0.8267 0.7386 0.6506 -0.1380 -0.0053 0.0465  456 ASN C CG  
8079  O OD1 . ASN C 155 ? 0.9829 0.8953 0.7977 -0.1454 -0.0030 0.0498  456 ASN C OD1 
8080  N ND2 . ASN C 155 ? 0.7370 0.6238 0.5496 -0.1422 -0.0097 0.0464  456 ASN C ND2 
8081  N N   . LYS C 156 ? 0.6397 0.6732 0.5093 -0.1387 0.0117  0.0413  457 LYS C N   
8082  C CA  . LYS C 156 ? 0.6607 0.7256 0.5325 -0.1542 0.0146  0.0418  457 LYS C CA  
8083  C C   . LYS C 156 ? 0.7224 0.7944 0.5999 -0.1582 0.0115  0.0398  457 LYS C C   
8084  O O   . LYS C 156 ? 0.8122 0.8964 0.6844 -0.1771 0.0113  0.0404  457 LYS C O   
8085  C CB  . LYS C 156 ? 0.7668 0.8202 0.6195 -0.1761 0.0150  0.0457  457 LYS C CB  
8086  C CG  . LYS C 156 ? 0.7574 0.8147 0.6042 -0.1760 0.0193  0.0481  457 LYS C CG  
8087  C CD  . LYS C 156 ? 0.9109 0.9462 0.7344 -0.1976 0.0184  0.0532  457 LYS C CD  
8088  C CE  . LYS C 156 ? 0.9454 0.9875 0.7618 -0.1995 0.0230  0.0559  457 LYS C CE  
8089  N NZ  . LYS C 156 ? 0.9669 1.0602 0.7981 -0.1990 0.0306  0.0538  457 LYS C NZ  
8090  N N   . GLY C 157 ? 0.8206 0.8852 0.7076 -0.1419 0.0089  0.0373  458 GLY C N   
8091  C CA  . GLY C 157 ? 0.7586 0.8303 0.6511 -0.1435 0.0058  0.0351  458 GLY C CA  
8092  C C   . GLY C 157 ? 0.7634 0.7960 0.6427 -0.1480 0.0000  0.0344  458 GLY C C   
8093  O O   . GLY C 157 ? 0.7928 0.8277 0.6767 -0.1456 -0.0027 0.0318  458 GLY C O   
8094  N N   . ASN C 158 ? 0.6360 0.6333 0.4978 -0.1535 -0.0021 0.0365  459 ASN C N   
8095  C CA  . ASN C 158 ? 0.5887 0.5465 0.4365 -0.1533 -0.0075 0.0356  459 ASN C CA  
8096  C C   . ASN C 158 ? 0.7055 0.6484 0.5595 -0.1325 -0.0090 0.0352  459 ASN C C   
8097  O O   . ASN C 158 ? 0.7437 0.6631 0.5879 -0.1286 -0.0104 0.0374  459 ASN C O   
8098  C CB  . ASN C 158 ? 0.6154 0.5418 0.4385 -0.1696 -0.0092 0.0387  459 ASN C CB  
8099  C CG  . ASN C 158 ? 0.8600 0.7412 0.6660 -0.1645 -0.0147 0.0381  459 ASN C CG  
8100  O OD1 . ASN C 158 ? 1.0227 0.8989 0.8326 -0.1571 -0.0173 0.0343  459 ASN C OD1 
8101  N ND2 . ASN C 158 ? 0.8349 0.6838 0.6212 -0.1671 -0.0164 0.0420  459 ASN C ND2 
8102  N N   . LEU C 159 ? 0.7036 0.6615 0.5734 -0.1197 -0.0090 0.0324  460 LEU C N   
8103  C CA  . LEU C 159 ? 0.6093 0.5639 0.4884 -0.1018 -0.0089 0.0320  460 LEU C CA  
8104  C C   . LEU C 159 ? 0.6849 0.6060 0.5530 -0.0960 -0.0133 0.0322  460 LEU C C   
8105  O O   . LEU C 159 ? 0.6362 0.5358 0.4915 -0.1011 -0.0168 0.0315  460 LEU C O   
8106  C CB  . LEU C 159 ? 0.4415 0.4152 0.3362 -0.0912 -0.0082 0.0297  460 LEU C CB  
8107  C CG  . LEU C 159 ? 0.5701 0.5799 0.4775 -0.0911 -0.0042 0.0296  460 LEU C CG  
8108  C CD1 . LEU C 159 ? 0.5316 0.5513 0.4517 -0.0743 -0.0026 0.0290  460 LEU C CD1 
8109  C CD2 . LEU C 159 ? 0.5860 0.6127 0.4929 -0.0975 0.0000  0.0313  460 LEU C CD2 
8110  N N   . ARG C 160 ? 0.5009 0.4185 0.3732 -0.0847 -0.0131 0.0330  461 ARG C N   
8111  C CA  . ARG C 160 ? 0.4909 0.3853 0.3566 -0.0763 -0.0172 0.0332  461 ARG C CA  
8112  C C   . ARG C 160 ? 0.5574 0.4617 0.4368 -0.0630 -0.0167 0.0315  461 ARG C C   
8113  O O   . ARG C 160 ? 0.6579 0.5794 0.5475 -0.0600 -0.0131 0.0312  461 ARG C O   
8114  C CB  . ARG C 160 ? 0.5759 0.4545 0.4286 -0.0789 -0.0183 0.0366  461 ARG C CB  
8115  C CG  . ARG C 160 ? 0.7686 0.6309 0.6033 -0.0932 -0.0192 0.0390  461 ARG C CG  
8116  C CD  . ARG C 160 ? 0.8441 0.6910 0.6644 -0.0962 -0.0201 0.0433  461 ARG C CD  
8117  N NE  . ARG C 160 ? 0.8046 0.6730 0.6312 -0.1010 -0.0154 0.0445  461 ARG C NE  
8118  C CZ  . ARG C 160 ? 0.7874 0.6481 0.6016 -0.1068 -0.0149 0.0483  461 ARG C CZ  
8119  N NH1 . ARG C 160 ? 0.8545 0.6849 0.6489 -0.1081 -0.0193 0.0521  461 ARG C NH1 
8120  N NH2 . ARG C 160 ? 0.7653 0.6474 0.5852 -0.1101 -0.0101 0.0485  461 ARG C NH2 
8121  N N   . SER C 161 ? 0.5841 0.4770 0.4625 -0.0551 -0.0202 0.0303  462 SER C N   
8122  C CA  . SER C 161 ? 0.6697 0.5723 0.5597 -0.0449 -0.0198 0.0290  462 SER C CA  
8123  C C   . SER C 161 ? 0.6379 0.5373 0.5261 -0.0415 -0.0206 0.0305  462 SER C C   
8124  O O   . SER C 161 ? 0.5874 0.4727 0.4641 -0.0429 -0.0233 0.0325  462 SER C O   
8125  C CB  . SER C 161 ? 0.6853 0.5826 0.5760 -0.0378 -0.0227 0.0269  462 SER C CB  
8126  O OG  . SER C 161 ? 0.8125 0.6909 0.6896 -0.0406 -0.0257 0.0263  462 SER C OG  
8127  N N   . ALA C 162 ? 0.4428 0.3539 0.3405 -0.0374 -0.0183 0.0296  463 ALA C N   
8128  C CA  . ALA C 162 ? 0.4011 0.3111 0.2965 -0.0364 -0.0188 0.0303  463 ALA C CA  
8129  C C   . ALA C 162 ? 0.4774 0.3968 0.3815 -0.0326 -0.0169 0.0286  463 ALA C C   
8130  O O   . ALA C 162 ? 0.4469 0.3733 0.3575 -0.0317 -0.0135 0.0277  463 ALA C O   
8131  C CB  . ALA C 162 ? 0.4996 0.4100 0.3893 -0.0427 -0.0160 0.0315  463 ALA C CB  
8132  N N   . ILE C 163 ? 0.6495 0.5684 0.5520 -0.0312 -0.0191 0.0285  464 ILE C N   
8133  C CA  . ILE C 163 ? 0.5477 0.4727 0.4548 -0.0310 -0.0176 0.0268  464 ILE C CA  
8134  C C   . ILE C 163 ? 0.6904 0.6132 0.5906 -0.0344 -0.0182 0.0265  464 ILE C C   
8135  O O   . ILE C 163 ? 0.6374 0.5569 0.5312 -0.0346 -0.0218 0.0281  464 ILE C O   
8136  C CB  . ILE C 163 ? 0.4973 0.4292 0.4103 -0.0272 -0.0204 0.0263  464 ILE C CB  
8137  C CG1 . ILE C 163 ? 0.5133 0.4508 0.4299 -0.0298 -0.0180 0.0249  464 ILE C CG1 
8138  C CG2 . ILE C 163 ? 0.4294 0.3622 0.3387 -0.0238 -0.0258 0.0273  464 ILE C CG2 
8139  C CD1 . ILE C 163 ? 0.3746 0.3232 0.2978 -0.0276 -0.0199 0.0247  464 ILE C CD1 
8140  N N   . THR C 164 ? 0.6139 0.5363 0.5131 -0.0370 -0.0146 0.0244  465 THR C N   
8141  C CA  . THR C 164 ? 0.6778 0.5974 0.5691 -0.0412 -0.0147 0.0230  465 THR C CA  
8142  C C   . THR C 164 ? 0.5624 0.4845 0.4548 -0.0442 -0.0150 0.0208  465 THR C C   
8143  O O   . THR C 164 ? 0.5606 0.4794 0.4550 -0.0440 -0.0114 0.0198  465 THR C O   
8144  C CB  . THR C 164 ? 0.6291 0.5433 0.5145 -0.0423 -0.0093 0.0215  465 THR C CB  
8145  O OG1 . THR C 164 ? 0.5299 0.4446 0.4123 -0.0428 -0.0094 0.0237  465 THR C OG1 
8146  C CG2 . THR C 164 ? 0.6197 0.5288 0.4958 -0.0466 -0.0083 0.0184  465 THR C CG2 
8147  N N   . ILE C 165 ? 0.5264 0.4549 0.4165 -0.0475 -0.0195 0.0204  466 ILE C N   
8148  C CA  . ILE C 165 ? 0.5430 0.4793 0.4354 -0.0524 -0.0209 0.0188  466 ILE C CA  
8149  C C   . ILE C 165 ? 0.5678 0.5004 0.4500 -0.0611 -0.0207 0.0156  466 ILE C C   
8150  O O   . ILE C 165 ? 0.5372 0.4759 0.4150 -0.0629 -0.0248 0.0156  466 ILE C O   
8151  C CB  . ILE C 165 ? 0.6109 0.5642 0.5107 -0.0488 -0.0266 0.0207  466 ILE C CB  
8152  C CG1 . ILE C 165 ? 0.4750 0.4292 0.3826 -0.0406 -0.0263 0.0227  466 ILE C CG1 
8153  C CG2 . ILE C 165 ? 0.7060 0.6725 0.6088 -0.0558 -0.0276 0.0190  466 ILE C CG2 
8154  C CD1 . ILE C 165 ? 0.3915 0.3607 0.3045 -0.0341 -0.0315 0.0241  466 ILE C CD1 
8155  N N   . PHE C 166 ? 0.6145 0.5361 0.4911 -0.0665 -0.0164 0.0128  467 PHE C N   
8156  C CA  . PHE C 166 ? 0.4474 0.3589 0.3107 -0.0755 -0.0151 0.0086  467 PHE C CA  
8157  C C   . PHE C 166 ? 0.5905 0.5143 0.4536 -0.0863 -0.0188 0.0072  467 PHE C C   
8158  O O   . PHE C 166 ? 0.7223 0.6643 0.5970 -0.0849 -0.0220 0.0098  467 PHE C O   
8159  C CB  . PHE C 166 ? 0.5123 0.4015 0.3668 -0.0744 -0.0082 0.0064  467 PHE C CB  
8160  C CG  . PHE C 166 ? 0.6026 0.4843 0.4550 -0.0654 -0.0044 0.0067  467 PHE C CG  
8161  C CD1 . PHE C 166 ? 0.5970 0.4766 0.4407 -0.0665 -0.0044 0.0045  467 PHE C CD1 
8162  C CD2 . PHE C 166 ? 0.5274 0.4070 0.3862 -0.0564 -0.0009 0.0090  467 PHE C CD2 
8163  C CE1 . PHE C 166 ? 0.5926 0.4692 0.4345 -0.0593 -0.0004 0.0047  467 PHE C CE1 
8164  C CE2 . PHE C 166 ? 0.5923 0.4704 0.4501 -0.0491 0.0026  0.0092  467 PHE C CE2 
8165  C CZ  . PHE C 166 ? 0.7158 0.5930 0.5654 -0.0508 0.0031  0.0070  467 PHE C CZ  
8166  N N   . PRO C 167 ? 0.6877 0.6041 0.5375 -0.0976 -0.0187 0.0029  468 PRO C N   
8167  C CA  . PRO C 167 ? 0.6318 0.5654 0.4819 -0.1102 -0.0230 0.0015  468 PRO C CA  
8168  C C   . PRO C 167 ? 0.6101 0.5477 0.4660 -0.1148 -0.0214 0.0029  468 PRO C C   
8169  O O   . PRO C 167 ? 0.7495 0.6655 0.6003 -0.1138 -0.0159 0.0030  468 PRO C O   
8170  C CB  . PRO C 167 ? 0.6855 0.6019 0.5161 -0.1227 -0.0215 -0.0043 468 PRO C CB  
8171  C CG  . PRO C 167 ? 0.6781 0.5803 0.5020 -0.1138 -0.0191 -0.0052 468 PRO C CG  
8172  C CD  . PRO C 167 ? 0.7115 0.6066 0.5448 -0.1000 -0.0151 -0.0015 468 PRO C CD  
8173  N N   . GLN C 168 ? 0.7078 0.6747 0.5738 -0.1197 -0.0262 0.0042  469 GLN C N   
8174  C CA  . GLN C 168 ? 0.7279 0.7035 0.5993 -0.1260 -0.0247 0.0055  469 GLN C CA  
8175  C C   . GLN C 168 ? 0.8251 0.7810 0.6793 -0.1443 -0.0213 0.0020  469 GLN C C   
8176  O O   . GLN C 168 ? 0.8137 0.7561 0.6528 -0.1539 -0.0215 -0.0024 469 GLN C O   
8177  C CB  . GLN C 168 ? 0.6951 0.7110 0.5807 -0.1268 -0.0304 0.0072  469 GLN C CB  
8178  C CG  . GLN C 168 ? 0.4622 0.4975 0.3434 -0.1383 -0.0356 0.0044  469 GLN C CG  
8179  C CD  . GLN C 168 ? 0.6016 0.6757 0.4977 -0.1285 -0.0423 0.0070  469 GLN C CD  
8180  O OE1 . GLN C 168 ? 0.5738 0.6470 0.4754 -0.1113 -0.0442 0.0097  469 GLN C OE1 
8181  N NE2 . GLN C 168 ? 0.5259 0.6345 0.4274 -0.1394 -0.0458 0.0063  469 GLN C NE2 
8182  N N   . ARG C 169 ? 0.8791 0.8312 0.7337 -0.1495 -0.0179 0.0040  470 ARG C N   
8183  C CA  . ARG C 169 ? 0.8572 0.7886 0.6936 -0.1685 -0.0147 0.0016  470 ARG C CA  
8184  C C   . ARG C 169 ? 0.8102 0.7697 0.6460 -0.1880 -0.0193 -0.0009 470 ARG C C   
8185  O O   . ARG C 169 ? 0.7695 0.7705 0.6233 -0.1860 -0.0239 0.0010  470 ARG C O   
8186  C CB  . ARG C 169 ? 0.8261 0.7480 0.6630 -0.1685 -0.0102 0.0056  470 ARG C CB  
8187  C CG  . ARG C 169 ? 0.8409 0.7377 0.6561 -0.1891 -0.0066 0.0043  470 ARG C CG  
8188  C CD  . ARG C 169 ? 0.7944 0.6836 0.6099 -0.1886 -0.0024 0.0094  470 ARG C CD  
8189  N NE  . ARG C 169 ? 0.8107 0.6687 0.6214 -0.1707 0.0019  0.0117  470 ARG C NE  
8190  C CZ  . ARG C 169 ? 0.9573 0.8184 0.7770 -0.1601 0.0040  0.0169  470 ARG C CZ  
8191  N NH1 . ARG C 169 ? 1.0384 0.9309 0.8718 -0.1654 0.0026  0.0199  470 ARG C NH1 
8192  N NH2 . ARG C 169 ? 0.9552 0.7913 0.7706 -0.1438 0.0075  0.0189  470 ARG C NH2 
8193  N N   . THR C 170 ? 0.7415 0.6792 0.5557 -0.2065 -0.0181 -0.0057 471 THR C N   
8194  C CA  . THR C 170 ? 0.7881 0.7534 0.5998 -0.2281 -0.0227 -0.0087 471 THR C CA  
8195  C C   . THR C 170 ? 0.8832 0.8339 0.6786 -0.2520 -0.0193 -0.0094 471 THR C C   
8196  O O   . THR C 170 ? 0.8780 0.8628 0.6848 -0.2621 -0.0208 -0.0068 471 THR C O   
8197  C CB  . THR C 170 ? 0.8289 0.7876 0.6284 -0.2327 -0.0259 -0.0144 471 THR C CB  
8198  O OG1 . THR C 170 ? 0.8683 0.7753 0.6405 -0.2388 -0.0206 -0.0189 471 THR C OG1 
8199  C CG2 . THR C 170 ? 0.7697 0.7418 0.5841 -0.2093 -0.0291 -0.0125 471 THR C CG2 
8200  N N   . ASP C 171 ? 0.9533 0.8537 0.7208 -0.2614 -0.0144 -0.0128 472 ASP C N   
8201  C CA  . ASP C 171 ? 1.0097 0.8887 0.7570 -0.2852 -0.0108 -0.0130 472 ASP C CA  
8202  C C   . ASP C 171 ? 1.0407 0.8717 0.7739 -0.2756 -0.0036 -0.0095 472 ASP C C   
8203  O O   . ASP C 171 ? 1.0962 0.8947 0.8052 -0.2936 0.0002  -0.0096 472 ASP C O   
8204  C CB  . ASP C 171 ? 1.0824 0.9410 0.8024 -0.3102 -0.0119 -0.0206 472 ASP C CB  
8205  C CG  . ASP C 171 ? 1.1347 0.9378 0.8294 -0.3016 -0.0079 -0.0256 472 ASP C CG  
8206  O OD1 . ASP C 171 ? 1.2000 0.9885 0.9019 -0.2754 -0.0053 -0.0234 472 ASP C OD1 
8207  O OD2 . ASP C 171 ? 1.1594 0.9339 0.8258 -0.3217 -0.0073 -0.0322 472 ASP C OD2 
8208  N N   . GLY C 172 ? 1.0073 0.8332 0.7537 -0.2482 -0.0020 -0.0062 473 GLY C N   
8209  C CA  . GLY C 172 ? 1.0807 0.8663 0.8158 -0.2358 0.0042  -0.0025 473 GLY C CA  
8210  C C   . GLY C 172 ? 1.2349 0.9670 0.9422 -0.2303 0.0084  -0.0069 473 GLY C C   
8211  O O   . GLY C 172 ? 1.3753 1.0852 1.0815 -0.2089 0.0122  -0.0046 473 GLY C O   
8212  N N   . LYS C 173 ? 1.2491 0.9614 0.9330 -0.2493 0.0080  -0.0136 474 LYS C N   
8213  C CA  . LYS C 173 ? 1.2439 0.9043 0.8986 -0.2441 0.0122  -0.0191 474 LYS C CA  
8214  C C   . LYS C 173 ? 1.2130 0.8842 0.8770 -0.2271 0.0104  -0.0234 474 LYS C C   
8215  O O   . LYS C 173 ? 1.1710 0.8041 0.8122 -0.2210 0.0140  -0.0287 474 LYS C O   
8216  C CB  . LYS C 173 ? 1.2328 0.8628 0.8543 -0.2733 0.0127  -0.0252 474 LYS C CB  
8217  C CG  . LYS C 173 ? 1.2446 0.8403 0.8431 -0.2890 0.0168  -0.0214 474 LYS C CG  
8218  C CD  . LYS C 173 ? 1.3527 0.9384 0.9266 -0.3252 0.0152  -0.0267 474 LYS C CD  
8219  C CE  . LYS C 173 ? 1.4359 0.9633 0.9717 -0.3410 0.0208  -0.0250 474 LYS C CE  
8220  N NZ  . LYS C 173 ? 1.4287 0.9479 0.9398 -0.3804 0.0191  -0.0301 474 LYS C NZ  
8221  N N   . HIS C 174 ? 1.1617 0.8823 0.8566 -0.2193 0.0053  -0.0211 475 HIS C N   
8222  C CA  . HIS C 174 ? 1.1387 0.8713 0.8430 -0.2038 0.0035  -0.0238 475 HIS C CA  
8223  C C   . HIS C 174 ? 1.0433 0.7992 0.7749 -0.1802 0.0033  -0.0175 475 HIS C C   
8224  O O   . HIS C 174 ? 1.0013 0.7875 0.7514 -0.1715 -0.0007 -0.0168 475 HIS C O   
8225  C CB  . HIS C 174 ? 1.1544 0.9218 0.8659 -0.2174 -0.0033 -0.0274 475 HIS C CB  
8226  C CG  . HIS C 174 ? 1.0906 0.8363 0.7740 -0.2409 -0.0037 -0.0351 475 HIS C CG  
8227  N ND1 . HIS C 174 ? 1.1176 0.8170 0.7712 -0.2538 0.0013  -0.0380 475 HIS C ND1 
8228  C CD2 . HIS C 174 ? 1.0036 0.7669 0.6825 -0.2546 -0.0087 -0.0406 475 HIS C CD2 
8229  C CE1 . HIS C 174 ? 1.1167 0.8044 0.7478 -0.2756 -0.0004 -0.0455 475 HIS C CE1 
8230  N NE2 . HIS C 174 ? 1.1274 0.8555 0.7742 -0.2766 -0.0067 -0.0474 475 HIS C NE2 
8231  N N   . ASP C 175 ? 1.0008 0.7418 0.7335 -0.1704 0.0074  -0.0126 476 ASP C N   
8232  C CA  . ASP C 175 ? 0.9128 0.6763 0.6703 -0.1506 0.0071  -0.0067 476 ASP C CA  
8233  C C   . ASP C 175 ? 0.8607 0.6201 0.6208 -0.1322 0.0087  -0.0084 476 ASP C C   
8234  O O   . ASP C 175 ? 0.9731 0.7008 0.7129 -0.1282 0.0129  -0.0126 476 ASP C O   
8235  C CB  . ASP C 175 ? 0.9795 0.7257 0.7343 -0.1444 0.0114  -0.0014 476 ASP C CB  
8236  C CG  . ASP C 175 ? 0.9335 0.7018 0.6986 -0.1568 0.0092  0.0028  476 ASP C CG  
8237  O OD1 . ASP C 175 ? 1.0172 0.8119 0.7887 -0.1719 0.0047  0.0009  476 ASP C OD1 
8238  O OD2 . ASP C 175 ? 0.9297 0.6918 0.6967 -0.1510 0.0119  0.0081  476 ASP C OD2 
8239  N N   . PHE C 176 ? 0.7679 0.5588 0.5515 -0.1211 0.0055  -0.0052 477 PHE C N   
8240  C CA  . PHE C 176 ? 0.7181 0.5081 0.5076 -0.1028 0.0078  -0.0045 477 PHE C CA  
8241  C C   . PHE C 176 ? 0.7779 0.5669 0.5766 -0.0901 0.0105  0.0009  477 PHE C C   
8242  O O   . PHE C 176 ? 0.9231 0.7279 0.7340 -0.0930 0.0084  0.0049  477 PHE C O   
8243  C CB  . PHE C 176 ? 0.6853 0.5060 0.4919 -0.0992 0.0028  -0.0036 477 PHE C CB  
8244  C CG  . PHE C 176 ? 0.7684 0.5891 0.5645 -0.1072 0.0006  -0.0087 477 PHE C CG  
8245  C CD1 . PHE C 176 ? 0.7826 0.6093 0.5724 -0.1242 -0.0032 -0.0114 477 PHE C CD1 
8246  C CD2 . PHE C 176 ? 0.7286 0.5455 0.5209 -0.0984 0.0024  -0.0106 477 PHE C CD2 
8247  C CE1 . PHE C 176 ? 0.8427 0.6706 0.6221 -0.1320 -0.0056 -0.0162 477 PHE C CE1 
8248  C CE2 . PHE C 176 ? 0.7858 0.6028 0.5673 -0.1057 0.0005  -0.0152 477 PHE C CE2 
8249  C CZ  . PHE C 176 ? 0.8016 0.6235 0.5764 -0.1222 -0.0038 -0.0181 477 PHE C CZ  
8250  N N   . ARG C 177 ? 0.7820 0.5550 0.5748 -0.0755 0.0153  0.0008  478 ARG C N   
8251  C CA  . ARG C 177 ? 0.8509 0.6223 0.6500 -0.0631 0.0180  0.0058  478 ARG C CA  
8252  C C   . ARG C 177 ? 0.8139 0.5877 0.6164 -0.0458 0.0212  0.0058  478 ARG C C   
8253  O O   . ARG C 177 ? 0.9343 0.6885 0.7210 -0.0401 0.0252  0.0019  478 ARG C O   
8254  C CB  . ARG C 177 ? 0.8567 0.5955 0.6358 -0.0658 0.0218  0.0066  478 ARG C CB  
8255  C CG  . ARG C 177 ? 0.9436 0.6839 0.7216 -0.0825 0.0195  0.0087  478 ARG C CG  
8256  C CD  . ARG C 177 ? 0.8745 0.6494 0.6775 -0.0811 0.0158  0.0137  478 ARG C CD  
8257  N NE  . ARG C 177 ? 0.8710 0.6445 0.6790 -0.0678 0.0182  0.0188  478 ARG C NE  
8258  C CZ  . ARG C 177 ? 0.9007 0.6589 0.6993 -0.0705 0.0203  0.0228  478 ARG C CZ  
8259  N NH1 . ARG C 177 ? 0.8751 0.6165 0.6580 -0.0874 0.0209  0.0221  478 ARG C NH1 
8260  N NH2 . ARG C 177 ? 0.9043 0.6646 0.7082 -0.0575 0.0219  0.0277  478 ARG C NH2 
8261  N N   . VAL C 178 ? 0.6958 0.4940 0.5178 -0.0377 0.0196  0.0099  479 VAL C N   
8262  C CA  . VAL C 178 ? 0.7198 0.5214 0.5448 -0.0216 0.0232  0.0114  479 VAL C CA  
8263  C C   . VAL C 178 ? 0.8704 0.6545 0.6870 -0.0141 0.0263  0.0146  479 VAL C C   
8264  O O   . VAL C 178 ? 0.8291 0.6189 0.6527 -0.0177 0.0242  0.0187  479 VAL C O   
8265  C CB  . VAL C 178 ? 0.5930 0.4255 0.4395 -0.0181 0.0202  0.0144  479 VAL C CB  
8266  C CG1 . VAL C 178 ? 0.5408 0.3810 0.3901 -0.0036 0.0239  0.0155  479 VAL C CG1 
8267  C CG2 . VAL C 178 ? 0.6283 0.4744 0.4806 -0.0260 0.0165  0.0124  479 VAL C CG2 
8268  N N   . TRP C 179 ? 0.9016 0.6634 0.7013 -0.0030 0.0314  0.0129  480 TRP C N   
8269  C CA  . TRP C 179 ? 0.7941 0.5352 0.5821 0.0063  0.0345  0.0166  480 TRP C CA  
8270  C C   . TRP C 179 ? 0.7776 0.5420 0.5807 0.0212  0.0346  0.0215  480 TRP C C   
8271  O O   . TRP C 179 ? 0.8011 0.5573 0.6004 0.0268  0.0352  0.0264  480 TRP C O   
8272  C CB  . TRP C 179 ? 0.7134 0.4181 0.4742 0.0149  0.0399  0.0128  480 TRP C CB  
8273  C CG  . TRP C 179 ? 0.8163 0.4888 0.5559 -0.0013 0.0399  0.0092  480 TRP C CG  
8274  C CD1 . TRP C 179 ? 0.9047 0.5856 0.6489 -0.0211 0.0359  0.0062  480 TRP C CD1 
8275  C CD2 . TRP C 179 ? 0.7920 0.4184 0.5009 -0.0002 0.0438  0.0082  480 TRP C CD2 
8276  N NE1 . TRP C 179 ? 0.8507 0.4967 0.5700 -0.0342 0.0371  0.0031  480 TRP C NE1 
8277  C CE2 . TRP C 179 ? 0.8604 0.4698 0.5565 -0.0224 0.0421  0.0042  480 TRP C CE2 
8278  C CE3 . TRP C 179 ? 0.8172 0.4141 0.5063 0.0177  0.0486  0.0103  480 TRP C CE3 
8279  C CZ2 . TRP C 179 ? 0.9433 0.5051 0.6066 -0.0296 0.0450  0.0020  480 TRP C CZ2 
8280  C CZ3 . TRP C 179 ? 0.9054 0.4516 0.5606 0.0128  0.0516  0.0086  480 TRP C CZ3 
8281  C CH2 . TRP C 179 ? 0.9497 0.4778 0.5918 -0.0119 0.0499  0.0042  480 TRP C CH2 
8282  N N   . ASN C 180 ? 0.7215 0.5149 0.5404 0.0266  0.0341  0.0205  481 ASN C N   
8283  C CA  . ASN C 180 ? 0.6405 0.4612 0.4755 0.0367  0.0334  0.0248  481 ASN C CA  
8284  C C   . ASN C 180 ? 0.8073 0.6418 0.6562 0.0270  0.0286  0.0285  481 ASN C C   
8285  O O   . ASN C 180 ? 0.9501 0.7870 0.8039 0.0130  0.0252  0.0270  481 ASN C O   
8286  C CB  . ASN C 180 ? 0.5478 0.3969 0.3957 0.0392  0.0335  0.0226  481 ASN C CB  
8287  C CG  . ASN C 180 ? 0.6710 0.5110 0.5062 0.0483  0.0385  0.0182  481 ASN C CG  
8288  O OD1 . ASN C 180 ? 0.7400 0.5533 0.5586 0.0439  0.0401  0.0141  481 ASN C OD1 
8289  N ND2 . ASN C 180 ? 0.6606 0.5247 0.5030 0.0605  0.0411  0.0185  481 ASN C ND2 
8290  N N   . SER C 181 ? 0.7441 0.5893 0.5989 0.0355  0.0283  0.0332  482 SER C N   
8291  C CA  . SER C 181 ? 0.5447 0.4054 0.4127 0.0276  0.0241  0.0361  482 SER C CA  
8292  C C   . SER C 181 ? 0.4823 0.3727 0.3685 0.0235  0.0208  0.0348  482 SER C C   
8293  O O   . SER C 181 ? 0.6157 0.5139 0.5103 0.0132  0.0171  0.0344  482 SER C O   
8294  C CB  . SER C 181 ? 0.6213 0.4820 0.4872 0.0373  0.0247  0.0416  482 SER C CB  
8295  O OG  . SER C 181 ? 0.8302 0.6993 0.6949 0.0536  0.0274  0.0426  482 SER C OG  
8296  N N   . GLN C 182 ? 0.5278 0.4345 0.4187 0.0312  0.0224  0.0339  483 GLN C N   
8297  C CA  . GLN C 182 ? 0.6445 0.5725 0.5473 0.0245  0.0201  0.0319  483 GLN C CA  
8298  C C   . GLN C 182 ? 0.6849 0.6127 0.5825 0.0272  0.0234  0.0286  483 GLN C C   
8299  O O   . GLN C 182 ? 0.8612 0.7792 0.7486 0.0382  0.0278  0.0280  483 GLN C O   
8300  C CB  . GLN C 182 ? 0.6123 0.5674 0.5273 0.0271  0.0184  0.0340  483 GLN C CB  
8301  C CG  . GLN C 182 ? 0.6017 0.5606 0.5226 0.0233  0.0148  0.0364  483 GLN C CG  
8302  C CD  . GLN C 182 ? 0.6669 0.6496 0.5954 0.0295  0.0141  0.0388  483 GLN C CD  
8303  O OE1 . GLN C 182 ? 0.6723 0.6764 0.6080 0.0272  0.0135  0.0377  483 GLN C OE1 
8304  N NE2 . GLN C 182 ? 0.5947 0.5744 0.5205 0.0364  0.0142  0.0424  483 GLN C NE2 
8305  N N   . LEU C 183 ? 0.5967 0.5345 0.4997 0.0179  0.0215  0.0267  484 LEU C N   
8306  C CA  . LEU C 183 ? 0.6142 0.5539 0.5121 0.0188  0.0247  0.0237  484 LEU C CA  
8307  C C   . LEU C 183 ? 0.6909 0.6511 0.5915 0.0305  0.0288  0.0242  484 LEU C C   
8308  O O   . LEU C 183 ? 0.6911 0.6465 0.5827 0.0397  0.0336  0.0219  484 LEU C O   
8309  C CB  . LEU C 183 ? 0.4605 0.4077 0.3630 0.0063  0.0214  0.0228  484 LEU C CB  
8310  C CG  . LEU C 183 ? 0.4573 0.3884 0.3570 -0.0033 0.0172  0.0222  484 LEU C CG  
8311  C CD1 . LEU C 183 ? 0.4502 0.3856 0.3505 -0.0126 0.0144  0.0216  484 LEU C CD1 
8312  C CD2 . LEU C 183 ? 0.4897 0.3983 0.3767 -0.0016 0.0195  0.0197  484 LEU C CD2 
8313  N N   . ILE C 184 ? 0.6912 0.6755 0.6036 0.0308  0.0270  0.0269  485 ILE C N   
8314  C CA  . ILE C 184 ? 0.6848 0.6968 0.6023 0.0407  0.0302  0.0277  485 ILE C CA  
8315  C C   . ILE C 184 ? 0.7599 0.7775 0.6807 0.0508  0.0292  0.0313  485 ILE C C   
8316  O O   . ILE C 184 ? 0.7820 0.8084 0.7110 0.0437  0.0250  0.0333  485 ILE C O   
8317  C CB  . ILE C 184 ? 0.5840 0.6243 0.5117 0.0293  0.0288  0.0278  485 ILE C CB  
8318  C CG1 . ILE C 184 ? 0.5845 0.6142 0.5069 0.0178  0.0287  0.0254  485 ILE C CG1 
8319  C CG2 . ILE C 184 ? 0.4635 0.5376 0.3965 0.0382  0.0326  0.0281  485 ILE C CG2 
8320  C CD1 . ILE C 184 ? 0.5555 0.5999 0.4838 0.0025  0.0256  0.0263  485 ILE C CD1 
8321  N N   . ARG C 185 ? 0.6409 0.6508 0.5530 0.0680  0.0331  0.0320  486 ARG C N   
8322  C CA  . ARG C 185 ? 0.6070 0.6237 0.5198 0.0810  0.0327  0.0362  486 ARG C CA  
8323  C C   . ARG C 185 ? 0.6888 0.7208 0.5978 0.1011  0.0377  0.0364  486 ARG C C   
8324  O O   . ARG C 185 ? 0.5791 0.6019 0.4792 0.1068  0.0422  0.0328  486 ARG C O   
8325  C CB  . ARG C 185 ? 0.5990 0.5794 0.4992 0.0840  0.0322  0.0384  486 ARG C CB  
8326  C CG  . ARG C 185 ? 0.6741 0.6407 0.5772 0.0673  0.0277  0.0386  486 ARG C CG  
8327  C CD  . ARG C 185 ? 0.9051 0.8910 0.8191 0.0648  0.0237  0.0421  486 ARG C CD  
8328  N NE  . ARG C 185 ? 1.0113 0.9934 0.9192 0.0786  0.0243  0.0470  486 ARG C NE  
8329  C CZ  . ARG C 185 ? 0.8864 0.8446 0.7855 0.0775  0.0235  0.0499  486 ARG C CZ  
8330  N NH1 . ARG C 185 ? 0.8097 0.7489 0.7066 0.0635  0.0221  0.0481  486 ARG C NH1 
8331  N NH2 . ARG C 185 ? 0.8603 0.8152 0.7523 0.0906  0.0241  0.0551  486 ARG C NH2 
8332  N N   . TYR C 186 ? 0.6292 0.6851 0.5439 0.1133  0.0370  0.0403  487 TYR C N   
8333  C CA  . TYR C 186 ? 0.6109 0.6828 0.5213 0.1356  0.0417  0.0407  487 TYR C CA  
8334  C C   . TYR C 186 ? 0.7430 0.7770 0.6332 0.1546  0.0442  0.0430  487 TYR C C   
8335  O O   . TYR C 186 ? 0.8891 0.8937 0.7716 0.1505  0.0416  0.0459  487 TYR C O   
8336  C CB  . TYR C 186 ? 0.5594 0.6815 0.4854 0.1413  0.0398  0.0438  487 TYR C CB  
8337  C CG  . TYR C 186 ? 0.5585 0.7176 0.5014 0.1217  0.0378  0.0416  487 TYR C CG  
8338  C CD1 . TYR C 186 ? 0.6288 0.8009 0.5823 0.1056  0.0321  0.0432  487 TYR C CD1 
8339  C CD2 . TYR C 186 ? 0.5872 0.7659 0.5332 0.1187  0.0417  0.0379  487 TYR C CD2 
8340  C CE1 . TYR C 186 ? 0.6077 0.8080 0.5728 0.0866  0.0302  0.0413  487 TYR C CE1 
8341  C CE2 . TYR C 186 ? 0.6507 0.8605 0.6094 0.0989  0.0398  0.0367  487 TYR C CE2 
8342  C CZ  . TYR C 186 ? 0.6017 0.8203 0.5691 0.0826  0.0339  0.0384  487 TYR C CZ  
8343  O OH  . TYR C 186 ? 0.5968 0.8402 0.5731 0.0614  0.0319  0.0371  487 TYR C OH  
8344  N N   . ALA C 187 ? 0.8100 0.8442 0.6898 0.1757  0.0496  0.0415  488 ALA C N   
8345  C CA  . ALA C 187 ? 0.7538 0.7461 0.6094 0.1950  0.0529  0.0429  488 ALA C CA  
8346  C C   . ALA C 187 ? 0.8836 0.8848 0.7374 0.2135  0.0511  0.0502  488 ALA C C   
8347  O O   . ALA C 187 ? 0.9302 0.9789 0.8018 0.2171  0.0486  0.0530  488 ALA C O   
8348  C CB  . ALA C 187 ? 0.7642 0.7520 0.6072 0.2128  0.0597  0.0380  488 ALA C CB  
8349  N N   . GLY C 188 ? 0.8582 0.8121 0.6882 0.2246  0.0523  0.0532  489 GLY C N   
8350  C CA  . GLY C 188 ? 0.8320 0.7855 0.6542 0.2447  0.0510  0.0609  489 GLY C CA  
8351  C C   . GLY C 188 ? 0.9263 0.8422 0.7195 0.2727  0.0563  0.0619  489 GLY C C   
8352  O O   . GLY C 188 ? 1.0127 0.8752 0.7823 0.2694  0.0594  0.0588  489 GLY C O   
8353  N N   . TYR C 189 ? 0.8597 0.8023 0.6526 0.3007  0.0572  0.0661  490 TYR C N   
8354  C CA  . TYR C 189 ? 0.8625 0.7763 0.6284 0.3323  0.0627  0.0663  490 TYR C CA  
8355  C C   . TYR C 189 ? 0.9839 0.8842 0.7346 0.3544  0.0606  0.0761  490 TYR C C   
8356  O O   . TYR C 189 ? 1.0912 1.0396 0.8608 0.3599  0.0563  0.0818  490 TYR C O   
8357  C CB  . TYR C 189 ? 0.8701 0.8328 0.6483 0.3507  0.0668  0.0616  490 TYR C CB  
8358  C CG  . TYR C 189 ? 0.8874 0.8650 0.6790 0.3299  0.0692  0.0525  490 TYR C CG  
8359  C CD1 . TYR C 189 ? 0.8793 0.9205 0.7026 0.3157  0.0671  0.0508  490 TYR C CD1 
8360  C CD2 . TYR C 189 ? 0.8719 0.7990 0.6425 0.3234  0.0735  0.0457  490 TYR C CD2 
8361  C CE1 . TYR C 189 ? 0.9116 0.9645 0.7450 0.2966  0.0692  0.0434  490 TYR C CE1 
8362  C CE2 . TYR C 189 ? 0.9335 0.8750 0.7153 0.3049  0.0754  0.0380  490 TYR C CE2 
8363  C CZ  . TYR C 189 ? 0.9575 0.9616 0.7706 0.2922  0.0733  0.0372  490 TYR C CZ  
8364  O OH  . TYR C 189 ? 0.9219 0.9389 0.7443 0.2736  0.0751  0.0305  490 TYR C OH  
8365  N N   . LYS C 190 ? 0.9945 0.8279 0.7093 0.3658  0.0635  0.0783  491 LYS C N   
8366  C CA  . LYS C 190 ? 1.0026 0.8106 0.6960 0.3866  0.0619  0.0886  491 LYS C CA  
8367  C C   . LYS C 190 ? 1.1738 0.9926 0.8541 0.4287  0.0657  0.0901  491 LYS C C   
8368  O O   . LYS C 190 ? 1.2816 1.0612 0.9364 0.4448  0.0718  0.0851  491 LYS C O   
8369  C CB  . LYS C 190 ? 1.1423 0.8701 0.8007 0.3759  0.0632  0.0904  491 LYS C CB  
8370  C CG  . LYS C 190 ? 1.3227 1.0234 0.9619 0.3851  0.0602  0.1023  491 LYS C CG  
8371  C CD  . LYS C 190 ? 1.3452 1.0390 0.9938 0.3506  0.0555  0.1054  491 LYS C CD  
8372  C CE  . LYS C 190 ? 1.2445 1.0078 0.9311 0.3413  0.0494  0.1084  491 LYS C CE  
8373  N NZ  . LYS C 190 ? 1.2296 1.0164 0.9134 0.3694  0.0467  0.1183  491 LYS C NZ  
8374  N N   . GLN C 191 ? 1.3115 1.1834 1.0078 0.4471  0.0621  0.0970  492 GLN C N   
8375  C CA  . GLN C 191 ? 1.3738 1.2819 1.0696 0.4855  0.0650  0.0976  492 GLN C CA  
8376  C C   . GLN C 191 ? 1.3679 1.2241 1.0240 0.5104  0.0675  0.1019  492 GLN C C   
8377  O O   . GLN C 191 ? 1.3425 1.1401 0.9733 0.5027  0.0662  0.1072  492 GLN C O   
8378  C CB  . GLN C 191 ? 1.3624 1.3548 1.0931 0.4887  0.0595  0.1022  492 GLN C CB  
8379  C CG  . GLN C 191 ? 1.3024 1.3557 1.0723 0.4585  0.0577  0.0950  492 GLN C CG  
8380  C CD  . GLN C 191 ? 1.2359 1.3210 1.0149 0.4675  0.0638  0.0860  492 GLN C CD  
8381  O OE1 . GLN C 191 ? 1.2160 1.2598 0.9703 0.4853  0.0702  0.0817  492 GLN C OE1 
8382  N NE2 . GLN C 191 ? 1.2154 1.3738 1.0288 0.4540  0.0619  0.0830  492 GLN C NE2 
8383  N N   . PRO C 192 ? 1.3435 1.2216 0.9926 0.5360  0.0712  0.0988  493 PRO C N   
8384  C CA  . PRO C 192 ? 1.3590 1.1940 0.9708 0.5581  0.0732  0.1025  493 PRO C CA  
8385  C C   . PRO C 192 ? 1.4381 1.2715 1.0455 0.5597  0.0677  0.1135  493 PRO C C   
8386  O O   . PRO C 192 ? 1.4351 1.2017 1.0097 0.5576  0.0681  0.1176  493 PRO C O   
8387  C CB  . PRO C 192 ? 1.2291 1.1149 0.8466 0.5848  0.0762  0.0988  493 PRO C CB  
8388  C CG  . PRO C 192 ? 1.1712 1.0922 0.8138 0.5741  0.0790  0.0896  493 PRO C CG  
8389  C CD  . PRO C 192 ? 1.1970 1.1311 0.8673 0.5445  0.0748  0.0908  493 PRO C CD  
8390  N N   . ASP C 193 ? 1.4419 1.3488 1.0813 0.5616  0.0626  0.1180  494 ASP C N   
8391  C CA  . ASP C 193 ? 1.3536 1.2653 0.9891 0.5652  0.0574  0.1281  494 ASP C CA  
8392  C C   . ASP C 193 ? 1.3522 1.2160 0.9805 0.5398  0.0541  0.1331  494 ASP C C   
8393  O O   . ASP C 193 ? 1.4638 1.2813 1.0652 0.5425  0.0534  0.1398  494 ASP C O   
8394  C CB  . ASP C 193 ? 1.2214 1.2247 0.8942 0.5677  0.0523  0.1308  494 ASP C CB  
8395  C CG  . ASP C 193 ? 1.1435 1.1998 0.8555 0.5460  0.0502  0.1255  494 ASP C CG  
8396  O OD1 . ASP C 193 ? 1.1084 1.2301 0.8433 0.5526  0.0510  0.1210  494 ASP C OD1 
8397  O OD2 . ASP C 193 ? 1.1677 1.2007 0.8865 0.5218  0.0477  0.1261  494 ASP C OD2 
8398  N N   . GLY C 194 ? 1.2693 1.1438 0.9205 0.5148  0.0522  0.1303  495 GLY C N   
8399  C CA  . GLY C 194 ? 1.2219 1.0577 0.8680 0.4897  0.0488  0.1354  495 GLY C CA  
8400  C C   . GLY C 194 ? 1.2678 1.1510 0.9507 0.4675  0.0438  0.1352  495 GLY C C   
8401  O O   . GLY C 194 ? 1.3623 1.2151 1.0453 0.4358  0.0430  0.1331  495 GLY C O   
8402  N N   . SER C 195 ? 1.2657 1.2274 0.9819 0.4730  0.0410  0.1334  496 SER C N   
8403  C CA  . SER C 195 ? 1.2634 1.2746 1.0165 0.4382  0.0371  0.1277  496 SER C CA  
8404  C C   . SER C 195 ? 1.2263 1.2247 0.9869 0.4168  0.0418  0.1160  496 SER C C   
8405  O O   . SER C 195 ? 1.3435 1.2892 1.0797 0.4242  0.0474  0.1124  496 SER C O   
8406  C CB  . SER C 195 ? 1.2720 1.3690 1.0553 0.4477  0.0328  0.1290  496 SER C CB  
8407  O OG  . SER C 195 ? 1.2252 1.3665 1.0314 0.4423  0.0357  0.1196  496 SER C OG  
8408  N N   . THR C 196 ? 1.0307 1.0759 0.8236 0.3895  0.0392  0.1099  497 THR C N   
8409  C CA  . THR C 196 ? 0.9557 0.9815 0.7542 0.3631  0.0422  0.1005  497 THR C CA  
8410  C C   . THR C 196 ? 0.9788 1.0688 0.8098 0.3500  0.0416  0.0935  497 THR C C   
8411  O O   . THR C 196 ? 0.9983 1.1389 0.8526 0.3390  0.0364  0.0952  497 THR C O   
8412  C CB  . THR C 196 ? 0.9666 0.9571 0.7631 0.3321  0.0392  0.1011  497 THR C CB  
8413  O OG1 . THR C 196 ? 1.0948 1.0282 0.8603 0.3424  0.0396  0.1086  497 THR C OG1 
8414  C CG2 . THR C 196 ? 0.8883 0.8551 0.6873 0.3079  0.0422  0.0919  497 THR C CG2 
8415  N N   . LEU C 197 ? 1.0141 1.0996 0.8446 0.3496  0.0470  0.0857  498 LEU C N   
8416  C CA  . LEU C 197 ? 1.0379 1.1783 0.8952 0.3362  0.0476  0.0790  498 LEU C CA  
8417  C C   . LEU C 197 ? 0.9372 1.0568 0.8017 0.3011  0.0470  0.0727  498 LEU C C   
8418  O O   . LEU C 197 ? 0.9347 0.9976 0.7803 0.2949  0.0496  0.0703  498 LEU C O   
8419  C CB  . LEU C 197 ? 1.0534 1.2083 0.9054 0.3607  0.0543  0.0746  498 LEU C CB  
8420  C CG  . LEU C 197 ? 1.0217 1.2201 0.8948 0.3456  0.0570  0.0667  498 LEU C CG  
8421  C CD1 . LEU C 197 ? 0.9749 1.2452 0.8788 0.3307  0.0521  0.0679  498 LEU C CD1 
8422  C CD2 . LEU C 197 ? 1.0792 1.2872 0.9428 0.3737  0.0644  0.0627  498 LEU C CD2 
8423  N N   . GLY C 198 ? 0.8234 0.9891 0.7139 0.2784  0.0436  0.0702  499 GLY C N   
8424  C CA  . GLY C 198 ? 0.8071 0.9586 0.7056 0.2465  0.0424  0.0649  499 GLY C CA  
8425  C C   . GLY C 198 ? 0.8932 1.0239 0.7931 0.2268  0.0368  0.0679  499 GLY C C   
8426  O O   . GLY C 198 ? 0.9858 1.1415 0.8937 0.2277  0.0322  0.0728  499 GLY C O   
8427  N N   . ASP C 199 ? 0.8755 0.9628 0.7673 0.2090  0.0372  0.0649  500 ASP C N   
8428  C CA  . ASP C 199 ? 0.8408 0.9080 0.7333 0.1905  0.0326  0.0670  500 ASP C CA  
8429  C C   . ASP C 199 ? 0.8518 0.8668 0.7199 0.2002  0.0341  0.0714  500 ASP C C   
8430  O O   . ASP C 199 ? 0.8266 0.8009 0.6786 0.1993  0.0379  0.0683  500 ASP C O   
8431  C CB  . ASP C 199 ? 0.9520 1.0101 0.8524 0.1639  0.0317  0.0610  500 ASP C CB  
8432  C CG  . ASP C 199 ? 1.0010 1.0477 0.9053 0.1451  0.0270  0.0625  500 ASP C CG  
8433  O OD1 . ASP C 199 ? 0.9810 0.9975 0.8721 0.1487  0.0266  0.0667  500 ASP C OD1 
8434  O OD2 . ASP C 199 ? 1.0140 1.0813 0.9334 0.1267  0.0240  0.0592  500 ASP C OD2 
8435  N N   . PRO C 200 ? 0.8538 0.8670 0.7166 0.2083  0.0313  0.0785  501 PRO C N   
8436  C CA  . PRO C 200 ? 0.8464 0.8074 0.6822 0.2181  0.0332  0.0836  501 PRO C CA  
8437  C C   . PRO C 200 ? 0.8627 0.7811 0.6895 0.1958  0.0335  0.0812  501 PRO C C   
8438  O O   . PRO C 200 ? 0.8241 0.6939 0.6257 0.2004  0.0364  0.0833  501 PRO C O   
8439  C CB  . PRO C 200 ? 0.7501 0.7269 0.5861 0.2272  0.0291  0.0921  501 PRO C CB  
8440  C CG  . PRO C 200 ? 0.6867 0.7258 0.5462 0.2321  0.0264  0.0911  501 PRO C CG  
8441  C CD  . PRO C 200 ? 0.6483 0.7077 0.5268 0.2110  0.0266  0.0826  501 PRO C CD  
8442  N N   . ALA C 201 ? 0.8381 0.7732 0.6834 0.1718  0.0306  0.0768  502 ALA C N   
8443  C CA  . ALA C 201 ? 0.8759 0.7783 0.7152 0.1509  0.0303  0.0747  502 ALA C CA  
8444  C C   . ALA C 201 ? 0.9342 0.8010 0.7583 0.1488  0.0346  0.0697  502 ALA C C   
8445  O O   . ALA C 201 ? 0.8264 0.6553 0.6354 0.1378  0.0356  0.0697  502 ALA C O   
8446  C CB  . ALA C 201 ? 0.8340 0.7645 0.6959 0.1295  0.0264  0.0707  502 ALA C CB  
8447  N N   . ASN C 202 ? 0.9949 0.8754 0.8225 0.1582  0.0374  0.0651  503 ASN C N   
8448  C CA  . ASN C 202 ? 0.9093 0.7627 0.7253 0.1543  0.0411  0.0589  503 ASN C CA  
8449  C C   . ASN C 202 ? 1.0046 0.8241 0.7941 0.1762  0.0462  0.0596  503 ASN C C   
8450  O O   . ASN C 202 ? 1.2087 1.0062 0.9862 0.1761  0.0500  0.0536  503 ASN C O   
8451  C CB  . ASN C 202 ? 0.8509 0.7402 0.6864 0.1487  0.0412  0.0529  503 ASN C CB  
8452  C CG  . ASN C 202 ? 0.8436 0.7601 0.7012 0.1278  0.0362  0.0521  503 ASN C CG  
8453  O OD1 . ASN C 202 ? 0.9033 0.8021 0.7596 0.1122  0.0337  0.0526  503 ASN C OD1 
8454  N ND2 . ASN C 202 ? 0.7365 0.6961 0.6134 0.1272  0.0348  0.0508  503 ASN C ND2 
8455  N N   . VAL C 203 ? 0.9967 0.8100 0.7749 0.1957  0.0465  0.0666  504 VAL C N   
8456  C CA  . VAL C 203 ? 1.0207 0.7997 0.7710 0.2203  0.0514  0.0676  504 VAL C CA  
8457  C C   . VAL C 203 ? 1.1030 0.8225 0.8259 0.2097  0.0545  0.0638  504 VAL C C   
8458  O O   . VAL C 203 ? 1.2144 0.9101 0.9197 0.2206  0.0593  0.0586  504 VAL C O   
8459  C CB  . VAL C 203 ? 1.0158 0.7901 0.7548 0.2406  0.0502  0.0772  504 VAL C CB  
8460  C CG1 . VAL C 203 ? 0.9869 0.7082 0.6889 0.2634  0.0552  0.0789  504 VAL C CG1 
8461  C CG2 . VAL C 203 ? 1.0368 0.8724 0.7998 0.2561  0.0479  0.0797  504 VAL C CG2 
8462  N N   . GLN C 204 ? 0.9861 0.6829 0.7048 0.1872  0.0520  0.0659  505 GLN C N   
8463  C CA  . GLN C 204 ? 1.0320 0.6748 0.7242 0.1743  0.0547  0.0623  505 GLN C CA  
8464  C C   . GLN C 204 ? 1.1652 0.8154 0.8657 0.1614  0.0558  0.0525  505 GLN C C   
8465  O O   . GLN C 204 ? 1.2203 0.8329 0.8971 0.1633  0.0598  0.0471  505 GLN C O   
8466  C CB  . GLN C 204 ? 1.0535 0.6772 0.7412 0.1512  0.0518  0.0667  505 GLN C CB  
8467  C CG  . GLN C 204 ? 1.2034 0.7614 0.8518 0.1473  0.0553  0.0675  505 GLN C CG  
8468  C CD  . GLN C 204 ? 1.2826 0.8240 0.9277 0.1160  0.0534  0.0674  505 GLN C CD  
8469  O OE1 . GLN C 204 ? 1.2430 0.8219 0.9159 0.0984  0.0496  0.0660  505 GLN C OE1 
8470  N NE2 . GLN C 204 ? 1.2782 0.7628 0.8878 0.1091  0.0561  0.0689  505 GLN C NE2 
8471  N N   . PHE C 205 ? 1.0347 0.7317 0.7669 0.1485  0.0523  0.0500  506 PHE C N   
8472  C CA  . PHE C 205 ? 0.9022 0.6079 0.6421 0.1369  0.0530  0.0417  506 PHE C CA  
8473  C C   . PHE C 205 ? 1.0302 0.7440 0.7655 0.1580  0.0577  0.0373  506 PHE C C   
8474  O O   . PHE C 205 ? 1.1116 0.7995 0.8300 0.1573  0.0613  0.0306  506 PHE C O   
8475  C CB  . PHE C 205 ? 0.7322 0.4828 0.5040 0.1197  0.0482  0.0409  506 PHE C CB  
8476  C CG  . PHE C 205 ? 0.7464 0.5024 0.5243 0.1051  0.0481  0.0335  506 PHE C CG  
8477  C CD1 . PHE C 205 ? 0.6996 0.4285 0.4671 0.0858  0.0471  0.0305  506 PHE C CD1 
8478  C CD2 . PHE C 205 ? 0.7819 0.5721 0.5753 0.1098  0.0489  0.0301  506 PHE C CD2 
8479  C CE1 . PHE C 205 ? 0.8564 0.5919 0.6290 0.0729  0.0464  0.0242  506 PHE C CE1 
8480  C CE2 . PHE C 205 ? 0.8873 0.6816 0.6847 0.0962  0.0487  0.0240  506 PHE C CE2 
8481  C CZ  . PHE C 205 ? 0.8564 0.6231 0.6433 0.0786  0.0472  0.0212  506 PHE C CZ  
8482  N N   . THR C 206 ? 0.8935 0.6453 0.6433 0.1769  0.0578  0.0406  507 THR C N   
8483  C CA  . THR C 206 ? 0.8633 0.6279 0.6091 0.1995  0.0627  0.0369  507 THR C CA  
8484  C C   . THR C 206 ? 0.9118 0.6223 0.6209 0.2172  0.0681  0.0351  507 THR C C   
8485  O O   . THR C 206 ? 1.0144 0.7213 0.7136 0.2302  0.0731  0.0288  507 THR C O   
8486  C CB  . THR C 206 ? 0.7945 0.6073 0.5585 0.2183  0.0617  0.0422  507 THR C CB  
8487  O OG1 . THR C 206 ? 0.7728 0.6334 0.5681 0.2006  0.0571  0.0427  507 THR C OG1 
8488  C CG2 . THR C 206 ? 0.6930 0.5230 0.4526 0.2438  0.0673  0.0386  507 THR C CG2 
8489  N N   . GLU C 207 ? 0.9882 0.6540 0.6748 0.2170  0.0675  0.0401  508 GLU C N   
8490  C CA  . GLU C 207 ? 1.1478 0.7544 0.7949 0.2316  0.0727  0.0379  508 GLU C CA  
8491  C C   . GLU C 207 ? 1.1910 0.7614 0.8221 0.2108  0.0744  0.0292  508 GLU C C   
8492  O O   . GLU C 207 ? 1.2443 0.7842 0.8507 0.2231  0.0797  0.0227  508 GLU C O   
8493  C CB  . GLU C 207 ? 1.3074 0.8744 0.9317 0.2377  0.0717  0.0467  508 GLU C CB  
8494  C CG  . GLU C 207 ? 1.5602 1.1240 1.1700 0.2747  0.0746  0.0518  508 GLU C CG  
8495  C CD  . GLU C 207 ? 1.7856 1.3432 1.3910 0.2806  0.0712  0.0633  508 GLU C CD  
8496  O OE1 . GLU C 207 ? 1.8672 1.4058 1.4706 0.2558  0.0681  0.0668  508 GLU C OE1 
8497  O OE2 . GLU C 207 ? 1.8056 1.3800 1.4097 0.3102  0.0717  0.0690  508 GLU C OE2 
8498  N N   . ILE C 208 ? 1.1748 0.7506 0.8193 0.1800  0.0700  0.0286  509 ILE C N   
8499  C CA  . ILE C 208 ? 1.1052 0.6522 0.7360 0.1589  0.0708  0.0205  509 ILE C CA  
8500  C C   . ILE C 208 ? 1.1653 0.7376 0.8058 0.1632  0.0734  0.0122  509 ILE C C   
8501  O O   . ILE C 208 ? 1.1519 0.6915 0.7686 0.1632  0.0773  0.0044  509 ILE C O   
8502  C CB  . ILE C 208 ? 1.0143 0.5718 0.6614 0.1271  0.0651  0.0221  509 ILE C CB  
8503  C CG1 . ILE C 208 ? 1.0145 0.5510 0.6529 0.1215  0.0630  0.0306  509 ILE C CG1 
8504  C CG2 . ILE C 208 ? 1.0210 0.5530 0.6541 0.1058  0.0655  0.0139  509 ILE C CG2 
8505  C CD1 . ILE C 208 ? 0.9593 0.5180 0.6190 0.0939  0.0575  0.0328  509 ILE C CD1 
8506  N N   . CYS C 209 ? 1.0863 0.7167 0.7605 0.1652  0.0713  0.0136  510 CYS C N   
8507  C CA  . CYS C 209 ? 1.0195 0.6790 0.7038 0.1702  0.0741  0.0069  510 CYS C CA  
8508  C C   . CYS C 209 ? 1.1248 0.7655 0.7854 0.1990  0.0812  0.0029  510 CYS C C   
8509  O O   . CYS C 209 ? 1.1435 0.7657 0.7878 0.1991  0.0853  -0.0055 510 CYS C O   
8510  C CB  . CYS C 209 ? 0.9920 0.7146 0.7131 0.1692  0.0710  0.0107  510 CYS C CB  
8511  S SG  . CYS C 209 ? 1.0439 0.7872 0.7908 0.1374  0.0630  0.0141  510 CYS C SG  
8512  N N   . ILE C 210 ? 1.1340 0.7799 0.7916 0.2249  0.0829  0.0085  511 ILE C N   
8513  C CA  . ILE C 210 ? 1.2300 0.8603 0.8648 0.2559  0.0899  0.0047  511 ILE C CA  
8514  C C   . ILE C 210 ? 1.2576 0.8138 0.8491 0.2562  0.0934  -0.0004 511 ILE C C   
8515  O O   . ILE C 210 ? 1.2434 0.7792 0.8137 0.2686  0.0992  -0.0087 511 ILE C O   
8516  C CB  . ILE C 210 ? 1.1639 0.8153 0.8028 0.2855  0.0905  0.0124  511 ILE C CB  
8517  C CG1 . ILE C 210 ? 1.1142 0.8362 0.7945 0.2800  0.0859  0.0178  511 ILE C CG1 
8518  C CG2 . ILE C 210 ? 1.2094 0.8630 0.8330 0.3187  0.0977  0.0077  511 ILE C CG2 
8519  C CD1 . ILE C 210 ? 1.1009 0.8431 0.7860 0.3036  0.0845  0.0268  511 ILE C CD1 
8520  N N   . GLN C 211 ? 1.2992 0.8142 0.8759 0.2412  0.0901  0.0043  512 GLN C N   
8521  C CA  . GLN C 211 ? 1.3940 0.8371 0.9293 0.2333  0.0925  -0.0002 512 GLN C CA  
8522  C C   . GLN C 211 ? 1.4148 0.8505 0.9481 0.2071  0.0923  -0.0099 512 GLN C C   
8523  O O   . GLN C 211 ? 1.5149 0.8938 1.0123 0.2008  0.0950  -0.0162 512 GLN C O   
8524  C CB  . GLN C 211 ? 1.4862 0.8971 1.0110 0.2199  0.0886  0.0084  512 GLN C CB  
8525  C CG  . GLN C 211 ? 1.6581 0.9931 1.1387 0.2075  0.0905  0.0056  512 GLN C CG  
8526  C CD  . GLN C 211 ? 1.7665 1.0987 1.2536 0.1681  0.0864  0.0019  512 GLN C CD  
8527  O OE1 . GLN C 211 ? 1.7501 1.1278 1.2719 0.1496  0.0810  0.0058  512 GLN C OE1 
8528  N NE2 . GLN C 211 ? 1.8221 1.1014 1.2746 0.1554  0.0890  -0.0062 512 GLN C NE2 
8529  N N   . GLN C 212 ? 1.3228 0.8130 0.8916 0.1917  0.0890  -0.0113 513 GLN C N   
8530  C CA  . GLN C 212 ? 1.2437 0.7347 0.8124 0.1710  0.0887  -0.0202 513 GLN C CA  
8531  C C   . GLN C 212 ? 1.2300 0.7490 0.8036 0.1876  0.0938  -0.0271 513 GLN C C   
8532  O O   . GLN C 212 ? 1.2404 0.7748 0.8215 0.1716  0.0931  -0.0332 513 GLN C O   
8533  C CB  . GLN C 212 ? 1.2783 0.8072 0.8797 0.1420  0.0816  -0.0169 513 GLN C CB  
8534  C CG  . GLN C 212 ? 1.2790 0.7753 0.8696 0.1163  0.0773  -0.0148 513 GLN C CG  
8535  C CD  . GLN C 212 ? 1.3330 0.7813 0.8906 0.1028  0.0793  -0.0238 513 GLN C CD  
8536  O OE1 . GLN C 212 ? 1.3818 0.7748 0.9034 0.1084  0.0827  -0.0254 513 GLN C OE1 
8537  N NE2 . GLN C 212 ? 1.3558 0.8234 0.9236 0.0845  0.0771  -0.0298 513 GLN C NE2 
8538  N N   . GLY C 213 ? 1.3095 0.8383 0.8794 0.2196  0.0987  -0.0259 514 GLY C N   
8539  C CA  . GLY C 213 ? 1.2499 0.8083 0.8237 0.2370  0.1043  -0.0325 514 GLY C CA  
8540  C C   . GLY C 213 ? 1.1585 0.7914 0.7738 0.2380  0.1026  -0.0283 514 GLY C C   
8541  O O   . GLY C 213 ? 1.0989 0.7622 0.7198 0.2482  0.1072  -0.0336 514 GLY C O   
8542  N N   . TRP C 214 ? 1.0648 0.7277 0.7078 0.2267  0.0963  -0.0194 515 TRP C N   
8543  C CA  . TRP C 214 ? 0.9713 0.7021 0.6504 0.2281  0.0948  -0.0154 515 TRP C CA  
8544  C C   . TRP C 214 ? 1.1225 0.8781 0.8012 0.2623  0.1001  -0.0141 515 TRP C C   
8545  O O   . TRP C 214 ? 1.1413 0.8679 0.8009 0.2839  0.1017  -0.0111 515 TRP C O   
8546  C CB  . TRP C 214 ? 0.9161 0.6688 0.6209 0.2107  0.0871  -0.0066 515 TRP C CB  
8547  C CG  . TRP C 214 ? 0.9519 0.7707 0.6918 0.2065  0.0849  -0.0033 515 TRP C CG  
8548  C CD1 . TRP C 214 ? 0.9612 0.8124 0.7159 0.1933  0.0853  -0.0071 515 TRP C CD1 
8549  C CD2 . TRP C 214 ? 0.9652 0.8236 0.7271 0.2138  0.0820  0.0043  515 TRP C CD2 
8550  N NE1 . TRP C 214 ? 0.9431 0.8490 0.7263 0.1910  0.0831  -0.0023 515 TRP C NE1 
8551  C CE2 . TRP C 214 ? 0.9047 0.8172 0.6933 0.2031  0.0809  0.0043  515 TRP C CE2 
8552  C CE3 . TRP C 214 ? 1.0219 0.8748 0.7819 0.2275  0.0801  0.0113  515 TRP C CE3 
8553  C CZ2 . TRP C 214 ? 0.8898 0.8506 0.7029 0.2047  0.0779  0.0103  515 TRP C CZ2 
8554  C CZ3 . TRP C 214 ? 1.0465 0.9500 0.8322 0.2304  0.0769  0.0174  515 TRP C CZ3 
8555  C CH2 . TRP C 214 ? 1.0222 0.9789 0.8340 0.2185  0.0758  0.0164  515 TRP C CH2 
8556  N N   . LYS C 215 ? 1.1707 0.9807 0.8694 0.2672  0.1029  -0.0163 516 LYS C N   
8557  C CA  . LYS C 215 ? 1.2230 1.0714 0.9272 0.2981  0.1078  -0.0151 516 LYS C CA  
8558  C C   . LYS C 215 ? 1.2077 1.1092 0.9440 0.2954  0.1025  -0.0060 516 LYS C C   
8559  O O   . LYS C 215 ? 1.2402 1.1906 1.0039 0.2775  0.1002  -0.0050 516 LYS C O   
8560  C CB  . LYS C 215 ? 1.2438 1.1264 0.9515 0.3040  0.1142  -0.0225 516 LYS C CB  
8561  C CG  . LYS C 215 ? 1.4113 1.2678 1.0887 0.3363  0.1228  -0.0294 516 LYS C CG  
8562  C CD  . LYS C 215 ? 1.4820 1.3415 1.1532 0.3705  0.1243  -0.0240 516 LYS C CD  
8563  C CE  . LYS C 215 ? 1.5586 1.4180 1.2085 0.4067  0.1338  -0.0310 516 LYS C CE  
8564  N NZ  . LYS C 215 ? 1.5774 1.3802 1.1937 0.4039  0.1388  -0.0418 516 LYS C NZ  
8565  N N   . PRO C 216 ? 1.0861 0.9781 0.8181 0.3118  0.1005  0.0007  517 PRO C N   
8566  C CA  . PRO C 216 ? 1.0061 0.9455 0.7667 0.3074  0.0949  0.0091  517 PRO C CA  
8567  C C   . PRO C 216 ? 1.0242 1.0292 0.8025 0.3283  0.0982  0.0099  517 PRO C C   
8568  O O   . PRO C 216 ? 1.1237 1.1276 0.8871 0.3614  0.1032  0.0093  517 PRO C O   
8569  C CB  . PRO C 216 ? 1.1507 1.0490 0.8942 0.3192  0.0920  0.0157  517 PRO C CB  
8570  C CG  . PRO C 216 ? 1.1790 1.0271 0.8858 0.3461  0.0987  0.0112  517 PRO C CG  
8571  C CD  . PRO C 216 ? 1.1030 0.9358 0.8004 0.3346  0.1031  0.0011  517 PRO C CD  
8572  N N   . PRO C 217 ? 0.9185 0.9823 0.7275 0.3100  0.0955  0.0112  518 PRO C N   
8573  C CA  . PRO C 217 ? 0.8820 1.0151 0.7104 0.3270  0.0976  0.0134  518 PRO C CA  
8574  C C   . PRO C 217 ? 0.8422 0.9925 0.6763 0.3450  0.0936  0.0216  518 PRO C C   
8575  O O   . PRO C 217 ? 0.7880 0.9927 0.6336 0.3659  0.0956  0.0235  518 PRO C O   
8576  C CB  . PRO C 217 ? 0.8137 0.9948 0.6700 0.2956  0.0948  0.0130  518 PRO C CB  
8577  C CG  . PRO C 217 ? 0.6967 0.8348 0.5513 0.2650  0.0889  0.0137  518 PRO C CG  
8578  C CD  . PRO C 217 ? 0.7579 0.8265 0.5822 0.2736  0.0913  0.0101  518 PRO C CD  
8579  N N   . ARG C 218 ? 0.8417 0.9497 0.6675 0.3379  0.0881  0.0267  519 ARG C N   
8580  C CA  . ARG C 218 ? 0.9844 1.0981 0.8097 0.3562  0.0844  0.0349  519 ARG C CA  
8581  C C   . ARG C 218 ? 1.0520 1.2425 0.9090 0.3523  0.0805  0.0393  519 ARG C C   
8582  O O   . ARG C 218 ? 1.0003 1.2375 0.8636 0.3776  0.0827  0.0410  519 ARG C O   
8583  C CB  . ARG C 218 ? 0.9739 1.0622 0.7722 0.3966  0.0898  0.0353  519 ARG C CB  
8584  C CG  . ARG C 218 ? 1.0693 1.0729 0.8321 0.3979  0.0922  0.0323  519 ARG C CG  
8585  C CD  . ARG C 218 ? 1.2077 1.1721 0.9394 0.4351  0.0951  0.0358  519 ARG C CD  
8586  N NE  . ARG C 218 ? 1.3418 1.2211 1.0379 0.4302  0.0967  0.0334  519 ARG C NE  
8587  C CZ  . ARG C 218 ? 1.4000 1.2311 1.0802 0.4233  0.0925  0.0399  519 ARG C CZ  
8588  N NH1 . ARG C 218 ? 1.5039 1.2600 1.1510 0.4162  0.0945  0.0369  519 ARG C NH1 
8589  N NH2 . ARG C 218 ? 1.2248 1.0829 0.9208 0.4228  0.0865  0.0493  519 ARG C NH2 
8590  N N   . GLY C 219 ? 1.1129 1.3148 0.9885 0.3199  0.0743  0.0409  520 GLY C N   
8591  C CA  . GLY C 219 ? 1.1194 1.3844 1.0219 0.3102  0.0693  0.0450  520 GLY C CA  
8592  C C   . GLY C 219 ? 1.1289 1.3776 1.0380 0.2866  0.0616  0.0494  520 GLY C C   
8593  O O   . GLY C 219 ? 1.1388 1.3296 1.0312 0.2827  0.0601  0.0506  520 GLY C O   
8594  N N   . ARG C 220 ? 1.0761 1.3757 1.0084 0.2701  0.0567  0.0515  521 ARG C N   
8595  C CA  . ARG C 220 ? 0.9529 1.2389 0.8915 0.2463  0.0497  0.0543  521 ARG C CA  
8596  C C   . ARG C 220 ? 0.9152 1.1686 0.8532 0.2174  0.0494  0.0495  521 ARG C C   
8597  O O   . ARG C 220 ? 0.9869 1.1868 0.9113 0.2114  0.0484  0.0495  521 ARG C O   
8598  C CB  . ARG C 220 ? 0.9091 1.2576 0.8703 0.2361  0.0447  0.0569  521 ARG C CB  
8599  C CG  . ARG C 220 ? 0.9582 1.3000 0.9208 0.2310  0.0377  0.0624  521 ARG C CG  
8600  C CD  . ARG C 220 ? 1.0571 1.4202 1.0158 0.2617  0.0368  0.0689  521 ARG C CD  
8601  N NE  . ARG C 220 ? 1.0037 1.3546 0.9601 0.2584  0.0305  0.0746  521 ARG C NE  
8602  C CZ  . ARG C 220 ? 0.9272 1.3227 0.8991 0.2477  0.0246  0.0767  521 ARG C CZ  
8603  N NH1 . ARG C 220 ? 0.8830 1.3391 0.8739 0.2378  0.0240  0.0738  521 ARG C NH1 
8604  N NH2 . ARG C 220 ? 0.8611 1.2406 0.8283 0.2455  0.0195  0.0816  521 ARG C NH2 
8605  N N   . PHE C 221 ? 0.8509 1.1367 0.8022 0.2002  0.0506  0.0454  522 PHE C N   
8606  C CA  . PHE C 221 ? 0.8821 1.1462 0.8355 0.1709  0.0488  0.0419  522 PHE C CA  
8607  C C   . PHE C 221 ? 0.9478 1.1876 0.8901 0.1712  0.0546  0.0365  522 PHE C C   
8608  O O   . PHE C 221 ? 0.9539 1.2135 0.9031 0.1560  0.0564  0.0332  522 PHE C O   
8609  C CB  . PHE C 221 ? 0.8836 1.1943 0.8560 0.1480  0.0453  0.0417  522 PHE C CB  
8610  C CG  . PHE C 221 ? 0.8921 1.2274 0.8742 0.1465  0.0394  0.0461  522 PHE C CG  
8611  C CD1 . PHE C 221 ? 0.8334 1.2268 0.8314 0.1383  0.0375  0.0467  522 PHE C CD1 
8612  C CD2 . PHE C 221 ? 0.9043 1.2053 0.8785 0.1521  0.0358  0.0496  522 PHE C CD2 
8613  C CE1 . PHE C 221 ? 0.8129 1.2293 0.8184 0.1364  0.0318  0.0502  522 PHE C CE1 
8614  C CE2 . PHE C 221 ? 0.8586 1.1822 0.8403 0.1509  0.0304  0.0535  522 PHE C CE2 
8615  C CZ  . PHE C 221 ? 0.8013 1.1824 0.7986 0.1434  0.0282  0.0536  522 PHE C CZ  
8616  N N   . ASP C 222 ? 0.8919 1.0853 0.8147 0.1875  0.0575  0.0358  523 ASP C N   
8617  C CA  . ASP C 222 ? 0.7945 0.9552 0.7026 0.1874  0.0624  0.0303  523 ASP C CA  
8618  C C   . ASP C 222 ? 0.7675 0.8865 0.6710 0.1636  0.0585  0.0291  523 ASP C C   
8619  O O   . ASP C 222 ? 0.8105 0.8928 0.7048 0.1638  0.0557  0.0315  523 ASP C O   
8620  C CB  . ASP C 222 ? 0.9040 1.0322 0.7900 0.2159  0.0674  0.0295  523 ASP C CB  
8621  C CG  . ASP C 222 ? 1.0044 1.1740 0.8931 0.2435  0.0719  0.0300  523 ASP C CG  
8622  O OD1 . ASP C 222 ? 1.0622 1.2889 0.9704 0.2380  0.0723  0.0298  523 ASP C OD1 
8623  O OD2 . ASP C 222 ? 0.9763 1.1211 0.8463 0.2707  0.0753  0.0306  523 ASP C OD2 
8624  N N   . VAL C 223 ? 0.6429 0.7680 0.5519 0.1436  0.0585  0.0257  524 VAL C N   
8625  C CA  . VAL C 223 ? 0.4998 0.5886 0.4044 0.1230  0.0548  0.0245  524 VAL C CA  
8626  C C   . VAL C 223 ? 0.5432 0.5832 0.4260 0.1314  0.0577  0.0214  524 VAL C C   
8627  O O   . VAL C 223 ? 0.6098 0.6447 0.4816 0.1418  0.0633  0.0171  524 VAL C O   
8628  C CB  . VAL C 223 ? 0.5246 0.6298 0.4372 0.1020  0.0541  0.0222  524 VAL C CB  
8629  C CG1 . VAL C 223 ? 0.5003 0.5688 0.4072 0.0841  0.0501  0.0212  524 VAL C CG1 
8630  C CG2 . VAL C 223 ? 0.4405 0.5906 0.3716 0.0911  0.0511  0.0251  524 VAL C CG2 
8631  N N   . LEU C 224 ? 0.5011 0.5056 0.3767 0.1261  0.0541  0.0233  525 LEU C N   
8632  C CA  . LEU C 224 ? 0.7662 0.7223 0.6194 0.1306  0.0565  0.0206  525 LEU C CA  
8633  C C   . LEU C 224 ? 0.7551 0.6970 0.6031 0.1149  0.0569  0.0152  525 LEU C C   
8634  O O   . LEU C 224 ? 0.8255 0.7862 0.6871 0.0974  0.0536  0.0153  525 LEU C O   
8635  C CB  . LEU C 224 ? 0.7686 0.6949 0.6163 0.1252  0.0523  0.0245  525 LEU C CB  
8636  C CG  . LEU C 224 ? 0.8487 0.7733 0.6920 0.1437  0.0526  0.0300  525 LEU C CG  
8637  C CD1 . LEU C 224 ? 0.7375 0.6549 0.5866 0.1319  0.0470  0.0350  525 LEU C CD1 
8638  C CD2 . LEU C 224 ? 0.9241 0.8072 0.7401 0.1614  0.0575  0.0285  525 LEU C CD2 
8639  N N   . PRO C 225 ? 0.6349 0.5424 0.4614 0.1208  0.0609  0.0104  526 PRO C N   
8640  C CA  . PRO C 225 ? 0.5655 0.4580 0.3854 0.1052  0.0607  0.0053  526 PRO C CA  
8641  C C   . PRO C 225 ? 0.7410 0.6115 0.5614 0.0859  0.0548  0.0068  526 PRO C C   
8642  O O   . PRO C 225 ? 0.9432 0.8034 0.7649 0.0856  0.0519  0.0111  526 PRO C O   
8643  C CB  . PRO C 225 ? 0.6855 0.5449 0.4794 0.1190  0.0667  -0.0004 526 PRO C CB  
8644  C CG  . PRO C 225 ? 0.8062 0.6429 0.5887 0.1349  0.0677  0.0029  526 PRO C CG  
8645  C CD  . PRO C 225 ? 0.7442 0.6207 0.5486 0.1417  0.0654  0.0095  526 PRO C CD  
8646  N N   . LEU C 226 ? 0.7160 0.5816 0.5350 0.0700  0.0529  0.0035  527 LEU C N   
8647  C CA  . LEU C 226 ? 0.7805 0.6242 0.5965 0.0532  0.0480  0.0037  527 LEU C CA  
8648  C C   . LEU C 226 ? 0.8906 0.6921 0.6813 0.0549  0.0506  -0.0005 527 LEU C C   
8649  O O   . LEU C 226 ? 1.0446 0.8332 0.8193 0.0637  0.0557  -0.0058 527 LEU C O   
8650  C CB  . LEU C 226 ? 0.7624 0.6192 0.5860 0.0368  0.0445  0.0022  527 LEU C CB  
8651  C CG  . LEU C 226 ? 0.6809 0.5715 0.5262 0.0313  0.0409  0.0067  527 LEU C CG  
8652  C CD1 . LEU C 226 ? 0.4895 0.3887 0.3385 0.0169  0.0376  0.0059  527 LEU C CD1 
8653  C CD2 . LEU C 226 ? 0.5082 0.3998 0.3639 0.0283  0.0364  0.0115  527 LEU C CD2 
8654  N N   . LEU C 227 ? 0.8780 0.6577 0.6636 0.0464  0.0475  0.0016  528 LEU C N   
8655  C CA  . LEU C 227 ? 0.8257 0.5632 0.5859 0.0420  0.0491  -0.0022 528 LEU C CA  
8656  C C   . LEU C 227 ? 0.8434 0.5802 0.6076 0.0194  0.0436  -0.0030 528 LEU C C   
8657  O O   . LEU C 227 ? 0.8027 0.5353 0.5706 0.0104  0.0402  0.0007  528 LEU C O   
8658  C CB  . LEU C 227 ? 0.7962 0.5069 0.5432 0.0510  0.0509  0.0015  528 LEU C CB  
8659  C CG  . LEU C 227 ? 0.8288 0.4978 0.5451 0.0654  0.0568  -0.0016 528 LEU C CG  
8660  C CD1 . LEU C 227 ? 0.8164 0.4557 0.5194 0.0655  0.0564  0.0036  528 LEU C CD1 
8661  C CD2 . LEU C 227 ? 0.8319 0.4721 0.5255 0.0568  0.0590  -0.0101 528 LEU C CD2 
8662  N N   . LEU C 228 ? 0.9006 0.6438 0.6638 0.0107  0.0426  -0.0077 529 LEU C N   
8663  C CA  . LEU C 228 ? 0.7875 0.5379 0.5571 -0.0086 0.0367  -0.0079 529 LEU C CA  
8664  C C   . LEU C 228 ? 0.7869 0.5048 0.5335 -0.0209 0.0368  -0.0129 529 LEU C C   
8665  O O   . LEU C 228 ? 0.7290 0.4202 0.4530 -0.0158 0.0415  -0.0185 529 LEU C O   
8666  C CB  . LEU C 228 ? 0.7018 0.4781 0.4823 -0.0118 0.0349  -0.0092 529 LEU C CB  
8667  C CG  . LEU C 228 ? 0.6470 0.4520 0.4468 -0.0009 0.0356  -0.0044 529 LEU C CG  
8668  C CD1 . LEU C 228 ? 0.5238 0.3525 0.3328 -0.0050 0.0340  -0.0045 529 LEU C CD1 
8669  C CD2 . LEU C 228 ? 0.5404 0.3572 0.3566 -0.0032 0.0315  0.0016  529 LEU C CD2 
8670  N N   . GLN C 229 ? 0.8130 0.5335 0.5643 -0.0370 0.0317  -0.0111 530 GLN C N   
8671  C CA  . GLN C 229 ? 0.7568 0.4510 0.4879 -0.0531 0.0309  -0.0151 530 GLN C CA  
8672  C C   . GLN C 229 ? 0.8348 0.5520 0.5763 -0.0705 0.0243  -0.0159 530 GLN C C   
8673  O O   . GLN C 229 ? 0.7554 0.4986 0.5173 -0.0744 0.0198  -0.0109 530 GLN C O   
8674  C CB  . GLN C 229 ? 0.8311 0.5048 0.5543 -0.0569 0.0316  -0.0115 530 GLN C CB  
8675  C CG  . GLN C 229 ? 0.9189 0.5797 0.6291 -0.0799 0.0287  -0.0142 530 GLN C CG  
8676  C CD  . GLN C 229 ? 0.9677 0.6045 0.6657 -0.0865 0.0302  -0.0106 530 GLN C CD  
8677  O OE1 . GLN C 229 ? 0.8818 0.5277 0.5921 -0.0780 0.0305  -0.0040 530 GLN C OE1 
8678  N NE2 . GLN C 229 ? 1.0418 0.6467 0.7135 -0.1030 0.0311  -0.0149 530 GLN C NE2 
8679  N N   . ALA C 230 ? 0.8944 0.6016 0.6204 -0.0802 0.0238  -0.0224 531 ALA C N   
8680  C CA  . ALA C 230 ? 0.7327 0.4619 0.4655 -0.0960 0.0174  -0.0236 531 ALA C CA  
8681  C C   . ALA C 230 ? 0.8018 0.5114 0.5152 -0.1158 0.0160  -0.0280 531 ALA C C   
8682  O O   . ALA C 230 ? 0.7729 0.4447 0.4603 -0.1178 0.0207  -0.0328 531 ALA C O   
8683  C CB  . ALA C 230 ? 0.7604 0.4999 0.4917 -0.0930 0.0170  -0.0272 531 ALA C CB  
8684  N N   . ASN C 231 ? 0.8410 0.5772 0.5664 -0.1304 0.0095  -0.0263 532 ASN C N   
8685  C CA  . ASN C 231 ? 0.8879 0.6172 0.5990 -0.1529 0.0069  -0.0301 532 ASN C CA  
8686  C C   . ASN C 231 ? 0.9155 0.6004 0.5996 -0.1600 0.0122  -0.0328 532 ASN C C   
8687  O O   . ASN C 231 ? 1.0042 0.6602 0.6615 -0.1706 0.0139  -0.0401 532 ASN C O   
8688  C CB  . ASN C 231 ? 0.9674 0.7019 0.6680 -0.1627 0.0038  -0.0365 532 ASN C CB  
8689  C CG  . ASN C 231 ? 1.0894 0.8387 0.7866 -0.1865 -0.0019 -0.0386 532 ASN C CG  
8690  O OD1 . ASN C 231 ? 1.2420 1.0170 0.9561 -0.1925 -0.0054 -0.0336 532 ASN C OD1 
8691  N ND2 . ASN C 231 ? 1.0538 0.7888 0.7288 -0.2005 -0.0026 -0.0463 532 ASN C ND2 
8692  N N   . GLY C 232 ? 0.8625 0.5393 0.5512 -0.1541 0.0148  -0.0271 533 GLY C N   
8693  C CA  . GLY C 232 ? 0.9478 0.5803 0.6100 -0.1596 0.0197  -0.0279 533 GLY C CA  
8694  C C   . GLY C 232 ? 1.0540 0.6408 0.6888 -0.1464 0.0264  -0.0328 533 GLY C C   
8695  O O   . GLY C 232 ? 0.9789 0.5235 0.5887 -0.1477 0.0308  -0.0328 533 GLY C O   
8696  N N   . ASN C 233 ? 0.9929 0.5860 0.6301 -0.1329 0.0275  -0.0367 534 ASN C N   
8697  C CA  . ASN C 233 ? 1.0218 0.5739 0.6310 -0.1208 0.0340  -0.0429 534 ASN C CA  
8698  C C   . ASN C 233 ? 0.9947 0.5323 0.6047 -0.0961 0.0395  -0.0380 534 ASN C C   
8699  O O   . ASN C 233 ? 1.0250 0.5882 0.6596 -0.0881 0.0380  -0.0300 534 ASN C O   
8700  C CB  . ASN C 233 ? 1.0900 0.6577 0.7014 -0.1158 0.0336  -0.0488 534 ASN C CB  
8701  C CG  . ASN C 233 ? 1.0977 0.6710 0.6997 -0.1400 0.0286  -0.0550 534 ASN C CG  
8702  O OD1 . ASN C 233 ? 1.1663 0.7063 0.7405 -0.1571 0.0293  -0.0604 534 ASN C OD1 
8703  N ND2 . ASN C 233 ? 1.0042 0.6194 0.6282 -0.1422 0.0233  -0.0539 534 ASN C ND2 
8704  N N   . ASP C 234 ? 0.9691 0.4646 0.5501 -0.0835 0.0459  -0.0431 535 ASP C N   
8705  C CA  . ASP C 234 ? 0.9256 0.4101 0.5062 -0.0568 0.0512  -0.0389 535 ASP C CA  
8706  C C   . ASP C 234 ? 0.9586 0.4915 0.5726 -0.0398 0.0504  -0.0352 535 ASP C C   
8707  O O   . ASP C 234 ? 1.1302 0.6874 0.7539 -0.0424 0.0488  -0.0391 535 ASP C O   
8708  C CB  . ASP C 234 ? 0.9881 0.4231 0.5317 -0.0430 0.0583  -0.0462 535 ASP C CB  
8709  C CG  . ASP C 234 ? 1.1228 0.5002 0.6285 -0.0559 0.0602  -0.0484 535 ASP C CG  
8710  O OD1 . ASP C 234 ? 1.2449 0.5747 0.7164 -0.0432 0.0662  -0.0539 535 ASP C OD1 
8711  O OD2 . ASP C 234 ? 1.1422 0.5212 0.6506 -0.0789 0.0560  -0.0448 535 ASP C OD2 
8712  N N   . PRO C 235 ? 0.9653 0.5128 0.5959 -0.0236 0.0513  -0.0277 536 PRO C N   
8713  C CA  . PRO C 235 ? 0.9594 0.5528 0.6207 -0.0107 0.0503  -0.0241 536 PRO C CA  
8714  C C   . PRO C 235 ? 0.8910 0.4841 0.5450 0.0095  0.0561  -0.0288 536 PRO C C   
8715  O O   . PRO C 235 ? 1.0132 0.5690 0.6390 0.0207  0.0617  -0.0336 536 PRO C O   
8716  C CB  . PRO C 235 ? 0.8821 0.4864 0.5585 -0.0014 0.0496  -0.0152 536 PRO C CB  
8717  C CG  . PRO C 235 ? 0.7714 0.3283 0.4186 0.0011  0.0531  -0.0148 536 PRO C CG  
8718  C CD  . PRO C 235 ? 0.8256 0.3523 0.4495 -0.0208 0.0522  -0.0212 536 PRO C CD  
8719  N N   . GLU C 236 ? 0.7946 0.4300 0.4735 0.0144  0.0548  -0.0272 537 GLU C N   
8720  C CA  . GLU C 236 ? 0.8354 0.4813 0.5115 0.0294  0.0598  -0.0317 537 GLU C CA  
8721  C C   . GLU C 236 ? 0.8613 0.5474 0.5635 0.0442  0.0605  -0.0257 537 GLU C C   
8722  O O   . GLU C 236 ? 0.8301 0.5472 0.5573 0.0354  0.0553  -0.0201 537 GLU C O   
8723  C CB  . GLU C 236 ? 0.8186 0.4762 0.4947 0.0149  0.0576  -0.0371 537 GLU C CB  
8724  C CG  . GLU C 236 ? 0.9297 0.5499 0.5792 -0.0012 0.0566  -0.0437 537 GLU C CG  
8725  C CD  . GLU C 236 ? 0.9783 0.6077 0.6234 -0.0139 0.0547  -0.0498 537 GLU C CD  
8726  O OE1 . GLU C 236 ? 0.9286 0.5799 0.5797 -0.0049 0.0573  -0.0515 537 GLU C OE1 
8727  O OE2 . GLU C 236 ? 1.0157 0.6314 0.6505 -0.0338 0.0504  -0.0527 537 GLU C OE2 
8728  N N   . LEU C 237 ? 0.7719 0.4579 0.4670 0.0667  0.0668  -0.0272 538 LEU C N   
8729  C CA  . LEU C 237 ? 0.7129 0.4402 0.4317 0.0803  0.0678  -0.0219 538 LEU C CA  
8730  C C   . LEU C 237 ? 0.8355 0.6011 0.5706 0.0743  0.0674  -0.0231 538 LEU C C   
8731  O O   . LEU C 237 ? 0.8182 0.5770 0.5405 0.0714  0.0700  -0.0296 538 LEU C O   
8732  C CB  . LEU C 237 ? 0.7430 0.4618 0.4488 0.1076  0.0747  -0.0229 538 LEU C CB  
8733  C CG  . LEU C 237 ? 0.9321 0.6206 0.6252 0.1189  0.0751  -0.0187 538 LEU C CG  
8734  C CD1 . LEU C 237 ? 0.9944 0.6735 0.6712 0.1488  0.0822  -0.0205 538 LEU C CD1 
8735  C CD2 . LEU C 237 ? 0.8627 0.5768 0.5806 0.1142  0.0697  -0.0095 538 LEU C CD2 
8736  N N   . PHE C 238 ? 0.8451 0.6494 0.6066 0.0716  0.0642  -0.0169 539 PHE C N   
8737  C CA  . PHE C 238 ? 0.7923 0.6338 0.5682 0.0679  0.0648  -0.0169 539 PHE C CA  
8738  C C   . PHE C 238 ? 0.7784 0.6576 0.5753 0.0766  0.0651  -0.0111 539 PHE C C   
8739  O O   . PHE C 238 ? 0.7085 0.5918 0.5174 0.0742  0.0609  -0.0056 539 PHE C O   
8740  C CB  . PHE C 238 ? 0.8197 0.6682 0.6046 0.0455  0.0583  -0.0154 539 PHE C CB  
8741  C CG  . PHE C 238 ? 0.8555 0.6739 0.6224 0.0343  0.0567  -0.0206 539 PHE C CG  
8742  C CD1 . PHE C 238 ? 0.9696 0.7597 0.7286 0.0271  0.0533  -0.0204 539 PHE C CD1 
8743  C CD2 . PHE C 238 ? 0.7499 0.5702 0.5072 0.0294  0.0585  -0.0255 539 PHE C CD2 
8744  C CE1 . PHE C 238 ? 1.0161 0.7813 0.7581 0.0146  0.0515  -0.0255 539 PHE C CE1 
8745  C CE2 . PHE C 238 ? 0.7491 0.5435 0.4889 0.0179  0.0565  -0.0307 539 PHE C CE2 
8746  C CZ  . PHE C 238 ? 0.8603 0.6280 0.5928 0.0101  0.0529  -0.0309 539 PHE C CZ  
8747  N N   . GLN C 239 ? 0.7478 0.6568 0.5491 0.0855  0.0700  -0.0125 540 GLN C N   
8748  C CA  . GLN C 239 ? 0.7620 0.7131 0.5838 0.0907  0.0702  -0.0075 540 GLN C CA  
8749  C C   . GLN C 239 ? 0.6880 0.6643 0.5258 0.0701  0.0657  -0.0041 540 GLN C C   
8750  O O   . GLN C 239 ? 0.5353 0.5197 0.3696 0.0622  0.0675  -0.0066 540 GLN C O   
8751  C CB  . GLN C 239 ? 0.7339 0.7094 0.5527 0.1103  0.0781  -0.0104 540 GLN C CB  
8752  C CG  . GLN C 239 ? 0.8040 0.8304 0.6448 0.1117  0.0782  -0.0056 540 GLN C CG  
8753  C CD  . GLN C 239 ? 0.9450 1.0073 0.7870 0.1193  0.0852  -0.0087 540 GLN C CD  
8754  O OE1 . GLN C 239 ? 1.1191 1.1667 0.9443 0.1271  0.0905  -0.0149 540 GLN C OE1 
8755  N NE2 . GLN C 239 ? 0.9177 1.0284 0.7786 0.1158  0.0853  -0.0048 540 GLN C NE2 
8756  N N   . ILE C 240 ? 0.6754 0.6617 0.5285 0.0617  0.0601  0.0015  541 ILE C N   
8757  C CA  . ILE C 240 ? 0.6500 0.6558 0.5156 0.0430  0.0557  0.0048  541 ILE C CA  
8758  C C   . ILE C 240 ? 0.6604 0.7058 0.5333 0.0438  0.0601  0.0052  541 ILE C C   
8759  O O   . ILE C 240 ? 0.6726 0.7441 0.5533 0.0561  0.0631  0.0063  541 ILE C O   
8760  C CB  . ILE C 240 ? 0.6439 0.6527 0.5227 0.0363  0.0495  0.0100  541 ILE C CB  
8761  C CG1 . ILE C 240 ? 0.6743 0.6482 0.5465 0.0351  0.0456  0.0098  541 ILE C CG1 
8762  C CG2 . ILE C 240 ? 0.5907 0.6127 0.4779 0.0179  0.0450  0.0129  541 ILE C CG2 
8763  C CD1 . ILE C 240 ? 0.6571 0.6333 0.5409 0.0280  0.0397  0.0142  541 ILE C CD1 
8764  N N   . PRO C 241 ? 0.6178 0.6714 0.4880 0.0311  0.0607  0.0046  542 PRO C N   
8765  C CA  . PRO C 241 ? 0.5468 0.6404 0.4232 0.0295  0.0654  0.0053  542 PRO C CA  
8766  C C   . PRO C 241 ? 0.5608 0.6846 0.4539 0.0242  0.0629  0.0102  542 PRO C C   
8767  O O   . PRO C 241 ? 0.4448 0.5598 0.3434 0.0101  0.0564  0.0139  542 PRO C O   
8768  C CB  . PRO C 241 ? 0.6718 0.7611 0.5410 0.0118  0.0644  0.0056  542 PRO C CB  
8769  C CG  . PRO C 241 ? 0.6206 0.6708 0.4817 0.0051  0.0585  0.0053  542 PRO C CG  
8770  C CD  . PRO C 241 ? 0.7263 0.7535 0.5852 0.0191  0.0579  0.0030  542 PRO C CD  
8771  N N   . PRO C 242 ? 0.5628 0.7228 0.4636 0.0364  0.0678  0.0099  543 PRO C N   
8772  C CA  . PRO C 242 ? 0.5430 0.7363 0.4596 0.0317  0.0654  0.0141  543 PRO C CA  
8773  C C   . PRO C 242 ? 0.6443 0.8467 0.5655 0.0061  0.0612  0.0178  543 PRO C C   
8774  O O   . PRO C 242 ? 0.6899 0.8946 0.6193 -0.0024 0.0558  0.0209  543 PRO C O   
8775  C CB  . PRO C 242 ? 0.5231 0.7606 0.4445 0.0465  0.0728  0.0124  543 PRO C CB  
8776  C CG  . PRO C 242 ? 0.5130 0.7259 0.4209 0.0690  0.0776  0.0075  543 PRO C CG  
8777  C CD  . PRO C 242 ? 0.6023 0.7709 0.4961 0.0585  0.0754  0.0054  543 PRO C CD  
8778  N N   . GLU C 243 ? 0.5933 0.7987 0.5073 -0.0066 0.0635  0.0175  544 GLU C N   
8779  C CA  . GLU C 243 ? 0.5741 0.7850 0.4887 -0.0312 0.0599  0.0215  544 GLU C CA  
8780  C C   . GLU C 243 ? 0.5998 0.7729 0.5117 -0.0407 0.0518  0.0238  544 GLU C C   
8781  O O   . GLU C 243 ? 0.7028 0.8749 0.6138 -0.0594 0.0479  0.0272  544 GLU C O   
8782  C CB  . GLU C 243 ? 0.5824 0.7960 0.4860 -0.0425 0.0637  0.0214  544 GLU C CB  
8783  C CG  . GLU C 243 ? 0.5372 0.7117 0.4267 -0.0385 0.0630  0.0189  544 GLU C CG  
8784  C CD  . GLU C 243 ? 0.6873 0.8667 0.5713 -0.0193 0.0701  0.0132  544 GLU C CD  
8785  O OE1 . GLU C 243 ? 0.4855 0.6925 0.3777 -0.0040 0.0747  0.0113  544 GLU C OE1 
8786  O OE2 . GLU C 243 ? 0.8702 1.0265 0.7405 -0.0191 0.0711  0.0105  544 GLU C OE2 
8787  N N   . LEU C 244 ? 0.5109 0.6530 0.4200 -0.0284 0.0494  0.0219  545 LEU C N   
8788  C CA  . LEU C 244 ? 0.4952 0.6053 0.4028 -0.0353 0.0421  0.0237  545 LEU C CA  
8789  C C   . LEU C 244 ? 0.4641 0.5757 0.3817 -0.0289 0.0387  0.0246  545 LEU C C   
8790  O O   . LEU C 244 ? 0.5633 0.6529 0.4805 -0.0349 0.0329  0.0260  545 LEU C O   
8791  C CB  . LEU C 244 ? 0.4831 0.5587 0.3803 -0.0295 0.0410  0.0213  545 LEU C CB  
8792  C CG  . LEU C 244 ? 0.5633 0.6293 0.4482 -0.0369 0.0423  0.0206  545 LEU C CG  
8793  C CD1 . LEU C 244 ? 0.4411 0.4772 0.3174 -0.0292 0.0411  0.0173  545 LEU C CD1 
8794  C CD2 . LEU C 244 ? 0.4362 0.4946 0.3168 -0.0552 0.0374  0.0250  545 LEU C CD2 
8795  N N   . VAL C 245 ? 0.5760 0.7130 0.5017 -0.0158 0.0422  0.0239  546 VAL C N   
8796  C CA  . VAL C 245 ? 0.6224 0.7614 0.5565 -0.0087 0.0390  0.0251  546 VAL C CA  
8797  C C   . VAL C 245 ? 0.5467 0.7212 0.4905 -0.0193 0.0379  0.0273  546 VAL C C   
8798  O O   . VAL C 245 ? 0.5425 0.7544 0.4935 -0.0126 0.0419  0.0272  546 VAL C O   
8799  C CB  . VAL C 245 ? 0.6187 0.7585 0.5528 0.0141  0.0427  0.0236  546 VAL C CB  
8800  C CG1 . VAL C 245 ? 0.6657 0.8113 0.6079 0.0206  0.0394  0.0259  546 VAL C CG1 
8801  C CG2 . VAL C 245 ? 0.6329 0.7335 0.5546 0.0211  0.0434  0.0210  546 VAL C CG2 
8802  N N   . LEU C 246 ? 0.4932 0.6563 0.4362 -0.0362 0.0324  0.0289  547 LEU C N   
8803  C CA  . LEU C 246 ? 0.4925 0.6842 0.4421 -0.0493 0.0306  0.0304  547 LEU C CA  
8804  C C   . LEU C 246 ? 0.4525 0.6625 0.4124 -0.0371 0.0292  0.0307  547 LEU C C   
8805  O O   . LEU C 246 ? 0.4481 0.6346 0.4076 -0.0266 0.0267  0.0307  547 LEU C O   
8806  C CB  . LEU C 246 ? 0.4592 0.6261 0.4012 -0.0688 0.0249  0.0315  547 LEU C CB  
8807  C CG  . LEU C 246 ? 0.4827 0.6723 0.4272 -0.0862 0.0226  0.0324  547 LEU C CG  
8808  C CD1 . LEU C 246 ? 0.4085 0.6403 0.3567 -0.0941 0.0276  0.0330  547 LEU C CD1 
8809  C CD2 . LEU C 246 ? 0.4127 0.5684 0.3440 -0.1042 0.0178  0.0332  547 LEU C CD2 
8810  N N   . GLU C 247 ? 0.3775 0.6321 0.3464 -0.0382 0.0311  0.0313  548 GLU C N   
8811  C CA  . GLU C 247 ? 0.3954 0.6748 0.3742 -0.0245 0.0303  0.0321  548 GLU C CA  
8812  C C   . GLU C 247 ? 0.5112 0.8296 0.4973 -0.0408 0.0279  0.0328  548 GLU C C   
8813  O O   . GLU C 247 ? 0.5125 0.8562 0.4989 -0.0562 0.0302  0.0327  548 GLU C O   
8814  C CB  . GLU C 247 ? 0.4349 0.7366 0.4175 -0.0008 0.0362  0.0318  548 GLU C CB  
8815  C CG  . GLU C 247 ? 0.3817 0.6447 0.3555 0.0176  0.0384  0.0307  548 GLU C CG  
8816  C CD  . GLU C 247 ? 0.5564 0.8404 0.5318 0.0435  0.0436  0.0306  548 GLU C CD  
8817  O OE1 . GLU C 247 ? 0.6494 0.9700 0.6288 0.0464  0.0484  0.0296  548 GLU C OE1 
8818  O OE2 . GLU C 247 ? 0.6700 0.9351 0.6418 0.0615  0.0431  0.0316  548 GLU C OE2 
8819  N N   . VAL C 248 ? 0.4778 0.8017 0.4687 -0.0388 0.0234  0.0335  549 VAL C N   
8820  C CA  . VAL C 248 ? 0.5195 0.8767 0.5155 -0.0565 0.0201  0.0335  549 VAL C CA  
8821  C C   . VAL C 248 ? 0.6367 1.0412 0.6452 -0.0401 0.0208  0.0349  549 VAL C C   
8822  O O   . VAL C 248 ? 0.7142 1.1080 0.7243 -0.0204 0.0194  0.0362  549 VAL C O   
8823  C CB  . VAL C 248 ? 0.5681 0.8939 0.5574 -0.0703 0.0136  0.0325  549 VAL C CB  
8824  C CG1 . VAL C 248 ? 0.6811 1.0399 0.6729 -0.0905 0.0103  0.0317  549 VAL C CG1 
8825  C CG2 . VAL C 248 ? 0.5284 0.8071 0.5043 -0.0827 0.0128  0.0316  549 VAL C CG2 
8826  N N   . PRO C 249 ? 0.6164 1.0747 0.6333 -0.0469 0.0229  0.0350  550 PRO C N   
8827  C CA  . PRO C 249 ? 0.5451 1.0535 0.5743 -0.0317 0.0225  0.0367  550 PRO C CA  
8828  C C   . PRO C 249 ? 0.6651 1.1815 0.6959 -0.0458 0.0155  0.0365  550 PRO C C   
8829  O O   . PRO C 249 ? 0.7753 1.2884 0.8011 -0.0740 0.0125  0.0345  550 PRO C O   
8830  C CB  . PRO C 249 ? 0.5110 1.0765 0.5484 -0.0378 0.0273  0.0364  550 PRO C CB  
8831  C CG  . PRO C 249 ? 0.5692 1.1165 0.5975 -0.0686 0.0277  0.0348  550 PRO C CG  
8832  C CD  . PRO C 249 ? 0.5445 1.0220 0.5594 -0.0680 0.0262  0.0342  550 PRO C CD  
8833  N N   . ILE C 250 ? 0.6187 1.1420 0.6540 -0.0264 0.0128  0.0385  551 ILE C N   
8834  C CA  . ILE C 250 ? 0.5809 1.1077 0.6162 -0.0371 0.0060  0.0381  551 ILE C CA  
8835  C C   . ILE C 250 ? 0.5680 1.1629 0.6144 -0.0456 0.0043  0.0384  551 ILE C C   
8836  O O   . ILE C 250 ? 0.4861 1.1245 0.5429 -0.0240 0.0059  0.0412  551 ILE C O   
8837  C CB  . ILE C 250 ? 0.5174 1.0197 0.5509 -0.0138 0.0037  0.0407  551 ILE C CB  
8838  C CG1 . ILE C 250 ? 0.4332 0.8773 0.4572 -0.0018 0.0067  0.0410  551 ILE C CG1 
8839  C CG2 . ILE C 250 ? 0.5064 1.0013 0.5364 -0.0282 -0.0031 0.0394  551 ILE C CG2 
8840  C CD1 . ILE C 250 ? 0.3496 0.7486 0.3638 -0.0226 0.0048  0.0379  551 ILE C CD1 
8841  N N   . ARG C 251 ? 0.6268 1.2311 0.6699 -0.0770 0.0008  0.0354  552 ARG C N   
8842  C CA  . ARG C 251 ? 0.6223 1.2891 0.6743 -0.0900 -0.0025 0.0350  552 ARG C CA  
8843  C C   . ARG C 251 ? 0.5524 1.2015 0.5957 -0.1109 -0.0096 0.0320  552 ARG C C   
8844  O O   . ARG C 251 ? 0.5284 1.1188 0.5581 -0.1201 -0.0113 0.0296  552 ARG C O   
8845  C CB  . ARG C 251 ? 0.4720 1.1787 0.5274 -0.1122 0.0010  0.0337  552 ARG C CB  
8846  C CG  . ARG C 251 ? 0.6110 1.2724 0.6508 -0.1416 0.0014  0.0309  552 ARG C CG  
8847  C CD  . ARG C 251 ? 0.6110 1.2363 0.6461 -0.1310 0.0077  0.0320  552 ARG C CD  
8848  N NE  . ARG C 251 ? 0.4959 1.0809 0.5150 -0.1593 0.0076  0.0301  552 ARG C NE  
8849  C CZ  . ARG C 251 ? 0.5879 1.1207 0.5967 -0.1554 0.0102  0.0304  552 ARG C CZ  
8850  N NH1 . ARG C 251 ? 0.6583 1.1566 0.6510 -0.1812 0.0094  0.0293  552 ARG C NH1 
8851  N NH2 . ARG C 251 ? 0.5365 1.0504 0.5493 -0.1263 0.0133  0.0319  552 ARG C NH2 
8852  N N   . HIS C 252 ? 0.5601 1.2628 0.6111 -0.1172 -0.0140 0.0318  553 HIS C N   
8853  C CA  . HIS C 252 ? 0.4582 1.1522 0.5015 -0.1332 -0.0211 0.0287  553 HIS C CA  
8854  C C   . HIS C 252 ? 0.5022 1.2260 0.5410 -0.1712 -0.0238 0.0244  553 HIS C C   
8855  O O   . HIS C 252 ? 0.5272 1.3108 0.5769 -0.1788 -0.0218 0.0254  553 HIS C O   
8856  C CB  . HIS C 252 ? 0.4905 1.2205 0.5436 -0.1107 -0.0249 0.0319  553 HIS C CB  
8857  C CG  . HIS C 252 ? 0.5037 1.2145 0.5473 -0.1211 -0.0317 0.0290  553 HIS C CG  
8858  N ND1 . HIS C 252 ? 0.5246 1.2709 0.5661 -0.1474 -0.0372 0.0250  553 HIS C ND1 
8859  C CD2 . HIS C 252 ? 0.4085 1.0693 0.4431 -0.1094 -0.0336 0.0290  553 HIS C CD2 
8860  C CE1 . HIS C 252 ? 0.4763 1.1935 0.5074 -0.1504 -0.0422 0.0224  553 HIS C CE1 
8861  N NE2 . HIS C 252 ? 0.5326 1.1989 0.5598 -0.1274 -0.0400 0.0249  553 HIS C NE2 
8862  N N   . PRO C 253 ? 0.5472 1.2309 0.5690 -0.1956 -0.0281 0.0195  554 PRO C N   
8863  C CA  . PRO C 253 ? 0.5120 1.2122 0.5240 -0.2353 -0.0304 0.0150  554 PRO C CA  
8864  C C   . PRO C 253 ? 0.5908 1.3614 0.6116 -0.2475 -0.0351 0.0138  554 PRO C C   
8865  O O   . PRO C 253 ? 0.5966 1.3959 0.6127 -0.2805 -0.0360 0.0109  554 PRO C O   
8866  C CB  . PRO C 253 ? 0.5015 1.1300 0.4897 -0.2518 -0.0337 0.0098  554 PRO C CB  
8867  C CG  . PRO C 253 ? 0.5136 1.1102 0.5040 -0.2218 -0.0350 0.0112  554 PRO C CG  
8868  C CD  . PRO C 253 ? 0.4977 1.1116 0.5056 -0.1888 -0.0300 0.0176  554 PRO C CD  
8869  N N   . LYS C 254 ? 0.6328 1.4322 0.6650 -0.2240 -0.0385 0.0161  555 LYS C N   
8870  C CA  . LYS C 254 ? 0.6293 1.5033 0.6717 -0.2333 -0.0434 0.0156  555 LYS C CA  
8871  C C   . LYS C 254 ? 0.5812 1.5144 0.6443 -0.1998 -0.0403 0.0223  555 LYS C C   
8872  O O   . LYS C 254 ? 0.5837 1.5647 0.6477 -0.2042 -0.0371 0.0231  555 LYS C O   
8873  C CB  . LYS C 254 ? 0.8000 1.6597 0.8325 -0.2377 -0.0509 0.0121  555 LYS C CB  
8874  C CG  . LYS C 254 ? 0.9559 1.7675 0.9635 -0.2749 -0.0539 0.0041  555 LYS C CG  
8875  C CD  . LYS C 254 ? 1.0444 1.8708 1.0399 -0.3063 -0.0491 0.0020  555 LYS C CD  
8876  C CE  . LYS C 254 ? 1.0551 1.8244 1.0214 -0.3414 -0.0510 -0.0054 555 LYS C CE  
8877  N NZ  . LYS C 254 ? 1.0192 1.7793 0.9743 -0.3467 -0.0565 -0.0102 555 LYS C NZ  
8878  N N   . PHE C 255 ? 0.6308 1.5444 0.7015 -0.1631 -0.0387 0.0271  556 PHE C N   
8879  C CA  . PHE C 255 ? 0.6287 1.5945 0.7176 -0.1280 -0.0366 0.0336  556 PHE C CA  
8880  C C   . PHE C 255 ? 0.5575 1.5396 0.6546 -0.1225 -0.0286 0.0353  556 PHE C C   
8881  O O   . PHE C 255 ? 0.5226 1.4549 0.6154 -0.1057 -0.0232 0.0368  556 PHE C O   
8882  C CB  . PHE C 255 ? 0.6763 1.6003 0.7627 -0.0919 -0.0367 0.0381  556 PHE C CB  
8883  C CG  . PHE C 255 ? 0.7084 1.6135 0.7855 -0.0967 -0.0439 0.0366  556 PHE C CG  
8884  C CD1 . PHE C 255 ? 0.6714 1.5137 0.7385 -0.0794 -0.0439 0.0381  556 PHE C CD1 
8885  C CD2 . PHE C 255 ? 0.6081 1.5607 0.6862 -0.1196 -0.0506 0.0333  556 PHE C CD2 
8886  C CE1 . PHE C 255 ? 0.7179 1.5458 0.7763 -0.0837 -0.0500 0.0366  556 PHE C CE1 
8887  C CE2 . PHE C 255 ? 0.5992 1.5351 0.6676 -0.1240 -0.0570 0.0313  556 PHE C CE2 
8888  C CZ  . PHE C 255 ? 0.6580 1.5318 0.7167 -0.1054 -0.0565 0.0330  556 PHE C CZ  
8889  N N   . GLU C 256 ? 0.5346 1.5630 0.6307 -0.1345 -0.0255 0.0345  557 GLU C N   
8890  C CA  . GLU C 256 ? 0.6690 1.7168 0.7706 -0.1274 -0.0180 0.0360  557 GLU C CA  
8891  C C   . GLU C 256 ? 0.6830 1.7385 0.7968 -0.0818 -0.0142 0.0414  557 GLU C C   
8892  O O   . GLU C 256 ? 0.8540 1.9026 0.9725 -0.0711 -0.0077 0.0423  557 GLU C O   
8893  C CB  . GLU C 256 ? 0.7884 1.8890 0.8845 -0.1435 -0.0165 0.0347  557 GLU C CB  
8894  C CG  . GLU C 256 ? 0.9014 1.9919 0.9813 -0.1891 -0.0193 0.0295  557 GLU C CG  
8895  C CD  . GLU C 256 ? 1.0966 2.1745 1.1679 -0.2156 -0.0149 0.0273  557 GLU C CD  
8896  O OE1 . GLU C 256 ? 1.1565 2.2474 1.2135 -0.2480 -0.0154 0.0243  557 GLU C OE1 
8897  O OE2 . GLU C 256 ? 1.1271 2.1814 1.2047 -0.2043 -0.0105 0.0288  557 GLU C OE2 
8898  N N   . TRP C 257 ? 0.5800 1.6453 0.6966 -0.0545 -0.0178 0.0451  558 TRP C N   
8899  C CA  . TRP C 257 ? 0.6031 1.6708 0.7259 -0.0097 -0.0144 0.0506  558 TRP C CA  
8900  C C   . TRP C 257 ? 0.6078 1.6114 0.7286 0.0064  -0.0129 0.0521  558 TRP C C   
8901  O O   . TRP C 257 ? 0.7134 1.7041 0.8338 0.0431  -0.0094 0.0564  558 TRP C O   
8902  C CB  . TRP C 257 ? 0.6967 1.7899 0.8174 0.0132  -0.0183 0.0547  558 TRP C CB  
8903  C CG  . TRP C 257 ? 0.6663 1.7383 0.7825 -0.0004 -0.0260 0.0539  558 TRP C CG  
8904  C CD1 . TRP C 257 ? 0.7611 1.8546 0.8716 -0.0277 -0.0305 0.0505  558 TRP C CD1 
8905  C CD2 . TRP C 257 ? 0.5396 1.5638 0.6544 0.0124  -0.0301 0.0562  558 TRP C CD2 
8906  N NE1 . TRP C 257 ? 0.6995 1.7612 0.8053 -0.0322 -0.0369 0.0501  558 TRP C NE1 
8907  C CE2 . TRP C 257 ? 0.5766 1.5964 0.6848 -0.0080 -0.0373 0.0538  558 TRP C CE2 
8908  C CE3 . TRP C 257 ? 0.5938 1.5612 0.7030 0.0383  -0.0263 0.0594  558 TRP C CE3 
8909  C CZ2 . TRP C 257 ? 0.6247 1.5932 0.7239 -0.0025 -0.0416 0.0548  558 TRP C CZ2 
8910  C CZ3 . TRP C 257 ? 0.6498 1.5565 0.7459 0.0416  -0.0293 0.0603  558 TRP C CZ3 
8911  C CH2 . TRP C 257 ? 0.6689 1.5778 0.7606 0.0222  -0.0366 0.0581  558 TRP C CH2 
8912  N N   . PHE C 258 ? 0.5566 1.4987 0.6643 -0.0194 -0.0145 0.0481  559 PHE C N   
8913  C CA  . PHE C 258 ? 0.5925 1.4549 0.6875 -0.0049 -0.0121 0.0489  559 PHE C CA  
8914  C C   . PHE C 258 ? 0.5456 1.3882 0.6398 0.0073  -0.0039 0.0490  559 PHE C C   
8915  O O   . PHE C 258 ? 0.5974 1.4052 0.6868 0.0366  -0.0005 0.0519  559 PHE C O   
8916  C CB  . PHE C 258 ? 0.5111 1.3170 0.5926 -0.0341 -0.0157 0.0443  559 PHE C CB  
8917  C CG  . PHE C 258 ? 0.5651 1.3021 0.6353 -0.0180 -0.0159 0.0458  559 PHE C CG  
8918  C CD1 . PHE C 258 ? 0.5274 1.2491 0.5921 -0.0178 -0.0219 0.0462  559 PHE C CD1 
8919  C CD2 . PHE C 258 ? 0.5571 1.2474 0.6220 -0.0032 -0.0101 0.0467  559 PHE C CD2 
8920  C CE1 . PHE C 258 ? 0.4711 1.1334 0.5257 -0.0040 -0.0216 0.0478  559 PHE C CE1 
8921  C CE2 . PHE C 258 ? 0.4790 1.1097 0.5336 0.0098  -0.0103 0.0481  559 PHE C CE2 
8922  C CZ  . PHE C 258 ? 0.4127 1.0303 0.4625 0.0092  -0.0159 0.0488  559 PHE C CZ  
8923  N N   . LYS C 259 ? 0.4687 1.3325 0.5660 -0.0161 -0.0004 0.0457  560 LYS C N   
8924  C CA  . LYS C 259 ? 0.5275 1.3717 0.6225 -0.0075 0.0075  0.0453  560 LYS C CA  
8925  C C   . LYS C 259 ? 0.5923 1.4621 0.6940 0.0329  0.0123  0.0489  560 LYS C C   
8926  O O   . LYS C 259 ? 0.5269 1.3548 0.6212 0.0517  0.0177  0.0492  560 LYS C O   
8927  C CB  . LYS C 259 ? 0.4837 1.3608 0.5819 -0.0385 0.0105  0.0422  560 LYS C CB  
8928  C CG  . LYS C 259 ? 0.4621 1.4257 0.5745 -0.0515 0.0086  0.0422  560 LYS C CG  
8929  C CD  . LYS C 259 ? 0.4578 1.4420 0.5692 -0.0867 0.0120  0.0393  560 LYS C CD  
8930  C CE  . LYS C 259 ? 0.5018 1.5548 0.6164 -0.0986 0.0100  0.0387  560 LYS C CE  
8931  N NZ  . LYS C 259 ? 0.6127 1.6727 0.7199 -0.1253 0.0020  0.0366  560 LYS C NZ  
8932  N N   . ASP C 260 ? 0.6238 1.5595 0.7376 0.0477  0.0101  0.0518  561 ASP C N   
8933  C CA  . ASP C 260 ? 0.5895 1.5516 0.7080 0.0890  0.0143  0.0555  561 ASP C CA  
8934  C C   . ASP C 260 ? 0.5145 1.4173 0.6205 0.1199  0.0136  0.0592  561 ASP C C   
8935  O O   . ASP C 260 ? 0.5568 1.4669 0.6614 0.1561  0.0175  0.0623  561 ASP C O   
8936  C CB  . ASP C 260 ? 0.7078 1.7480 0.8367 0.0962  0.0110  0.0577  561 ASP C CB  
8937  C CG  . ASP C 260 ? 0.7993 1.8807 0.9298 0.0589  0.0099  0.0536  561 ASP C CG  
8938  O OD1 . ASP C 260 ? 0.8268 1.8996 0.9580 0.0376  0.0145  0.0502  561 ASP C OD1 
8939  O OD2 . ASP C 260 ? 0.7900 1.9106 0.9187 0.0504  0.0047  0.0540  561 ASP C OD2 
8940  N N   . LEU C 261 ? 0.5086 1.3529 0.6040 0.1071  0.0090  0.0590  562 LEU C N   
8941  C CA  . LEU C 261 ? 0.5671 1.3516 0.6490 0.1331  0.0092  0.0625  562 LEU C CA  
8942  C C   . LEU C 261 ? 0.7805 1.5134 0.8517 0.1447  0.0165  0.0608  562 LEU C C   
8943  O O   . LEU C 261 ? 0.8942 1.5818 0.9529 0.1693  0.0180  0.0637  562 LEU C O   
8944  C CB  . LEU C 261 ? 0.3651 1.1038 0.4390 0.1148  0.0030  0.0622  562 LEU C CB  
8945  C CG  . LEU C 261 ? 0.5201 1.2920 0.5984 0.1121  -0.0048 0.0650  562 LEU C CG  
8946  C CD1 . LEU C 261 ? 0.4683 1.1981 0.5390 0.0851  -0.0099 0.0620  562 LEU C CD1 
8947  C CD2 . LEU C 261 ? 0.5310 1.3000 0.6040 0.1492  -0.0056 0.0720  562 LEU C CD2 
8948  N N   . GLY C 262 ? 0.7700 1.5079 0.8441 0.1263  0.0210  0.0562  563 GLY C N   
8949  C CA  . GLY C 262 ? 0.8000 1.4972 0.8645 0.1365  0.0281  0.0540  563 GLY C CA  
8950  C C   . GLY C 262 ? 0.7528 1.3710 0.8025 0.1292  0.0272  0.0530  563 GLY C C   
8951  O O   . GLY C 262 ? 0.7462 1.3218 0.7839 0.1491  0.0314  0.0532  563 GLY C O   
8952  N N   . LEU C 263 ? 0.6850 1.2833 0.7342 0.1012  0.0219  0.0516  564 LEU C N   
8953  C CA  . LEU C 263 ? 0.6343 1.1641 0.6711 0.0943  0.0203  0.0509  564 LEU C CA  
8954  C C   . LEU C 263 ? 0.5746 1.0809 0.6085 0.0667  0.0215  0.0464  564 LEU C C   
8955  O O   . LEU C 263 ? 0.4655 1.0037 0.5062 0.0433  0.0203  0.0443  564 LEU C O   
8956  C CB  . LEU C 263 ? 0.6510 1.1719 0.6871 0.0874  0.0132  0.0529  564 LEU C CB  
8957  C CG  . LEU C 263 ? 0.7503 1.2954 0.7883 0.1114  0.0104  0.0583  564 LEU C CG  
8958  C CD1 . LEU C 263 ? 0.7478 1.3038 0.7887 0.0948  0.0030  0.0587  564 LEU C CD1 
8959  C CD2 . LEU C 263 ? 0.7044 1.2023 0.7287 0.1384  0.0127  0.0621  564 LEU C CD2 
8960  N N   . LYS C 264 ? 0.6628 1.1131 0.6854 0.0690  0.0237  0.0452  565 LYS C N   
8961  C CA  . LYS C 264 ? 0.6136 1.0331 0.6309 0.0453  0.0239  0.0418  565 LYS C CA  
8962  C C   . LYS C 264 ? 0.5488 0.9072 0.5547 0.0483  0.0226  0.0418  565 LYS C C   
8963  O O   . LYS C 264 ? 0.6403 0.9784 0.6407 0.0696  0.0237  0.0440  565 LYS C O   
8964  C CB  . LYS C 264 ? 0.6122 1.0427 0.6290 0.0445  0.0303  0.0396  565 LYS C CB  
8965  C CG  . LYS C 264 ? 0.6274 1.0252 0.6344 0.0670  0.0357  0.0390  565 LYS C CG  
8966  C CD  . LYS C 264 ? 0.6687 1.0942 0.6770 0.0730  0.0427  0.0369  565 LYS C CD  
8967  C CE  . LYS C 264 ? 0.8583 1.2437 0.8533 0.0922  0.0477  0.0351  565 LYS C CE  
8968  N NZ  . LYS C 264 ? 1.0035 1.4216 0.9992 0.1156  0.0547  0.0340  565 LYS C NZ  
8969  N N   . TRP C 265 ? 0.4338 0.7635 0.4353 0.0266  0.0200  0.0395  566 TRP C N   
8970  C CA  . TRP C 265 ? 0.4140 0.6901 0.4055 0.0275  0.0190  0.0391  566 TRP C CA  
8971  C C   . TRP C 265 ? 0.6001 0.8534 0.5858 0.0126  0.0205  0.0363  566 TRP C C   
8972  O O   . TRP C 265 ? 0.6368 0.9122 0.6250 -0.0021 0.0215  0.0351  566 TRP C O   
8973  C CB  . TRP C 265 ? 0.3891 0.6492 0.3797 0.0195  0.0131  0.0396  566 TRP C CB  
8974  C CG  . TRP C 265 ? 0.4104 0.6276 0.3930 0.0294  0.0129  0.0407  566 TRP C CG  
8975  C CD1 . TRP C 265 ? 0.4509 0.6316 0.4273 0.0191  0.0108  0.0390  566 TRP C CD1 
8976  C CD2 . TRP C 265 ? 0.5120 0.7188 0.4904 0.0512  0.0148  0.0439  566 TRP C CD2 
8977  N NE1 . TRP C 265 ? 0.5617 0.7135 0.5319 0.0311  0.0115  0.0407  566 TRP C NE1 
8978  C CE2 . TRP C 265 ? 0.4794 0.6437 0.4493 0.0500  0.0139  0.0438  566 TRP C CE2 
8979  C CE3 . TRP C 265 ? 0.4874 0.7165 0.4669 0.0719  0.0171  0.0470  566 TRP C CE3 
8980  C CZ2 . TRP C 265 ? 0.4804 0.6217 0.4420 0.0659  0.0155  0.0468  566 TRP C CZ2 
8981  C CZ3 . TRP C 265 ? 0.4066 0.6089 0.3763 0.0901  0.0185  0.0502  566 TRP C CZ3 
8982  C CH2 . TRP C 265 ? 0.5414 0.6993 0.5018 0.0856  0.0178  0.0501  566 TRP C CH2 
8983  N N   . TYR C 266 ? 0.5238 0.7339 0.5008 0.0159  0.0207  0.0357  567 TYR C N   
8984  C CA  . TYR C 266 ? 0.4777 0.6635 0.4479 0.0034  0.0214  0.0336  567 TYR C CA  
8985  C C   . TYR C 266 ? 0.5489 0.7157 0.5164 -0.0149 0.0160  0.0329  567 TYR C C   
8986  O O   . TYR C 266 ? 0.6421 0.8091 0.6120 -0.0168 0.0121  0.0334  567 TYR C O   
8987  C CB  . TYR C 266 ? 0.4549 0.6070 0.4165 0.0154  0.0240  0.0329  567 TYR C CB  
8988  C CG  . TYR C 266 ? 0.4907 0.6175 0.4490 0.0252  0.0220  0.0343  567 TYR C CG  
8989  C CD1 . TYR C 266 ? 0.6555 0.7527 0.6098 0.0163  0.0184  0.0338  567 TYR C CD1 
8990  C CD2 . TYR C 266 ? 0.4388 0.5713 0.3965 0.0439  0.0241  0.0364  567 TYR C CD2 
8991  C CE1 . TYR C 266 ? 0.6820 0.7587 0.6331 0.0235  0.0170  0.0352  567 TYR C CE1 
8992  C CE2 . TYR C 266 ? 0.4705 0.5776 0.4229 0.0512  0.0225  0.0383  567 TYR C CE2 
8993  C CZ  . TYR C 266 ? 0.6160 0.6967 0.5656 0.0398  0.0191  0.0376  567 TYR C CZ  
8994  O OH  . TYR C 266 ? 0.6555 0.7140 0.5999 0.0451  0.0179  0.0397  567 TYR C OH  
8995  N N   . GLY C 267 ? 0.4999 0.6494 0.4608 -0.0275 0.0159  0.0317  568 GLY C N   
8996  C CA  . GLY C 267 ? 0.4048 0.5386 0.3607 -0.0449 0.0112  0.0311  568 GLY C CA  
8997  C C   . GLY C 267 ? 0.4903 0.5856 0.4397 -0.0432 0.0083  0.0305  568 GLY C C   
8998  O O   . GLY C 267 ? 0.6063 0.6867 0.5518 -0.0517 0.0040  0.0298  568 GLY C O   
8999  N N   . LEU C 268 ? 0.4680 0.5479 0.4155 -0.0319 0.0107  0.0305  569 LEU C N   
9000  C CA  . LEU C 268 ? 0.4887 0.5366 0.4299 -0.0321 0.0083  0.0299  569 LEU C CA  
9001  C C   . LEU C 268 ? 0.5843 0.6220 0.5275 -0.0197 0.0083  0.0303  569 LEU C C   
9002  O O   . LEU C 268 ? 0.5002 0.5377 0.4427 -0.0088 0.0120  0.0305  569 LEU C O   
9003  C CB  . LEU C 268 ? 0.4380 0.4746 0.3724 -0.0337 0.0105  0.0294  569 LEU C CB  
9004  C CG  . LEU C 268 ? 0.5084 0.5164 0.4365 -0.0347 0.0075  0.0290  569 LEU C CG  
9005  C CD1 . LEU C 268 ? 0.5617 0.5588 0.4846 -0.0461 0.0030  0.0294  569 LEU C CD1 
9006  C CD2 . LEU C 268 ? 0.6180 0.6167 0.5399 -0.0321 0.0102  0.0281  569 LEU C CD2 
9007  N N   . PRO C 269 ? 0.5688 0.5974 0.5128 -0.0210 0.0046  0.0303  570 PRO C N   
9008  C CA  . PRO C 269 ? 0.4326 0.4484 0.3765 -0.0120 0.0046  0.0310  570 PRO C CA  
9009  C C   . PRO C 269 ? 0.4863 0.4797 0.4246 -0.0140 0.0039  0.0300  570 PRO C C   
9010  O O   . PRO C 269 ? 0.5045 0.4894 0.4401 -0.0215 0.0008  0.0290  570 PRO C O   
9011  C CB  . PRO C 269 ? 0.3552 0.3737 0.3020 -0.0143 0.0010  0.0311  570 PRO C CB  
9012  C CG  . PRO C 269 ? 0.4827 0.5003 0.4269 -0.0264 -0.0020 0.0293  570 PRO C CG  
9013  C CD  . PRO C 269 ? 0.5802 0.6094 0.5237 -0.0312 0.0005  0.0295  570 PRO C CD  
9014  N N   . ALA C 270 ? 0.4681 0.4512 0.4029 -0.0072 0.0066  0.0302  571 ALA C N   
9015  C CA  . ALA C 270 ? 0.4385 0.4042 0.3674 -0.0104 0.0060  0.0289  571 ALA C CA  
9016  C C   . ALA C 270 ? 0.3768 0.3295 0.3019 -0.0054 0.0075  0.0293  571 ALA C C   
9017  O O   . ALA C 270 ? 0.6530 0.5999 0.5723 0.0010  0.0114  0.0292  571 ALA C O   
9018  C CB  . ALA C 270 ? 0.5041 0.4703 0.4284 -0.0119 0.0086  0.0276  571 ALA C CB  
9019  N N   . VAL C 271 ? 0.4375 0.3848 0.3640 -0.0083 0.0047  0.0297  572 VAL C N   
9020  C CA  . VAL C 271 ? 0.5094 0.4457 0.4316 -0.0061 0.0061  0.0308  572 VAL C CA  
9021  C C   . VAL C 271 ? 0.6002 0.5220 0.5145 -0.0109 0.0067  0.0288  572 VAL C C   
9022  O O   . VAL C 271 ? 0.6920 0.6151 0.6075 -0.0168 0.0038  0.0272  572 VAL C O   
9023  C CB  . VAL C 271 ? 0.4166 0.3574 0.3437 -0.0083 0.0034  0.0319  572 VAL C CB  
9024  C CG1 . VAL C 271 ? 0.3827 0.3126 0.3039 -0.0084 0.0052  0.0336  572 VAL C CG1 
9025  C CG2 . VAL C 271 ? 0.4162 0.3707 0.3493 -0.0048 0.0025  0.0331  572 VAL C CG2 
9026  N N   . SER C 272 ? 0.4984 0.4052 0.4029 -0.0083 0.0101  0.0290  573 SER C N   
9027  C CA  . SER C 272 ? 0.6076 0.4994 0.5020 -0.0136 0.0110  0.0262  573 SER C CA  
9028  C C   . SER C 272 ? 0.6682 0.5420 0.5521 -0.0180 0.0124  0.0266  573 SER C C   
9029  O O   . SER C 272 ? 0.6262 0.4865 0.4998 -0.0244 0.0129  0.0237  573 SER C O   
9030  C CB  . SER C 272 ? 0.5423 0.4288 0.4296 -0.0075 0.0148  0.0242  573 SER C CB  
9031  O OG  . SER C 272 ? 0.6296 0.5095 0.5112 0.0034  0.0189  0.0259  573 SER C OG  
9032  N N   . ASN C 273 ? 0.6482 0.5210 0.5326 -0.0161 0.0129  0.0300  574 ASN C N   
9033  C CA  . ASN C 273 ? 0.6119 0.4655 0.4837 -0.0218 0.0146  0.0311  574 ASN C CA  
9034  C C   . ASN C 273 ? 0.6267 0.4911 0.5047 -0.0327 0.0116  0.0319  574 ASN C C   
9035  O O   . ASN C 273 ? 0.7508 0.6026 0.6189 -0.0400 0.0130  0.0335  574 ASN C O   
9036  C CB  . ASN C 273 ? 0.7423 0.5841 0.6063 -0.0119 0.0179  0.0353  574 ASN C CB  
9037  C CG  . ASN C 273 ? 0.7118 0.5751 0.5895 -0.0057 0.0162  0.0388  574 ASN C CG  
9038  O OD1 . ASN C 273 ? 0.7067 0.5907 0.5983 -0.0094 0.0127  0.0379  574 ASN C OD1 
9039  N ND2 . ASN C 273 ? 0.6959 0.5528 0.5677 0.0044  0.0185  0.0428  574 ASN C ND2 
9040  N N   . MET C 274 ? 0.5731 0.4600 0.4657 -0.0340 0.0077  0.0309  575 MET C N   
9041  C CA  . MET C 274 ? 0.5022 0.4042 0.4020 -0.0410 0.0050  0.0316  575 MET C CA  
9042  C C   . MET C 274 ? 0.6295 0.5370 0.5290 -0.0510 0.0023  0.0286  575 MET C C   
9043  O O   . MET C 274 ? 0.5438 0.4433 0.4377 -0.0529 0.0021  0.0259  575 MET C O   
9044  C CB  . MET C 274 ? 0.3959 0.3176 0.3095 -0.0343 0.0024  0.0321  575 MET C CB  
9045  C CG  . MET C 274 ? 0.5088 0.4301 0.4226 -0.0279 0.0045  0.0356  575 MET C CG  
9046  S SD  . MET C 274 ? 0.6773 0.6198 0.6039 -0.0224 0.0016  0.0356  575 MET C SD  
9047  C CE  . MET C 274 ? 0.6126 0.5671 0.5418 -0.0290 0.0010  0.0362  575 MET C CE  
9048  N N   . LEU C 275 ? 0.5203 0.4446 0.4259 -0.0571 0.0003  0.0290  576 LEU C N   
9049  C CA  . LEU C 275 ? 0.4709 0.4048 0.3758 -0.0679 -0.0022 0.0268  576 LEU C CA  
9050  C C   . LEU C 275 ? 0.5400 0.5009 0.4589 -0.0636 -0.0067 0.0261  576 LEU C C   
9051  O O   . LEU C 275 ? 0.5603 0.5354 0.4869 -0.0600 -0.0068 0.0275  576 LEU C O   
9052  C CB  . LEU C 275 ? 0.5206 0.4517 0.4176 -0.0810 0.0000  0.0281  576 LEU C CB  
9053  C CG  . LEU C 275 ? 0.5878 0.5318 0.4832 -0.0951 -0.0025 0.0256  576 LEU C CG  
9054  C CD1 . LEU C 275 ? 0.5131 0.4353 0.3905 -0.1105 0.0008  0.0257  576 LEU C CD1 
9055  C CD2 . LEU C 275 ? 0.6118 0.5902 0.5211 -0.0964 -0.0052 0.0262  576 LEU C CD2 
9056  N N   . LEU C 276 ? 0.6288 0.5961 0.5495 -0.0630 -0.0102 0.0239  577 LEU C N   
9057  C CA  . LEU C 276 ? 0.5353 0.5250 0.4663 -0.0567 -0.0148 0.0235  577 LEU C CA  
9058  C C   . LEU C 276 ? 0.5482 0.5605 0.4819 -0.0655 -0.0172 0.0226  577 LEU C C   
9059  O O   . LEU C 276 ? 0.7048 0.7162 0.6324 -0.0747 -0.0184 0.0210  577 LEU C O   
9060  C CB  . LEU C 276 ? 0.5581 0.5423 0.4880 -0.0500 -0.0178 0.0226  577 LEU C CB  
9061  C CG  . LEU C 276 ? 0.5976 0.5988 0.5338 -0.0418 -0.0229 0.0226  577 LEU C CG  
9062  C CD1 . LEU C 276 ? 0.6188 0.6287 0.5621 -0.0338 -0.0226 0.0232  577 LEU C CD1 
9063  C CD2 . LEU C 276 ? 0.7727 0.7617 0.7044 -0.0359 -0.0250 0.0229  577 LEU C CD2 
9064  N N   . GLU C 277 ? 0.5369 0.5714 0.4792 -0.0631 -0.0177 0.0233  578 GLU C N   
9065  C CA  . GLU C 277 ? 0.4478 0.5115 0.3949 -0.0712 -0.0196 0.0227  578 GLU C CA  
9066  C C   . GLU C 277 ? 0.5637 0.6523 0.5204 -0.0582 -0.0245 0.0220  578 GLU C C   
9067  O O   . GLU C 277 ? 0.5402 0.6304 0.5017 -0.0450 -0.0245 0.0222  578 GLU C O   
9068  C CB  . GLU C 277 ? 0.6385 0.7114 0.5872 -0.0782 -0.0157 0.0244  578 GLU C CB  
9069  C CG  . GLU C 277 ? 0.7679 0.8685 0.7183 -0.0930 -0.0162 0.0240  578 GLU C CG  
9070  C CD  . GLU C 277 ? 0.8742 1.0141 0.8382 -0.0848 -0.0182 0.0236  578 GLU C CD  
9071  O OE1 . GLU C 277 ? 0.8921 1.0642 0.8610 -0.0927 -0.0205 0.0227  578 GLU C OE1 
9072  O OE2 . GLU C 277 ? 0.9528 1.0926 0.9221 -0.0703 -0.0175 0.0240  578 GLU C OE2 
9073  N N   . ILE C 278 ? 0.5583 0.6644 0.5157 -0.0613 -0.0288 0.0209  579 ILE C N   
9074  C CA  . ILE C 278 ? 0.4641 0.5954 0.4287 -0.0481 -0.0340 0.0207  579 ILE C CA  
9075  C C   . ILE C 278 ? 0.5245 0.6921 0.4937 -0.0580 -0.0369 0.0199  579 ILE C C   
9076  O O   . ILE C 278 ? 0.4945 0.6590 0.4574 -0.0734 -0.0374 0.0190  579 ILE C O   
9077  C CB  . ILE C 278 ? 0.4211 0.5346 0.3799 -0.0383 -0.0379 0.0210  579 ILE C CB  
9078  C CG1 . ILE C 278 ? 0.3781 0.4594 0.3323 -0.0307 -0.0351 0.0217  579 ILE C CG1 
9079  C CG2 . ILE C 278 ? 0.4247 0.5621 0.3882 -0.0233 -0.0434 0.0215  579 ILE C CG2 
9080  C CD1 . ILE C 278 ? 0.4592 0.5189 0.4053 -0.0263 -0.0374 0.0225  579 ILE C CD1 
9081  N N   . GLY C 279 ? 0.5108 0.7139 0.4903 -0.0489 -0.0388 0.0198  580 GLY C N   
9082  C CA  . GLY C 279 ? 0.4205 0.6675 0.4071 -0.0568 -0.0414 0.0191  580 GLY C CA  
9083  C C   . GLY C 279 ? 0.5287 0.7765 0.5096 -0.0829 -0.0397 0.0183  580 GLY C C   
9084  O O   . GLY C 279 ? 0.7372 1.0011 0.7164 -0.0916 -0.0439 0.0173  580 GLY C O   
9085  N N   . GLY C 280 ? 0.4751 0.7031 0.4509 -0.0957 -0.0338 0.0188  581 GLY C N   
9086  C CA  . GLY C 280 ? 0.5549 0.7794 0.5218 -0.1213 -0.0315 0.0181  581 GLY C CA  
9087  C C   . GLY C 280 ? 0.5854 0.7658 0.5364 -0.1297 -0.0304 0.0171  581 GLY C C   
9088  O O   . GLY C 280 ? 0.7020 0.8663 0.6410 -0.1499 -0.0272 0.0164  581 GLY C O   
9089  N N   . LEU C 281 ? 0.5401 0.6994 0.4892 -0.1147 -0.0326 0.0169  582 LEU C N   
9090  C CA  . LEU C 281 ? 0.5839 0.7060 0.5188 -0.1198 -0.0318 0.0154  582 LEU C CA  
9091  C C   . LEU C 281 ? 0.5335 0.6167 0.4623 -0.1135 -0.0264 0.0167  582 LEU C C   
9092  O O   . LEU C 281 ? 0.6228 0.7051 0.5593 -0.0983 -0.0256 0.0186  582 LEU C O   
9093  C CB  . LEU C 281 ? 0.5563 0.6810 0.4920 -0.1081 -0.0373 0.0149  582 LEU C CB  
9094  C CG  . LEU C 281 ? 0.4958 0.6639 0.4394 -0.1092 -0.0435 0.0144  582 LEU C CG  
9095  C CD1 . LEU C 281 ? 0.4604 0.6304 0.4048 -0.0924 -0.0491 0.0155  582 LEU C CD1 
9096  C CD2 . LEU C 281 ? 0.4248 0.5998 0.3594 -0.1332 -0.0441 0.0115  582 LEU C CD2 
9097  N N   . GLU C 282 ? 0.5697 0.6205 0.4832 -0.1242 -0.0230 0.0154  583 GLU C N   
9098  C CA  . GLU C 282 ? 0.5958 0.6119 0.5020 -0.1193 -0.0175 0.0168  583 GLU C CA  
9099  C C   . GLU C 282 ? 0.6532 0.6406 0.5497 -0.1137 -0.0168 0.0150  583 GLU C C   
9100  O O   . GLU C 282 ? 0.7196 0.6884 0.6014 -0.1246 -0.0156 0.0122  583 GLU C O   
9101  C CB  . GLU C 282 ? 0.7163 0.7172 0.6104 -0.1355 -0.0129 0.0174  583 GLU C CB  
9102  C CG  . GLU C 282 ? 0.6501 0.6807 0.5528 -0.1430 -0.0128 0.0194  583 GLU C CG  
9103  C CD  . GLU C 282 ? 0.8273 0.8373 0.7152 -0.1591 -0.0077 0.0211  583 GLU C CD  
9104  O OE1 . GLU C 282 ? 0.7469 0.7278 0.6161 -0.1713 -0.0061 0.0191  583 GLU C OE1 
9105  O OE2 . GLU C 282 ? 1.0468 1.0673 0.9397 -0.1593 -0.0052 0.0245  583 GLU C OE2 
9106  N N   . PHE C 283 ? 0.5919 0.5750 0.4952 -0.0973 -0.0171 0.0165  584 PHE C N   
9107  C CA  . PHE C 283 ? 0.5194 0.4795 0.4154 -0.0907 -0.0158 0.0154  584 PHE C CA  
9108  C C   . PHE C 283 ? 0.5775 0.5113 0.4667 -0.0869 -0.0100 0.0166  584 PHE C C   
9109  O O   . PHE C 283 ? 0.7062 0.6400 0.6028 -0.0758 -0.0088 0.0190  584 PHE C O   
9110  C CB  . PHE C 283 ? 0.4327 0.4036 0.3382 -0.0773 -0.0194 0.0168  584 PHE C CB  
9111  C CG  . PHE C 283 ? 0.5129 0.5083 0.4233 -0.0779 -0.0255 0.0164  584 PHE C CG  
9112  C CD1 . PHE C 283 ? 0.5489 0.5704 0.4709 -0.0728 -0.0286 0.0179  584 PHE C CD1 
9113  C CD2 . PHE C 283 ? 0.6038 0.5973 0.5063 -0.0822 -0.0281 0.0145  584 PHE C CD2 
9114  C CE1 . PHE C 283 ? 0.5859 0.6322 0.5121 -0.0704 -0.0345 0.0180  584 PHE C CE1 
9115  C CE2 . PHE C 283 ? 0.5644 0.5823 0.4708 -0.0813 -0.0344 0.0148  584 PHE C CE2 
9116  C CZ  . PHE C 283 ? 0.6907 0.7355 0.6092 -0.0747 -0.0377 0.0167  584 PHE C CZ  
9117  N N   . SER C 284 ? 0.5945 0.5050 0.4679 -0.0957 -0.0064 0.0147  585 SER C N   
9118  C CA  . SER C 284 ? 0.5120 0.3968 0.3766 -0.0909 -0.0010 0.0162  585 SER C CA  
9119  C C   . SER C 284 ? 0.5451 0.4169 0.4080 -0.0776 0.0013  0.0158  585 SER C C   
9120  O O   . SER C 284 ? 0.6232 0.4771 0.4796 -0.0708 0.0055  0.0172  585 SER C O   
9121  C CB  . SER C 284 ? 0.7223 0.5815 0.5665 -0.1038 0.0022  0.0142  585 SER C CB  
9122  O OG  . SER C 284 ? 0.7291 0.5837 0.5640 -0.1115 0.0005  0.0094  585 SER C OG  
9123  N N   . ALA C 285 ? 0.6250 0.5055 0.4920 -0.0741 -0.0013 0.0140  586 ALA C N   
9124  C CA  . ALA C 285 ? 0.5495 0.4235 0.4166 -0.0627 0.0009  0.0140  586 ALA C CA  
9125  C C   . ALA C 285 ? 0.5983 0.4933 0.4792 -0.0577 -0.0033 0.0157  586 ALA C C   
9126  O O   . ALA C 285 ? 0.6141 0.5173 0.4948 -0.0615 -0.0070 0.0144  586 ALA C O   
9127  C CB  . ALA C 285 ? 0.5387 0.3957 0.3909 -0.0647 0.0033  0.0098  586 ALA C CB  
9128  N N   . CYS C 286 ? 0.5559 0.4578 0.4466 -0.0495 -0.0030 0.0185  587 CYS C N   
9129  C CA  . CYS C 286 ? 0.5289 0.4458 0.4298 -0.0452 -0.0070 0.0201  587 CYS C CA  
9130  C C   . CYS C 286 ? 0.6715 0.5888 0.5772 -0.0373 -0.0051 0.0219  587 CYS C C   
9131  O O   . CYS C 286 ? 0.7396 0.6657 0.6533 -0.0339 -0.0070 0.0235  587 CYS C O   
9132  C CB  . CYS C 286 ? 0.6209 0.5526 0.5300 -0.0466 -0.0105 0.0212  587 CYS C CB  
9133  S SG  . CYS C 286 ? 0.5991 0.5298 0.5111 -0.0462 -0.0072 0.0230  587 CYS C SG  
9134  N N   . PRO C 287 ? 0.7239 0.6340 0.6247 -0.0343 -0.0016 0.0213  588 PRO C N   
9135  C CA  . PRO C 287 ? 0.6150 0.5303 0.5209 -0.0279 0.0003  0.0229  588 PRO C CA  
9136  C C   . PRO C 287 ? 0.6644 0.5892 0.5769 -0.0281 -0.0037 0.0243  588 PRO C C   
9137  O O   . PRO C 287 ? 0.7011 0.6259 0.6111 -0.0310 -0.0065 0.0241  588 PRO C O   
9138  C CB  . PRO C 287 ? 0.6595 0.5705 0.5587 -0.0257 0.0041  0.0215  588 PRO C CB  
9139  C CG  . PRO C 287 ? 0.6005 0.5035 0.4909 -0.0315 0.0033  0.0190  588 PRO C CG  
9140  C CD  . PRO C 287 ? 0.6355 0.5348 0.5253 -0.0365 0.0010  0.0186  588 PRO C CD  
9141  N N   . PHE C 288 ? 0.5645 0.4957 0.4835 -0.0249 -0.0039 0.0256  589 PHE C N   
9142  C CA  . PHE C 288 ? 0.4440 0.3800 0.3662 -0.0252 -0.0072 0.0263  589 PHE C CA  
9143  C C   . PHE C 288 ? 0.4642 0.4068 0.3892 -0.0237 -0.0051 0.0270  589 PHE C C   
9144  O O   . PHE C 288 ? 0.4398 0.3866 0.3668 -0.0199 -0.0018 0.0275  589 PHE C O   
9145  C CB  . PHE C 288 ? 0.3837 0.3227 0.3098 -0.0237 -0.0105 0.0262  589 PHE C CB  
9146  C CG  . PHE C 288 ? 0.5424 0.4856 0.4728 -0.0215 -0.0086 0.0267  589 PHE C CG  
9147  C CD1 . PHE C 288 ? 0.5528 0.5014 0.4868 -0.0186 -0.0078 0.0273  589 PHE C CD1 
9148  C CD2 . PHE C 288 ? 0.5204 0.4622 0.4497 -0.0235 -0.0076 0.0267  589 PHE C CD2 
9149  C CE1 . PHE C 288 ? 0.4701 0.4222 0.4066 -0.0165 -0.0061 0.0285  589 PHE C CE1 
9150  C CE2 . PHE C 288 ? 0.6139 0.5575 0.5448 -0.0228 -0.0057 0.0279  589 PHE C CE2 
9151  C CZ  . PHE C 288 ? 0.5236 0.4721 0.4581 -0.0185 -0.0049 0.0291  589 PHE C CZ  
9152  N N   . SER C 289 ? 0.4030 0.3464 0.3266 -0.0270 -0.0074 0.0272  590 SER C N   
9153  C CA  . SER C 289 ? 0.4020 0.3542 0.3268 -0.0292 -0.0058 0.0276  590 SER C CA  
9154  C C   . SER C 289 ? 0.4493 0.3985 0.3718 -0.0333 -0.0094 0.0273  590 SER C C   
9155  O O   . SER C 289 ? 0.5706 0.5076 0.4872 -0.0344 -0.0128 0.0271  590 SER C O   
9156  C CB  . SER C 289 ? 0.3787 0.3328 0.2991 -0.0328 -0.0033 0.0280  590 SER C CB  
9157  O OG  . SER C 289 ? 0.5859 0.5410 0.5022 -0.0406 -0.0047 0.0287  590 SER C OG  
9158  N N   . GLY C 290 ? 0.4645 0.4238 0.3901 -0.0349 -0.0089 0.0270  591 GLY C N   
9159  C CA  . GLY C 290 ? 0.4300 0.3839 0.3500 -0.0411 -0.0120 0.0260  591 GLY C CA  
9160  C C   . GLY C 290 ? 0.6314 0.6008 0.5528 -0.0480 -0.0103 0.0262  591 GLY C C   
9161  O O   . GLY C 290 ? 0.7598 0.7364 0.6803 -0.0525 -0.0080 0.0274  591 GLY C O   
9162  N N   . TRP C 291 ? 0.5962 0.5742 0.5202 -0.0491 -0.0114 0.0249  592 TRP C N   
9163  C CA  . TRP C 291 ? 0.5852 0.5847 0.5124 -0.0554 -0.0101 0.0250  592 TRP C CA  
9164  C C   . TRP C 291 ? 0.6034 0.6170 0.5371 -0.0507 -0.0107 0.0243  592 TRP C C   
9165  O O   . TRP C 291 ? 0.6473 0.6509 0.5805 -0.0453 -0.0125 0.0232  592 TRP C O   
9166  C CB  . TRP C 291 ? 0.5481 0.5408 0.4645 -0.0704 -0.0120 0.0241  592 TRP C CB  
9167  C CG  . TRP C 291 ? 0.6526 0.6222 0.5582 -0.0734 -0.0160 0.0215  592 TRP C CG  
9168  C CD1 . TRP C 291 ? 0.6208 0.5925 0.5255 -0.0743 -0.0181 0.0187  592 TRP C CD1 
9169  C CD2 . TRP C 291 ? 0.7085 0.6485 0.6013 -0.0740 -0.0184 0.0213  592 TRP C CD2 
9170  N NE1 . TRP C 291 ? 0.6788 0.6227 0.5702 -0.0751 -0.0213 0.0162  592 TRP C NE1 
9171  C CE2 . TRP C 291 ? 0.6509 0.5750 0.5348 -0.0741 -0.0217 0.0180  592 TRP C CE2 
9172  C CE3 . TRP C 291 ? 0.7989 0.7245 0.6857 -0.0734 -0.0184 0.0237  592 TRP C CE3 
9173  C CZ2 . TRP C 291 ? 0.6875 0.5813 0.5566 -0.0720 -0.0246 0.0171  592 TRP C CZ2 
9174  C CZ3 . TRP C 291 ? 0.7693 0.6660 0.6418 -0.0721 -0.0218 0.0234  592 TRP C CZ3 
9175  C CH2 . TRP C 291 ? 0.7604 0.6412 0.6241 -0.0706 -0.0248 0.0201  592 TRP C CH2 
9176  N N   . TYR C 292 ? 0.4865 0.5259 0.4261 -0.0522 -0.0092 0.0251  593 TYR C N   
9177  C CA  . TYR C 292 ? 0.4833 0.5402 0.4299 -0.0450 -0.0094 0.0257  593 TYR C CA  
9178  C C   . TYR C 292 ? 0.5241 0.5814 0.4662 -0.0530 -0.0131 0.0227  593 TYR C C   
9179  O O   . TYR C 292 ? 0.4796 0.5335 0.4141 -0.0666 -0.0151 0.0203  593 TYR C O   
9180  C CB  . TYR C 292 ? 0.4219 0.5100 0.3763 -0.0421 -0.0067 0.0279  593 TYR C CB  
9181  C CG  . TYR C 292 ? 0.4745 0.5649 0.4334 -0.0273 -0.0028 0.0308  593 TYR C CG  
9182  C CD1 . TYR C 292 ? 0.4836 0.5889 0.4450 -0.0251 0.0009  0.0318  593 TYR C CD1 
9183  C CD2 . TYR C 292 ? 0.4394 0.5171 0.3984 -0.0161 -0.0024 0.0323  593 TYR C CD2 
9184  C CE1 . TYR C 292 ? 0.5260 0.6301 0.4885 -0.0103 0.0048  0.0338  593 TYR C CE1 
9185  C CE2 . TYR C 292 ? 0.5041 0.5789 0.4634 -0.0035 0.0012  0.0348  593 TYR C CE2 
9186  C CZ  . TYR C 292 ? 0.6150 0.7015 0.5755 0.0001  0.0047  0.0352  593 TYR C CZ  
9187  O OH  . TYR C 292 ? 0.8043 0.8832 0.7620 0.0137  0.0084  0.0370  593 TYR C OH  
9188  N N   . MET C 293 ? 0.5134 0.5733 0.4583 -0.0450 -0.0140 0.0228  594 MET C N   
9189  C CA  . MET C 293 ? 0.4484 0.5199 0.3914 -0.0503 -0.0169 0.0204  594 MET C CA  
9190  C C   . MET C 293 ? 0.4429 0.5490 0.3948 -0.0471 -0.0160 0.0232  594 MET C C   
9191  O O   . MET C 293 ? 0.5025 0.6167 0.4610 -0.0338 -0.0134 0.0273  594 MET C O   
9192  C CB  . MET C 293 ? 0.3937 0.4532 0.3347 -0.0429 -0.0181 0.0194  594 MET C CB  
9193  C CG  . MET C 293 ? 0.5988 0.6682 0.5358 -0.0482 -0.0211 0.0161  594 MET C CG  
9194  S SD  . MET C 293 ? 0.5567 0.6038 0.4868 -0.0426 -0.0222 0.0128  594 MET C SD  
9195  C CE  . MET C 293 ? 0.5557 0.6128 0.4956 -0.0276 -0.0193 0.0188  594 MET C CE  
9196  N N   . GLY C 294 ? 0.4112 0.5376 0.3620 -0.0594 -0.0181 0.0212  595 GLY C N   
9197  C CA  . GLY C 294 ? 0.3616 0.5271 0.3215 -0.0568 -0.0175 0.0238  595 GLY C CA  
9198  C C   . GLY C 294 ? 0.5122 0.6902 0.4784 -0.0394 -0.0169 0.0278  595 GLY C C   
9199  O O   . GLY C 294 ? 0.6408 0.8414 0.6145 -0.0284 -0.0147 0.0319  595 GLY C O   
9200  N N   . THR C 295 ? 0.4698 0.6320 0.4316 -0.0359 -0.0187 0.0269  596 THR C N   
9201  C CA  . THR C 295 ? 0.5050 0.6759 0.4700 -0.0208 -0.0183 0.0314  596 THR C CA  
9202  C C   . THR C 295 ? 0.4359 0.5955 0.4034 -0.0056 -0.0142 0.0364  596 THR C C   
9203  O O   . THR C 295 ? 0.5814 0.7527 0.5506 0.0078  -0.0133 0.0414  596 THR C O   
9204  C CB  . THR C 295 ? 0.5120 0.6656 0.4706 -0.0212 -0.0203 0.0293  596 THR C CB  
9205  O OG1 . THR C 295 ? 0.4846 0.6057 0.4388 -0.0223 -0.0189 0.0272  596 THR C OG1 
9206  C CG2 . THR C 295 ? 0.4244 0.5888 0.3778 -0.0348 -0.0245 0.0238  596 THR C CG2 
9207  N N   . GLU C 296 ? 0.5345 0.6699 0.5000 -0.0072 -0.0118 0.0353  597 GLU C N   
9208  C CA  . GLU C 296 ? 0.4608 0.5819 0.4259 0.0055  -0.0080 0.0392  597 GLU C CA  
9209  C C   . GLU C 296 ? 0.5331 0.6759 0.5025 0.0155  -0.0055 0.0425  597 GLU C C   
9210  O O   . GLU C 296 ? 0.5992 0.7378 0.5663 0.0302  -0.0031 0.0469  597 GLU C O   
9211  C CB  . GLU C 296 ? 0.6010 0.6954 0.5629 0.0004  -0.0065 0.0368  597 GLU C CB  
9212  C CG  . GLU C 296 ? 0.6350 0.7109 0.5928 -0.0080 -0.0091 0.0331  597 GLU C CG  
9213  C CD  . GLU C 296 ? 0.6073 0.6602 0.5619 -0.0116 -0.0082 0.0314  597 GLU C CD  
9214  O OE1 . GLU C 296 ? 0.4705 0.5106 0.4243 -0.0049 -0.0058 0.0335  597 GLU C OE1 
9215  O OE2 . GLU C 296 ? 0.4532 0.4998 0.4046 -0.0215 -0.0102 0.0279  597 GLU C OE2 
9216  N N   . ILE C 297 ? 0.5332 0.6991 0.5072 0.0077  -0.0058 0.0404  598 ILE C N   
9217  C CA  . ILE C 297 ? 0.4849 0.6792 0.4642 0.0175  -0.0034 0.0430  598 ILE C CA  
9218  C C   . ILE C 297 ? 0.6017 0.8284 0.5851 0.0249  -0.0058 0.0460  598 ILE C C   
9219  O O   . ILE C 297 ? 0.6863 0.9211 0.6696 0.0433  -0.0039 0.0507  598 ILE C O   
9220  C CB  . ILE C 297 ? 0.4469 0.6585 0.4299 0.0043  -0.0026 0.0398  598 ILE C CB  
9221  C CG1 . ILE C 297 ? 0.4951 0.6746 0.4727 -0.0025 -0.0007 0.0375  598 ILE C CG1 
9222  C CG2 . ILE C 297 ? 0.4504 0.6973 0.4400 0.0153  0.0003  0.0422  598 ILE C CG2 
9223  C CD1 . ILE C 297 ? 0.4536 0.6395 0.4305 -0.0212 -0.0016 0.0342  598 ILE C CD1 
9224  N N   . GLY C 298 ? 0.6504 0.8957 0.6360 0.0107  -0.0100 0.0431  599 GLY C N   
9225  C CA  . GLY C 298 ? 0.6723 0.9565 0.6627 0.0147  -0.0130 0.0453  599 GLY C CA  
9226  C C   . GLY C 298 ? 0.6138 0.8906 0.6000 0.0266  -0.0148 0.0492  599 GLY C C   
9227  O O   . GLY C 298 ? 0.5197 0.8216 0.5081 0.0414  -0.0154 0.0541  599 GLY C O   
9228  N N   . VAL C 299 ? 0.6393 0.8831 0.6187 0.0215  -0.0156 0.0475  600 VAL C N   
9229  C CA  . VAL C 299 ? 0.6769 0.9143 0.6513 0.0315  -0.0169 0.0516  600 VAL C CA  
9230  C C   . VAL C 299 ? 0.7667 0.9808 0.7359 0.0492  -0.0128 0.0575  600 VAL C C   
9231  O O   . VAL C 299 ? 0.7404 0.9642 0.7067 0.0650  -0.0128 0.0637  600 VAL C O   
9232  C CB  . VAL C 299 ? 0.6936 0.9098 0.6623 0.0191  -0.0191 0.0472  600 VAL C CB  
9233  C CG1 . VAL C 299 ? 0.6843 0.8966 0.6474 0.0287  -0.0200 0.0517  600 VAL C CG1 
9234  C CG2 . VAL C 299 ? 0.6827 0.9171 0.6524 0.0013  -0.0231 0.0407  600 VAL C CG2 
9235  N N   . ARG C 300 ? 0.7475 0.9294 0.7136 0.0467  -0.0095 0.0557  601 ARG C N   
9236  C CA  . ARG C 300 ? 0.6464 0.7993 0.6043 0.0593  -0.0058 0.0603  601 ARG C CA  
9237  C C   . ARG C 300 ? 0.7364 0.8922 0.6937 0.0728  -0.0021 0.0627  601 ARG C C   
9238  O O   . ARG C 300 ? 0.7930 0.9436 0.7429 0.0899  -0.0004 0.0685  601 ARG C O   
9239  C CB  . ARG C 300 ? 0.4808 0.5996 0.4347 0.0496  -0.0044 0.0571  601 ARG C CB  
9240  C CG  . ARG C 300 ? 0.5157 0.6286 0.4689 0.0386  -0.0071 0.0542  601 ARG C CG  
9241  C CD  . ARG C 300 ? 0.6705 0.7857 0.6180 0.0457  -0.0081 0.0593  601 ARG C CD  
9242  N NE  . ARG C 300 ? 0.6662 0.7585 0.6043 0.0562  -0.0047 0.0655  601 ARG C NE  
9243  C CZ  . ARG C 300 ? 0.6085 0.6734 0.5409 0.0516  -0.0025 0.0653  601 ARG C CZ  
9244  N NH1 . ARG C 300 ? 0.5879 0.6475 0.5246 0.0392  -0.0034 0.0595  601 ARG C NH1 
9245  N NH2 . ARG C 300 ? 0.6214 0.6644 0.5427 0.0592  0.0006  0.0710  601 ARG C NH2 
9246  N N   . ASP C 301 ? 0.7589 0.9210 0.7220 0.0661  -0.0007 0.0583  602 ASP C N   
9247  C CA  . ASP C 301 ? 0.7359 0.8996 0.6977 0.0787  0.0036  0.0594  602 ASP C CA  
9248  C C   . ASP C 301 ? 0.7529 0.9530 0.7182 0.0947  0.0033  0.0634  602 ASP C C   
9249  O O   . ASP C 301 ? 0.7677 0.9607 0.7255 0.1146  0.0064  0.0676  602 ASP C O   
9250  C CB  . ASP C 301 ? 0.7262 0.8929 0.6933 0.0662  0.0050  0.0539  602 ASP C CB  
9251  C CG  . ASP C 301 ? 0.7595 0.8878 0.7208 0.0566  0.0061  0.0510  602 ASP C CG  
9252  O OD1 . ASP C 301 ? 0.6046 0.7037 0.5564 0.0648  0.0085  0.0531  602 ASP C OD1 
9253  O OD2 . ASP C 301 ? 0.7776 0.9048 0.7425 0.0405  0.0044  0.0468  602 ASP C OD2 
9254  N N   . TYR C 302 ? 0.6929 0.9323 0.6684 0.0868  -0.0005 0.0621  603 TYR C N   
9255  C CA  . TYR C 302 ? 0.6564 0.9379 0.6371 0.1015  -0.0012 0.0658  603 TYR C CA  
9256  C C   . TYR C 302 ? 0.6815 0.9667 0.6566 0.1151  -0.0040 0.0721  603 TYR C C   
9257  O O   . TYR C 302 ? 0.6644 0.9716 0.6386 0.1358  -0.0036 0.0772  603 TYR C O   
9258  C CB  . TYR C 302 ? 0.6825 1.0083 0.6759 0.0852  -0.0041 0.0617  603 TYR C CB  
9259  C CG  . TYR C 302 ? 0.7372 1.0719 0.7358 0.0778  -0.0005 0.0576  603 TYR C CG  
9260  C CD1 . TYR C 302 ? 0.7201 1.0687 0.7246 0.0536  -0.0023 0.0524  603 TYR C CD1 
9261  C CD2 . TYR C 302 ? 0.6913 1.0197 0.6870 0.0951  0.0049  0.0590  603 TYR C CD2 
9262  C CE1 . TYR C 302 ? 0.6616 1.0190 0.6695 0.0459  0.0011  0.0494  603 TYR C CE1 
9263  C CE2 . TYR C 302 ? 0.7615 1.1000 0.7614 0.0883  0.0085  0.0552  603 TYR C CE2 
9264  C CZ  . TYR C 302 ? 0.7567 1.1105 0.7630 0.0632  0.0065  0.0508  603 TYR C CZ  
9265  O OH  . TYR C 302 ? 0.9537 1.3174 0.9628 0.0552  0.0102  0.0478  603 TYR C OH  
9266  N N   . CYS C 303 ? 0.6652 0.9300 0.6356 0.1054  -0.0069 0.0723  604 CYS C N   
9267  C CA  . CYS C 303 ? 0.7335 1.0128 0.7007 0.1130  -0.0107 0.0775  604 CYS C CA  
9268  C C   . CYS C 303 ? 0.7569 0.9970 0.7093 0.1218  -0.0097 0.0831  604 CYS C C   
9269  O O   . CYS C 303 ? 0.7932 1.0445 0.7405 0.1323  -0.0123 0.0891  604 CYS C O   
9270  C CB  . CYS C 303 ? 0.7712 1.0738 0.7455 0.0928  -0.0159 0.0728  604 CYS C CB  
9271  S SG  . CYS C 303 ? 0.8457 1.2063 0.8346 0.0841  -0.0185 0.0689  604 CYS C SG  
9272  N N   . ASP C 304 ? 0.8076 1.0042 0.7523 0.1173  -0.0061 0.0818  605 ASP C N   
9273  C CA  . ASP C 304 ? 0.8781 1.0384 0.8066 0.1271  -0.0041 0.0882  605 ASP C CA  
9274  C C   . ASP C 304 ? 1.0416 1.2028 0.9601 0.1528  -0.0024 0.0958  605 ASP C C   
9275  O O   . ASP C 304 ? 1.1716 1.3565 1.0960 0.1638  -0.0014 0.0950  605 ASP C O   
9276  C CB  . ASP C 304 ? 0.8188 0.9360 0.7405 0.1186  -0.0002 0.0854  605 ASP C CB  
9277  C CG  . ASP C 304 ? 0.7956 0.9020 0.7202 0.0989  -0.0018 0.0812  605 ASP C CG  
9278  O OD1 . ASP C 304 ? 0.7797 0.9111 0.7127 0.0897  -0.0057 0.0784  605 ASP C OD1 
9279  O OD2 . ASP C 304 ? 0.8475 0.9208 0.7651 0.0929  0.0009  0.0804  605 ASP C OD2 
9280  N N   . ASN C 305 ? 0.9818 1.1165 0.8834 0.1629  -0.0019 0.1035  606 ASN C N   
9281  C CA  . ASN C 305 ? 0.8673 0.9966 0.7550 0.1894  -0.0004 0.1115  606 ASN C CA  
9282  C C   . ASN C 305 ? 0.9630 1.0552 0.8385 0.1988  0.0054  0.1107  606 ASN C C   
9283  O O   . ASN C 305 ? 0.9763 1.0783 0.8486 0.2197  0.0072  0.1125  606 ASN C O   
9284  C CB  . ASN C 305 ? 0.8353 0.9449 0.7055 0.1965  -0.0018 0.1208  606 ASN C CB  
9285  C CG  . ASN C 305 ? 0.8340 0.9879 0.7112 0.2023  -0.0074 0.1247  606 ASN C CG  
9286  O OD1 . ASN C 305 ? 0.7270 0.8951 0.6112 0.1860  -0.0108 0.1226  606 ASN C OD1 
9287  N ND2 . ASN C 305 ? 0.9035 1.0811 0.7785 0.2261  -0.0085 0.1301  606 ASN C ND2 
9288  N N   . SER C 306 ? 0.9565 1.0075 0.8245 0.1840  0.0083  0.1076  607 SER C N   
9289  C CA  . SER C 306 ? 0.9622 0.9750 0.8170 0.1890  0.0135  0.1057  607 SER C CA  
9290  C C   . SER C 306 ? 0.9812 1.0102 0.8518 0.1800  0.0150  0.0965  607 SER C C   
9291  O O   . SER C 306 ? 0.9849 0.9823 0.8476 0.1754  0.0188  0.0927  607 SER C O   
9292  C CB  . SER C 306 ? 0.9881 0.9518 0.8266 0.1756  0.0156  0.1069  607 SER C CB  
9293  O OG  . SER C 306 ? 1.0750 1.0374 0.9083 0.1714  0.0130  0.1130  607 SER C OG  
9294  N N   . ARG C 307 ? 0.9357 1.0130 0.8271 0.1759  0.0120  0.0931  608 ARG C N   
9295  C CA  . ARG C 307 ? 0.8350 0.9314 0.7405 0.1674  0.0133  0.0854  608 ARG C CA  
9296  C C   . ARG C 307 ? 0.8612 1.0046 0.7770 0.1826  0.0129  0.0860  608 ARG C C   
9297  O O   . ARG C 307 ? 0.9383 1.0825 0.8438 0.2070  0.0144  0.0914  608 ARG C O   
9298  C CB  . ARG C 307 ? 0.6744 0.7808 0.5943 0.1412  0.0101  0.0797  608 ARG C CB  
9299  C CG  . ARG C 307 ? 0.6671 0.7318 0.5783 0.1272  0.0109  0.0786  608 ARG C CG  
9300  C CD  . ARG C 307 ? 0.7062 0.7353 0.6069 0.1274  0.0156  0.0758  608 ARG C CD  
9301  N NE  . ARG C 307 ? 0.7545 0.7995 0.6661 0.1212  0.0167  0.0694  608 ARG C NE  
9302  C CZ  . ARG C 307 ? 0.7971 0.8526 0.7210 0.1023  0.0145  0.0641  608 ARG C CZ  
9303  N NH1 . ARG C 307 ? 0.8365 0.8891 0.7638 0.0891  0.0112  0.0639  608 ARG C NH1 
9304  N NH2 . ARG C 307 ? 0.6794 0.7476 0.6105 0.0972  0.0158  0.0593  608 ARG C NH2 
9305  N N   . TYR C 308 ? 0.7203 0.9035 0.6550 0.1690  0.0110  0.0807  609 TYR C N   
9306  C CA  . TYR C 308 ? 0.7481 0.9781 0.6927 0.1819  0.0116  0.0806  609 TYR C CA  
9307  C C   . TYR C 308 ? 0.7462 1.0147 0.6948 0.1945  0.0074  0.0864  609 TYR C C   
9308  O O   . TYR C 308 ? 0.9353 1.2365 0.8864 0.2147  0.0084  0.0889  609 TYR C O   
9309  C CB  . TYR C 308 ? 0.8189 1.0785 0.7802 0.1615  0.0114  0.0734  609 TYR C CB  
9310  C CG  . TYR C 308 ? 0.9226 1.1657 0.8800 0.1648  0.0171  0.0694  609 TYR C CG  
9311  C CD1 . TYR C 308 ? 0.8353 1.0338 0.7851 0.1519  0.0191  0.0658  609 TYR C CD1 
9312  C CD2 . TYR C 308 ? 0.9757 1.2491 0.9360 0.1822  0.0208  0.0693  609 TYR C CD2 
9313  C CE1 . TYR C 308 ? 0.8220 1.0056 0.7669 0.1547  0.0242  0.0620  609 TYR C CE1 
9314  C CE2 . TYR C 308 ? 0.9412 1.1995 0.8965 0.1859  0.0264  0.0652  609 TYR C CE2 
9315  C CZ  . TYR C 308 ? 0.8935 1.1058 0.8406 0.1717  0.0280  0.0615  609 TYR C CZ  
9316  O OH  . TYR C 308 ? 0.8533 1.0516 0.7943 0.1751  0.0334  0.0572  609 TYR C OH  
9317  N N   . ASN C 309 ? 0.6716 0.9389 0.6205 0.1838  0.0025  0.0886  610 ASN C N   
9318  C CA  . ASN C 309 ? 0.7446 1.0360 0.6911 0.1983  -0.0016 0.0958  610 ASN C CA  
9319  C C   . ASN C 309 ? 0.6794 1.0363 0.6413 0.2049  -0.0042 0.0957  610 ASN C C   
9320  O O   . ASN C 309 ? 0.6122 0.9921 0.5705 0.2292  -0.0053 0.1022  610 ASN C O   
9321  C CB  . ASN C 309 ? 0.8198 1.0746 0.7448 0.2246  0.0011  0.1039  610 ASN C CB  
9322  C CG  . ASN C 309 ? 0.8935 1.1592 0.8112 0.2366  -0.0034 0.1125  610 ASN C CG  
9323  O OD1 . ASN C 309 ? 0.8951 1.1852 0.8220 0.2216  -0.0085 0.1119  610 ASN C OD1 
9324  N ND2 . ASN C 309 ? 0.8581 1.1032 0.7572 0.2641  -0.0016 0.1207  610 ASN C ND2 
9325  N N   . ILE C 310 ? 0.7387 1.1269 0.7168 0.1829  -0.0055 0.0886  611 ILE C N   
9326  C CA  . ILE C 310 ? 0.7934 1.2466 0.7869 0.1850  -0.0073 0.0876  611 ILE C CA  
9327  C C   . ILE C 310 ? 0.7301 1.2229 0.7318 0.1718  -0.0144 0.0879  611 ILE C C   
9328  O O   . ILE C 310 ? 0.6637 1.2101 0.6796 0.1617  -0.0167 0.0848  611 ILE C O   
9329  C CB  . ILE C 310 ? 0.7901 1.2576 0.7945 0.1686  -0.0039 0.0802  611 ILE C CB  
9330  C CG1 . ILE C 310 ? 0.7432 1.1968 0.7516 0.1352  -0.0066 0.0738  611 ILE C CG1 
9331  C CG2 . ILE C 310 ? 0.9467 1.3752 0.9417 0.1813  0.0030  0.0793  611 ILE C CG2 
9332  C CD1 . ILE C 310 ? 0.7758 1.2633 0.7964 0.1160  -0.0058 0.0679  611 ILE C CD1 
9333  N N   . LEU C 311 ? 0.7011 1.1693 0.6934 0.1705  -0.0178 0.0913  612 LEU C N   
9334  C CA  . LEU C 311 ? 0.6142 1.1180 0.6120 0.1585  -0.0247 0.0912  612 LEU C CA  
9335  C C   . LEU C 311 ? 0.6258 1.1879 0.6295 0.1785  -0.0280 0.0969  612 LEU C C   
9336  O O   . LEU C 311 ? 0.6943 1.3100 0.7105 0.1651  -0.0325 0.0937  612 LEU C O   
9337  C CB  . LEU C 311 ? 0.4290 0.8938 0.4140 0.1551  -0.0269 0.0939  612 LEU C CB  
9338  C CG  . LEU C 311 ? 0.4476 0.8768 0.4314 0.1279  -0.0266 0.0865  612 LEU C CG  
9339  C CD1 . LEU C 311 ? 0.4042 0.7954 0.3746 0.1290  -0.0273 0.0900  612 LEU C CD1 
9340  C CD2 . LEU C 311 ? 0.3827 0.8466 0.3769 0.1024  -0.0310 0.0789  612 LEU C CD2 
9341  N N   . GLU C 312 ? 0.6279 1.1803 0.6213 0.2105  -0.0261 0.1054  613 GLU C N   
9342  C CA  . GLU C 312 ? 0.7146 1.3226 0.7123 0.2343  -0.0294 0.1117  613 GLU C CA  
9343  C C   . GLU C 312 ? 0.7445 1.4146 0.7613 0.2297  -0.0289 0.1068  613 GLU C C   
9344  O O   . GLU C 312 ? 0.6746 1.4077 0.7033 0.2258  -0.0343 0.1071  613 GLU C O   
9345  C CB  . GLU C 312 ? 0.7834 1.3636 0.7645 0.2717  -0.0259 0.1209  613 GLU C CB  
9346  C CG  . GLU C 312 ? 0.9094 1.4250 0.8686 0.2773  -0.0253 0.1268  613 GLU C CG  
9347  C CD  . GLU C 312 ? 0.9629 1.4123 0.9120 0.2697  -0.0186 0.1229  613 GLU C CD  
9348  O OE1 . GLU C 312 ? 0.7857 1.2301 0.7456 0.2436  -0.0170 0.1140  613 GLU C OE1 
9349  O OE2 . GLU C 312 ? 1.0761 1.4775 1.0046 0.2896  -0.0151 0.1291  613 GLU C OE2 
9350  N N   . GLU C 313 ? 0.8524 1.5072 0.8719 0.2292  -0.0223 0.1024  614 GLU C N   
9351  C CA  . GLU C 313 ? 0.8597 1.5733 0.8958 0.2276  -0.0206 0.0986  614 GLU C CA  
9352  C C   . GLU C 313 ? 0.7659 1.5164 0.8165 0.1902  -0.0246 0.0912  614 GLU C C   
9353  O O   . GLU C 313 ? 0.7361 1.5553 0.8011 0.1861  -0.0269 0.0901  614 GLU C O   
9354  C CB  . GLU C 313 ? 0.9220 1.6051 0.9549 0.2348  -0.0124 0.0954  614 GLU C CB  
9355  C CG  . GLU C 313 ? 0.9220 1.6605 0.9718 0.2262  -0.0096 0.0902  614 GLU C CG  
9356  C CD  . GLU C 313 ? 0.9730 1.7064 1.0187 0.2538  -0.0020 0.0909  614 GLU C CD  
9357  O OE1 . GLU C 313 ? 0.9097 1.7021 0.9642 0.2751  -0.0013 0.0933  614 GLU C OE1 
9358  O OE2 . GLU C 313 ? 1.0277 1.6992 1.0609 0.2550  0.0031  0.0889  614 GLU C OE2 
9359  N N   . VAL C 314 ? 0.6663 1.3718 0.7118 0.1624  -0.0253 0.0859  615 VAL C N   
9360  C CA  . VAL C 314 ? 0.5534 1.2852 0.6077 0.1269  -0.0294 0.0789  615 VAL C CA  
9361  C C   . VAL C 314 ? 0.5612 1.3316 0.6173 0.1226  -0.0373 0.0809  615 VAL C C   
9362  O O   . VAL C 314 ? 0.6573 1.4787 0.7234 0.1013  -0.0414 0.0767  615 VAL C O   
9363  C CB  . VAL C 314 ? 0.5189 1.1895 0.5650 0.1020  -0.0278 0.0728  615 VAL C CB  
9364  C CG1 . VAL C 314 ? 0.4587 1.1476 0.5084 0.0671  -0.0328 0.0659  615 VAL C CG1 
9365  C CG2 . VAL C 314 ? 0.5224 1.1676 0.5688 0.1017  -0.0207 0.0700  615 VAL C CG2 
9366  N N   . ALA C 315 ? 0.5980 1.3459 0.6434 0.1416  -0.0398 0.0874  616 ALA C N   
9367  C CA  . ALA C 315 ? 0.5654 1.3532 0.6117 0.1403  -0.0475 0.0901  616 ALA C CA  
9368  C C   . ALA C 315 ? 0.4662 1.3317 0.5253 0.1567  -0.0500 0.0941  616 ALA C C   
9369  O O   . ALA C 315 ? 0.4785 1.3923 0.5447 0.1375  -0.0538 0.0901  616 ALA C O   
9370  C CB  . ALA C 315 ? 0.5527 1.2992 0.5833 0.1589  -0.0490 0.0974  616 ALA C CB  
9371  N N   . LYS C 316 ? 0.5142 1.3828 0.5725 0.1902  -0.0454 0.1003  617 LYS C N   
9372  C CA  . LYS C 316 ? 0.5721 1.4904 0.6342 0.2041  -0.0412 0.1011  617 LYS C CA  
9373  C C   . LYS C 316 ? 0.5739 1.5435 0.6502 0.1746  -0.0405 0.0929  617 LYS C C   
9374  O O   . LYS C 316 ? 0.5035 1.5202 0.5825 0.1642  -0.0420 0.0913  617 LYS C O   
9375  C CB  . LYS C 316 ? 0.6484 1.5493 0.7043 0.2392  -0.0339 0.1057  617 LYS C CB  
9376  C CG  . LYS C 316 ? 0.7367 1.5901 0.7737 0.2723  -0.0329 0.1146  617 LYS C CG  
9377  C CD  . LYS C 316 ? 0.8783 1.7089 0.9072 0.3024  -0.0251 0.1168  617 LYS C CD  
9378  C CE  . LYS C 316 ? 0.9164 1.7387 0.9276 0.3380  -0.0223 0.1242  617 LYS C CE  
9379  N NZ  . LYS C 316 ? 0.9336 1.6916 0.9248 0.3517  -0.0237 0.1315  617 LYS C NZ  
9380  N N   . LYS C 317 ? 0.6407 1.6005 0.7248 0.1599  -0.0380 0.0880  618 LYS C N   
9381  C CA  . LYS C 317 ? 0.6527 1.6544 0.7473 0.1295  -0.0367 0.0806  618 LYS C CA  
9382  C C   . LYS C 317 ? 0.6903 1.7050 0.7850 0.0926  -0.0430 0.0750  618 LYS C C   
9383  O O   . LYS C 317 ? 0.7146 1.7714 0.8133 0.0690  -0.0423 0.0701  618 LYS C O   
9384  C CB  . LYS C 317 ? 0.5795 1.5599 0.6806 0.1200  -0.0327 0.0768  618 LYS C CB  
9385  C CG  . LYS C 317 ? 0.6460 1.6389 0.7493 0.1450  -0.0244 0.0785  618 LYS C CG  
9386  C CD  . LYS C 317 ? 0.7363 1.7897 0.8444 0.1321  -0.0217 0.0750  618 LYS C CD  
9387  C CE  . LYS C 317 ? 0.7979 1.8687 0.9040 0.1637  -0.0147 0.0776  618 LYS C CE  
9388  N NZ  . LYS C 317 ? 0.8437 1.9044 0.9389 0.2028  -0.0147 0.0848  618 LYS C NZ  
9389  N N   . MET C 318 ? 0.6242 1.6022 0.7119 0.0869  -0.0491 0.0755  619 MET C N   
9390  C CA  . MET C 318 ? 0.5478 1.5338 0.6321 0.0543  -0.0550 0.0697  619 MET C CA  
9391  C C   . MET C 318 ? 0.6370 1.6563 0.7174 0.0624  -0.0570 0.0727  619 MET C C   
9392  O O   . MET C 318 ? 0.6730 1.7073 0.7505 0.0354  -0.0608 0.0674  619 MET C O   
9393  C CB  . MET C 318 ? 0.4854 1.4115 0.5596 0.0424  -0.0593 0.0674  619 MET C CB  
9394  C CG  . MET C 318 ? 0.3620 1.2390 0.4325 0.0207  -0.0536 0.0606  619 MET C CG  
9395  S SD  . MET C 318 ? 0.4974 1.2856 0.5497 0.0070  -0.0530 0.0561  619 MET C SD  
9396  C CE  . MET C 318 ? 0.5588 1.3684 0.6045 -0.0144 -0.0621 0.0519  619 MET C CE  
9397  N N   . ASN C 319 ? 0.6866 1.7168 0.7656 0.0986  -0.0541 0.0807  620 ASN C N   
9398  C CA  . ASN C 319 ? 0.6800 1.7409 0.7549 0.1109  -0.0558 0.0848  620 ASN C CA  
9399  C C   . ASN C 319 ? 0.6258 1.6580 0.6916 0.1031  -0.0622 0.0851  620 ASN C C   
9400  O O   . ASN C 319 ? 0.6914 1.7483 0.7558 0.0831  -0.0658 0.0814  620 ASN C O   
9401  C CB  . ASN C 319 ? 0.7535 1.8770 0.8342 0.0911  -0.0547 0.0802  620 ASN C CB  
9402  C CG  . ASN C 319 ? 0.8422 2.0039 0.9279 0.1114  -0.0484 0.0829  620 ASN C CG  
9403  O OD1 . ASN C 319 ? 0.8130 1.9841 0.9045 0.0990  -0.0448 0.0788  620 ASN C OD1 
9404  N ND2 . ASN C 319 ? 0.9003 2.0835 0.9821 0.1431  -0.0470 0.0898  620 ASN C ND2 
9405  N N   . LEU C 320 ? 0.5602 1.5390 0.6183 0.1189  -0.0633 0.0897  621 LEU C N   
9406  C CA  . LEU C 320 ? 0.4455 1.3912 0.4928 0.1109  -0.0691 0.0898  621 LEU C CA  
9407  C C   . LEU C 320 ? 0.6769 1.6167 0.7144 0.1410  -0.0694 0.0994  621 LEU C C   
9408  O O   . LEU C 320 ? 0.6247 1.5624 0.6601 0.1725  -0.0649 0.1069  621 LEU C O   
9409  C CB  . LEU C 320 ? 0.3994 1.2885 0.4412 0.1054  -0.0705 0.0887  621 LEU C CB  
9410  C CG  . LEU C 320 ? 0.4955 1.3768 0.5418 0.0700  -0.0713 0.0781  621 LEU C CG  
9411  C CD1 . LEU C 320 ? 0.4240 1.2247 0.4594 0.0666  -0.0653 0.0757  621 LEU C CD1 
9412  C CD2 . LEU C 320 ? 0.5149 1.4157 0.5580 0.0381  -0.0769 0.0701  621 LEU C CD2 
9413  N N   . ASP C 321 ? 0.8126 1.7491 0.8425 0.1302  -0.0744 0.0987  622 ASP C N   
9414  C CA  . ASP C 321 ? 0.9397 1.8634 0.9577 0.1541  -0.0755 0.1077  622 ASP C CA  
9415  C C   . ASP C 321 ? 0.9015 1.7649 0.9075 0.1760  -0.0736 0.1152  622 ASP C C   
9416  O O   . ASP C 321 ? 0.9651 1.7889 0.9610 0.1662  -0.0766 0.1149  622 ASP C O   
9417  C CB  . ASP C 321 ? 1.0739 2.0014 1.0856 0.1326  -0.0814 0.1036  622 ASP C CB  
9418  C CG  . ASP C 321 ? 1.1900 2.1116 1.1898 0.1544  -0.0828 0.1126  622 ASP C CG  
9419  O OD1 . ASP C 321 ? 1.1368 2.0582 1.1298 0.1393  -0.0873 0.1099  622 ASP C OD1 
9420  O OD2 . ASP C 321 ? 1.2914 2.2079 1.2874 0.1861  -0.0792 0.1221  622 ASP C OD2 
9421  N N   . MET C 322 ? 0.7549 1.6092 0.7597 0.2049  -0.0682 0.1218  623 MET C N   
9422  C CA  . MET C 322 ? 0.7674 1.5609 0.7580 0.2252  -0.0657 0.1292  623 MET C CA  
9423  C C   . MET C 322 ? 0.8688 1.6391 0.8417 0.2493  -0.0655 0.1395  623 MET C C   
9424  O O   . MET C 322 ? 0.9100 1.6297 0.8681 0.2693  -0.0621 0.1468  623 MET C O   
9425  C CB  . MET C 322 ? 0.6281 1.4135 0.6227 0.2430  -0.0594 0.1302  623 MET C CB  
9426  C CG  . MET C 322 ? 0.7165 1.5142 0.7264 0.2192  -0.0593 0.1211  623 MET C CG  
9427  S SD  . MET C 322 ? 0.8514 1.6403 0.8657 0.2402  -0.0514 0.1218  623 MET C SD  
9428  C CE  . MET C 322 ? 0.9009 1.6120 0.8916 0.2674  -0.0487 0.1317  623 MET C CE  
9429  N N   . ARG C 323 ? 0.9002 1.7049 0.8731 0.2466  -0.0690 0.1402  624 ARG C N   
9430  C CA  . ARG C 323 ? 0.8662 1.6531 0.8223 0.2664  -0.0697 0.1498  624 ARG C CA  
9431  C C   . ARG C 323 ? 0.7497 1.4753 0.6879 0.2645  -0.0706 0.1547  624 ARG C C   
9432  O O   . ARG C 323 ? 0.6253 1.3057 0.5468 0.2872  -0.0670 0.1637  624 ARG C O   
9433  C CB  . ARG C 323 ? 0.9496 1.7856 0.9105 0.2552  -0.0744 0.1476  624 ARG C CB  
9434  C CG  . ARG C 323 ? 1.0333 1.9291 1.0054 0.2652  -0.0728 0.1469  624 ARG C CG  
9435  C CD  . ARG C 323 ? 1.1013 1.9996 1.0604 0.2953  -0.0722 0.1573  624 ARG C CD  
9436  N NE  . ARG C 323 ? 1.1042 1.9670 1.0468 0.2960  -0.0756 0.1633  624 ARG C NE  
9437  C CZ  . ARG C 323 ? 1.0703 1.9574 1.0132 0.2801  -0.0809 0.1614  624 ARG C CZ  
9438  N NH1 . ARG C 323 ? 1.0255 1.9710 0.9839 0.2608  -0.0834 0.1533  624 ARG C NH1 
9439  N NH2 . ARG C 323 ? 1.0849 1.9370 1.0111 0.2823  -0.0834 0.1675  624 ARG C NH2 
9440  N N   . LYS C 324 ? 0.7691 1.4921 0.7083 0.2370  -0.0750 0.1486  625 LYS C N   
9441  C CA  . LYS C 324 ? 0.9057 1.5769 0.8280 0.2312  -0.0758 0.1521  625 LYS C CA  
9442  C C   . LYS C 324 ? 0.8662 1.5225 0.7940 0.2059  -0.0768 0.1432  625 LYS C C   
9443  O O   . LYS C 324 ? 0.9700 1.6574 0.9145 0.1902  -0.0780 0.1340  625 LYS C O   
9444  C CB  . LYS C 324 ? 0.9709 1.6524 0.8843 0.2245  -0.0800 0.1538  625 LYS C CB  
9445  C CG  . LYS C 324 ? 1.0160 1.7470 0.9430 0.1979  -0.0851 0.1425  625 LYS C CG  
9446  C CD  . LYS C 324 ? 1.0678 1.8474 0.9990 0.2064  -0.0871 0.1447  625 LYS C CD  
9447  C CE  . LYS C 324 ? 1.0232 1.8600 0.9737 0.1862  -0.0893 0.1339  625 LYS C CE  
9448  N NZ  . LYS C 324 ? 0.9310 1.7645 0.8851 0.1521  -0.0923 0.1217  625 LYS C NZ  
9449  N N   . THR C 325 ? 0.6710 1.2738 0.5851 0.1988  -0.0741 0.1441  626 THR C N   
9450  C CA  . THR C 325 ? 0.5879 1.1619 0.5092 0.1717  -0.0700 0.1315  626 THR C CA  
9451  C C   . THR C 325 ? 0.5529 1.1513 0.4792 0.1435  -0.0747 0.1204  626 THR C C   
9452  O O   . THR C 325 ? 0.5284 1.1168 0.4630 0.1213  -0.0727 0.1090  626 THR C O   
9453  C CB  . THR C 325 ? 0.4891 0.9961 0.3964 0.1709  -0.0634 0.1337  626 THR C CB  
9454  O OG1 . THR C 325 ? 0.6306 1.1239 0.5196 0.1819  -0.0647 0.1438  626 THR C OG1 
9455  C CG2 . THR C 325 ? 0.6548 1.1278 0.5614 0.1860  -0.0568 0.1374  626 THR C CG2 
9456  N N   . SER C 326 ? 0.5128 1.1412 0.4322 0.1441  -0.0810 0.1235  627 SER C N   
9457  C CA  . SER C 326 ? 0.5297 1.1772 0.4498 0.1175  -0.0855 0.1125  627 SER C CA  
9458  C C   . SER C 326 ? 0.5696 1.2559 0.5058 0.0978  -0.0883 0.1015  627 SER C C   
9459  O O   . SER C 326 ? 0.5288 1.2133 0.4643 0.0714  -0.0899 0.0896  627 SER C O   
9460  C CB  . SER C 326 ? 0.5070 1.1870 0.4169 0.1239  -0.0923 0.1185  627 SER C CB  
9461  O OG  . SER C 326 ? 0.6297 1.2919 0.5299 0.1515  -0.0895 0.1325  627 SER C OG  
9462  N N   . SER C 327 ? 0.5658 1.2868 0.5148 0.1099  -0.0888 0.1051  628 SER C N   
9463  C CA  . SER C 327 ? 0.5126 1.2700 0.4767 0.0899  -0.0906 0.0952  628 SER C CA  
9464  C C   . SER C 327 ? 0.5537 1.2674 0.5211 0.0715  -0.0843 0.0858  628 SER C C   
9465  O O   . SER C 327 ? 0.5826 1.3163 0.5583 0.0487  -0.0856 0.0762  628 SER C O   
9466  C CB  . SER C 327 ? 0.4643 1.2603 0.4422 0.1082  -0.0883 0.1005  628 SER C CB  
9467  O OG  . SER C 327 ? 0.4817 1.2480 0.4591 0.1297  -0.0840 0.1075  628 SER C OG  
9468  N N   . LEU C 328 ? 0.5833 1.2389 0.5436 0.0805  -0.0778 0.0886  629 LEU C N   
9469  C CA  . LEU C 328 ? 0.5770 1.1900 0.5395 0.0649  -0.0722 0.0804  629 LEU C CA  
9470  C C   . LEU C 328 ? 0.6124 1.2440 0.5891 0.0654  -0.0697 0.0790  629 LEU C C   
9471  O O   . LEU C 328 ? 0.5339 1.1568 0.5152 0.0441  -0.0680 0.0698  629 LEU C O   
9472  C CB  . LEU C 328 ? 0.5196 1.1229 0.4771 0.0353  -0.0744 0.0680  629 LEU C CB  
9473  C CG  . LEU C 328 ? 0.4918 1.0746 0.4345 0.0330  -0.0760 0.0674  629 LEU C CG  
9474  C CD1 . LEU C 328 ? 0.4177 0.9685 0.3539 0.0085  -0.0748 0.0547  629 LEU C CD1 
9475  C CD2 . LEU C 328 ? 0.4563 1.0022 0.3912 0.0552  -0.0713 0.0778  629 LEU C CD2 
9476  N N   . TRP C 329 ? 0.4792 1.1361 0.4611 0.0908  -0.0692 0.0884  630 TRP C N   
9477  C CA  . TRP C 329 ? 0.4644 1.1462 0.4600 0.0939  -0.0666 0.0875  630 TRP C CA  
9478  C C   . TRP C 329 ? 0.5498 1.1790 0.5447 0.0930  -0.0590 0.0850  630 TRP C C   
9479  O O   . TRP C 329 ? 0.4598 1.0955 0.4637 0.0784  -0.0568 0.0785  630 TRP C O   
9480  C CB  . TRP C 329 ? 0.5231 1.2449 0.5227 0.1248  -0.0679 0.0981  630 TRP C CB  
9481  C CG  . TRP C 329 ? 0.5870 1.2671 0.5740 0.1547  -0.0640 0.1087  630 TRP C CG  
9482  C CD1 . TRP C 329 ? 0.6180 1.2874 0.5912 0.1705  -0.0666 0.1174  630 TRP C CD1 
9483  C CD2 . TRP C 329 ? 0.6309 1.2730 0.6154 0.1712  -0.0567 0.1117  630 TRP C CD2 
9484  N NE1 . TRP C 329 ? 0.6633 1.2879 0.6245 0.1948  -0.0614 0.1259  630 TRP C NE1 
9485  C CE2 . TRP C 329 ? 0.6883 1.2953 0.6561 0.1956  -0.0553 0.1221  630 TRP C CE2 
9486  C CE3 . TRP C 329 ? 0.5896 1.2227 0.5828 0.1668  -0.0512 0.1065  630 TRP C CE3 
9487  C CZ2 . TRP C 329 ? 0.6458 1.2078 0.6045 0.2149  -0.0487 0.1269  630 TRP C CZ2 
9488  C CZ3 . TRP C 329 ? 0.5384 1.1290 0.5236 0.1870  -0.0448 0.1111  630 TRP C CZ3 
9489  C CH2 . TRP C 329 ? 0.5828 1.1376 0.5505 0.2103  -0.0436 0.1209  630 TRP C CH2 
9490  N N   . LYS C 330 ? 0.5027 1.0801 0.4861 0.1068  -0.0550 0.0902  631 LYS C N   
9491  C CA  . LYS C 330 ? 0.4239 0.9499 0.4052 0.1028  -0.0484 0.0870  631 LYS C CA  
9492  C C   . LYS C 330 ? 0.5705 1.0807 0.5536 0.0727  -0.0486 0.0758  631 LYS C C   
9493  O O   . LYS C 330 ? 0.5311 1.0271 0.5193 0.0630  -0.0450 0.0707  631 LYS C O   
9494  C CB  . LYS C 330 ? 0.5152 0.9903 0.4821 0.1171  -0.0451 0.0937  631 LYS C CB  
9495  C CG  . LYS C 330 ? 0.5689 1.0372 0.5295 0.1474  -0.0423 0.1043  631 LYS C CG  
9496  C CD  . LYS C 330 ? 0.5534 0.9633 0.4975 0.1552  -0.0382 0.1096  631 LYS C CD  
9497  C CE  . LYS C 330 ? 0.5910 0.9929 0.5231 0.1855  -0.0368 0.1213  631 LYS C CE  
9498  N NZ  . LYS C 330 ? 0.6717 1.0277 0.5844 0.1907  -0.0350 0.1283  631 LYS C NZ  
9499  N N   . ASP C 331 ? 0.6225 1.1320 0.5992 0.0587  -0.0527 0.0719  632 ASP C N   
9500  C CA  . ASP C 331 ? 0.6336 1.1234 0.6081 0.0321  -0.0530 0.0611  632 ASP C CA  
9501  C C   . ASP C 331 ? 0.6017 1.1235 0.5856 0.0139  -0.0547 0.0545  632 ASP C C   
9502  O O   . ASP C 331 ? 0.5436 1.0413 0.5276 -0.0015 -0.0520 0.0480  632 ASP C O   
9503  C CB  . ASP C 331 ? 0.5103 0.9998 0.4749 0.0222  -0.0574 0.0578  632 ASP C CB  
9504  C CG  . ASP C 331 ? 0.5423 1.0031 0.4970 0.0383  -0.0555 0.0648  632 ASP C CG  
9505  O OD1 . ASP C 331 ? 0.6912 1.1701 0.6446 0.0579  -0.0568 0.0744  632 ASP C OD1 
9506  O OD2 . ASP C 331 ? 0.5611 0.9820 0.5082 0.0316  -0.0528 0.0611  632 ASP C OD2 
9507  N N   . GLN C 332 ? 0.6037 1.1813 0.5948 0.0156  -0.0590 0.0566  633 GLN C N   
9508  C CA  . GLN C 332 ? 0.5866 1.2013 0.5859 -0.0048 -0.0610 0.0504  633 GLN C CA  
9509  C C   . GLN C 332 ? 0.5120 1.1231 0.5203 -0.0006 -0.0554 0.0513  633 GLN C C   
9510  O O   . GLN C 332 ? 0.3695 0.9738 0.3787 -0.0222 -0.0541 0.0444  633 GLN C O   
9511  C CB  . GLN C 332 ? 0.5592 1.2406 0.5654 -0.0019 -0.0670 0.0533  633 GLN C CB  
9512  C CG  . GLN C 332 ? 0.6323 1.3464 0.6390 -0.0331 -0.0717 0.0443  633 GLN C CG  
9513  C CD  . GLN C 332 ? 0.6428 1.4100 0.6499 -0.0333 -0.0792 0.0459  633 GLN C CD  
9514  O OE1 . GLN C 332 ? 0.6169 1.4059 0.6269 -0.0070 -0.0807 0.0551  633 GLN C OE1 
9515  N NE2 . GLN C 332 ? 0.7028 1.4896 0.7050 -0.0632 -0.0841 0.0369  633 GLN C NE2 
9516  N N   . ALA C 333 ? 0.4467 1.0610 0.4598 0.0274  -0.0519 0.0598  634 ALA C N   
9517  C CA  . ALA C 333 ? 0.4723 1.0855 0.4930 0.0337  -0.0463 0.0605  634 ALA C CA  
9518  C C   . ALA C 333 ? 0.4961 1.0494 0.5102 0.0245  -0.0415 0.0563  634 ALA C C   
9519  O O   . ALA C 333 ? 0.5059 1.0572 0.5240 0.0111  -0.0387 0.0519  634 ALA C O   
9520  C CB  . ALA C 333 ? 0.4495 1.0735 0.4727 0.0679  -0.0437 0.0701  634 ALA C CB  
9521  N N   . LEU C 334 ? 0.5228 1.0295 0.5267 0.0310  -0.0406 0.0578  635 LEU C N   
9522  C CA  . LEU C 334 ? 0.4785 0.9309 0.4763 0.0237  -0.0365 0.0542  635 LEU C CA  
9523  C C   . LEU C 334 ? 0.5800 1.0239 0.5755 -0.0050 -0.0381 0.0449  635 LEU C C   
9524  O O   . LEU C 334 ? 0.6223 1.0379 0.6166 -0.0128 -0.0346 0.0417  635 LEU C O   
9525  C CB  . LEU C 334 ? 0.3826 0.7954 0.3699 0.0335  -0.0360 0.0573  635 LEU C CB  
9526  C CG  . LEU C 334 ? 0.3927 0.7555 0.3734 0.0221  -0.0333 0.0522  635 LEU C CG  
9527  C CD1 . LEU C 334 ? 0.4180 0.7560 0.4006 0.0299  -0.0277 0.0538  635 LEU C CD1 
9528  C CD2 . LEU C 334 ? 0.4171 0.7525 0.3880 0.0263  -0.0338 0.0538  635 LEU C CD2 
9529  N N   . VAL C 335 ? 0.6024 1.0688 0.5952 -0.0212 -0.0434 0.0405  636 VAL C N   
9530  C CA  . VAL C 335 ? 0.6344 1.0894 0.6215 -0.0489 -0.0448 0.0316  636 VAL C CA  
9531  C C   . VAL C 335 ? 0.6527 1.1339 0.6479 -0.0594 -0.0430 0.0305  636 VAL C C   
9532  O O   . VAL C 335 ? 0.6466 1.1013 0.6372 -0.0745 -0.0408 0.0261  636 VAL C O   
9533  C CB  . VAL C 335 ? 0.4928 0.9643 0.4725 -0.0652 -0.0509 0.0263  636 VAL C CB  
9534  C CG1 . VAL C 335 ? 0.4098 0.8756 0.3821 -0.0948 -0.0524 0.0176  636 VAL C CG1 
9535  C CG2 . VAL C 335 ? 0.5976 1.0325 0.5663 -0.0593 -0.0515 0.0253  636 VAL C CG2 
9536  N N   . GLU C 336 ? 0.4641 0.9984 0.4710 -0.0504 -0.0438 0.0350  637 GLU C N   
9537  C CA  . GLU C 336 ? 0.3758 0.9431 0.3912 -0.0609 -0.0419 0.0340  637 GLU C CA  
9538  C C   . GLU C 336 ? 0.5289 1.0684 0.5467 -0.0505 -0.0352 0.0361  637 GLU C C   
9539  O O   . GLU C 336 ? 0.4207 0.9569 0.4381 -0.0675 -0.0329 0.0327  637 GLU C O   
9540  C CB  . GLU C 336 ? 0.3614 0.9965 0.3895 -0.0502 -0.0441 0.0385  637 GLU C CB  
9541  C CG  . GLU C 336 ? 0.4768 1.1484 0.5028 -0.0668 -0.0513 0.0352  637 GLU C CG  
9542  C CD  . GLU C 336 ? 0.4805 1.1630 0.5014 -0.1037 -0.0536 0.0270  637 GLU C CD  
9543  O OE1 . GLU C 336 ? 0.6017 1.2565 0.6186 -0.1180 -0.0499 0.0237  637 GLU C OE1 
9544  O OE2 . GLU C 336 ? 0.5462 1.2651 0.5657 -0.1195 -0.0594 0.0238  637 GLU C OE2 
9545  N N   . ILE C 337 ? 0.5662 1.0838 0.5846 -0.0239 -0.0321 0.0417  638 ILE C N   
9546  C CA  . ILE C 337 ? 0.4770 0.9660 0.4958 -0.0136 -0.0260 0.0433  638 ILE C CA  
9547  C C   . ILE C 337 ? 0.5627 1.0055 0.5727 -0.0332 -0.0248 0.0377  638 ILE C C   
9548  O O   . ILE C 337 ? 0.5886 1.0269 0.5995 -0.0415 -0.0215 0.0361  638 ILE C O   
9549  C CB  . ILE C 337 ? 0.3505 0.8140 0.3666 0.0148  -0.0235 0.0494  638 ILE C CB  
9550  C CG1 . ILE C 337 ? 0.4290 0.9365 0.4513 0.0363  -0.0249 0.0556  638 ILE C CG1 
9551  C CG2 . ILE C 337 ? 0.3501 0.7812 0.3645 0.0230  -0.0173 0.0499  638 ILE C CG2 
9552  C CD1 . ILE C 337 ? 0.5125 1.0135 0.5350 0.0640  -0.0199 0.0613  638 ILE C CD1 
9553  N N   . ASN C 338 ? 0.6179 1.0267 0.6182 -0.0401 -0.0276 0.0349  639 ASN C N   
9554  C CA  . ASN C 338 ? 0.5658 0.9281 0.5562 -0.0545 -0.0267 0.0301  639 ASN C CA  
9555  C C   . ASN C 338 ? 0.6175 0.9880 0.6033 -0.0818 -0.0285 0.0245  639 ASN C C   
9556  O O   . ASN C 338 ? 0.7499 1.0912 0.7296 -0.0918 -0.0263 0.0223  639 ASN C O   
9557  C CB  . ASN C 338 ? 0.5768 0.9062 0.5580 -0.0529 -0.0291 0.0283  639 ASN C CB  
9558  C CG  . ASN C 338 ? 0.5736 0.8786 0.5554 -0.0308 -0.0261 0.0333  639 ASN C CG  
9559  O OD1 . ASN C 338 ? 0.6679 0.9346 0.6449 -0.0298 -0.0237 0.0324  639 ASN C OD1 
9560  N ND2 . ASN C 338 ? 0.4725 0.7997 0.4589 -0.0133 -0.0263 0.0391  639 ASN C ND2 
9561  N N   . ILE C 339 ? 0.6102 1.0189 0.5972 -0.0951 -0.0325 0.0224  640 ILE C N   
9562  C CA  . ILE C 339 ? 0.6039 1.0234 0.5854 -0.1233 -0.0338 0.0176  640 ILE C CA  
9563  C C   . ILE C 339 ? 0.6432 1.0811 0.6327 -0.1239 -0.0291 0.0203  640 ILE C C   
9564  O O   . ILE C 339 ? 0.6669 1.0869 0.6482 -0.1430 -0.0277 0.0176  640 ILE C O   
9565  C CB  . ILE C 339 ? 0.4590 0.9241 0.4416 -0.1374 -0.0390 0.0152  640 ILE C CB  
9566  C CG1 . ILE C 339 ? 0.5673 1.0044 0.5359 -0.1452 -0.0436 0.0100  640 ILE C CG1 
9567  C CG2 . ILE C 339 ? 0.4030 0.8949 0.3835 -0.1656 -0.0394 0.0119  640 ILE C CG2 
9568  C CD1 . ILE C 339 ? 0.4085 0.8889 0.3775 -0.1565 -0.0489 0.0077  640 ILE C CD1 
9569  N N   . ALA C 340 ? 0.5573 1.0296 0.5611 -0.1022 -0.0263 0.0257  641 ALA C N   
9570  C CA  . ALA C 340 ? 0.4077 0.9043 0.4196 -0.1010 -0.0215 0.0278  641 ALA C CA  
9571  C C   . ALA C 340 ? 0.4983 0.9466 0.5044 -0.0956 -0.0169 0.0282  641 ALA C C   
9572  O O   . ALA C 340 ? 0.6063 1.0548 0.6106 -0.1086 -0.0138 0.0273  641 ALA C O   
9573  C CB  . ALA C 340 ? 0.4812 1.0256 0.5080 -0.0757 -0.0198 0.0331  641 ALA C CB  
9574  N N   . VAL C 341 ? 0.4790 0.8871 0.4816 -0.0777 -0.0164 0.0297  642 VAL C N   
9575  C CA  . VAL C 341 ? 0.4786 0.8417 0.4754 -0.0727 -0.0126 0.0299  642 VAL C CA  
9576  C C   . VAL C 341 ? 0.6002 0.9310 0.5842 -0.0971 -0.0140 0.0256  642 VAL C C   
9577  O O   . VAL C 341 ? 0.4805 0.8027 0.4614 -0.1050 -0.0109 0.0255  642 VAL C O   
9578  C CB  . VAL C 341 ? 0.4001 0.7292 0.3946 -0.0522 -0.0125 0.0320  642 VAL C CB  
9579  C CG1 . VAL C 341 ? 0.3939 0.6752 0.3807 -0.0525 -0.0103 0.0310  642 VAL C CG1 
9580  C CG2 . VAL C 341 ? 0.3477 0.6989 0.3509 -0.0265 -0.0097 0.0371  642 VAL C CG2 
9581  N N   . LEU C 342 ? 0.6648 0.9767 0.6393 -0.1089 -0.0186 0.0220  643 LEU C N   
9582  C CA  . LEU C 342 ? 0.6042 0.8803 0.5628 -0.1302 -0.0202 0.0178  643 LEU C CA  
9583  C C   . LEU C 342 ? 0.7046 1.0035 0.6602 -0.1533 -0.0194 0.0169  643 LEU C C   
9584  O O   . LEU C 342 ? 0.6192 0.8913 0.5643 -0.1652 -0.0178 0.0165  643 LEU C O   
9585  C CB  . LEU C 342 ? 0.4154 0.6731 0.3631 -0.1384 -0.0251 0.0133  643 LEU C CB  
9586  C CG  . LEU C 342 ? 0.4737 0.7041 0.4211 -0.1195 -0.0258 0.0136  643 LEU C CG  
9587  C CD1 . LEU C 342 ? 0.4135 0.6423 0.3529 -0.1264 -0.0305 0.0091  643 LEU C CD1 
9588  C CD2 . LEU C 342 ? 0.3994 0.5814 0.3376 -0.1165 -0.0242 0.0130  643 LEU C CD2 
9589  N N   . TYR C 343 ? 0.7046 1.0545 0.6685 -0.1611 -0.0207 0.0169  644 TYR C N   
9590  C CA  . TYR C 343 ? 0.6958 1.0736 0.6573 -0.1855 -0.0198 0.0161  644 TYR C CA  
9591  C C   . TYR C 343 ? 0.7380 1.1250 0.7063 -0.1792 -0.0138 0.0198  644 TYR C C   
9592  O O   . TYR C 343 ? 0.7519 1.1249 0.7097 -0.1982 -0.0120 0.0194  644 TYR C O   
9593  C CB  . TYR C 343 ? 0.4136 0.8523 0.3858 -0.1918 -0.0224 0.0157  644 TYR C CB  
9594  C CG  . TYR C 343 ? 0.4206 0.9068 0.3969 -0.2126 -0.0206 0.0160  644 TYR C CG  
9595  C CD1 . TYR C 343 ? 0.4447 0.9218 0.4044 -0.2470 -0.0227 0.0122  644 TYR C CD1 
9596  C CD2 . TYR C 343 ? 0.4208 0.9626 0.4162 -0.1981 -0.0169 0.0199  644 TYR C CD2 
9597  C CE1 . TYR C 343 ? 0.5141 1.0378 0.4771 -0.2688 -0.0209 0.0127  644 TYR C CE1 
9598  C CE2 . TYR C 343 ? 0.5058 1.0980 0.5062 -0.2173 -0.0149 0.0202  644 TYR C CE2 
9599  C CZ  . TYR C 343 ? 0.6033 1.1874 0.5879 -0.2540 -0.0169 0.0167  644 TYR C CZ  
9600  O OH  . TYR C 343 ? 0.6256 1.2616 0.6145 -0.2760 -0.0147 0.0172  644 TYR C OH  
9601  N N   . SER C 344 ? 0.6772 1.0835 0.6605 -0.1520 -0.0105 0.0234  645 SER C N   
9602  C CA  . SER C 344 ? 0.5762 0.9933 0.5655 -0.1438 -0.0045 0.0262  645 SER C CA  
9603  C C   . SER C 344 ? 0.6153 0.9770 0.5915 -0.1467 -0.0027 0.0260  645 SER C C   
9604  O O   . SER C 344 ? 0.7710 1.1328 0.7422 -0.1593 0.0005  0.0267  645 SER C O   
9605  C CB  . SER C 344 ? 0.5842 1.0233 0.5879 -0.1120 -0.0017 0.0294  645 SER C CB  
9606  O OG  . SER C 344 ? 0.5974 1.0939 0.6133 -0.1080 -0.0031 0.0304  645 SER C OG  
9607  N N   . PHE C 345 ? 0.5924 0.9087 0.5627 -0.1350 -0.0048 0.0254  646 PHE C N   
9608  C CA  . PHE C 345 ? 0.5728 0.8388 0.5309 -0.1366 -0.0040 0.0253  646 PHE C CA  
9609  C C   . PHE C 345 ? 0.6961 0.9400 0.6369 -0.1641 -0.0061 0.0233  646 PHE C C   
9610  O O   . PHE C 345 ? 0.7575 0.9806 0.6893 -0.1713 -0.0039 0.0246  646 PHE C O   
9611  C CB  . PHE C 345 ? 0.4021 0.6299 0.3577 -0.1207 -0.0063 0.0247  646 PHE C CB  
9612  C CG  . PHE C 345 ? 0.4830 0.7051 0.4466 -0.0965 -0.0028 0.0272  646 PHE C CG  
9613  C CD1 . PHE C 345 ? 0.4766 0.7311 0.4528 -0.0789 -0.0008 0.0293  646 PHE C CD1 
9614  C CD2 . PHE C 345 ? 0.4339 0.6170 0.3905 -0.0913 -0.0018 0.0275  646 PHE C CD2 
9615  C CE1 . PHE C 345 ? 0.5096 0.7528 0.4892 -0.0574 0.0025  0.0314  646 PHE C CE1 
9616  C CE2 . PHE C 345 ? 0.4764 0.6522 0.4380 -0.0715 0.0013  0.0293  646 PHE C CE2 
9617  C CZ  . PHE C 345 ? 0.4949 0.6985 0.4670 -0.0550 0.0036  0.0310  646 PHE C CZ  
9618  N N   . GLN C 346 ? 0.7704 1.0157 0.7041 -0.1800 -0.0105 0.0202  647 GLN C N   
9619  C CA  . GLN C 346 ? 0.7759 0.9932 0.6887 -0.2066 -0.0126 0.0182  647 GLN C CA  
9620  C C   . GLN C 346 ? 0.6782 0.9260 0.5898 -0.2272 -0.0095 0.0200  647 GLN C C   
9621  O O   . GLN C 346 ? 0.7064 0.9249 0.5999 -0.2454 -0.0091 0.0205  647 GLN C O   
9622  C CB  . GLN C 346 ? 0.7969 1.0083 0.7001 -0.2196 -0.0179 0.0135  647 GLN C CB  
9623  C CG  . GLN C 346 ? 0.7934 0.9522 0.6840 -0.2105 -0.0211 0.0108  647 GLN C CG  
9624  C CD  . GLN C 346 ? 0.6954 0.8617 0.5864 -0.2097 -0.0251 0.0066  647 GLN C CD  
9625  O OE1 . GLN C 346 ? 0.6447 0.8487 0.5393 -0.2233 -0.0267 0.0050  647 GLN C OE1 
9626  N NE2 . GLN C 346 ? 0.6796 0.8133 0.5671 -0.1939 -0.0269 0.0049  647 GLN C NE2 
9627  N N   . SER C 347 ? 0.6423 0.9496 0.5722 -0.2242 -0.0071 0.0212  648 SER C N   
9628  C CA  . SER C 347 ? 0.5436 0.8902 0.4747 -0.2441 -0.0037 0.0227  648 SER C CA  
9629  C C   . SER C 347 ? 0.6380 0.9766 0.5691 -0.2377 0.0019  0.0262  648 SER C C   
9630  O O   . SER C 347 ? 0.7702 1.1205 0.6937 -0.2590 0.0047  0.0278  648 SER C O   
9631  C CB  . SER C 347 ? 0.5138 0.9310 0.4662 -0.2383 -0.0029 0.0230  648 SER C CB  
9632  O OG  . SER C 347 ? 0.6222 1.0509 0.5724 -0.2497 -0.0085 0.0197  648 SER C OG  
9633  N N   . ASP C 348 ? 0.5255 0.8455 0.4640 -0.2100 0.0037  0.0275  649 ASP C N   
9634  C CA  . ASP C 348 ? 0.4935 0.8005 0.4300 -0.2027 0.0086  0.0301  649 ASP C CA  
9635  C C   . ASP C 348 ? 0.6070 0.8497 0.5244 -0.2056 0.0063  0.0305  649 ASP C C   
9636  O O   . ASP C 348 ? 0.5798 0.8037 0.4958 -0.1938 0.0091  0.0323  649 ASP C O   
9637  C CB  . ASP C 348 ? 0.4163 0.7428 0.3703 -0.1716 0.0123  0.0310  649 ASP C CB  
9638  C CG  . ASP C 348 ? 0.5131 0.9052 0.4844 -0.1663 0.0154  0.0314  649 ASP C CG  
9639  O OD1 . ASP C 348 ? 0.4162 0.8433 0.3873 -0.1888 0.0152  0.0312  649 ASP C OD1 
9640  O OD2 . ASP C 348 ? 0.5469 0.9558 0.5308 -0.1397 0.0179  0.0320  649 ASP C OD2 
9641  N N   . LYS C 349 ? 0.6660 0.8757 0.5677 -0.2206 0.0012  0.0285  650 LYS C N   
9642  C CA  . LYS C 349 ? 0.6950 0.8438 0.5774 -0.2212 -0.0019 0.0285  650 LYS C CA  
9643  C C   . LYS C 349 ? 0.7376 0.8643 0.6272 -0.1940 -0.0013 0.0293  650 LYS C C   
9644  O O   . LYS C 349 ? 0.8188 0.9076 0.6960 -0.1921 -0.0017 0.0310  650 LYS C O   
9645  C CB  . LYS C 349 ? 0.6934 0.8218 0.5556 -0.2432 -0.0005 0.0314  650 LYS C CB  
9646  C CG  . LYS C 349 ? 0.8606 0.9786 0.7031 -0.2735 -0.0034 0.0299  650 LYS C CG  
9647  C CD  . LYS C 349 ? 1.0389 1.1715 0.8705 -0.2992 0.0003  0.0335  650 LYS C CD  
9648  C CE  . LYS C 349 ? 1.1184 1.1933 0.9161 -0.3206 -0.0023 0.0352  650 LYS C CE  
9649  N NZ  . LYS C 349 ? 1.1702 1.2150 0.9504 -0.3336 -0.0078 0.0308  650 LYS C NZ  
9650  N N   . VAL C 350 ? 0.5853 0.7352 0.4934 -0.1735 -0.0006 0.0284  651 VAL C N   
9651  C CA  . VAL C 350 ? 0.5414 0.6707 0.4555 -0.1496 -0.0004 0.0286  651 VAL C CA  
9652  C C   . VAL C 350 ? 0.6955 0.7967 0.6052 -0.1444 -0.0053 0.0261  651 VAL C C   
9653  O O   . VAL C 350 ? 0.7296 0.8470 0.6435 -0.1470 -0.0076 0.0240  651 VAL C O   
9654  C CB  . VAL C 350 ? 0.4080 0.5737 0.3410 -0.1304 0.0036  0.0294  651 VAL C CB  
9655  C CG1 . VAL C 350 ? 0.4357 0.5775 0.3718 -0.1090 0.0042  0.0297  651 VAL C CG1 
9656  C CG2 . VAL C 350 ? 0.4089 0.6084 0.3462 -0.1354 0.0089  0.0311  651 VAL C CG2 
9657  N N   . THR C 351 ? 0.6547 0.7162 0.5558 -0.1369 -0.0070 0.0263  652 THR C N   
9658  C CA  . THR C 351 ? 0.5687 0.6022 0.4629 -0.1332 -0.0114 0.0236  652 THR C CA  
9659  C C   . THR C 351 ? 0.6293 0.6824 0.5383 -0.1188 -0.0118 0.0223  652 THR C C   
9660  O O   . THR C 351 ? 0.7310 0.7992 0.6530 -0.1035 -0.0090 0.0241  652 THR C O   
9661  C CB  . THR C 351 ? 0.5630 0.5583 0.4484 -0.1242 -0.0128 0.0244  652 THR C CB  
9662  O OG1 . THR C 351 ? 0.8235 0.7969 0.6917 -0.1380 -0.0132 0.0262  652 THR C OG1 
9663  C CG2 . THR C 351 ? 0.5841 0.5544 0.4634 -0.1178 -0.0168 0.0213  652 THR C CG2 
9664  N N   . ILE C 352 ? 0.5655 0.6158 0.4701 -0.1240 -0.0152 0.0192  653 ILE C N   
9665  C CA  . ILE C 352 ? 0.4882 0.5544 0.4040 -0.1115 -0.0160 0.0182  653 ILE C CA  
9666  C C   . ILE C 352 ? 0.5210 0.5660 0.4250 -0.1173 -0.0202 0.0139  653 ILE C C   
9667  O O   . ILE C 352 ? 0.5259 0.5508 0.4134 -0.1330 -0.0223 0.0115  653 ILE C O   
9668  C CB  . ILE C 352 ? 0.4323 0.5449 0.3614 -0.1123 -0.0144 0.0195  653 ILE C CB  
9669  C CG1 . ILE C 352 ? 0.4235 0.5508 0.3649 -0.0935 -0.0140 0.0208  653 ILE C CG1 
9670  C CG2 . ILE C 352 ? 0.4165 0.5425 0.3384 -0.1327 -0.0170 0.0167  653 ILE C CG2 
9671  C CD1 . ILE C 352 ? 0.4008 0.5741 0.3550 -0.0896 -0.0124 0.0229  653 ILE C CD1 
9672  N N   . VAL C 353 ? 0.5137 0.5606 0.4236 -0.1045 -0.0212 0.0129  654 VAL C N   
9673  C CA  . VAL C 353 ? 0.5426 0.5709 0.4414 -0.1075 -0.0247 0.0081  654 VAL C CA  
9674  C C   . VAL C 353 ? 0.5991 0.6553 0.5079 -0.1014 -0.0254 0.0077  654 VAL C C   
9675  O O   . VAL C 353 ? 0.5621 0.6341 0.4844 -0.0866 -0.0234 0.0113  654 VAL C O   
9676  C CB  . VAL C 353 ? 0.6401 0.6326 0.5316 -0.0965 -0.0253 0.0072  654 VAL C CB  
9677  C CG1 . VAL C 353 ? 0.5712 0.5719 0.4773 -0.0783 -0.0229 0.0105  654 VAL C CG1 
9678  C CG2 . VAL C 353 ? 0.6964 0.6673 0.5737 -0.0985 -0.0284 0.0015  654 VAL C CG2 
9679  N N   . ASP C 354 ? 0.4686 0.5311 0.3694 -0.1138 -0.0284 0.0034  655 ASP C N   
9680  C CA  . ASP C 354 ? 0.5321 0.6202 0.4405 -0.1080 -0.0298 0.0029  655 ASP C CA  
9681  C C   . ASP C 354 ? 0.5862 0.6533 0.4918 -0.0944 -0.0302 0.0013  655 ASP C C   
9682  O O   . ASP C 354 ? 0.6498 0.6844 0.5473 -0.0904 -0.0298 -0.0003 655 ASP C O   
9683  C CB  . ASP C 354 ? 0.4928 0.5967 0.3930 -0.1264 -0.0331 -0.0015 655 ASP C CB  
9684  C CG  . ASP C 354 ? 0.6976 0.7635 0.5752 -0.1383 -0.0359 -0.0086 655 ASP C CG  
9685  O OD1 . ASP C 354 ? 0.8819 0.9382 0.7459 -0.1582 -0.0372 -0.0113 655 ASP C OD1 
9686  O OD2 . ASP C 354 ? 0.7937 0.8389 0.6656 -0.1281 -0.0367 -0.0115 655 ASP C OD2 
9687  N N   . HIS C 355 ? 0.6072 0.6949 0.5192 -0.0871 -0.0309 0.0018  656 HIS C N   
9688  C CA  . HIS C 355 ? 0.5137 0.5863 0.4244 -0.0742 -0.0305 0.0010  656 HIS C CA  
9689  C C   . HIS C 355 ? 0.6245 0.6764 0.5186 -0.0806 -0.0332 -0.0065 656 HIS C C   
9690  O O   . HIS C 355 ? 0.7335 0.7672 0.6238 -0.0707 -0.0325 -0.0083 656 HIS C O   
9691  C CB  . HIS C 355 ? 0.4838 0.5837 0.4062 -0.0624 -0.0297 0.0058  656 HIS C CB  
9692  C CG  . HIS C 355 ? 0.5929 0.7254 0.5172 -0.0696 -0.0323 0.0055  656 HIS C CG  
9693  N ND1 . HIS C 355 ? 0.5356 0.6942 0.4669 -0.0760 -0.0324 0.0080  656 HIS C ND1 
9694  C CD2 . HIS C 355 ? 0.5159 0.6620 0.4360 -0.0716 -0.0351 0.0029  656 HIS C CD2 
9695  C CE1 . HIS C 355 ? 0.6435 0.8324 0.5756 -0.0817 -0.0354 0.0070  656 HIS C CE1 
9696  N NE2 . HIS C 355 ? 0.5737 0.7546 0.4986 -0.0793 -0.0372 0.0040  656 HIS C NE2 
9697  N N   . HIS C 356 ? 0.6490 0.7027 0.5320 -0.0975 -0.0361 -0.0114 657 HIS C N   
9698  C CA  . HIS C 356 ? 0.6644 0.6903 0.5271 -0.1042 -0.0385 -0.0196 657 HIS C CA  
9699  C C   . HIS C 356 ? 0.7191 0.7037 0.5686 -0.1035 -0.0378 -0.0217 657 HIS C C   
9700  O O   . HIS C 356 ? 0.7808 0.7407 0.6212 -0.0935 -0.0376 -0.0254 657 HIS C O   
9701  C CB  . HIS C 356 ? 0.6350 0.6721 0.4869 -0.1248 -0.0419 -0.0244 657 HIS C CB  
9702  C CG  . HIS C 356 ? 0.6791 0.7614 0.5444 -0.1249 -0.0431 -0.0217 657 HIS C CG  
9703  N ND1 . HIS C 356 ? 0.6767 0.7700 0.5427 -0.1163 -0.0441 -0.0232 657 HIS C ND1 
9704  C CD2 . HIS C 356 ? 0.6744 0.7953 0.5532 -0.1303 -0.0434 -0.0170 657 HIS C CD2 
9705  C CE1 . HIS C 356 ? 0.6847 0.8199 0.5631 -0.1166 -0.0454 -0.0191 657 HIS C CE1 
9706  N NE2 . HIS C 356 ? 0.6321 0.7856 0.5188 -0.1243 -0.0450 -0.0155 657 HIS C NE2 
9707  N N   . SER C 357 ? 0.7687 0.7475 0.6173 -0.1127 -0.0373 -0.0189 658 SER C N   
9708  C CA  A SER C 357 ? 0.7207 0.6605 0.5558 -0.1118 -0.0370 -0.0196 658 SER C CA  
9709  C CA  B SER C 357 ? 0.7220 0.6616 0.5570 -0.1117 -0.0371 -0.0197 658 SER C CA  
9710  C C   . SER C 357 ? 0.6918 0.6253 0.5375 -0.0914 -0.0347 -0.0160 658 SER C C   
9711  O O   . SER C 357 ? 0.5554 0.4586 0.3893 -0.0833 -0.0351 -0.0187 658 SER C O   
9712  C CB  A SER C 357 ? 0.6932 0.6333 0.5266 -0.1263 -0.0366 -0.0162 658 SER C CB  
9713  C CB  B SER C 357 ? 0.6934 0.6324 0.5258 -0.1268 -0.0367 -0.0165 658 SER C CB  
9714  O OG  A SER C 357 ? 0.6713 0.5786 0.4956 -0.1217 -0.0359 -0.0145 658 SER C OG  
9715  O OG  B SER C 357 ? 0.7098 0.6569 0.5315 -0.1480 -0.0389 -0.0202 658 SER C OG  
9716  N N   . ALA C 358 ? 0.6072 0.5694 0.4742 -0.0827 -0.0323 -0.0100 659 ALA C N   
9717  C CA  . ALA C 358 ? 0.5104 0.4682 0.3871 -0.0666 -0.0301 -0.0063 659 ALA C CA  
9718  C C   . ALA C 358 ? 0.7057 0.6559 0.5793 -0.0549 -0.0302 -0.0099 659 ALA C C   
9719  O O   . ALA C 358 ? 0.7058 0.6367 0.5748 -0.0456 -0.0299 -0.0108 659 ALA C O   
9720  C CB  . ALA C 358 ? 0.4857 0.4728 0.3821 -0.0606 -0.0275 0.0001  659 ALA C CB  
9721  N N   . THR C 359 ? 0.7292 0.6976 0.6052 -0.0548 -0.0306 -0.0116 660 THR C N   
9722  C CA  . THR C 359 ? 0.4443 0.4106 0.3182 -0.0439 -0.0300 -0.0147 660 THR C CA  
9723  C C   . THR C 359 ? 0.5100 0.4460 0.3630 -0.0445 -0.0319 -0.0227 660 THR C C   
9724  O O   . THR C 359 ? 0.6098 0.5352 0.4595 -0.0321 -0.0309 -0.0250 660 THR C O   
9725  C CB  . THR C 359 ? 0.5839 0.5774 0.4639 -0.0444 -0.0301 -0.0141 660 THR C CB  
9726  O OG1 . THR C 359 ? 0.6424 0.6410 0.5139 -0.0586 -0.0329 -0.0178 660 THR C OG1 
9727  C CG2 . THR C 359 ? 0.5654 0.5831 0.4632 -0.0396 -0.0279 -0.0059 660 THR C CG2 
9728  N N   . GLU C 360 ? 0.5202 0.4419 0.3577 -0.0588 -0.0344 -0.0271 661 GLU C N   
9729  C CA  . GLU C 360 ? 0.5277 0.4131 0.3404 -0.0599 -0.0362 -0.0348 661 GLU C CA  
9730  C C   . GLU C 360 ? 0.7133 0.5721 0.5207 -0.0492 -0.0357 -0.0334 661 GLU C C   
9731  O O   . GLU C 360 ? 0.8361 0.6726 0.6301 -0.0377 -0.0359 -0.0384 661 GLU C O   
9732  C CB  . GLU C 360 ? 0.6188 0.4918 0.4147 -0.0807 -0.0389 -0.0385 661 GLU C CB  
9733  C CG  . GLU C 360 ? 0.8957 0.7223 0.6605 -0.0847 -0.0409 -0.0463 661 GLU C CG  
9734  C CD  . GLU C 360 ? 1.0906 0.9042 0.8378 -0.1096 -0.0435 -0.0489 661 GLU C CD  
9735  O OE1 . GLU C 360 ? 1.0555 0.8979 0.8169 -0.1226 -0.0434 -0.0439 661 GLU C OE1 
9736  O OE2 . GLU C 360 ? 1.1755 0.9501 0.8934 -0.1164 -0.0453 -0.0563 661 GLU C OE2 
9737  N N   . SER C 361 ? 0.7262 0.5887 0.5437 -0.0517 -0.0351 -0.0268 662 SER C N   
9738  C CA  . SER C 361 ? 0.7043 0.5444 0.5169 -0.0420 -0.0351 -0.0247 662 SER C CA  
9739  C C   . SER C 361 ? 0.6714 0.5251 0.4974 -0.0233 -0.0332 -0.0232 662 SER C C   
9740  O O   . SER C 361 ? 0.8507 0.6855 0.6675 -0.0109 -0.0337 -0.0252 662 SER C O   
9741  C CB  . SER C 361 ? 0.8218 0.6655 0.6416 -0.0504 -0.0347 -0.0181 662 SER C CB  
9742  O OG  . SER C 361 ? 1.0628 0.8895 0.8661 -0.0682 -0.0365 -0.0197 662 SER C OG  
9743  N N   . PHE C 362 ? 0.6394 0.5259 0.4858 -0.0211 -0.0310 -0.0197 663 PHE C N   
9744  C CA  . PHE C 362 ? 0.6237 0.5243 0.4817 -0.0064 -0.0289 -0.0181 663 PHE C CA  
9745  C C   . PHE C 362 ? 0.6747 0.5672 0.5213 0.0040  -0.0289 -0.0251 663 PHE C C   
9746  O O   . PHE C 362 ? 0.7707 0.6616 0.6178 0.0176  -0.0283 -0.0257 663 PHE C O   
9747  C CB  . PHE C 362 ? 0.5334 0.4659 0.4110 -0.0075 -0.0264 -0.0129 663 PHE C CB  
9748  C CG  . PHE C 362 ? 0.5504 0.4976 0.4392 0.0039  -0.0240 -0.0106 663 PHE C CG  
9749  C CD1 . PHE C 362 ? 0.4289 0.3765 0.3253 0.0080  -0.0235 -0.0064 663 PHE C CD1 
9750  C CD2 . PHE C 362 ? 0.5243 0.4856 0.4146 0.0095  -0.0224 -0.0128 663 PHE C CD2 
9751  C CE1 . PHE C 362 ? 0.4049 0.3684 0.3109 0.0160  -0.0214 -0.0045 663 PHE C CE1 
9752  C CE2 . PHE C 362 ? 0.5497 0.5268 0.4496 0.0179  -0.0199 -0.0106 663 PHE C CE2 
9753  C CZ  . PHE C 362 ? 0.6145 0.5932 0.5223 0.0205  -0.0194 -0.0065 663 PHE C CZ  
9754  N N   . ILE C 363 ? 0.7036 0.5928 0.5394 -0.0018 -0.0297 -0.0306 664 ILE C N   
9755  C CA  . ILE C 363 ? 0.6820 0.5601 0.5035 0.0083  -0.0295 -0.0384 664 ILE C CA  
9756  C C   . ILE C 363 ? 0.7278 0.5710 0.5305 0.0173  -0.0311 -0.0421 664 ILE C C   
9757  O O   . ILE C 363 ? 0.7400 0.5821 0.5404 0.0341  -0.0300 -0.0446 664 ILE C O   
9758  C CB  . ILE C 363 ? 0.7634 0.6397 0.5729 -0.0021 -0.0306 -0.0445 664 ILE C CB  
9759  C CG1 . ILE C 363 ? 0.5727 0.4857 0.4003 -0.0073 -0.0292 -0.0402 664 ILE C CG1 
9760  C CG2 . ILE C 363 ? 0.5605 0.4189 0.3504 0.0084  -0.0304 -0.0540 664 ILE C CG2 
9761  C CD1 . ILE C 363 ? 0.5854 0.5201 0.4212 0.0052  -0.0262 -0.0404 664 ILE C CD1 
9762  N N   . LYS C 364 ? 0.8381 0.6536 0.6267 0.0065  -0.0337 -0.0418 665 LYS C N   
9763  C CA  . LYS C 364 ? 0.8390 0.6185 0.6089 0.0147  -0.0355 -0.0429 665 LYS C CA  
9764  C C   . LYS C 364 ? 0.8119 0.6046 0.5966 0.0297  -0.0347 -0.0373 665 LYS C C   
9765  O O   . LYS C 364 ? 0.9342 0.7116 0.7081 0.0467  -0.0353 -0.0398 665 LYS C O   
9766  C CB  . LYS C 364 ? 0.7389 0.4930 0.4953 -0.0031 -0.0378 -0.0409 665 LYS C CB  
9767  C CG  . LYS C 364 ? 1.0502 0.7635 0.7845 0.0026  -0.0400 -0.0405 665 LYS C CG  
9768  C CD  . LYS C 364 ? 1.2617 0.9687 0.9963 -0.0149 -0.0411 -0.0339 665 LYS C CD  
9769  C CE  . LYS C 364 ? 1.4264 1.0876 1.1340 -0.0132 -0.0435 -0.0328 665 LYS C CE  
9770  N NZ  . LYS C 364 ? 1.4841 1.1045 1.1595 -0.0285 -0.0453 -0.0384 665 LYS C NZ  
9771  N N   . HIS C 365 ? 0.6722 0.4935 0.4805 0.0242  -0.0334 -0.0300 666 HIS C N   
9772  C CA  . HIS C 365 ? 0.6666 0.5027 0.4888 0.0359  -0.0329 -0.0250 666 HIS C CA  
9773  C C   . HIS C 365 ? 0.7698 0.6271 0.5995 0.0518  -0.0308 -0.0278 666 HIS C C   
9774  O O   . HIS C 365 ? 0.8525 0.7113 0.6822 0.0667  -0.0313 -0.0275 666 HIS C O   
9775  C CB  . HIS C 365 ? 0.5496 0.4104 0.3933 0.0257  -0.0315 -0.0176 666 HIS C CB  
9776  C CG  . HIS C 365 ? 0.6815 0.5593 0.5393 0.0346  -0.0310 -0.0129 666 HIS C CG  
9777  N ND1 . HIS C 365 ? 0.6904 0.5531 0.5413 0.0412  -0.0333 -0.0109 666 HIS C ND1 
9778  C CD2 . HIS C 365 ? 0.6586 0.5672 0.5357 0.0366  -0.0285 -0.0097 666 HIS C CD2 
9779  C CE1 . HIS C 365 ? 0.6329 0.5190 0.4993 0.0468  -0.0326 -0.0072 666 HIS C CE1 
9780  N NE2 . HIS C 365 ? 0.5589 0.4719 0.4408 0.0432  -0.0295 -0.0066 666 HIS C NE2 
9781  N N   . MET C 366 ? 0.6977 0.5738 0.5336 0.0488  -0.0285 -0.0304 667 MET C N   
9782  C CA  . MET C 366 ? 0.5905 0.4897 0.4332 0.0619  -0.0259 -0.0331 667 MET C CA  
9783  C C   . MET C 366 ? 0.6148 0.4934 0.4383 0.0792  -0.0268 -0.0402 667 MET C C   
9784  O O   . MET C 366 ? 0.5499 0.4442 0.3789 0.0949  -0.0258 -0.0403 667 MET C O   
9785  C CB  . MET C 366 ? 0.5984 0.5161 0.4462 0.0545  -0.0237 -0.0348 667 MET C CB  
9786  C CG  . MET C 366 ? 0.6623 0.6117 0.5322 0.0467  -0.0213 -0.0274 667 MET C CG  
9787  S SD  . MET C 366 ? 0.6857 0.6590 0.5590 0.0442  -0.0183 -0.0292 667 MET C SD  
9788  C CE  . MET C 366 ? 0.6284 0.6296 0.5113 0.0577  -0.0145 -0.0291 667 MET C CE  
9789  N N   . GLU C 367 ? 0.7245 0.5683 0.5241 0.0767  -0.0287 -0.0464 668 GLU C N   
9790  C CA  . GLU C 367 ? 0.8060 0.6223 0.5823 0.0942  -0.0295 -0.0536 668 GLU C CA  
9791  C C   . GLU C 367 ? 0.8578 0.6673 0.6334 0.1088  -0.0313 -0.0497 668 GLU C C   
9792  O O   . GLU C 367 ? 0.7643 0.5883 0.5421 0.1289  -0.0303 -0.0516 668 GLU C O   
9793  C CB  . GLU C 367 ? 0.9396 0.7112 0.6868 0.0847  -0.0318 -0.0596 668 GLU C CB  
9794  C CG  . GLU C 367 ? 1.1264 0.9041 0.8691 0.0755  -0.0304 -0.0660 668 GLU C CG  
9795  C CD  . GLU C 367 ? 1.1861 0.9265 0.9046 0.0580  -0.0331 -0.0703 668 GLU C CD  
9796  O OE1 . GLU C 367 ? 1.2659 0.9695 0.9665 0.0559  -0.0357 -0.0692 668 GLU C OE1 
9797  O OE2 . GLU C 367 ? 1.0273 0.7763 0.7442 0.0455  -0.0327 -0.0742 668 GLU C OE2 
9798  N N   . ASN C 368 ? 0.8651 0.6561 0.6383 0.0985  -0.0341 -0.0440 669 ASN C N   
9799  C CA  . ASN C 368 ? 0.7356 0.5200 0.5078 0.1099  -0.0365 -0.0391 669 ASN C CA  
9800  C C   . ASN C 368 ? 0.7851 0.6139 0.5815 0.1223  -0.0349 -0.0358 669 ASN C C   
9801  O O   . ASN C 368 ? 0.8122 0.6435 0.6036 0.1432  -0.0357 -0.0372 669 ASN C O   
9802  C CB  . ASN C 368 ? 0.7381 0.5116 0.5130 0.0922  -0.0385 -0.0320 669 ASN C CB  
9803  C CG  . ASN C 368 ? 0.8854 0.6144 0.6342 0.0792  -0.0404 -0.0344 669 ASN C CG  
9804  O OD1 . ASN C 368 ? 0.8259 0.5205 0.5479 0.0871  -0.0414 -0.0410 669 ASN C OD1 
9805  N ND2 . ASN C 368 ? 0.8819 0.6107 0.6365 0.0588  -0.0409 -0.0293 669 ASN C ND2 
9806  N N   . GLU C 369 ? 0.6712 0.5353 0.4926 0.1093  -0.0326 -0.0314 670 GLU C N   
9807  C CA  . GLU C 369 ? 0.6065 0.5124 0.4503 0.1160  -0.0310 -0.0278 670 GLU C CA  
9808  C C   . GLU C 369 ? 0.8130 0.7397 0.6569 0.1341  -0.0286 -0.0334 670 GLU C C   
9809  O O   . GLU C 369 ? 0.8504 0.8000 0.7018 0.1485  -0.0289 -0.0322 670 GLU C O   
9810  C CB  . GLU C 369 ? 0.5161 0.4487 0.3813 0.0977  -0.0284 -0.0228 670 GLU C CB  
9811  C CG  . GLU C 369 ? 0.6337 0.5536 0.5020 0.0819  -0.0301 -0.0169 670 GLU C CG  
9812  C CD  . GLU C 369 ? 0.6662 0.5935 0.5411 0.0859  -0.0323 -0.0118 670 GLU C CD  
9813  O OE1 . GLU C 369 ? 0.4610 0.4082 0.3519 0.0758  -0.0312 -0.0068 670 GLU C OE1 
9814  O OE2 . GLU C 369 ? 0.4969 0.4096 0.3595 0.1000  -0.0352 -0.0129 670 GLU C OE2 
9815  N N   . TYR C 370 ? 0.7641 0.6868 0.6003 0.1336  -0.0262 -0.0396 671 TYR C N   
9816  C CA  . TYR C 370 ? 0.6719 0.6163 0.5078 0.1509  -0.0232 -0.0454 671 TYR C CA  
9817  C C   . TYR C 370 ? 0.7812 0.7018 0.5961 0.1747  -0.0254 -0.0505 671 TYR C C   
9818  O O   . TYR C 370 ? 0.9363 0.8833 0.7560 0.1941  -0.0240 -0.0524 671 TYR C O   
9819  C CB  . TYR C 370 ? 0.6303 0.5745 0.4608 0.1442  -0.0202 -0.0511 671 TYR C CB  
9820  C CG  . TYR C 370 ? 0.5716 0.5560 0.4249 0.1312  -0.0165 -0.0467 671 TYR C CG  
9821  C CD1 . TYR C 370 ? 0.5805 0.5638 0.4429 0.1104  -0.0169 -0.0410 671 TYR C CD1 
9822  C CD2 . TYR C 370 ? 0.6900 0.7134 0.5547 0.1400  -0.0126 -0.0478 671 TYR C CD2 
9823  C CE1 . TYR C 370 ? 0.6092 0.6242 0.4891 0.0998  -0.0137 -0.0364 671 TYR C CE1 
9824  C CE2 . TYR C 370 ? 0.6679 0.7241 0.5504 0.1268  -0.0092 -0.0430 671 TYR C CE2 
9825  C CZ  . TYR C 370 ? 0.6634 0.7130 0.5525 0.1072  -0.0099 -0.0371 671 TYR C CZ  
9826  O OH  . TYR C 370 ? 0.6410 0.7185 0.5445 0.0954  -0.0066 -0.0317 671 TYR C OH  
9827  N N   . ARG C 371 ? 0.7308 0.6014 0.5213 0.1736  -0.0288 -0.0522 672 ARG C N   
9828  C CA  . ARG C 371 ? 0.8669 0.7049 0.6315 0.1967  -0.0311 -0.0568 672 ARG C CA  
9829  C C   . ARG C 371 ? 0.9098 0.7610 0.6816 0.2112  -0.0339 -0.0507 672 ARG C C   
9830  O O   . ARG C 371 ? 0.9174 0.7715 0.6802 0.2373  -0.0344 -0.0538 672 ARG C O   
9831  C CB  . ARG C 371 ? 0.9901 0.7680 0.7244 0.1873  -0.0339 -0.0595 672 ARG C CB  
9832  C CG  . ARG C 371 ? 1.1676 0.8996 0.8719 0.2060  -0.0375 -0.0608 672 ARG C CG  
9833  C CD  . ARG C 371 ? 1.3746 1.0740 1.0703 0.1905  -0.0415 -0.0534 672 ARG C CD  
9834  N NE  . ARG C 371 ? 1.4621 1.1525 1.1606 0.1605  -0.0411 -0.0523 672 ARG C NE  
9835  C CZ  . ARG C 371 ? 1.5850 1.2371 1.2590 0.1494  -0.0411 -0.0585 672 ARG C CZ  
9836  N NH1 . ARG C 371 ? 1.6100 1.2240 1.2527 0.1655  -0.0415 -0.0667 672 ARG C NH1 
9837  N NH2 . ARG C 371 ? 1.6486 1.3013 1.3286 0.1222  -0.0409 -0.0569 672 ARG C NH2 
9838  N N   . CYS C 372 ? 0.8371 0.6986 0.6250 0.1955  -0.0359 -0.0421 673 CYS C N   
9839  C CA  A CYS C 372 ? 0.8682 0.7403 0.6610 0.2073  -0.0393 -0.0362 673 CYS C CA  
9840  C CA  B CYS C 372 ? 0.8688 0.7404 0.6618 0.2063  -0.0394 -0.0360 673 CYS C CA  
9841  C C   . CYS C 372 ? 0.8993 0.8304 0.7238 0.2047  -0.0378 -0.0316 673 CYS C C   
9842  O O   . CYS C 372 ? 1.1533 1.1036 0.9826 0.2192  -0.0404 -0.0285 673 CYS C O   
9843  C CB  A CYS C 372 ? 0.8694 0.7068 0.6527 0.1933  -0.0432 -0.0299 673 CYS C CB  
9844  C CB  B CYS C 372 ? 0.8633 0.7025 0.6488 0.1904  -0.0430 -0.0295 673 CYS C CB  
9845  S SG  A CYS C 372 ? 0.7841 0.6512 0.5963 0.1648  -0.0421 -0.0224 673 CYS C SG  
9846  S SG  B CYS C 372 ? 0.9395 0.7047 0.6827 0.1942  -0.0464 -0.0321 673 CYS C SG  
9847  N N   . ARG C 373 ? 0.8493 0.8093 0.6939 0.1868  -0.0340 -0.0309 674 ARG C N   
9848  C CA  . ARG C 373 ? 0.7888 0.7993 0.6605 0.1801  -0.0326 -0.0261 674 ARG C CA  
9849  C C   . ARG C 373 ? 0.8306 0.8828 0.7158 0.1832  -0.0276 -0.0296 674 ARG C C   
9850  O O   . ARG C 373 ? 0.7296 0.8262 0.6347 0.1804  -0.0263 -0.0263 674 ARG C O   
9851  C CB  . ARG C 373 ? 0.7734 0.7819 0.6570 0.1536  -0.0324 -0.0201 674 ARG C CB  
9852  C CG  . ARG C 373 ? 0.6774 0.7188 0.5806 0.1454  -0.0332 -0.0138 674 ARG C CG  
9853  C CD  . ARG C 373 ? 0.6093 0.6421 0.5200 0.1210  -0.0322 -0.0093 674 ARG C CD  
9854  N NE  . ARG C 373 ? 0.6863 0.7508 0.6150 0.1101  -0.0317 -0.0044 674 ARG C NE  
9855  C CZ  . ARG C 373 ? 0.6918 0.7560 0.6286 0.0905  -0.0298 -0.0008 674 ARG C CZ  
9856  N NH1 . ARG C 373 ? 0.7771 0.8162 0.7081 0.0810  -0.0284 -0.0011 674 ARG C NH1 
9857  N NH2 . ARG C 373 ? 0.6123 0.7018 0.5621 0.0806  -0.0294 0.0029  674 ARG C NH2 
9858  N N   . GLY C 374 ? 0.9198 0.9594 0.7938 0.1874  -0.0247 -0.0362 675 GLY C N   
9859  C CA  . GLY C 374 ? 0.8677 0.9457 0.7533 0.1881  -0.0195 -0.0393 675 GLY C CA  
9860  C C   . GLY C 374 ? 0.7739 0.8650 0.6733 0.1635  -0.0163 -0.0357 675 GLY C C   
9861  O O   . GLY C 374 ? 0.7444 0.8741 0.6571 0.1604  -0.0121 -0.0354 675 GLY C O   
9862  N N   . GLY C 375 ? 0.6306 0.6919 0.5267 0.1462  -0.0181 -0.0324 676 GLY C N   
9863  C CA  . GLY C 375 ? 0.6373 0.7096 0.5449 0.1254  -0.0153 -0.0286 676 GLY C CA  
9864  C C   . GLY C 375 ? 0.7490 0.7976 0.6576 0.1088  -0.0178 -0.0231 676 GLY C C   
9865  O O   . GLY C 375 ? 0.8532 0.8805 0.7556 0.1113  -0.0216 -0.0216 676 GLY C O   
9866  N N   . CYS C 376 ? 0.6191 0.6728 0.5349 0.0923  -0.0155 -0.0198 677 CYS C N   
9867  C CA  . CYS C 376 ? 0.5472 0.5849 0.4660 0.0769  -0.0170 -0.0145 677 CYS C CA  
9868  C C   . CYS C 376 ? 0.5951 0.6494 0.5245 0.0629  -0.0137 -0.0100 677 CYS C C   
9869  O O   . CYS C 376 ? 0.6189 0.6707 0.5440 0.0596  -0.0121 -0.0118 677 CYS C O   
9870  C CB  . CYS C 376 ? 0.4365 0.4379 0.3395 0.0747  -0.0196 -0.0175 677 CYS C CB  
9871  S SG  . CYS C 376 ? 0.5679 0.5562 0.4752 0.0564  -0.0206 -0.0116 677 CYS C SG  
9872  N N   . PRO C 377 ? 0.5162 0.5852 0.4573 0.0542  -0.0127 -0.0041 678 PRO C N   
9873  C CA  . PRO C 377 ? 0.4211 0.5015 0.3689 0.0419  -0.0094 0.0008  678 PRO C CA  
9874  C C   . PRO C 377 ? 0.4584 0.5175 0.4018 0.0338  -0.0101 0.0027  678 PRO C C   
9875  O O   . PRO C 377 ? 0.5922 0.6333 0.5337 0.0308  -0.0126 0.0039  678 PRO C O   
9876  C CB  . PRO C 377 ? 0.4713 0.5652 0.4285 0.0347  -0.0088 0.0057  678 PRO C CB  
9877  C CG  . PRO C 377 ? 0.5287 0.6085 0.4838 0.0394  -0.0129 0.0048  678 PRO C CG  
9878  C CD  . PRO C 377 ? 0.5980 0.6697 0.5442 0.0544  -0.0149 -0.0014 678 PRO C CD  
9879  N N   . ALA C 378 ? 0.6101 0.6738 0.5518 0.0305  -0.0080 0.0032  679 ALA C N   
9880  C CA  . ALA C 378 ? 0.6205 0.6703 0.5588 0.0239  -0.0088 0.0052  679 ALA C CA  
9881  C C   . ALA C 378 ? 0.5594 0.6213 0.5005 0.0179  -0.0057 0.0105  679 ALA C C   
9882  O O   . ALA C 378 ? 0.6667 0.7456 0.6086 0.0192  -0.0030 0.0106  679 ALA C O   
9883  C CB  . ALA C 378 ? 0.6288 0.6657 0.5567 0.0276  -0.0111 -0.0011 679 ALA C CB  
9884  N N   . ASP C 379 ? 0.5078 0.5611 0.4493 0.0119  -0.0060 0.0152  680 ASP C N   
9885  C CA  . ASP C 379 ? 0.4982 0.5576 0.4396 0.0076  -0.0034 0.0214  680 ASP C CA  
9886  C C   . ASP C 379 ? 0.5603 0.6176 0.4971 0.0081  -0.0051 0.0206  680 ASP C C   
9887  O O   . ASP C 379 ? 0.5027 0.5514 0.4396 0.0063  -0.0070 0.0217  680 ASP C O   
9888  C CB  . ASP C 379 ? 0.4696 0.5209 0.4137 0.0024  -0.0023 0.0276  680 ASP C CB  
9889  C CG  . ASP C 379 ? 0.5429 0.5954 0.4834 -0.0011 0.0007  0.0349  680 ASP C CG  
9890  O OD1 . ASP C 379 ? 0.5725 0.6233 0.5121 -0.0063 0.0032  0.0391  680 ASP C OD1 
9891  O OD2 . ASP C 379 ? 0.6758 0.7299 0.6125 0.0010  0.0003  0.0367  680 ASP C OD2 
9892  N N   . TRP C 380 ? 0.5994 0.6675 0.5319 0.0101  -0.0045 0.0185  681 TRP C N   
9893  C CA  . TRP C 380 ? 0.4671 0.5367 0.3943 0.0098  -0.0066 0.0169  681 TRP C CA  
9894  C C   . TRP C 380 ? 0.3849 0.4540 0.3135 0.0074  -0.0069 0.0240  681 TRP C C   
9895  O O   . TRP C 380 ? 0.3821 0.4503 0.3096 0.0060  -0.0097 0.0227  681 TRP C O   
9896  C CB  . TRP C 380 ? 0.5748 0.6582 0.4966 0.0119  -0.0050 0.0152  681 TRP C CB  
9897  C CG  . TRP C 380 ? 0.5763 0.6615 0.4907 0.0116  -0.0078 0.0103  681 TRP C CG  
9898  C CD1 . TRP C 380 ? 0.5633 0.6427 0.4702 0.0134  -0.0097 0.0009  681 TRP C CD1 
9899  C CD2 . TRP C 380 ? 0.6125 0.7055 0.5246 0.0091  -0.0094 0.0144  681 TRP C CD2 
9900  N NE1 . TRP C 380 ? 0.6318 0.7148 0.5317 0.0100  -0.0123 -0.0016 681 TRP C NE1 
9901  C CE2 . TRP C 380 ? 0.6899 0.7840 0.5940 0.0076  -0.0123 0.0067  681 TRP C CE2 
9902  C CE3 . TRP C 380 ? 0.5754 0.6739 0.4899 0.0087  -0.0087 0.0237  681 TRP C CE3 
9903  C CZ2 . TRP C 380 ? 0.6670 0.7721 0.5674 0.0046  -0.0149 0.0082  681 TRP C CZ2 
9904  C CZ3 . TRP C 380 ? 0.5199 0.6289 0.4307 0.0083  -0.0112 0.0256  681 TRP C CZ3 
9905  C CH2 . TRP C 380 ? 0.5227 0.6373 0.4275 0.0057  -0.0144 0.0179  681 TRP C CH2 
9906  N N   . VAL C 381 ? 0.4597 0.5295 0.3893 0.0068  -0.0040 0.0316  682 VAL C N   
9907  C CA  . VAL C 381 ? 0.4221 0.4899 0.3504 0.0075  -0.0038 0.0389  682 VAL C CA  
9908  C C   . VAL C 381 ? 0.6086 0.6680 0.5409 0.0075  -0.0057 0.0383  682 VAL C C   
9909  O O   . VAL C 381 ? 0.6745 0.7382 0.6063 0.0098  -0.0071 0.0412  682 VAL C O   
9910  C CB  . VAL C 381 ? 0.4440 0.5063 0.3692 0.0061  -0.0001 0.0466  682 VAL C CB  
9911  C CG1 . VAL C 381 ? 0.3773 0.4305 0.2990 0.0092  0.0002  0.0538  682 VAL C CG1 
9912  C CG2 . VAL C 381 ? 0.3780 0.4517 0.2977 0.0051  0.0022  0.0487  682 VAL C CG2 
9913  N N   . TRP C 382 ? 0.5002 0.5499 0.4363 0.0055  -0.0057 0.0350  683 TRP C N   
9914  C CA  . TRP C 382 ? 0.4072 0.4486 0.3465 0.0046  -0.0069 0.0344  683 TRP C CA  
9915  C C   . TRP C 382 ? 0.4763 0.5176 0.4158 0.0022  -0.0102 0.0277  683 TRP C C   
9916  O O   . TRP C 382 ? 0.5264 0.5671 0.4672 0.0004  -0.0115 0.0277  683 TRP C O   
9917  C CB  . TRP C 382 ? 0.5141 0.5440 0.4555 0.0029  -0.0052 0.0352  683 TRP C CB  
9918  C CG  . TRP C 382 ? 0.6113 0.6348 0.5498 0.0031  -0.0021 0.0418  683 TRP C CG  
9919  C CD1 . TRP C 382 ? 0.6281 0.6534 0.5620 0.0024  0.0003  0.0462  683 TRP C CD1 
9920  C CD2 . TRP C 382 ? 0.7273 0.7384 0.6645 0.0036  -0.0008 0.0448  683 TRP C CD2 
9921  N NE1 . TRP C 382 ? 0.7570 0.7686 0.6852 0.0018  0.0028  0.0519  683 TRP C NE1 
9922  C CE2 . TRP C 382 ? 0.7496 0.7522 0.6797 0.0033  0.0023  0.0507  683 TRP C CE2 
9923  C CE3 . TRP C 382 ? 0.6824 0.6880 0.6221 0.0039  -0.0016 0.0429  683 TRP C CE3 
9924  C CZ2 . TRP C 382 ? 0.6636 0.6496 0.5878 0.0043  0.0044  0.0541  683 TRP C CZ2 
9925  C CZ3 . TRP C 382 ? 0.6554 0.6485 0.5911 0.0055  0.0007  0.0462  683 TRP C CZ3 
9926  C CH2 . TRP C 382 ? 0.6860 0.6681 0.6135 0.0061  0.0036  0.0514  683 TRP C CH2 
9927  N N   . ILE C 383 ? 0.3893 0.4299 0.3257 0.0019  -0.0114 0.0219  684 ILE C N   
9928  C CA  . ILE C 383 ? 0.3841 0.4181 0.3162 -0.0011 -0.0144 0.0154  684 ILE C CA  
9929  C C   . ILE C 383 ? 0.6040 0.6478 0.5330 -0.0048 -0.0166 0.0143  684 ILE C C   
9930  O O   . ILE C 383 ? 0.6171 0.6576 0.5440 -0.0106 -0.0188 0.0117  684 ILE C O   
9931  C CB  . ILE C 383 ? 0.3770 0.4050 0.3037 0.0019  -0.0149 0.0092  684 ILE C CB  
9932  C CG1 . ILE C 383 ? 0.4528 0.4754 0.3835 0.0053  -0.0135 0.0101  684 ILE C CG1 
9933  C CG2 . ILE C 383 ? 0.5019 0.5170 0.4194 -0.0014 -0.0180 0.0024  684 ILE C CG2 
9934  C CD1 . ILE C 383 ? 0.5310 0.5411 0.4629 0.0027  -0.0148 0.0109  684 ILE C CD1 
9935  N N   . VAL C 384 ? 0.6082 0.6656 0.5362 -0.0025 -0.0161 0.0164  685 VAL C N   
9936  C CA  . VAL C 384 ? 0.5255 0.5961 0.4501 -0.0062 -0.0187 0.0150  685 VAL C CA  
9937  C C   . VAL C 384 ? 0.4682 0.5493 0.3987 -0.0069 -0.0192 0.0204  685 VAL C C   
9938  O O   . VAL C 384 ? 0.4841 0.5678 0.4189 -0.0007 -0.0169 0.0275  685 VAL C O   
9939  C CB  . VAL C 384 ? 0.3737 0.4571 0.2948 -0.0026 -0.0181 0.0165  685 VAL C CB  
9940  C CG1 . VAL C 384 ? 0.3763 0.4781 0.2960 -0.0049 -0.0208 0.0179  685 VAL C CG1 
9941  C CG2 . VAL C 384 ? 0.5871 0.6643 0.5003 -0.0026 -0.0182 0.0088  685 VAL C CG2 
9942  N N   . PRO C 385 ? 0.4281 0.5154 0.3577 -0.0141 -0.0220 0.0172  686 PRO C N   
9943  C CA  . PRO C 385 ? 0.4892 0.5902 0.4255 -0.0138 -0.0220 0.0220  686 PRO C CA  
9944  C C   . PRO C 385 ? 0.5979 0.7200 0.5367 -0.0062 -0.0220 0.0284  686 PRO C C   
9945  O O   . PRO C 385 ? 0.6962 0.8268 0.6305 -0.0054 -0.0233 0.0279  686 PRO C O   
9946  C CB  . PRO C 385 ? 0.4781 0.5849 0.4112 -0.0259 -0.0252 0.0163  686 PRO C CB  
9947  C CG  . PRO C 385 ? 0.4722 0.5554 0.3960 -0.0315 -0.0261 0.0092  686 PRO C CG  
9948  C CD  . PRO C 385 ? 0.4802 0.5570 0.4014 -0.0234 -0.0247 0.0089  686 PRO C CD  
9949  N N   . PRO C 386 ? 0.6549 0.7857 0.5994 0.0004  -0.0205 0.0345  687 PRO C N   
9950  C CA  . PRO C 386 ? 0.5120 0.6597 0.4568 0.0107  -0.0205 0.0417  687 PRO C CA  
9951  C C   . PRO C 386 ? 0.5621 0.7412 0.5084 0.0085  -0.0244 0.0412  687 PRO C C   
9952  O O   . PRO C 386 ? 0.7141 0.9103 0.6606 0.0188  -0.0248 0.0478  687 PRO C O   
9953  C CB  . PRO C 386 ? 0.4187 0.5602 0.3670 0.0200  -0.0172 0.0474  687 PRO C CB  
9954  C CG  . PRO C 386 ? 0.4897 0.6137 0.4404 0.0131  -0.0158 0.0429  687 PRO C CG  
9955  C CD  . PRO C 386 ? 0.5282 0.6520 0.4775 0.0002  -0.0187 0.0352  687 PRO C CD  
9956  N N   . MET C 387 ? 0.4932 0.6804 0.4394 -0.0048 -0.0273 0.0341  688 MET C N   
9957  C CA  . MET C 387 ? 0.5626 0.7797 0.5080 -0.0106 -0.0316 0.0322  688 MET C CA  
9958  C C   . MET C 387 ? 0.6581 0.8653 0.5947 -0.0253 -0.0342 0.0229  688 MET C C   
9959  O O   . MET C 387 ? 0.6078 0.7900 0.5407 -0.0327 -0.0332 0.0175  688 MET C O   
9960  C CB  . MET C 387 ? 0.5137 0.7580 0.4667 -0.0139 -0.0328 0.0331  688 MET C CB  
9961  C CG  . MET C 387 ? 0.5815 0.8202 0.5330 -0.0316 -0.0338 0.0256  688 MET C CG  
9962  S SD  . MET C 387 ? 0.6604 0.9365 0.6217 -0.0363 -0.0344 0.0273  688 MET C SD  
9963  C CE  . MET C 387 ? 0.7136 1.0168 0.6693 -0.0565 -0.0403 0.0206  688 MET C CE  
9964  N N   . SER C 388 ? 0.5483 0.7737 0.4796 -0.0283 -0.0377 0.0210  689 SER C N   
9965  C CA  . SER C 388 ? 0.4439 0.6629 0.3641 -0.0429 -0.0407 0.0113  689 SER C CA  
9966  C C   . SER C 388 ? 0.4460 0.6302 0.3577 -0.0415 -0.0383 0.0065  689 SER C C   
9967  O O   . SER C 388 ? 0.5078 0.6734 0.4091 -0.0523 -0.0395 -0.0021 689 SER C O   
9968  C CB  . SER C 388 ? 0.4831 0.7058 0.4018 -0.0598 -0.0429 0.0056  689 SER C CB  
9969  O OG  . SER C 388 ? 0.4914 0.7468 0.4214 -0.0586 -0.0436 0.0111  689 SER C OG  
9970  N N   . GLY C 389 ? 0.3921 0.5675 0.3068 -0.0283 -0.0349 0.0121  690 GLY C N   
9971  C CA  . GLY C 389 ? 0.4668 0.6164 0.3754 -0.0255 -0.0323 0.0083  690 GLY C CA  
9972  C C   . GLY C 389 ? 0.5773 0.7159 0.4722 -0.0336 -0.0343 -0.0021 690 GLY C C   
9973  O O   . GLY C 389 ? 0.5950 0.7091 0.4838 -0.0379 -0.0338 -0.0084 690 GLY C O   
9974  N N   . SER C 390 ? 0.4996 0.6550 0.3877 -0.0354 -0.0366 -0.0041 691 SER C N   
9975  C CA  . SER C 390 ? 0.5978 0.7400 0.4706 -0.0404 -0.0375 -0.0143 691 SER C CA  
9976  C C   . SER C 390 ? 0.5387 0.6673 0.4002 -0.0553 -0.0408 -0.0238 691 SER C C   
9977  O O   . SER C 390 ? 0.5646 0.6702 0.4107 -0.0581 -0.0408 -0.0332 691 SER C O   
9978  C CB  . SER C 390 ? 0.6542 0.8182 0.5213 -0.0385 -0.0390 -0.0140 691 SER C CB  
9979  O OG  . SER C 390 ? 0.7489 0.9348 0.6122 -0.0493 -0.0440 -0.0164 691 SER C OG  
9980  N N   . ILE C 391 ? 0.4872 0.6275 0.3542 -0.0650 -0.0432 -0.0219 692 ILE C N   
9981  C CA  . ILE C 391 ? 0.6628 0.7865 0.5164 -0.0818 -0.0460 -0.0306 692 ILE C CA  
9982  C C   . ILE C 391 ? 0.6871 0.7790 0.5399 -0.0813 -0.0436 -0.0312 692 ILE C C   
9983  O O   . ILE C 391 ? 0.8077 0.8824 0.6493 -0.0953 -0.0454 -0.0365 692 ILE C O   
9984  C CB  . ILE C 391 ? 0.5816 0.7354 0.4382 -0.0967 -0.0501 -0.0299 692 ILE C CB  
9985  C CG1 . ILE C 391 ? 0.5729 0.7525 0.4500 -0.0898 -0.0487 -0.0191 692 ILE C CG1 
9986  C CG2 . ILE C 391 ? 0.5612 0.7403 0.4107 -0.1019 -0.0539 -0.0332 692 ILE C CG2 
9987  C CD1 . ILE C 391 ? 0.5415 0.7397 0.4215 -0.1056 -0.0512 -0.0194 692 ILE C CD1 
9988  N N   . THR C 392 ? 0.5183 0.6017 0.3816 -0.0664 -0.0397 -0.0255 693 THR C N   
9989  C CA  . THR C 392 ? 0.6440 0.6961 0.5043 -0.0639 -0.0377 -0.0268 693 THR C CA  
9990  C C   . THR C 392 ? 0.6646 0.6953 0.5168 -0.0525 -0.0355 -0.0313 693 THR C C   
9991  O O   . THR C 392 ? 0.5492 0.5936 0.4047 -0.0436 -0.0340 -0.0300 693 THR C O   
9992  C CB  . THR C 392 ? 0.6664 0.7250 0.5441 -0.0569 -0.0350 -0.0177 693 THR C CB  
9993  O OG1 . THR C 392 ? 0.6173 0.6822 0.5045 -0.0423 -0.0319 -0.0124 693 THR C OG1 
9994  C CG2 . THR C 392 ? 0.6368 0.7242 0.5253 -0.0635 -0.0363 -0.0122 693 THR C CG2 
9995  N N   . PRO C 393 ? 0.5921 0.5906 0.4331 -0.0516 -0.0352 -0.0361 694 PRO C N   
9996  C CA  . PRO C 393 ? 0.6391 0.6193 0.4694 -0.0402 -0.0335 -0.0421 694 PRO C CA  
9997  C C   . PRO C 393 ? 0.7518 0.7423 0.5968 -0.0248 -0.0296 -0.0363 694 PRO C C   
9998  O O   . PRO C 393 ? 0.8228 0.8101 0.6622 -0.0147 -0.0277 -0.0405 694 PRO C O   
9999  C CB  . PRO C 393 ? 0.5208 0.4627 0.3340 -0.0430 -0.0347 -0.0477 694 PRO C CB  
10000 C CG  . PRO C 393 ? 0.6459 0.5899 0.4696 -0.0507 -0.0352 -0.0408 694 PRO C CG  
10001 C CD  . PRO C 393 ? 0.6448 0.6225 0.4810 -0.0602 -0.0363 -0.0362 694 PRO C CD  
10002 N N   . VAL C 394 ? 0.7046 0.7074 0.5668 -0.0229 -0.0282 -0.0274 695 VAL C N   
10003 C CA  . VAL C 394 ? 0.5694 0.5801 0.4429 -0.0108 -0.0247 -0.0225 695 VAL C CA  
10004 C C   . VAL C 394 ? 0.4938 0.5292 0.3729 -0.0075 -0.0229 -0.0191 695 VAL C C   
10005 O O   . VAL C 394 ? 0.5080 0.5499 0.3914 0.0011  -0.0198 -0.0173 695 VAL C O   
10006 C CB  . VAL C 394 ? 0.4838 0.4954 0.3709 -0.0102 -0.0235 -0.0148 695 VAL C CB  
10007 C CG1 . VAL C 394 ? 0.4536 0.4397 0.3346 -0.0093 -0.0244 -0.0177 695 VAL C CG1 
10008 C CG2 . VAL C 394 ? 0.4625 0.4872 0.3562 -0.0187 -0.0249 -0.0100 695 VAL C CG2 
10009 N N   . PHE C 395 ? 0.4733 0.5241 0.3516 -0.0145 -0.0250 -0.0180 696 PHE C N   
10010 C CA  . PHE C 395 ? 0.5803 0.6533 0.4612 -0.0109 -0.0238 -0.0142 696 PHE C CA  
10011 C C   . PHE C 395 ? 0.5893 0.6600 0.4599 -0.0053 -0.0221 -0.0209 696 PHE C C   
10012 O O   . PHE C 395 ? 0.4957 0.5794 0.3705 0.0012  -0.0189 -0.0168 696 PHE C O   
10013 C CB  . PHE C 395 ? 0.5723 0.6632 0.4518 -0.0188 -0.0272 -0.0131 696 PHE C CB  
10014 C CG  . PHE C 395 ? 0.5629 0.6762 0.4427 -0.0147 -0.0266 -0.0087 696 PHE C CG  
10015 C CD1 . PHE C 395 ? 0.5293 0.6591 0.4191 -0.0109 -0.0259 0.0020  696 PHE C CD1 
10016 C CD2 . PHE C 395 ? 0.5516 0.6679 0.4195 -0.0144 -0.0268 -0.0152 696 PHE C CD2 
10017 C CE1 . PHE C 395 ? 0.6115 0.7594 0.4992 -0.0069 -0.0256 0.0070  696 PHE C CE1 
10018 C CE2 . PHE C 395 ? 0.5931 0.7302 0.4601 -0.0111 -0.0262 -0.0105 696 PHE C CE2 
10019 C CZ  . PHE C 395 ? 0.5532 0.7058 0.4299 -0.0076 -0.0258 0.0010  696 PHE C CZ  
10020 N N   . HIS C 396 ? 0.5282 0.5814 0.3837 -0.0079 -0.0240 -0.0313 697 HIS C N   
10021 C CA  . HIS C 396 ? 0.5920 0.6408 0.4346 -0.0015 -0.0224 -0.0396 697 HIS C CA  
10022 C C   . HIS C 396 ? 0.6490 0.6829 0.4908 0.0098  -0.0195 -0.0426 697 HIS C C   
10023 O O   . HIS C 396 ? 0.7370 0.7594 0.5646 0.0163  -0.0186 -0.0517 697 HIS C O   
10024 C CB  . HIS C 396 ? 0.6156 0.6500 0.4385 -0.0099 -0.0260 -0.0501 697 HIS C CB  
10025 C CG  . HIS C 396 ? 0.6604 0.7116 0.4845 -0.0227 -0.0298 -0.0475 697 HIS C CG  
10026 N ND1 . HIS C 396 ? 0.6299 0.7025 0.4498 -0.0249 -0.0307 -0.0482 697 HIS C ND1 
10027 C CD2 . HIS C 396 ? 0.6483 0.7024 0.4784 -0.0333 -0.0328 -0.0437 697 HIS C CD2 
10028 C CE1 . HIS C 396 ? 0.6789 0.7674 0.5022 -0.0358 -0.0346 -0.0450 697 HIS C CE1 
10029 N NE2 . HIS C 396 ? 0.6610 0.7399 0.4911 -0.0409 -0.0357 -0.0422 697 HIS C NE2 
10030 N N   . GLN C 397 ? 0.7218 0.7563 0.5776 0.0131  -0.0180 -0.0355 698 GLN C N   
10031 C CA  . GLN C 397 ? 0.6663 0.6897 0.5223 0.0236  -0.0160 -0.0379 698 GLN C CA  
10032 C C   . GLN C 397 ? 0.6208 0.6671 0.4921 0.0294  -0.0119 -0.0305 698 GLN C C   
10033 O O   . GLN C 397 ? 0.6579 0.7132 0.5420 0.0246  -0.0115 -0.0216 698 GLN C O   
10034 C CB  . GLN C 397 ? 0.6126 0.6133 0.4685 0.0207  -0.0185 -0.0372 698 GLN C CB  
10035 C CG  . GLN C 397 ? 0.5656 0.5579 0.4234 0.0323  -0.0171 -0.0379 698 GLN C CG  
10036 C CD  . GLN C 397 ? 0.6344 0.6082 0.4740 0.0431  -0.0172 -0.0480 698 GLN C CD  
10037 O OE1 . GLN C 397 ? 0.5632 0.5084 0.3848 0.0397  -0.0201 -0.0543 698 GLN C OE1 
10038 N NE2 . GLN C 397 ? 0.6598 0.6493 0.5024 0.0563  -0.0138 -0.0498 698 GLN C NE2 
10039 N N   . GLU C 398 ? 0.5823 0.6378 0.4507 0.0394  -0.0088 -0.0346 699 GLU C N   
10040 C CA  . GLU C 398 ? 0.5756 0.6540 0.4570 0.0433  -0.0046 -0.0284 699 GLU C CA  
10041 C C   . GLU C 398 ? 0.6484 0.7207 0.5389 0.0460  -0.0050 -0.0253 699 GLU C C   
10042 O O   . GLU C 398 ? 0.7046 0.7581 0.5884 0.0523  -0.0071 -0.0309 699 GLU C O   
10043 C CB  . GLU C 398 ? 0.6057 0.6995 0.4814 0.0534  -0.0009 -0.0344 699 GLU C CB  
10044 C CG  . GLU C 398 ? 0.6844 0.7880 0.5509 0.0504  -0.0001 -0.0369 699 GLU C CG  
10045 C CD  . GLU C 398 ? 0.7403 0.8613 0.6007 0.0607  0.0043  -0.0431 699 GLU C CD  
10046 O OE1 . GLU C 398 ? 0.6471 0.7824 0.5021 0.0577  0.0060  -0.0431 699 GLU C OE1 
10047 O OE2 . GLU C 398 ? 0.7772 0.8995 0.6378 0.0724  0.0061  -0.0477 699 GLU C OE2 
10048 N N   . MET C 399 ? 0.6099 0.6964 0.5138 0.0411  -0.0031 -0.0165 700 MET C N   
10049 C CA  . MET C 399 ? 0.5300 0.6132 0.4428 0.0417  -0.0036 -0.0130 700 MET C CA  
10050 C C   . MET C 399 ? 0.7104 0.8189 0.6331 0.0418  0.0005  -0.0084 700 MET C C   
10051 O O   . MET C 399 ? 0.8744 0.9979 0.7994 0.0358  0.0034  -0.0033 700 MET C O   
10052 C CB  . MET C 399 ? 0.4797 0.5498 0.3972 0.0324  -0.0058 -0.0069 700 MET C CB  
10053 C CG  . MET C 399 ? 0.5774 0.6244 0.4863 0.0302  -0.0099 -0.0112 700 MET C CG  
10054 S SD  . MET C 399 ? 0.5503 0.5924 0.4649 0.0191  -0.0115 -0.0038 700 MET C SD  
10055 C CE  . MET C 399 ? 0.4030 0.4276 0.3051 0.0143  -0.0156 -0.0104 700 MET C CE  
10056 N N   . LEU C 400 ? 0.5535 0.6672 0.4810 0.0482  0.0005  -0.0100 701 LEU C N   
10057 C CA  . LEU C 400 ? 0.4795 0.6186 0.4173 0.0459  0.0036  -0.0055 701 LEU C CA  
10058 C C   . LEU C 400 ? 0.5721 0.7030 0.5173 0.0370  0.0022  0.0009  701 LEU C C   
10059 O O   . LEU C 400 ? 0.6436 0.7553 0.5877 0.0392  -0.0014 -0.0005 701 LEU C O   
10060 C CB  . LEU C 400 ? 0.4947 0.6498 0.4336 0.0593  0.0043  -0.0115 701 LEU C CB  
10061 C CG  . LEU C 400 ? 0.6934 0.8653 0.6263 0.0688  0.0074  -0.0176 701 LEU C CG  
10062 C CD1 . LEU C 400 ? 0.7241 0.9062 0.6565 0.0856  0.0071  -0.0239 701 LEU C CD1 
10063 C CD2 . LEU C 400 ? 0.7874 0.9888 0.7270 0.0592  0.0123  -0.0119 701 LEU C CD2 
10064 N N   . ASN C 401 ? 0.5768 0.7203 0.5275 0.0263  0.0050  0.0079  702 ASN C N   
10065 C CA  . ASN C 401 ? 0.6052 0.7390 0.5603 0.0170  0.0041  0.0137  702 ASN C CA  
10066 C C   . ASN C 401 ? 0.7059 0.8628 0.6683 0.0125  0.0061  0.0157  702 ASN C C   
10067 O O   . ASN C 401 ? 0.6209 0.7994 0.5843 0.0072  0.0101  0.0180  702 ASN C O   
10068 C CB  . ASN C 401 ? 0.6887 0.8105 0.6402 0.0072  0.0055  0.0205  702 ASN C CB  
10069 C CG  . ASN C 401 ? 0.6238 0.7269 0.5766 0.0013  0.0038  0.0243  702 ASN C CG  
10070 O OD1 . ASN C 401 ? 0.5502 0.6460 0.5056 0.0046  0.0010  0.0214  702 ASN C OD1 
10071 N ND2 . ASN C 401 ? 0.7595 0.8535 0.7086 -0.0066 0.0056  0.0310  702 ASN C ND2 
10072 N N   . TYR C 402 ? 0.6785 0.8322 0.6452 0.0136  0.0034  0.0148  703 TYR C N   
10073 C CA  . TYR C 402 ? 0.4828 0.6596 0.4568 0.0082  0.0042  0.0164  703 TYR C CA  
10074 C C   . TYR C 402 ? 0.5395 0.6997 0.5148 0.0046  0.0007  0.0178  703 TYR C C   
10075 O O   . TYR C 402 ? 0.5666 0.7014 0.5379 0.0093  -0.0022 0.0165  703 TYR C O   
10076 C CB  . TYR C 402 ? 0.4423 0.6484 0.4210 0.0208  0.0043  0.0110  703 TYR C CB  
10077 C CG  . TYR C 402 ? 0.5507 0.7429 0.5248 0.0389  0.0008  0.0044  703 TYR C CG  
10078 C CD1 . TYR C 402 ? 0.6079 0.7953 0.5832 0.0470  -0.0034 0.0025  703 TYR C CD1 
10079 C CD2 . TYR C 402 ? 0.6338 0.8159 0.6000 0.0473  0.0015  0.0001  703 TYR C CD2 
10080 C CE1 . TYR C 402 ? 0.6052 0.7748 0.5726 0.0631  -0.0065 -0.0030 703 TYR C CE1 
10081 C CE2 . TYR C 402 ? 0.6608 0.8252 0.6190 0.0622  -0.0016 -0.0062 703 TYR C CE2 
10082 C CZ  . TYR C 402 ? 0.6490 0.8057 0.6071 0.0702  -0.0055 -0.0075 703 TYR C CZ  
10083 O OH  . TYR C 402 ? 0.6308 0.7649 0.5773 0.0846  -0.0084 -0.0132 703 TYR C OH  
10084 N N   . ARG C 403 ? 0.6681 0.8442 0.6481 -0.0053 0.0012  0.0203  704 ARG C N   
10085 C CA  . ARG C 403 ? 0.5387 0.7008 0.5186 -0.0127 -0.0013 0.0223  704 ARG C CA  
10086 C C   . ARG C 403 ? 0.7065 0.8877 0.6926 -0.0057 -0.0049 0.0192  704 ARG C C   
10087 O O   . ARG C 403 ? 0.6862 0.9010 0.6789 -0.0083 -0.0039 0.0188  704 ARG C O   
10088 C CB  . ARG C 403 ? 0.5775 0.7393 0.5546 -0.0315 0.0017  0.0275  704 ARG C CB  
10089 C CG  . ARG C 403 ? 0.5988 0.7344 0.5667 -0.0382 0.0046  0.0320  704 ARG C CG  
10090 C CD  . ARG C 403 ? 0.8532 0.9565 0.8147 -0.0424 0.0033  0.0340  704 ARG C CD  
10091 N NE  . ARG C 403 ? 0.8851 0.9816 0.8413 -0.0575 0.0043  0.0367  704 ARG C NE  
10092 C CZ  . ARG C 403 ? 0.7087 0.8112 0.6594 -0.0722 0.0078  0.0403  704 ARG C CZ  
10093 N NH1 . ARG C 403 ? 0.5872 0.7078 0.5385 -0.0743 0.0108  0.0422  704 ARG C NH1 
10094 N NH2 . ARG C 403 ? 0.6724 0.7625 0.6154 -0.0862 0.0082  0.0419  704 ARG C NH2 
10095 N N   . LEU C 404 ? 0.7455 0.9067 0.7292 0.0025  -0.0090 0.0174  705 LEU C N   
10096 C CA  . LEU C 404 ? 0.6182 0.7918 0.6053 0.0110  -0.0132 0.0153  705 LEU C CA  
10097 C C   . LEU C 404 ? 0.5745 0.7337 0.5598 0.0013  -0.0157 0.0176  705 LEU C C   
10098 O O   . LEU C 404 ? 0.5359 0.6657 0.5153 -0.0043 -0.0151 0.0193  705 LEU C O   
10099 C CB  . LEU C 404 ? 0.5333 0.6918 0.5152 0.0298  -0.0163 0.0114  705 LEU C CB  
10100 C CG  . LEU C 404 ? 0.4572 0.6239 0.4374 0.0427  -0.0145 0.0074  705 LEU C CG  
10101 C CD1 . LEU C 404 ? 0.4726 0.6188 0.4438 0.0599  -0.0182 0.0036  705 LEU C CD1 
10102 C CD2 . LEU C 404 ? 0.3809 0.5905 0.3698 0.0454  -0.0124 0.0064  705 LEU C CD2 
10103 N N   . THR C 405 ? 0.5577 0.7401 0.5478 -0.0001 -0.0184 0.0175  706 THR C N   
10104 C CA  A THR C 405 ? 0.4910 0.6603 0.4780 -0.0078 -0.0212 0.0189  706 THR C CA  
10105 C CA  B THR C 405 ? 0.4934 0.6617 0.4802 -0.0077 -0.0212 0.0189  706 THR C CA  
10106 C C   . THR C 405 ? 0.5215 0.6862 0.5066 0.0076  -0.0266 0.0174  706 THR C C   
10107 O O   . THR C 405 ? 0.4911 0.6738 0.4789 0.0230  -0.0285 0.0153  706 THR C O   
10108 C CB  A THR C 405 ? 0.4685 0.6645 0.4598 -0.0236 -0.0210 0.0201  706 THR C CB  
10109 C CB  B THR C 405 ? 0.4651 0.6571 0.4556 -0.0241 -0.0211 0.0202  706 THR C CB  
10110 O OG1 A THR C 405 ? 0.4745 0.6476 0.4590 -0.0370 -0.0214 0.0215  706 THR C OG1 
10111 O OG1 B THR C 405 ? 0.4605 0.6955 0.4601 -0.0186 -0.0223 0.0188  706 THR C OG1 
10112 C CG2 A THR C 405 ? 0.4543 0.6867 0.4531 -0.0150 -0.0252 0.0185  706 THR C CG2 
10113 C CG2 B THR C 405 ? 0.4186 0.6007 0.4050 -0.0418 -0.0159 0.0226  706 THR C CG2 
10114 N N   . PRO C 406 ? 0.5374 0.6770 0.5161 0.0048  -0.0290 0.0185  707 PRO C N   
10115 C CA  . PRO C 406 ? 0.5786 0.6935 0.5519 -0.0096 -0.0271 0.0202  707 PRO C CA  
10116 C C   . PRO C 406 ? 0.6219 0.7126 0.5914 -0.0117 -0.0230 0.0209  707 PRO C C   
10117 O O   . PRO C 406 ? 0.6477 0.7306 0.6160 -0.0009 -0.0230 0.0196  707 PRO C O   
10118 C CB  . PRO C 406 ? 0.5209 0.6186 0.4880 -0.0044 -0.0313 0.0205  707 PRO C CB  
10119 C CG  . PRO C 406 ? 0.6013 0.7228 0.5715 0.0081  -0.0360 0.0198  707 PRO C CG  
10120 C CD  . PRO C 406 ? 0.4669 0.6036 0.4419 0.0186  -0.0343 0.0180  707 PRO C CD  
10121 N N   . SER C 407 ? 0.5482 0.6265 0.5143 -0.0249 -0.0198 0.0226  708 SER C N   
10122 C CA  . SER C 407 ? 0.5701 0.6297 0.5327 -0.0266 -0.0159 0.0240  708 SER C CA  
10123 C C   . SER C 407 ? 0.5272 0.5624 0.4823 -0.0344 -0.0143 0.0254  708 SER C C   
10124 O O   . SER C 407 ? 0.7182 0.7519 0.6701 -0.0423 -0.0151 0.0251  708 SER C O   
10125 C CB  . SER C 407 ? 0.7311 0.8045 0.6959 -0.0330 -0.0122 0.0254  708 SER C CB  
10126 O OG  . SER C 407 ? 0.8430 0.9247 0.8060 -0.0472 -0.0111 0.0266  708 SER C OG  
10127 N N   . PHE C 408 ? 0.5208 0.5385 0.4728 -0.0314 -0.0119 0.0264  709 PHE C N   
10128 C CA  . PHE C 408 ? 0.4229 0.4200 0.3674 -0.0371 -0.0089 0.0282  709 PHE C CA  
10129 C C   . PHE C 408 ? 0.5282 0.5246 0.4694 -0.0434 -0.0051 0.0309  709 PHE C C   
10130 O O   . PHE C 408 ? 0.6162 0.6250 0.5616 -0.0408 -0.0043 0.0317  709 PHE C O   
10131 C CB  . PHE C 408 ? 0.3607 0.3435 0.3038 -0.0298 -0.0085 0.0283  709 PHE C CB  
10132 C CG  . PHE C 408 ? 0.4379 0.4176 0.3813 -0.0257 -0.0118 0.0265  709 PHE C CG  
10133 C CD1 . PHE C 408 ? 0.5929 0.5767 0.5390 -0.0182 -0.0145 0.0251  709 PHE C CD1 
10134 C CD2 . PHE C 408 ? 0.5066 0.4773 0.4451 -0.0296 -0.0121 0.0260  709 PHE C CD2 
10135 C CE1 . PHE C 408 ? 0.4763 0.4533 0.4195 -0.0153 -0.0175 0.0242  709 PHE C CE1 
10136 C CE2 . PHE C 408 ? 0.3630 0.3305 0.3002 -0.0265 -0.0150 0.0251  709 PHE C CE2 
10137 C CZ  . PHE C 408 ? 0.4328 0.4027 0.3720 -0.0196 -0.0177 0.0246  709 PHE C CZ  
10138 N N   . GLU C 409 ? 0.4071 0.3870 0.3387 -0.0517 -0.0025 0.0323  710 GLU C N   
10139 C CA  . GLU C 409 ? 0.4444 0.4179 0.3686 -0.0591 0.0012  0.0356  710 GLU C CA  
10140 C C   . GLU C 409 ? 0.5049 0.4493 0.4166 -0.0579 0.0042  0.0375  710 GLU C C   
10141 O O   . GLU C 409 ? 0.7697 0.7023 0.6788 -0.0544 0.0037  0.0355  710 GLU C O   
10142 C CB  . GLU C 409 ? 0.4350 0.4178 0.3558 -0.0740 0.0014  0.0353  710 GLU C CB  
10143 C CG  . GLU C 409 ? 0.5184 0.5355 0.4520 -0.0744 -0.0018 0.0331  710 GLU C CG  
10144 C CD  . GLU C 409 ? 0.7619 0.7989 0.7031 -0.0692 -0.0007 0.0345  710 GLU C CD  
10145 O OE1 . GLU C 409 ? 0.7838 0.8095 0.7197 -0.0687 0.0025  0.0377  710 GLU C OE1 
10146 O OE2 . GLU C 409 ? 0.7921 0.8569 0.7437 -0.0647 -0.0031 0.0322  710 GLU C OE2 
10147 N N   . TYR C 410 ? 0.5320 0.4651 0.4351 -0.0598 0.0075  0.0415  711 TYR C N   
10148 C CA  . TYR C 410 ? 0.5736 0.4767 0.4614 -0.0582 0.0106  0.0435  711 TYR C CA  
10149 C C   . TYR C 410 ? 0.7015 0.5875 0.5750 -0.0724 0.0121  0.0426  711 TYR C C   
10150 O O   . TYR C 410 ? 0.7634 0.6644 0.6397 -0.0851 0.0108  0.0413  711 TYR C O   
10151 C CB  . TYR C 410 ? 0.7508 0.6444 0.6315 -0.0532 0.0134  0.0490  711 TYR C CB  
10152 C CG  . TYR C 410 ? 0.7456 0.6557 0.6385 -0.0404 0.0118  0.0495  711 TYR C CG  
10153 C CD1 . TYR C 410 ? 0.8123 0.7437 0.7140 -0.0408 0.0109  0.0504  711 TYR C CD1 
10154 C CD2 . TYR C 410 ? 0.7785 0.6844 0.6737 -0.0290 0.0114  0.0486  711 TYR C CD2 
10155 C CE1 . TYR C 410 ? 0.7988 0.7435 0.7095 -0.0305 0.0092  0.0500  711 TYR C CE1 
10156 C CE2 . TYR C 410 ? 0.7969 0.7191 0.7023 -0.0199 0.0097  0.0486  711 TYR C CE2 
10157 C CZ  . TYR C 410 ? 0.8080 0.7478 0.7204 -0.0211 0.0084  0.0492  711 TYR C CZ  
10158 O OH  . TYR C 410 ? 0.9128 0.8666 0.8329 -0.0134 0.0066  0.0486  711 TYR C OH  
10159 N N   . GLN C 411 ? 0.7452 0.6003 0.6024 -0.0702 0.0148  0.0430  712 GLN C N   
10160 C CA  . GLN C 411 ? 0.7478 0.5785 0.5863 -0.0836 0.0166  0.0416  712 GLN C CA  
10161 C C   . GLN C 411 ? 0.7075 0.5003 0.5250 -0.0761 0.0208  0.0441  712 GLN C C   
10162 O O   . GLN C 411 ? 0.8027 0.5941 0.6239 -0.0591 0.0214  0.0456  712 GLN C O   
10163 C CB  . GLN C 411 ? 0.6454 0.4813 0.4870 -0.0878 0.0141  0.0355  712 GLN C CB  
10164 C CG  . GLN C 411 ? 0.6215 0.4494 0.4643 -0.0736 0.0143  0.0330  712 GLN C CG  
10165 C CD  . GLN C 411 ? 0.7356 0.5736 0.5830 -0.0785 0.0112  0.0276  712 GLN C CD  
10166 O OE1 . GLN C 411 ? 0.6812 0.5126 0.5186 -0.0927 0.0107  0.0249  712 GLN C OE1 
10167 N NE2 . GLN C 411 ? 0.6338 0.4884 0.4951 -0.0679 0.0089  0.0264  712 GLN C NE2 
10168 N N   . PRO C 412 ? 0.6540 0.4159 0.4481 -0.0882 0.0235  0.0448  713 PRO C N   
10169 C CA  . PRO C 412 ? 0.7870 0.5076 0.5571 -0.0792 0.0276  0.0475  713 PRO C CA  
10170 C C   . PRO C 412 ? 0.9287 0.6403 0.6980 -0.0631 0.0283  0.0434  713 PRO C C   
10171 O O   . PRO C 412 ? 1.0664 0.7940 0.8468 -0.0651 0.0260  0.0378  713 PRO C O   
10172 C CB  . PRO C 412 ? 0.8471 0.5354 0.5909 -0.0994 0.0298  0.0470  713 PRO C CB  
10173 C CG  . PRO C 412 ? 0.7105 0.4310 0.4676 -0.1190 0.0272  0.0470  713 PRO C CG  
10174 C CD  . PRO C 412 ? 0.6775 0.4414 0.4648 -0.1113 0.0230  0.0435  713 PRO C CD  
10175 N N   . ASP C 413 ? 0.9588 0.6477 0.7156 -0.0462 0.0314  0.0466  714 ASP C N   
10176 C CA  . ASP C 413 ? 0.9849 0.6611 0.7357 -0.0312 0.0332  0.0427  714 ASP C CA  
10177 C C   . ASP C 413 ? 1.0777 0.7193 0.8042 -0.0427 0.0353  0.0373  714 ASP C C   
10178 O O   . ASP C 413 ? 1.1210 0.7283 0.8229 -0.0533 0.0375  0.0393  714 ASP C O   
10179 C CB  . ASP C 413 ? 1.1094 0.7686 0.8493 -0.0096 0.0363  0.0476  714 ASP C CB  
10180 C CG  . ASP C 413 ? 1.1454 0.8377 0.9066 0.0006  0.0341  0.0530  714 ASP C CG  
10181 O OD1 . ASP C 413 ? 1.1413 0.8709 0.9279 0.0012  0.0309  0.0505  714 ASP C OD1 
10182 O OD2 . ASP C 413 ? 1.1143 0.7934 0.8646 0.0078  0.0355  0.0597  714 ASP C OD2 
10183 N N   . PRO C 414 ? 1.0513 0.6990 0.7818 -0.0423 0.0347  0.0304  715 PRO C N   
10184 C CA  . PRO C 414 ? 0.9461 0.5649 0.6543 -0.0570 0.0359  0.0244  715 PRO C CA  
10185 C C   . PRO C 414 ? 1.0959 0.6603 0.7678 -0.0524 0.0409  0.0245  715 PRO C C   
10186 O O   . PRO C 414 ? 1.2760 0.8100 0.9245 -0.0711 0.0418  0.0226  715 PRO C O   
10187 C CB  . PRO C 414 ? 0.8365 0.4736 0.5561 -0.0515 0.0347  0.0178  715 PRO C CB  
10188 C CG  . PRO C 414 ? 0.9042 0.5690 0.6451 -0.0312 0.0345  0.0208  715 PRO C CG  
10189 C CD  . PRO C 414 ? 0.9759 0.6576 0.7302 -0.0306 0.0328  0.0279  715 PRO C CD  
10190 N N   . TRP C 415 ? 1.0994 0.6502 0.7644 -0.0282 0.0443  0.0267  716 TRP C N   
10191 C CA  . TRP C 415 ? 1.1284 0.6240 0.7560 -0.0199 0.0493  0.0264  716 TRP C CA  
10192 C C   . TRP C 415 ? 1.2196 0.6814 0.8243 -0.0318 0.0504  0.0328  716 TRP C C   
10193 O O   . TRP C 415 ? 1.2923 0.7003 0.8601 -0.0333 0.0541  0.0316  716 TRP C O   
10194 C CB  . TRP C 415 ? 1.1741 0.6695 0.8017 0.0114  0.0523  0.0284  716 TRP C CB  
10195 C CG  . TRP C 415 ? 1.2228 0.7470 0.8706 0.0234  0.0506  0.0370  716 TRP C CG  
10196 C CD1 . TRP C 415 ? 1.3128 0.8155 0.9460 0.0291  0.0517  0.0451  716 TRP C CD1 
10197 C CD2 . TRP C 415 ? 1.1338 0.7125 0.8180 0.0302  0.0473  0.0382  716 TRP C CD2 
10198 N NE1 . TRP C 415 ? 1.2895 0.8324 0.9489 0.0396  0.0491  0.0511  716 TRP C NE1 
10199 C CE2 . TRP C 415 ? 1.1673 0.7562 0.8577 0.0399  0.0464  0.0466  716 TRP C CE2 
10200 C CE3 . TRP C 415 ? 1.0740 0.6915 0.7837 0.0285  0.0449  0.0332  716 TRP C CE3 
10201 C CZ2 . TRP C 415 ? 1.0677 0.7042 0.7887 0.0468  0.0433  0.0492  716 TRP C CZ2 
10202 C CZ3 . TRP C 415 ? 1.0239 0.6858 0.7628 0.0351  0.0420  0.0363  716 TRP C CZ3 
10203 C CH2 . TRP C 415 ? 1.0442 0.7153 0.7886 0.0438  0.0412  0.0438  716 TRP C CH2 
10204 N N   . ASN C 416 ? 1.2403 0.7301 0.8638 -0.0405 0.0475  0.0394  717 ASN C N   
10205 C CA  . ASN C 416 ? 1.2833 0.7445 0.8852 -0.0575 0.0485  0.0451  717 ASN C CA  
10206 C C   . ASN C 416 ? 1.3363 0.7809 0.9227 -0.0878 0.0480  0.0397  717 ASN C C   
10207 O O   . ASN C 416 ? 1.2838 0.6896 0.8409 -0.1036 0.0501  0.0428  717 ASN C O   
10208 C CB  . ASN C 416 ? 1.1942 0.6945 0.8210 -0.0621 0.0456  0.0525  717 ASN C CB  
10209 C CG  . ASN C 416 ? 1.1507 0.6738 0.7951 -0.0356 0.0452  0.0577  717 ASN C CG  
10210 O OD1 . ASN C 416 ? 1.1988 0.6984 0.8287 -0.0132 0.0479  0.0591  717 ASN C OD1 
10211 N ND2 . ASN C 416 ? 1.0669 0.6370 0.7419 -0.0377 0.0417  0.0604  717 ASN C ND2 
10212 N N   . THR C 417 ? 1.3791 0.8523 0.9831 -0.0969 0.0451  0.0319  718 THR C N   
10213 C CA  . THR C 417 ? 1.3597 0.8370 0.9594 -0.1273 0.0430  0.0275  718 THR C CA  
10214 C C   . THR C 417 ? 1.4170 0.8808 1.0048 -0.1341 0.0428  0.0174  718 THR C C   
10215 O O   . THR C 417 ? 1.4913 0.9581 1.0733 -0.1603 0.0407  0.0133  718 THR C O   
10216 C CB  . THR C 417 ? 1.1612 0.6999 0.7989 -0.1368 0.0380  0.0291  718 THR C CB  
10217 O OG1 . THR C 417 ? 1.1409 0.7160 0.8075 -0.1178 0.0356  0.0268  718 THR C OG1 
10218 C CG2 . THR C 417 ? 1.0789 0.6294 0.7242 -0.1364 0.0383  0.0383  718 THR C CG2 
10219 N N   . HIS C 418 ? 1.4327 0.8838 1.0162 -0.1120 0.0450  0.0132  719 HIS C N   
10220 C CA  . HIS C 418 ? 1.4845 0.9316 1.0616 -0.1162 0.0446  0.0034  719 HIS C CA  
10221 C C   . HIS C 418 ? 1.5916 0.9745 1.1228 -0.1234 0.0489  -0.0020 719 HIS C C   
10222 O O   . HIS C 418 ? 1.5214 0.8616 1.0280 -0.1050 0.0537  -0.0001 719 HIS C O   
10223 C CB  . HIS C 418 ? 1.4143 0.8841 1.0104 -0.0896 0.0452  0.0012  719 HIS C CB  
10224 C CG  . HIS C 418 ? 1.3946 0.8503 0.9768 -0.0890 0.0465  -0.0085 719 HIS C CG  
10225 N ND1 . HIS C 418 ? 1.4025 0.8851 0.9964 -0.1059 0.0423  -0.0142 719 HIS C ND1 
10226 C CD2 . HIS C 418 ? 1.4386 0.8572 0.9956 -0.0725 0.0516  -0.0136 719 HIS C CD2 
10227 C CE1 . HIS C 418 ? 1.4280 0.8904 1.0043 -0.1012 0.0448  -0.0224 719 HIS C CE1 
10228 N NE2 . HIS C 418 ? 1.4436 0.8670 0.9973 -0.0809 0.0506  -0.0226 719 HIS C NE2 
10229 N N   . VAL C 419 ? 1.8183 1.1944 1.3367 -0.1494 0.0470  -0.0090 720 VAL C N   
10230 C CA  . VAL C 419 ? 1.9779 1.2917 1.4502 -0.1604 0.0507  -0.0157 720 VAL C CA  
10231 C C   . VAL C 419 ? 2.0315 1.3339 1.4959 -0.1415 0.0531  -0.0245 720 VAL C C   
10232 O O   . VAL C 419 ? 2.1119 1.4448 1.5910 -0.1491 0.0499  -0.0309 720 VAL C O   
10233 C CB  . VAL C 419 ? 2.0352 1.3496 1.4965 -0.1986 0.0474  -0.0200 720 VAL C CB  
10234 C CG1 . VAL C 419 ? 2.1102 1.3537 1.5192 -0.2117 0.0514  -0.0270 720 VAL C CG1 
10235 C CG2 . VAL C 419 ? 2.0262 1.3631 1.5004 -0.2169 0.0451  -0.0112 720 VAL C CG2 
10236 N N   . TRP C 420 ? 1.8925 1.1517 1.3328 -0.1161 0.0589  -0.0245 721 TRP C N   
10237 C CA  . TRP C 420 ? 1.7980 1.0538 1.2350 -0.0929 0.0620  -0.0318 721 TRP C CA  
10238 C C   . TRP C 420 ? 1.7942 1.0152 1.1991 -0.1089 0.0632  -0.0439 721 TRP C C   
10239 O O   . TRP C 420 ? 1.8713 1.0483 1.2426 -0.1326 0.0636  -0.0467 721 TRP C O   
10240 C CB  . TRP C 420 ? 1.7801 1.0017 1.1994 -0.0597 0.0680  -0.0285 721 TRP C CB  
10241 C CG  . TRP C 420 ? 1.7193 0.9897 1.1768 -0.0357 0.0670  -0.0202 721 TRP C CG  
10242 C CD1 . TRP C 420 ? 1.6582 0.9451 1.1320 -0.0336 0.0651  -0.0095 721 TRP C CD1 
10243 C CD2 . TRP C 420 ? 1.6254 0.9354 1.1083 -0.0120 0.0678  -0.0222 721 TRP C CD2 
10244 N NE1 . TRP C 420 ? 1.5411 0.8745 1.0486 -0.0103 0.0644  -0.0052 721 TRP C NE1 
10245 C CE2 . TRP C 420 ? 1.5176 0.8662 1.0312 0.0026  0.0661  -0.0126 721 TRP C CE2 
10246 C CE3 . TRP C 420 ? 1.5570 0.8743 1.0387 -0.0029 0.0699  -0.0313 721 TRP C CE3 
10247 C CZ2 . TRP C 420 ? 1.3990 0.7926 0.9417 0.0243  0.0663  -0.0118 721 TRP C CZ2 
10248 C CZ3 . TRP C 420 ? 1.4398 0.8028 0.9509 0.0193  0.0706  -0.0299 721 TRP C CZ3 
10249 C CH2 . TRP C 420 ? 1.3906 0.7910 0.9316 0.0319  0.0687  -0.0203 721 TRP C CH2 
10250 N N   . LYS C 421 ? 1.6378 0.8785 1.0517 -0.0965 0.0638  -0.0512 722 LYS C N   
10251 C CA  . LYS C 421 ? 1.6498 0.8619 1.0345 -0.1093 0.0649  -0.0635 722 LYS C CA  
10252 C C   . LYS C 421 ? 1.6931 0.8645 1.0490 -0.0808 0.0723  -0.0704 722 LYS C C   
10253 O O   . LYS C 421 ? 1.7203 0.8321 1.0313 -0.0862 0.0761  -0.0788 722 LYS C O   
10254 C CB  . LYS C 421 ? 1.5616 0.8301 0.9766 -0.1223 0.0593  -0.0675 722 LYS C CB  
10255 C CG  . LYS C 421 ? 1.4402 0.7629 0.8926 -0.1413 0.0520  -0.0598 722 LYS C CG  
10256 C CD  . LYS C 421 ? 1.4171 0.7552 0.8673 -0.1732 0.0464  -0.0660 722 LYS C CD  
10257 C CE  . LYS C 421 ? 1.3755 0.7843 0.8713 -0.1791 0.0392  -0.0608 722 LYS C CE  
10258 N NZ  . LYS C 421 ? 1.3607 0.7903 0.8691 -0.2020 0.0346  -0.0545 722 LYS C NZ  
10259 N N   . ARG D 3   ? 1.2805 1.2503 1.1192 -0.2482 -0.0174 -0.0522 304 ARG D N   
10260 C CA  . ARG D 3   ? 1.4239 1.3890 1.2606 -0.2364 -0.0191 -0.0539 304 ARG D CA  
10261 C C   . ARG D 3   ? 1.4425 1.3925 1.2868 -0.2123 -0.0174 -0.0488 304 ARG D C   
10262 O O   . ARG D 3   ? 1.5007 1.4496 1.3551 -0.2036 -0.0162 -0.0432 304 ARG D O   
10263 C CB  . ARG D 3   ? 1.4626 1.4717 1.3149 -0.2374 -0.0266 -0.0521 304 ARG D CB  
10264 C CG  . ARG D 3   ? 1.3328 1.3747 1.2122 -0.2206 -0.0315 -0.0427 304 ARG D CG  
10265 C CD  . ARG D 3   ? 1.2994 1.3556 1.1910 -0.2234 -0.0309 -0.0386 304 ARG D CD  
10266 N NE  . ARG D 3   ? 1.2700 1.3677 1.1858 -0.2142 -0.0369 -0.0318 304 ARG D NE  
10267 C CZ  . ARG D 3   ? 1.2970 1.4004 1.2266 -0.1939 -0.0394 -0.0254 304 ARG D CZ  
10268 N NH1 . ARG D 3   ? 1.3445 1.4188 1.2677 -0.1814 -0.0365 -0.0249 304 ARG D NH1 
10269 N NH2 . ARG D 3   ? 1.2469 1.3856 1.1961 -0.1861 -0.0449 -0.0197 304 ARG D NH2 
10270 N N   . PHE D 4   ? 1.3359 1.2758 1.1750 -0.2023 -0.0173 -0.0513 305 PHE D N   
10271 C CA  . PHE D 4   ? 1.1865 1.1091 1.0285 -0.1817 -0.0149 -0.0484 305 PHE D CA  
10272 C C   . PHE D 4   ? 1.0818 1.0308 0.9391 -0.1700 -0.0196 -0.0445 305 PHE D C   
10273 O O   . PHE D 4   ? 1.1036 1.0820 0.9684 -0.1768 -0.0250 -0.0435 305 PHE D O   
10274 C CB  . PHE D 4   ? 1.2493 1.1300 1.0669 -0.1804 -0.0089 -0.0559 305 PHE D CB  
10275 C CG  . PHE D 4   ? 1.4486 1.2974 1.2469 -0.1924 -0.0042 -0.0596 305 PHE D CG  
10276 C CD1 . PHE D 4   ? 1.5733 1.4217 1.3584 -0.2153 -0.0043 -0.0650 305 PHE D CD1 
10277 C CD2 . PHE D 4   ? 1.4595 1.2776 1.2510 -0.1816 0.0003  -0.0576 305 PHE D CD2 
10278 C CE1 . PHE D 4   ? 1.5811 1.3975 1.3458 -0.2282 0.0003  -0.0681 305 PHE D CE1 
10279 C CE2 . PHE D 4   ? 1.4770 1.2622 1.2478 -0.1928 0.0046  -0.0603 305 PHE D CE2 
10280 C CZ  . PHE D 4   ? 1.5213 1.3044 1.2782 -0.2166 0.0048  -0.0655 305 PHE D CZ  
10281 N N   . LEU D 5   ? 0.9281 0.8668 0.7893 -0.1525 -0.0178 -0.0421 306 LEU D N   
10282 C CA  . LEU D 5   ? 0.7640 0.7232 0.6370 -0.1418 -0.0215 -0.0382 306 LEU D CA  
10283 C C   . LEU D 5   ? 0.8023 0.7411 0.6702 -0.1274 -0.0172 -0.0397 306 LEU D C   
10284 O O   . LEU D 5   ? 0.9374 0.8596 0.8063 -0.1182 -0.0140 -0.0379 306 LEU D O   
10285 C CB  . LEU D 5   ? 0.6870 0.6727 0.5820 -0.1345 -0.0263 -0.0290 306 LEU D CB  
10286 C CG  . LEU D 5   ? 0.7765 0.7958 0.6815 -0.1402 -0.0332 -0.0258 306 LEU D CG  
10287 C CD1 . LEU D 5   ? 0.7364 0.7763 0.6610 -0.1315 -0.0369 -0.0174 306 LEU D CD1 
10288 C CD2 . LEU D 5   ? 0.9243 0.9504 0.8258 -0.1369 -0.0355 -0.0263 306 LEU D CD2 
10289 N N   . LYS D 6   ? 0.7361 0.6780 0.5985 -0.1253 -0.0173 -0.0430 307 LYS D N   
10290 C CA  . LYS D 6   ? 0.6416 0.5664 0.4978 -0.1127 -0.0125 -0.0460 307 LYS D CA  
10291 C C   . LYS D 6   ? 0.6966 0.6417 0.5675 -0.1014 -0.0151 -0.0398 307 LYS D C   
10292 O O   . LYS D 6   ? 0.7910 0.7602 0.6707 -0.1049 -0.0204 -0.0352 307 LYS D O   
10293 C CB  . LYS D 6   ? 0.6932 0.6028 0.5292 -0.1183 -0.0090 -0.0559 307 LYS D CB  
10294 C CG  . LYS D 6   ? 0.7756 0.6566 0.5926 -0.1287 -0.0054 -0.0629 307 LYS D CG  
10295 C CD  . LYS D 6   ? 0.9320 0.7874 0.7274 -0.1272 0.0002  -0.0731 307 LYS D CD  
10296 C CE  . LYS D 6   ? 1.0892 0.9100 0.8629 -0.1369 0.0041  -0.0797 307 LYS D CE  
10297 N NZ  . LYS D 6   ? 1.1856 0.9725 0.9386 -0.1275 0.0107  -0.0884 307 LYS D NZ  
10298 N N   . VAL D 7   ? 0.6182 0.5530 0.4910 -0.0879 -0.0114 -0.0394 308 VAL D N   
10299 C CA  . VAL D 7   ? 0.6474 0.5978 0.5308 -0.0780 -0.0124 -0.0350 308 VAL D CA  
10300 C C   . VAL D 7   ? 0.6539 0.5928 0.5266 -0.0708 -0.0069 -0.0420 308 VAL D C   
10301 O O   . VAL D 7   ? 0.7604 0.6762 0.6195 -0.0694 -0.0023 -0.0489 308 VAL D O   
10302 C CB  . VAL D 7   ? 0.6274 0.5824 0.5261 -0.0683 -0.0136 -0.0274 308 VAL D CB  
10303 C CG1 . VAL D 7   ? 0.5798 0.5468 0.4887 -0.0743 -0.0187 -0.0213 308 VAL D CG1 
10304 C CG2 . VAL D 7   ? 0.7061 0.6391 0.6001 -0.0600 -0.0089 -0.0300 308 VAL D CG2 
10305 N N   . LYS D 8   ? 0.6146 0.5697 0.4925 -0.0660 -0.0072 -0.0401 309 LYS D N   
10306 C CA  . LYS D 8   ? 0.7096 0.6614 0.5777 -0.0611 -0.0022 -0.0473 309 LYS D CA  
10307 C C   . LYS D 8   ? 0.7159 0.6826 0.5951 -0.0510 -0.0014 -0.0432 309 LYS D C   
10308 O O   . LYS D 8   ? 0.7399 0.7239 0.6304 -0.0530 -0.0058 -0.0353 309 LYS D O   
10309 C CB  . LYS D 8   ? 0.6522 0.6126 0.5101 -0.0719 -0.0033 -0.0513 309 LYS D CB  
10310 C CG  . LYS D 8   ? 0.7644 0.7192 0.6092 -0.0678 0.0028  -0.0607 309 LYS D CG  
10311 C CD  . LYS D 8   ? 0.7762 0.7466 0.6140 -0.0774 0.0013  -0.0626 309 LYS D CD  
10312 C CE  . LYS D 8   ? 0.8182 0.7853 0.6437 -0.0723 0.0080  -0.0721 309 LYS D CE  
10313 N NZ  . LYS D 8   ? 0.9042 0.8831 0.7194 -0.0832 0.0070  -0.0754 309 LYS D NZ  
10314 N N   . ASN D 9   ? 0.7317 0.6915 0.6070 -0.0401 0.0041  -0.0486 310 ASN D N   
10315 C CA  . ASN D 9   ? 0.7201 0.6975 0.6042 -0.0320 0.0057  -0.0466 310 ASN D CA  
10316 C C   . ASN D 9   ? 0.6537 0.6424 0.5293 -0.0356 0.0084  -0.0520 310 ASN D C   
10317 O O   . ASN D 9   ? 0.6146 0.5919 0.4770 -0.0329 0.0132  -0.0613 310 ASN D O   
10318 C CB  . ASN D 9   ? 0.7669 0.7357 0.6529 -0.0172 0.0099  -0.0492 310 ASN D CB  
10319 C CG  . ASN D 9   ? 0.7505 0.7410 0.6494 -0.0104 0.0102  -0.0451 310 ASN D CG  
10320 O OD1 . ASN D 9   ? 0.7540 0.7591 0.6515 -0.0078 0.0136  -0.0490 310 ASN D OD1 
10321 N ND2 . ASN D 9   ? 0.8638 0.8572 0.7747 -0.0085 0.0068  -0.0376 310 ASN D ND2 
10322 N N   . TRP D 10  ? 0.7940 0.8035 0.6753 -0.0418 0.0054  -0.0464 311 TRP D N   
10323 C CA  . TRP D 10  ? 0.7269 0.7486 0.5994 -0.0471 0.0077  -0.0507 311 TRP D CA  
10324 C C   . TRP D 10  ? 0.7710 0.8039 0.6442 -0.0377 0.0139  -0.0556 311 TRP D C   
10325 O O   . TRP D 10  ? 0.8782 0.9204 0.7426 -0.0405 0.0174  -0.0612 311 TRP D O   
10326 C CB  . TRP D 10  ? 0.5564 0.5940 0.4321 -0.0578 0.0019  -0.0421 311 TRP D CB  
10327 C CG  . TRP D 10  ? 0.6295 0.6607 0.5017 -0.0672 -0.0037 -0.0396 311 TRP D CG  
10328 C CD1 . TRP D 10  ? 0.6351 0.6625 0.5162 -0.0685 -0.0091 -0.0326 311 TRP D CD1 
10329 C CD2 . TRP D 10  ? 0.6297 0.6597 0.4886 -0.0768 -0.0044 -0.0445 311 TRP D CD2 
10330 N NE1 . TRP D 10  ? 0.6733 0.6996 0.5484 -0.0781 -0.0132 -0.0328 311 TRP D NE1 
10331 C CE2 . TRP D 10  ? 0.6373 0.6649 0.4986 -0.0838 -0.0107 -0.0399 311 TRP D CE2 
10332 C CE3 . TRP D 10  ? 0.6370 0.6691 0.4819 -0.0802 -0.0002 -0.0528 311 TRP D CE3 
10333 C CZ2 . TRP D 10  ? 0.7803 0.8086 0.6309 -0.0947 -0.0133 -0.0431 311 TRP D CZ2 
10334 C CZ3 . TRP D 10  ? 0.7041 0.7346 0.5372 -0.0913 -0.0028 -0.0560 311 TRP D CZ3 
10335 C CH2 . TRP D 10  ? 0.7358 0.7651 0.5720 -0.0987 -0.0095 -0.0510 311 TRP D CH2 
10336 N N   . GLU D 11  ? 0.7305 0.7649 0.6142 -0.0269 0.0153  -0.0537 312 GLU D N   
10337 C CA  . GLU D 11  ? 0.7962 0.8428 0.6817 -0.0159 0.0213  -0.0593 312 GLU D CA  
10338 C C   . GLU D 11  ? 0.8368 0.8644 0.7116 -0.0045 0.0267  -0.0697 312 GLU D C   
10339 O O   . GLU D 11  ? 0.8934 0.9281 0.7611 0.0010  0.0324  -0.0781 312 GLU D O   
10340 C CB  . GLU D 11  ? 0.7491 0.8067 0.6500 -0.0094 0.0199  -0.0528 312 GLU D CB  
10341 C CG  . GLU D 11  ? 0.7645 0.8446 0.6707 -0.0011 0.0249  -0.0564 312 GLU D CG  
10342 C CD  . GLU D 11  ? 0.8720 0.9579 0.7916 0.0080  0.0238  -0.0521 312 GLU D CD  
10343 O OE1 . GLU D 11  ? 0.8476 0.9267 0.7741 0.0037  0.0185  -0.0440 312 GLU D OE1 
10344 O OE2 . GLU D 11  ? 0.8289 0.9274 0.7520 0.0200  0.0282  -0.0572 312 GLU D OE2 
10345 N N   . THR D 12  ? 0.7490 0.7515 0.6212 -0.0011 0.0250  -0.0693 313 THR D N   
10346 C CA  . THR D 12  ? 0.6731 0.6522 0.5341 0.0110  0.0295  -0.0777 313 THR D CA  
10347 C C   . THR D 12  ? 0.7900 0.7424 0.6331 0.0034  0.0300  -0.0835 313 THR D C   
10348 O O   . THR D 12  ? 0.8830 0.8133 0.7123 0.0124  0.0346  -0.0920 313 THR D O   
10349 C CB  . THR D 12  ? 0.7669 0.7341 0.6355 0.0212  0.0279  -0.0730 313 THR D CB  
10350 O OG1 . THR D 12  ? 0.7284 0.6787 0.5965 0.0114  0.0230  -0.0673 313 THR D OG1 
10351 C CG2 . THR D 12  ? 0.8159 0.8098 0.7026 0.0257  0.0263  -0.0662 313 THR D CG2 
10352 N N   . GLU D 13  ? 0.7905 0.7440 0.6327 -0.0128 0.0253  -0.0794 314 GLU D N   
10353 C CA  . GLU D 13  ? 0.8906 0.8223 0.7172 -0.0236 0.0246  -0.0840 314 GLU D CA  
10354 C C   . GLU D 13  ? 0.9364 0.8389 0.7578 -0.0215 0.0239  -0.0836 314 GLU D C   
10355 O O   . GLU D 13  ? 0.9197 0.8011 0.7262 -0.0309 0.0240  -0.0882 314 GLU D O   
10356 C CB  . GLU D 13  ? 0.9491 0.8728 0.7570 -0.0232 0.0302  -0.0960 314 GLU D CB  
10357 C CG  . GLU D 13  ? 0.9292 0.8793 0.7404 -0.0189 0.0338  -0.0988 314 GLU D CG  
10358 C CD  . GLU D 13  ? 1.1305 1.0903 0.9314 -0.0325 0.0336  -0.1025 314 GLU D CD  
10359 O OE1 . GLU D 13  ? 1.1910 1.1523 0.9920 -0.0471 0.0277  -0.0973 314 GLU D OE1 
10360 O OE2 . GLU D 13  ? 1.2232 1.1907 1.0159 -0.0280 0.0393  -0.1108 314 GLU D OE2 
10361 N N   . VAL D 14  ? 0.9126 0.8135 0.7450 -0.0109 0.0232  -0.0780 315 VAL D N   
10362 C CA  . VAL D 14  ? 0.8320 0.7074 0.6605 -0.0106 0.0220  -0.0757 315 VAL D CA  
10363 C C   . VAL D 14  ? 0.8613 0.7396 0.6938 -0.0275 0.0165  -0.0699 315 VAL D C   
10364 O O   . VAL D 14  ? 0.8631 0.7665 0.7101 -0.0335 0.0120  -0.0628 315 VAL D O   
10365 C CB  . VAL D 14  ? 0.8809 0.7603 0.7226 0.0032  0.0215  -0.0696 315 VAL D CB  
10366 C CG1 . VAL D 14  ? 0.7525 0.6086 0.5914 0.0017  0.0197  -0.0655 315 VAL D CG1 
10367 C CG2 . VAL D 14  ? 0.9566 0.8336 0.7939 0.0213  0.0268  -0.0759 315 VAL D CG2 
10368 N N   . VAL D 15  ? 0.8152 0.6679 0.6342 -0.0353 0.0167  -0.0726 316 VAL D N   
10369 C CA  . VAL D 15  ? 0.7602 0.6178 0.5826 -0.0517 0.0118  -0.0681 316 VAL D CA  
10370 C C   . VAL D 15  ? 0.7225 0.5598 0.5432 -0.0524 0.0113  -0.0647 316 VAL D C   
10371 O O   . VAL D 15  ? 0.8247 0.6316 0.6295 -0.0476 0.0154  -0.0695 316 VAL D O   
10372 C CB  . VAL D 15  ? 0.7709 0.6233 0.5776 -0.0665 0.0119  -0.0752 316 VAL D CB  
10373 C CG1 . VAL D 15  ? 0.6802 0.5449 0.4930 -0.0830 0.0062  -0.0701 316 VAL D CG1 
10374 C CG2 . VAL D 15  ? 0.7203 0.5916 0.5267 -0.0650 0.0130  -0.0789 316 VAL D CG2 
10375 N N   . LEU D 16  ? 0.7531 0.6068 0.5891 -0.0583 0.0065  -0.0563 317 LEU D N   
10376 C CA  . LEU D 16  ? 0.7657 0.6069 0.6037 -0.0594 0.0058  -0.0516 317 LEU D CA  
10377 C C   . LEU D 16  ? 0.8371 0.6878 0.6776 -0.0768 0.0019  -0.0492 317 LEU D C   
10378 O O   . LEU D 16  ? 0.8211 0.6973 0.6709 -0.0835 -0.0021 -0.0471 317 LEU D O   
10379 C CB  . LEU D 16  ? 0.6236 0.4792 0.4802 -0.0477 0.0039  -0.0434 317 LEU D CB  
10380 C CG  . LEU D 16  ? 0.6634 0.5216 0.5233 -0.0310 0.0065  -0.0444 317 LEU D CG  
10381 C CD1 . LEU D 16  ? 0.5818 0.4569 0.4601 -0.0232 0.0039  -0.0363 317 LEU D CD1 
10382 C CD2 . LEU D 16  ? 0.7903 0.6170 0.6326 -0.0215 0.0115  -0.0503 317 LEU D CD2 
10383 N N   . THR D 17  ? 0.9031 0.7344 0.7351 -0.0838 0.0030  -0.0492 318 THR D N   
10384 C CA  . THR D 17  ? 0.9102 0.7488 0.7415 -0.1019 0.0003  -0.0486 318 THR D CA  
10385 C C   . THR D 17  ? 0.9107 0.7601 0.7565 -0.1021 -0.0021 -0.0406 318 THR D C   
10386 O O   . THR D 17  ? 0.9826 0.8108 0.8220 -0.0998 0.0006  -0.0393 318 THR D O   
10387 C CB  . THR D 17  ? 0.8766 0.6835 0.6829 -0.1137 0.0041  -0.0563 318 THR D CB  
10388 O OG1 . THR D 17  ? 0.7888 0.5879 0.5815 -0.1142 0.0061  -0.0645 318 THR D OG1 
10389 C CG2 . THR D 17  ? 0.8855 0.7027 0.6917 -0.1338 0.0014  -0.0556 318 THR D CG2 
10390 N N   . ASP D 18  ? 0.8229 0.7045 0.6868 -0.1051 -0.0071 -0.0353 319 ASP D N   
10391 C CA  . ASP D 18  ? 0.7884 0.6844 0.6682 -0.1029 -0.0094 -0.0279 319 ASP D CA  
10392 C C   . ASP D 18  ? 0.8026 0.7031 0.6798 -0.1195 -0.0102 -0.0283 319 ASP D C   
10393 O O   . ASP D 18  ? 0.9281 0.8518 0.8106 -0.1296 -0.0140 -0.0287 319 ASP D O   
10394 C CB  . ASP D 18  ? 0.8105 0.7371 0.7097 -0.0960 -0.0142 -0.0222 319 ASP D CB  
10395 C CG  . ASP D 18  ? 0.8380 0.7781 0.7531 -0.0913 -0.0163 -0.0151 319 ASP D CG  
10396 O OD1 . ASP D 18  ? 0.8574 0.8052 0.7750 -0.1009 -0.0173 -0.0140 319 ASP D OD1 
10397 O OD2 . ASP D 18  ? 0.8241 0.7680 0.7487 -0.0786 -0.0169 -0.0109 319 ASP D OD2 
10398 N N   . THR D 19  ? 0.7288 0.6085 0.5975 -0.1227 -0.0068 -0.0280 320 THR D N   
10399 C CA  . THR D 19  ? 0.7435 0.6314 0.6124 -0.1382 -0.0073 -0.0272 320 THR D CA  
10400 C C   . THR D 19  ? 0.7766 0.6836 0.6637 -0.1329 -0.0089 -0.0199 320 THR D C   
10401 O O   . THR D 19  ? 0.8044 0.7307 0.6977 -0.1444 -0.0103 -0.0187 320 THR D O   
10402 C CB  . THR D 19  ? 0.7349 0.5867 0.5800 -0.1485 -0.0022 -0.0316 320 THR D CB  
10403 O OG1 . THR D 19  ? 0.7356 0.5669 0.5785 -0.1373 0.0007  -0.0276 320 THR D OG1 
10404 C CG2 . THR D 19  ? 0.6847 0.5107 0.5097 -0.1494 0.0003  -0.0392 320 THR D CG2 
10405 N N   . LEU D 20  ? 0.6692 0.5729 0.5647 -0.1161 -0.0087 -0.0155 321 LEU D N   
10406 C CA  . LEU D 20  ? 0.7650 0.6830 0.6753 -0.1106 -0.0096 -0.0092 321 LEU D CA  
10407 C C   . LEU D 20  ? 0.7508 0.7061 0.6804 -0.1117 -0.0146 -0.0061 321 LEU D C   
10408 O O   . LEU D 20  ? 0.7296 0.6998 0.6696 -0.1122 -0.0151 -0.0025 321 LEU D O   
10409 C CB  . LEU D 20  ? 0.6525 0.5606 0.5672 -0.0927 -0.0089 -0.0058 321 LEU D CB  
10410 C CG  . LEU D 20  ? 0.7467 0.6647 0.6741 -0.0856 -0.0093 0.0001  321 LEU D CG  
10411 C CD1 . LEU D 20  ? 0.7324 0.6325 0.6488 -0.0929 -0.0056 0.0006  321 LEU D CD1 
10412 C CD2 . LEU D 20  ? 0.7014 0.6163 0.6351 -0.0687 -0.0098 0.0030  321 LEU D CD2 
10413 N N   . HIS D 21  ? 0.7085 0.6789 0.6422 -0.1112 -0.0182 -0.0073 322 HIS D N   
10414 C CA  . HIS D 21  ? 0.6371 0.6410 0.5877 -0.1097 -0.0235 -0.0037 322 HIS D CA  
10415 C C   . HIS D 21  ? 0.5448 0.5687 0.4988 -0.1235 -0.0246 -0.0045 322 HIS D C   
10416 O O   . HIS D 21  ? 0.5492 0.6014 0.5187 -0.1202 -0.0283 -0.0008 322 HIS D O   
10417 C CB  . HIS D 21  ? 0.7548 0.7685 0.7057 -0.1080 -0.0273 -0.0047 322 HIS D CB  
10418 C CG  . HIS D 21  ? 0.7617 0.7760 0.7010 -0.1230 -0.0275 -0.0105 322 HIS D CG  
10419 N ND1 . HIS D 21  ? 0.7744 0.7618 0.6954 -0.1281 -0.0235 -0.0166 322 HIS D ND1 
10420 C CD2 . HIS D 21  ? 0.7349 0.7737 0.6774 -0.1341 -0.0314 -0.0115 322 HIS D CD2 
10421 C CE1 . HIS D 21  ? 0.7837 0.7772 0.6962 -0.1429 -0.0246 -0.0214 322 HIS D CE1 
10422 N NE2 . HIS D 21  ? 0.8048 0.8309 0.7307 -0.1471 -0.0296 -0.0183 322 HIS D NE2 
10423 N N   . LEU D 22  ? 0.6114 0.6214 0.5508 -0.1387 -0.0212 -0.0093 323 LEU D N   
10424 C CA  . LEU D 22  ? 0.6514 0.6816 0.5932 -0.1543 -0.0216 -0.0106 323 LEU D CA  
10425 C C   . LEU D 22  ? 0.7781 0.8223 0.7328 -0.1501 -0.0207 -0.0060 323 LEU D C   
10426 O O   . LEU D 22  ? 0.8197 0.8943 0.7847 -0.1574 -0.0226 -0.0056 323 LEU D O   
10427 C CB  . LEU D 22  ? 0.6445 0.6492 0.5646 -0.1719 -0.0170 -0.0164 323 LEU D CB  
10428 C CG  . LEU D 22  ? 0.7026 0.6882 0.6058 -0.1777 -0.0166 -0.0224 323 LEU D CG  
10429 C CD1 . LEU D 22  ? 0.7299 0.6796 0.6085 -0.1918 -0.0109 -0.0276 323 LEU D CD1 
10430 C CD2 . LEU D 22  ? 0.6175 0.6344 0.5265 -0.1869 -0.0218 -0.0247 323 LEU D CD2 
10431 N N   . LYS D 23  ? 0.7861 0.8104 0.7403 -0.1382 -0.0179 -0.0029 324 LYS D N   
10432 C CA  . LYS D 23  ? 0.6507 0.6817 0.6127 -0.1356 -0.0158 0.0006  324 LYS D CA  
10433 C C   . LYS D 23  ? 0.7487 0.8021 0.7302 -0.1195 -0.0193 0.0054  324 LYS D C   
10434 O O   . LYS D 23  ? 0.8830 0.9430 0.8714 -0.1159 -0.0176 0.0081  324 LYS D O   
10435 C CB  . LYS D 23  ? 0.6881 0.6830 0.6358 -0.1332 -0.0107 0.0012  324 LYS D CB  
10436 C CG  . LYS D 23  ? 0.9158 0.8908 0.8442 -0.1517 -0.0063 -0.0024 324 LYS D CG  
10437 C CD  . LYS D 23  ? 1.0575 0.9965 0.9708 -0.1484 -0.0016 -0.0008 324 LYS D CD  
10438 C CE  . LYS D 23  ? 1.1145 1.0250 1.0182 -0.1355 -0.0014 -0.0018 324 LYS D CE  
10439 N NZ  . LYS D 23  ? 1.1500 1.0481 1.0404 -0.1436 -0.0015 -0.0077 324 LYS D NZ  
10440 N N   . SER D 24  ? 0.7311 0.7944 0.7198 -0.1101 -0.0239 0.0066  325 SER D N   
10441 C CA  . SER D 24  ? 0.7883 0.8706 0.7931 -0.0956 -0.0275 0.0111  325 SER D CA  
10442 C C   . SER D 24  ? 0.8060 0.9243 0.8232 -0.0996 -0.0308 0.0114  325 SER D C   
10443 O O   . SER D 24  ? 0.8581 0.9902 0.8729 -0.1115 -0.0325 0.0085  325 SER D O   
10444 C CB  . SER D 24  ? 0.8173 0.8951 0.8230 -0.0850 -0.0312 0.0128  325 SER D CB  
10445 O OG  . SER D 24  ? 0.8536 0.9443 0.8575 -0.0918 -0.0349 0.0108  325 SER D OG  
10446 N N   . THR D 25  ? 0.8443 0.9788 0.8744 -0.0895 -0.0316 0.0146  326 THR D N   
10447 C CA  . THR D 25  ? 1.0047 1.1764 1.0483 -0.0893 -0.0351 0.0150  326 THR D CA  
10448 C C   . THR D 25  ? 0.9385 1.1198 0.9940 -0.0706 -0.0383 0.0192  326 THR D C   
10449 O O   . THR D 25  ? 0.9782 1.1815 1.0446 -0.0657 -0.0382 0.0199  326 THR D O   
10450 C CB  . THR D 25  ? 1.0902 1.2777 1.1360 -0.1015 -0.0310 0.0127  326 THR D CB  
10451 O OG1 . THR D 25  ? 1.1747 1.3366 1.2045 -0.1164 -0.0259 0.0098  326 THR D OG1 
10452 C CG2 . THR D 25  ? 0.9850 1.2120 1.0400 -0.1093 -0.0347 0.0109  326 THR D CG2 
10453 N N   . LEU D 26  ? 0.8967 1.0612 0.9492 -0.0602 -0.0410 0.0218  327 LEU D N   
10454 C CA  . LEU D 26  ? 0.9650 1.1347 1.0255 -0.0435 -0.0446 0.0259  327 LEU D CA  
10455 C C   . LEU D 26  ? 1.0073 1.1759 1.0649 -0.0393 -0.0503 0.0282  327 LEU D C   
10456 O O   . LEU D 26  ? 1.0818 1.2358 1.1297 -0.0465 -0.0499 0.0268  327 LEU D O   
10457 C CB  . LEU D 26  ? 1.0224 1.1678 1.0803 -0.0348 -0.0413 0.0275  327 LEU D CB  
10458 C CG  . LEU D 26  ? 0.9996 1.1432 1.0587 -0.0380 -0.0356 0.0259  327 LEU D CG  
10459 C CD1 . LEU D 26  ? 0.9486 1.0682 1.0038 -0.0296 -0.0331 0.0275  327 LEU D CD1 
10460 C CD2 . LEU D 26  ? 1.0129 1.1861 1.0840 -0.0343 -0.0362 0.0256  327 LEU D CD2 
10461 N N   . GLU D 27  ? 0.8808 1.0643 0.9456 -0.0272 -0.0555 0.0317  328 GLU D N   
10462 C CA  . GLU D 27  ? 0.7812 0.9656 0.8424 -0.0231 -0.0615 0.0348  328 GLU D CA  
10463 C C   . GLU D 27  ? 0.8453 1.0000 0.8970 -0.0194 -0.0607 0.0369  328 GLU D C   
10464 O O   . GLU D 27  ? 0.9146 1.0523 0.9657 -0.0130 -0.0577 0.0378  328 GLU D O   
10465 C CB  . GLU D 27  ? 0.7466 0.9507 0.8162 -0.0089 -0.0672 0.0388  328 GLU D CB  
10466 C CG  . GLU D 27  ? 0.7862 1.0271 0.8654 -0.0118 -0.0703 0.0373  328 GLU D CG  
10467 C CD  . GLU D 27  ? 0.9586 1.2175 1.0450 0.0054  -0.0765 0.0416  328 GLU D CD  
10468 O OE1 . GLU D 27  ? 1.0005 1.2929 1.0978 0.0070  -0.0784 0.0403  328 GLU D OE1 
10469 O OE2 . GLU D 27  ? 1.0252 1.2646 1.1057 0.0173  -0.0794 0.0462  328 GLU D OE2 
10470 N N   . THR D 28  ? 0.7889 0.9392 0.8328 -0.0241 -0.0633 0.0373  329 THR D N   
10471 C CA  . THR D 28  ? 0.6818 0.8099 0.7170 -0.0205 -0.0635 0.0398  329 THR D CA  
10472 C C   . THR D 28  ? 0.5930 0.7233 0.6273 -0.0097 -0.0697 0.0458  329 THR D C   
10473 O O   . THR D 28  ? 0.6387 0.7504 0.6659 -0.0060 -0.0698 0.0485  329 THR D O   
10474 C CB  . THR D 28  ? 0.8361 0.9576 0.8616 -0.0314 -0.0627 0.0369  329 THR D CB  
10475 O OG1 . THR D 28  ? 0.8343 0.9767 0.8600 -0.0365 -0.0675 0.0369  329 THR D OG1 
10476 C CG2 . THR D 28  ? 0.9101 1.0201 0.9321 -0.0409 -0.0561 0.0312  329 THR D CG2 
10477 N N   . GLY D 29  ? 0.6269 0.7798 0.6674 -0.0048 -0.0749 0.0479  330 GLY D N   
10478 C CA  . GLY D 29  ? 0.6610 0.8162 0.6985 0.0057  -0.0816 0.0539  330 GLY D CA  
10479 C C   . GLY D 29  ? 0.7117 0.8779 0.7432 -0.0003 -0.0866 0.0553  330 GLY D C   
10480 O O   . GLY D 29  ? 0.7475 0.9287 0.7799 0.0074  -0.0934 0.0597  330 GLY D O   
10481 N N   . CYS D 30  ? 0.6299 0.7889 0.6546 -0.0132 -0.0835 0.0516  331 CYS D N   
10482 C CA  . CYS D 30  ? 0.5164 0.6853 0.5341 -0.0204 -0.0877 0.0519  331 CYS D CA  
10483 C C   . CYS D 30  ? 0.5278 0.7282 0.5533 -0.0244 -0.0914 0.0499  331 CYS D C   
10484 O O   . CYS D 30  ? 0.6484 0.8594 0.6818 -0.0301 -0.0877 0.0451  331 CYS D O   
10485 C CB  . CYS D 30  ? 0.4882 0.6425 0.4968 -0.0333 -0.0825 0.0468  331 CYS D CB  
10486 S SG  . CYS D 30  ? 0.5814 0.7051 0.5798 -0.0309 -0.0787 0.0487  331 CYS D SG  
10487 N N   . THR D 31  ? 0.6086 0.8250 0.6311 -0.0224 -0.0987 0.0537  332 THR D N   
10488 C CA  . THR D 31  ? 0.5811 0.8302 0.6096 -0.0288 -0.1026 0.0513  332 THR D CA  
10489 C C   . THR D 31  ? 0.5284 0.7769 0.5466 -0.0453 -0.1018 0.0468  332 THR D C   
10490 O O   . THR D 31  ? 0.5618 0.7856 0.5693 -0.0502 -0.0979 0.0454  332 THR D O   
10491 C CB  . THR D 31  ? 0.7149 0.9857 0.7467 -0.0157 -0.1119 0.0581  332 THR D CB  
10492 O OG1 . THR D 31  ? 0.8321 1.0986 0.8510 -0.0176 -0.1171 0.0620  332 THR D OG1 
10493 C CG2 . THR D 31  ? 0.6512 0.9098 0.6866 0.0032  -0.1127 0.0637  332 THR D CG2 
10494 N N   . GLU D 32  ? 0.4906 0.7681 0.5121 -0.0541 -0.1054 0.0439  333 GLU D N   
10495 C CA  . GLU D 32  ? 0.6291 0.9072 0.6398 -0.0707 -0.1047 0.0387  333 GLU D CA  
10496 C C   . GLU D 32  ? 0.6181 0.8888 0.6162 -0.0684 -0.1095 0.0433  333 GLU D C   
10497 O O   . GLU D 32  ? 0.5828 0.8416 0.5687 -0.0800 -0.1068 0.0390  333 GLU D O   
10498 C CB  . GLU D 32  ? 0.7668 1.0805 0.7837 -0.0813 -0.1082 0.0347  333 GLU D CB  
10499 C CG  . GLU D 32  ? 0.8966 1.2047 0.9060 -0.1020 -0.1024 0.0255  333 GLU D CG  
10500 C CD  . GLU D 32  ? 0.9636 1.3005 0.9827 -0.1126 -0.1021 0.0207  333 GLU D CD  
10501 O OE1 . GLU D 32  ? 0.9216 1.2950 0.9510 -0.1082 -0.1092 0.0237  333 GLU D OE1 
10502 O OE2 . GLU D 32  ? 0.9732 1.2964 0.9890 -0.1252 -0.0948 0.0142  333 GLU D OE2 
10503 N N   . TYR D 33  ? 0.5083 0.7846 0.5078 -0.0533 -0.1164 0.0519  334 TYR D N   
10504 C CA  . TYR D 33  ? 0.4028 0.6750 0.3896 -0.0505 -0.1222 0.0578  334 TYR D CA  
10505 C C   . TYR D 33  ? 0.5083 0.7537 0.4893 -0.0372 -0.1222 0.0653  334 TYR D C   
10506 O O   . TYR D 33  ? 0.4759 0.7170 0.4456 -0.0334 -0.1276 0.0718  334 TYR D O   
10507 C CB  . TYR D 33  ? 0.5648 0.8705 0.5547 -0.0454 -0.1325 0.0625  334 TYR D CB  
10508 C CG  . TYR D 33  ? 0.6546 0.9902 0.6463 -0.0610 -0.1344 0.0559  334 TYR D CG  
10509 C CD1 . TYR D 33  ? 0.7182 1.0589 0.6967 -0.0718 -0.1378 0.0549  334 TYR D CD1 
10510 C CD2 . TYR D 33  ? 0.7161 1.0751 0.7218 -0.0660 -0.1327 0.0505  334 TYR D CD2 
10511 C CE1 . TYR D 33  ? 0.7423 1.1097 0.7212 -0.0874 -0.1396 0.0484  334 TYR D CE1 
10512 C CE2 . TYR D 33  ? 0.7437 1.1298 0.7499 -0.0822 -0.1343 0.0442  334 TYR D CE2 
10513 C CZ  . TYR D 33  ? 0.7218 1.1117 0.7144 -0.0929 -0.1379 0.0430  334 TYR D CZ  
10514 O OH  . TYR D 33  ? 0.7378 1.1540 0.7298 -0.1104 -0.1395 0.0361  334 TYR D OH  
10515 N N   . ILE D 34  ? 0.5857 0.8139 0.5733 -0.0302 -0.1169 0.0650  335 ILE D N   
10516 C CA  . ILE D 34  ? 0.5738 0.7738 0.5546 -0.0207 -0.1156 0.0707  335 ILE D CA  
10517 C C   . ILE D 34  ? 0.5021 0.6813 0.4855 -0.0255 -0.1062 0.0649  335 ILE D C   
10518 O O   . ILE D 34  ? 0.5906 0.7772 0.5846 -0.0284 -0.1021 0.0594  335 ILE D O   
10519 C CB  . ILE D 34  ? 0.5922 0.7938 0.5782 -0.0025 -0.1209 0.0780  335 ILE D CB  
10520 C CG1 . ILE D 34  ? 0.8404 1.0540 0.8187 0.0052  -0.1308 0.0859  335 ILE D CG1 
10521 C CG2 . ILE D 34  ? 0.5799 0.7494 0.5605 0.0047  -0.1171 0.0813  335 ILE D CG2 
10522 C CD1 . ILE D 34  ? 0.9756 1.2278 0.9641 0.0068  -0.1372 0.0850  335 ILE D CD1 
10523 N N   . CYS D 35  ? 0.4741 0.6287 0.4473 -0.0270 -0.1027 0.0663  336 CYS D N   
10524 C CA  . CYS D 35  ? 0.4756 0.6110 0.4511 -0.0293 -0.0944 0.0618  336 CYS D CA  
10525 C C   . CYS D 35  ? 0.6432 0.7600 0.6177 -0.0183 -0.0943 0.0674  336 CYS D C   
10526 O O   . CYS D 35  ? 0.6160 0.7233 0.5803 -0.0142 -0.0984 0.0741  336 CYS D O   
10527 C CB  . CYS D 35  ? 0.5630 0.6868 0.5286 -0.0404 -0.0892 0.0572  336 CYS D CB  
10528 S SG  . CYS D 35  ? 0.5748 0.6758 0.5426 -0.0409 -0.0797 0.0524  336 CYS D SG  
10529 N N   . MET D 36  ? 0.7388 0.8490 0.7224 -0.0145 -0.0897 0.0646  337 MET D N   
10530 C CA  . MET D 36  ? 0.7255 0.8182 0.7086 -0.0048 -0.0892 0.0687  337 MET D CA  
10531 C C   . MET D 36  ? 0.6076 0.6833 0.5907 -0.0091 -0.0817 0.0646  337 MET D C   
10532 O O   . MET D 36  ? 0.6963 0.7610 0.6826 -0.0027 -0.0797 0.0654  337 MET D O   
10533 C CB  . MET D 36  ? 0.6562 0.7590 0.6501 0.0064  -0.0916 0.0699  337 MET D CB  
10534 C CG  . MET D 36  ? 0.7087 0.8340 0.7047 0.0113  -0.0991 0.0732  337 MET D CG  
10535 S SD  . MET D 36  ? 0.8215 0.9576 0.8264 0.0293  -0.1038 0.0770  337 MET D SD  
10536 C CE  . MET D 36  ? 0.8963 0.9977 0.8878 0.0394  -0.1047 0.0836  337 MET D CE  
10537 N N   . GLY D 37  ? 0.5633 0.6374 0.5422 -0.0192 -0.0777 0.0601  338 GLY D N   
10538 C CA  . GLY D 37  ? 0.5965 0.6582 0.5759 -0.0227 -0.0707 0.0555  338 GLY D CA  
10539 C C   . GLY D 37  ? 0.5609 0.6060 0.5348 -0.0199 -0.0695 0.0590  338 GLY D C   
10540 O O   . GLY D 37  ? 0.6724 0.7096 0.6482 -0.0213 -0.0642 0.0555  338 GLY D O   
10541 N N   . SER D 38  ? 0.5639 0.6030 0.5297 -0.0165 -0.0743 0.0658  339 SER D N   
10542 C CA  . SER D 38  ? 0.5594 0.5809 0.5179 -0.0153 -0.0733 0.0694  339 SER D CA  
10543 C C   . SER D 38  ? 0.5060 0.5182 0.4652 -0.0050 -0.0767 0.0740  339 SER D C   
10544 O O   . SER D 38  ? 0.6053 0.6004 0.5566 -0.0044 -0.0763 0.0772  339 SER D O   
10545 C CB  . SER D 38  ? 0.6393 0.6556 0.5833 -0.0215 -0.0753 0.0737  339 SER D CB  
10546 O OG  . SER D 38  ? 0.6593 0.6769 0.5963 -0.0172 -0.0824 0.0803  339 SER D OG  
10547 N N   . ILE D 39  ? 0.5401 0.5632 0.5076 0.0028  -0.0798 0.0742  340 ILE D N   
10548 C CA  . ILE D 39  ? 0.5844 0.5998 0.5537 0.0142  -0.0822 0.0771  340 ILE D CA  
10549 C C   . ILE D 39  ? 0.5733 0.5832 0.5505 0.0148  -0.0764 0.0723  340 ILE D C   
10550 O O   . ILE D 39  ? 0.5936 0.6150 0.5808 0.0112  -0.0725 0.0668  340 ILE D O   
10551 C CB  . ILE D 39  ? 0.5009 0.5350 0.4781 0.0227  -0.0869 0.0781  340 ILE D CB  
10552 C CG1 . ILE D 39  ? 0.5728 0.6170 0.5432 0.0204  -0.0926 0.0820  340 ILE D CG1 
10553 C CG2 . ILE D 39  ? 0.6192 0.6451 0.5965 0.0366  -0.0898 0.0814  340 ILE D CG2 
10554 C CD1 . ILE D 39  ? 0.5165 0.5416 0.4698 0.0213  -0.0964 0.0893  340 ILE D CD1 
10555 N N   . MET D 40  ? 0.5169 0.5080 0.4880 0.0187  -0.0760 0.0745  341 MET D N   
10556 C CA  . MET D 40  ? 0.6837 0.6690 0.6604 0.0182  -0.0707 0.0702  341 MET D CA  
10557 C C   . MET D 40  ? 0.7119 0.7088 0.7013 0.0255  -0.0697 0.0669  341 MET D C   
10558 O O   . MET D 40  ? 0.7168 0.7205 0.7145 0.0218  -0.0651 0.0619  341 MET D O   
10559 C CB  . MET D 40  ? 0.8206 0.7831 0.7863 0.0195  -0.0708 0.0730  341 MET D CB  
10560 C CG  . MET D 40  ? 1.0716 1.0297 1.0418 0.0166  -0.0655 0.0683  341 MET D CG  
10561 S SD  . MET D 40  ? 1.2311 1.1663 1.1867 0.0102  -0.0645 0.0704  341 MET D SD  
10562 C CE  . MET D 40  ? 1.0866 1.0291 1.0375 -0.0022 -0.0632 0.0709  341 MET D CE  
10563 N N   . HIS D 41  ? 0.7604 0.7596 0.7507 0.0363  -0.0737 0.0695  342 HIS D N   
10564 C CA  . HIS D 41  ? 0.8492 0.8648 0.8522 0.0432  -0.0729 0.0664  342 HIS D CA  
10565 C C   . HIS D 41  ? 0.9599 0.9959 0.9673 0.0474  -0.0779 0.0683  342 HIS D C   
10566 O O   . HIS D 41  ? 1.0294 1.0613 1.0305 0.0569  -0.0833 0.0733  342 HIS D O   
10567 C CB  . HIS D 41  ? 0.9048 0.9090 0.9069 0.0542  -0.0726 0.0665  342 HIS D CB  
10568 C CG  . HIS D 41  ? 0.9285 0.9106 0.9232 0.0506  -0.0691 0.0654  342 HIS D CG  
10569 N ND1 . HIS D 41  ? 0.9234 0.9072 0.9235 0.0431  -0.0637 0.0609  342 HIS D ND1 
10570 C CD2 . HIS D 41  ? 0.9226 0.8806 0.9043 0.0533  -0.0704 0.0683  342 HIS D CD2 
10571 C CE1 . HIS D 41  ? 0.8981 0.8629 0.8900 0.0412  -0.0621 0.0609  342 HIS D CE1 
10572 N NE2 . HIS D 41  ? 0.8951 0.8434 0.8754 0.0464  -0.0659 0.0651  342 HIS D NE2 
10573 N N   . PRO D 42  ? 0.9689 1.0268 0.9858 0.0408  -0.0766 0.0648  343 PRO D N   
10574 C CA  . PRO D 42  ? 1.0010 1.0823 1.0233 0.0449  -0.0816 0.0662  343 PRO D CA  
10575 C C   . PRO D 42  ? 1.1195 1.2214 1.1553 0.0504  -0.0800 0.0626  343 PRO D C   
10576 O O   . PRO D 42  ? 1.2382 1.3402 1.2798 0.0454  -0.0742 0.0580  343 PRO D O   
10577 C CB  . PRO D 42  ? 0.9401 1.0315 0.9618 0.0314  -0.0812 0.0642  343 PRO D CB  
10578 C CG  . PRO D 42  ? 0.9762 1.0512 0.9946 0.0218  -0.0748 0.0606  343 PRO D CG  
10579 C CD  . PRO D 42  ? 0.9271 0.9874 0.9467 0.0283  -0.0715 0.0601  343 PRO D CD  
10580 N N   . SER D 43  ? 1.1108 1.2310 1.1513 0.0609  -0.0851 0.0648  344 SER D N   
10581 C CA  . SER D 43  ? 1.1023 1.2457 1.1562 0.0669  -0.0835 0.0613  344 SER D CA  
10582 C C   . SER D 43  ? 1.0909 1.2673 1.1545 0.0585  -0.0846 0.0587  344 SER D C   
10583 O O   . SER D 43  ? 1.1252 1.3270 1.2006 0.0616  -0.0836 0.0557  344 SER D O   
10584 C CB  . SER D 43  ? 1.0197 1.1644 1.0735 0.0862  -0.0878 0.0645  344 SER D CB  
10585 O OG  . SER D 43  ? 0.8728 1.0358 0.9269 0.0927  -0.0952 0.0685  344 SER D OG  
10586 N N   . PRO D 49  ? 1.3118 1.4574 1.3940 0.1677  -0.0327 0.0140  350 PRO D N   
10587 C CA  . PRO D 49  ? 1.3735 1.5367 1.4615 0.1676  -0.0254 0.0079  350 PRO D CA  
10588 C C   . PRO D 49  ? 1.4312 1.6411 1.5368 0.1628  -0.0228 0.0059  350 PRO D C   
10589 O O   . PRO D 49  ? 1.3653 1.5882 1.4752 0.1496  -0.0170 0.0035  350 PRO D O   
10590 C CB  . PRO D 49  ? 1.3454 1.4973 1.4264 0.1893  -0.0253 0.0041  350 PRO D CB  
10591 C CG  . PRO D 49  ? 1.3372 1.4463 1.4013 0.1925  -0.0305 0.0082  350 PRO D CG  
10592 C CD  . PRO D 49  ? 1.3172 1.4294 1.3845 0.1827  -0.0362 0.0150  350 PRO D CD  
10593 N N   . GLU D 50  ? 1.5574 1.7926 1.6723 0.1729  -0.0273 0.0072  351 GLU D N   
10594 C CA  . GLU D 50  ? 1.5793 1.8602 1.7107 0.1652  -0.0259 0.0060  351 GLU D CA  
10595 C C   . GLU D 50  ? 1.5450 1.8264 1.6777 0.1440  -0.0279 0.0103  351 GLU D C   
10596 O O   . GLU D 50  ? 1.4284 1.7448 1.5729 0.1345  -0.0270 0.0095  351 GLU D O   
10597 C CB  . GLU D 50  ? 1.5949 1.9066 1.7364 0.1842  -0.0304 0.0056  351 GLU D CB  
10598 C CG  . GLU D 50  ? 1.5650 1.9104 1.7168 0.1980  -0.0252 -0.0013 351 GLU D CG  
10599 C CD  . GLU D 50  ? 1.4726 1.7897 1.6128 0.2153  -0.0225 -0.0051 351 GLU D CD  
10600 O OE1 . GLU D 50  ? 1.4626 1.7553 1.5936 0.2055  -0.0172 -0.0071 351 GLU D OE1 
10601 O OE2 . GLU D 50  ? 1.3740 1.6928 1.5133 0.2390  -0.0257 -0.0063 351 GLU D OE2 
10602 N N   . ASP D 51  ? 1.6565 1.9005 1.7769 0.1364  -0.0302 0.0143  352 ASP D N   
10603 C CA  . ASP D 51  ? 1.6202 1.8599 1.7396 0.1166  -0.0310 0.0175  352 ASP D CA  
10604 C C   . ASP D 51  ? 1.5223 1.7619 1.6411 0.1002  -0.0239 0.0151  352 ASP D C   
10605 O O   . ASP D 51  ? 1.5997 1.8107 1.7087 0.0908  -0.0227 0.0167  352 ASP D O   
10606 C CB  . ASP D 51  ? 1.6345 1.8365 1.7411 0.1151  -0.0356 0.0223  352 ASP D CB  
10607 C CG  . ASP D 51  ? 1.6164 1.8018 1.7162 0.1342  -0.0410 0.0244  352 ASP D CG  
10608 O OD1 . ASP D 51  ? 1.5692 1.7262 1.6583 0.1409  -0.0397 0.0234  352 ASP D OD1 
10609 O OD2 . ASP D 51  ? 1.6122 1.8121 1.7160 0.1424  -0.0467 0.0270  352 ASP D OD2 
10610 N N   . VAL D 52  ? 1.1497 1.4222 1.2784 0.0974  -0.0191 0.0112  353 VAL D N   
10611 C CA  . VAL D 52  ? 0.8747 1.1504 1.0022 0.0809  -0.0123 0.0093  353 VAL D CA  
10612 C C   . VAL D 52  ? 0.6601 0.9725 0.7980 0.0680  -0.0109 0.0083  353 VAL D C   
10613 O O   . VAL D 52  ? 0.5582 0.9068 0.7080 0.0756  -0.0110 0.0056  353 VAL D O   
10614 C CB  . VAL D 52  ? 0.8489 1.1260 0.9751 0.0877  -0.0062 0.0049  353 VAL D CB  
10615 C CG1 . VAL D 52  ? 0.7891 1.0254 0.9015 0.0913  -0.0062 0.0059  353 VAL D CG1 
10616 C CG2 . VAL D 52  ? 0.9104 1.2148 1.0462 0.1070  -0.0066 0.0011  353 VAL D CG2 
10617 N N   . ALA D 53  ? 0.5803 0.8835 0.7129 0.0485  -0.0094 0.0101  354 ALA D N   
10618 C CA  . ALA D 53  ? 0.7655 1.0984 0.9048 0.0329  -0.0081 0.0092  354 ALA D CA  
10619 C C   . ALA D 53  ? 0.7540 1.1225 0.9020 0.0305  -0.0019 0.0048  354 ALA D C   
10620 O O   . ALA D 53  ? 0.8408 1.2029 0.9854 0.0336  0.0033  0.0028  354 ALA D O   
10621 C CB  . ALA D 53  ? 0.8405 1.1497 0.9686 0.0128  -0.0064 0.0114  354 ALA D CB  
10622 N N   . THR D 54  ? 0.7219 1.1304 0.8813 0.0247  -0.0026 0.0030  355 THR D N   
10623 C CA  . THR D 54  ? 0.7857 1.2335 0.9539 0.0180  0.0036  -0.0013 355 THR D CA  
10624 C C   . THR D 54  ? 0.8822 1.3211 1.0406 -0.0075 0.0097  -0.0010 355 THR D C   
10625 O O   . THR D 54  ? 0.9314 1.3368 1.0775 -0.0191 0.0084  0.0024  355 THR D O   
10626 C CB  . THR D 54  ? 0.8026 1.2988 0.9865 0.0196  0.0003  -0.0033 355 THR D CB  
10627 O OG1 . THR D 54  ? 0.8572 1.3527 1.0382 0.0015  -0.0030 -0.0012 355 THR D OG1 
10628 C CG2 . THR D 54  ? 0.8286 1.3300 1.0199 0.0460  -0.0065 -0.0028 355 THR D CG2 
10629 N N   . LYS D 55  ? 0.9257 1.3948 1.0887 -0.0160 0.0166  -0.0045 356 LYS D N   
10630 C CA  . LYS D 55  ? 0.8440 1.3076 0.9967 -0.0418 0.0224  -0.0040 356 LYS D CA  
10631 C C   . LYS D 55  ? 0.8376 1.3010 0.9872 -0.0596 0.0190  -0.0023 356 LYS D C   
10632 O O   . LYS D 55  ? 0.8279 1.2572 0.9619 -0.0749 0.0200  0.0005  356 LYS D O   
10633 C CB  . LYS D 55  ? 0.7193 1.2246 0.8794 -0.0495 0.0299  -0.0083 356 LYS D CB  
10634 C CG  . LYS D 55  ? 0.6138 1.1101 0.7694 -0.0412 0.0359  -0.0098 356 LYS D CG  
10635 C CD  . LYS D 55  ? 0.5352 1.0753 0.6976 -0.0513 0.0439  -0.0142 356 LYS D CD  
10636 C CE  . LYS D 55  ? 0.6759 1.2048 0.8317 -0.0441 0.0502  -0.0158 356 LYS D CE  
10637 N NZ  . LYS D 55  ? 0.6619 1.2321 0.8225 -0.0546 0.0590  -0.0201 356 LYS D NZ  
10638 N N   . ASP D 56  ? 0.8795 1.3805 1.0432 -0.0568 0.0146  -0.0041 357 ASP D N   
10639 C CA  . ASP D 56  ? 0.9258 1.4330 1.0871 -0.0756 0.0117  -0.0036 357 ASP D CA  
10640 C C   . ASP D 56  ? 0.8325 1.2992 0.9844 -0.0718 0.0052  0.0003  357 ASP D C   
10641 O O   . ASP D 56  ? 0.9238 1.3760 1.0656 -0.0899 0.0045  0.0011  357 ASP D O   
10642 C CB  . ASP D 56  ? 0.9408 1.5045 1.1206 -0.0737 0.0086  -0.0069 357 ASP D CB  
10643 C CG  . ASP D 56  ? 0.9100 1.5194 1.0997 -0.0807 0.0155  -0.0114 357 ASP D CG  
10644 O OD1 . ASP D 56  ? 0.8023 1.3991 0.9812 -0.0962 0.0231  -0.0117 357 ASP D OD1 
10645 O OD2 . ASP D 56  ? 0.9430 1.6019 1.1508 -0.0704 0.0133  -0.0145 357 ASP D OD2 
10646 N N   . GLN D 57  ? 0.6708 1.1189 0.8247 -0.0490 0.0007  0.0023  358 GLN D N   
10647 C CA  . GLN D 57  ? 0.5701 0.9781 0.7135 -0.0466 -0.0044 0.0061  358 GLN D CA  
10648 C C   . GLN D 57  ? 0.6451 1.0088 0.7710 -0.0567 -0.0001 0.0081  358 GLN D C   
10649 O O   . GLN D 57  ? 0.5746 0.9096 0.6896 -0.0640 -0.0025 0.0102  358 GLN D O   
10650 C CB  . GLN D 57  ? 0.6474 1.0460 0.7957 -0.0212 -0.0100 0.0079  358 GLN D CB  
10651 C CG  . GLN D 57  ? 0.7852 1.2217 0.9485 -0.0084 -0.0159 0.0071  358 GLN D CG  
10652 C CD  . GLN D 57  ? 0.8867 1.3078 1.0512 0.0169  -0.0212 0.0094  358 GLN D CD  
10653 O OE1 . GLN D 57  ? 0.8760 1.2830 1.0386 0.0298  -0.0185 0.0089  358 GLN D OE1 
10654 N NE2 . GLN D 57  ? 0.9264 1.3486 1.0923 0.0231  -0.0287 0.0121  358 GLN D NE2 
10655 N N   . LEU D 58  ? 0.7184 1.0769 0.8407 -0.0569 0.0060  0.0074  359 LEU D N   
10656 C CA  . LEU D 58  ? 0.6185 0.9345 0.7243 -0.0621 0.0092  0.0100  359 LEU D CA  
10657 C C   . LEU D 58  ? 0.6784 0.9826 0.7708 -0.0863 0.0130  0.0105  359 LEU D C   
10658 O O   . LEU D 58  ? 0.6219 0.8886 0.7000 -0.0912 0.0122  0.0130  359 LEU D O   
10659 C CB  . LEU D 58  ? 0.4516 0.7658 0.5569 -0.0536 0.0142  0.0093  359 LEU D CB  
10660 C CG  . LEU D 58  ? 0.4267 0.6970 0.5177 -0.0501 0.0149  0.0124  359 LEU D CG  
10661 C CD1 . LEU D 58  ? 0.5251 0.7726 0.6155 -0.0378 0.0083  0.0146  359 LEU D CD1 
10662 C CD2 . LEU D 58  ? 0.5536 0.8229 0.6440 -0.0406 0.0190  0.0114  359 LEU D CD2 
10663 N N   . PHE D 59  ? 0.7721 1.1072 0.8677 -0.1017 0.0173  0.0079  360 PHE D N   
10664 C CA  . PHE D 59  ? 0.8652 1.1874 0.9454 -0.1265 0.0215  0.0082  360 PHE D CA  
10665 C C   . PHE D 59  ? 0.7931 1.0855 0.8621 -0.1335 0.0174  0.0097  360 PHE D C   
10666 O O   . PHE D 59  ? 0.8653 1.1162 0.9166 -0.1381 0.0189  0.0123  360 PHE D O   
10667 C CB  . PHE D 59  ? 1.0017 1.3685 1.0896 -0.1434 0.0250  0.0046  360 PHE D CB  
10668 C CG  . PHE D 59  ? 1.0639 1.4598 1.1598 -0.1408 0.0308  0.0027  360 PHE D CG  
10669 C CD1 . PHE D 59  ? 1.0131 1.3847 1.0969 -0.1418 0.0363  0.0047  360 PHE D CD1 
10670 C CD2 . PHE D 59  ? 1.1210 1.5707 1.2365 -0.1372 0.0308  -0.0014 360 PHE D CD2 
10671 C CE1 . PHE D 59  ? 0.9927 1.3924 1.0832 -0.1400 0.0421  0.0025  360 PHE D CE1 
10672 C CE2 . PHE D 59  ? 1.0754 1.5543 1.1986 -0.1343 0.0367  -0.0039 360 PHE D CE2 
10673 C CZ  . PHE D 59  ? 1.0043 1.4577 1.1147 -0.1362 0.0425  -0.0021 360 PHE D CZ  
10674 N N   . PRO D 60  ? 0.6906 1.0017 0.7685 -0.1329 0.0120  0.0080  361 PRO D N   
10675 C CA  . PRO D 60  ? 0.6413 0.9250 0.7066 -0.1424 0.0090  0.0086  361 PRO D CA  
10676 C C   . PRO D 60  ? 0.6797 0.9218 0.7368 -0.1281 0.0062  0.0117  361 PRO D C   
10677 O O   . PRO D 60  ? 0.7941 1.0032 0.8355 -0.1364 0.0063  0.0124  361 PRO D O   
10678 C CB  . PRO D 60  ? 0.5941 0.9133 0.6732 -0.1420 0.0034  0.0062  361 PRO D CB  
10679 C CG  . PRO D 60  ? 0.5581 0.9059 0.6560 -0.1208 0.0008  0.0064  361 PRO D CG  
10680 C CD  . PRO D 60  ? 0.6221 0.9748 0.7208 -0.1195 0.0073  0.0062  361 PRO D CD  
10681 N N   . LEU D 61  ? 0.5972 0.8401 0.6641 -0.1070 0.0039  0.0133  362 LEU D N   
10682 C CA  . LEU D 61  ? 0.6369 0.8426 0.6961 -0.0949 0.0017  0.0162  362 LEU D CA  
10683 C C   . LEU D 61  ? 0.6698 0.8427 0.7126 -0.1009 0.0067  0.0180  362 LEU D C   
10684 O O   . LEU D 61  ? 0.6502 0.7898 0.6792 -0.1036 0.0063  0.0194  362 LEU D O   
10685 C CB  . LEU D 61  ? 0.5994 0.8129 0.6708 -0.0730 -0.0015 0.0172  362 LEU D CB  
10686 C CG  . LEU D 61  ? 0.5699 0.8086 0.6552 -0.0626 -0.0075 0.0166  362 LEU D CG  
10687 C CD1 . LEU D 61  ? 0.6452 0.8825 0.7378 -0.0415 -0.0099 0.0178  362 LEU D CD1 
10688 C CD2 . LEU D 61  ? 0.5101 0.7346 0.5898 -0.0663 -0.0122 0.0173  362 LEU D CD2 
10689 N N   . ALA D 62  ? 0.7107 0.8930 0.7542 -0.1023 0.0115  0.0181  363 ALA D N   
10690 C CA  . ALA D 62  ? 0.5936 0.7453 0.6207 -0.1074 0.0159  0.0206  363 ALA D CA  
10691 C C   . ALA D 62  ? 0.6349 0.7677 0.6443 -0.1279 0.0187  0.0207  363 ALA D C   
10692 O O   . ALA D 62  ? 0.6573 0.7527 0.6498 -0.1292 0.0195  0.0232  363 ALA D O   
10693 C CB  . ALA D 62  ? 0.5120 0.6804 0.5429 -0.1060 0.0207  0.0205  363 ALA D CB  
10694 N N   . LYS D 63  ? 0.6139 0.7717 0.6262 -0.1438 0.0200  0.0179  364 LYS D N   
10695 C CA  . LYS D 63  ? 0.6687 0.8058 0.6622 -0.1646 0.0225  0.0175  364 LYS D CA  
10696 C C   . LYS D 63  ? 0.7714 0.8752 0.7547 -0.1608 0.0186  0.0178  364 LYS D C   
10697 O O   . LYS D 63  ? 0.8440 0.9106 0.8062 -0.1689 0.0209  0.0192  364 LYS D O   
10698 C CB  . LYS D 63  ? 0.5106 0.6832 0.5103 -0.1826 0.0234  0.0136  364 LYS D CB  
10699 C CG  . LYS D 63  ? 0.5615 0.7129 0.5386 -0.2082 0.0279  0.0131  364 LYS D CG  
10700 C CD  . LYS D 63  ? 0.7352 0.8905 0.7095 -0.2210 0.0249  0.0094  364 LYS D CD  
10701 C CE  . LYS D 63  ? 0.7924 0.9287 0.7434 -0.2487 0.0297  0.0081  364 LYS D CE  
10702 N NZ  . LYS D 63  ? 0.8608 0.9406 0.7850 -0.2501 0.0326  0.0116  364 LYS D NZ  
10703 N N   . GLU D 64  ? 0.7546 0.8704 0.7514 -0.1481 0.0130  0.0167  365 GLU D N   
10704 C CA  . GLU D 64  ? 0.8215 0.9086 0.8090 -0.1447 0.0098  0.0166  365 GLU D CA  
10705 C C   . GLU D 64  ? 0.7018 0.7523 0.6786 -0.1328 0.0104  0.0199  365 GLU D C   
10706 O O   . GLU D 64  ? 0.6011 0.6177 0.5604 -0.1366 0.0112  0.0202  365 GLU D O   
10707 C CB  . GLU D 64  ? 0.8992 1.0078 0.9030 -0.1335 0.0036  0.0153  365 GLU D CB  
10708 C CG  . GLU D 64  ? 1.0217 1.1290 1.0197 -0.1446 0.0011  0.0122  365 GLU D CG  
10709 C CD  . GLU D 64  ? 1.1590 1.2262 1.1412 -0.1416 0.0005  0.0123  365 GLU D CD  
10710 O OE1 . GLU D 64  ? 1.2569 1.2918 1.2236 -0.1428 0.0042  0.0139  365 GLU D OE1 
10711 O OE2 . GLU D 64  ? 1.0701 1.1388 1.0552 -0.1374 -0.0037 0.0109  365 GLU D OE2 
10712 N N   . PHE D 65  ? 0.6529 0.7100 0.6394 -0.1181 0.0101  0.0223  366 PHE D N   
10713 C CA  . PHE D 65  ? 0.6694 0.6965 0.6475 -0.1061 0.0100  0.0253  366 PHE D CA  
10714 C C   . PHE D 65  ? 0.6588 0.6576 0.6164 -0.1156 0.0147  0.0275  366 PHE D C   
10715 O O   . PHE D 65  ? 0.8243 0.7902 0.7670 -0.1130 0.0145  0.0289  366 PHE D O   
10716 C CB  . PHE D 65  ? 0.6241 0.6654 0.6159 -0.0902 0.0087  0.0268  366 PHE D CB  
10717 C CG  . PHE D 65  ? 0.6023 0.6170 0.5854 -0.0801 0.0090  0.0298  366 PHE D CG  
10718 C CD1 . PHE D 65  ? 0.6309 0.6258 0.6105 -0.0709 0.0058  0.0305  366 PHE D CD1 
10719 C CD2 . PHE D 65  ? 0.6358 0.6469 0.6137 -0.0803 0.0125  0.0320  366 PHE D CD2 
10720 C CE1 . PHE D 65  ? 0.6223 0.5961 0.5944 -0.0616 0.0058  0.0331  366 PHE D CE1 
10721 C CE2 . PHE D 65  ? 0.6587 0.6472 0.6282 -0.0711 0.0122  0.0349  366 PHE D CE2 
10722 C CZ  . PHE D 65  ? 0.6437 0.6144 0.6108 -0.0615 0.0087  0.0355  366 PHE D CZ  
10723 N N   . ILE D 66  ? 0.6065 0.6175 0.5622 -0.1262 0.0190  0.0281  367 ILE D N   
10724 C CA  . ILE D 66  ? 0.6266 0.6087 0.5605 -0.1358 0.0235  0.0310  367 ILE D CA  
10725 C C   . ILE D 66  ? 0.7194 0.6727 0.6337 -0.1485 0.0242  0.0300  367 ILE D C   
10726 O O   . ILE D 66  ? 0.6275 0.5429 0.5221 -0.1469 0.0251  0.0326  367 ILE D O   
10727 C CB  . ILE D 66  ? 0.5970 0.6003 0.5317 -0.1481 0.0285  0.0313  367 ILE D CB  
10728 C CG1 . ILE D 66  ? 0.4473 0.4778 0.4004 -0.1340 0.0280  0.0315  367 ILE D CG1 
10729 C CG2 . ILE D 66  ? 0.6543 0.6252 0.5642 -0.1579 0.0330  0.0353  367 ILE D CG2 
10730 C CD1 . ILE D 66  ? 0.5280 0.5360 0.4763 -0.1182 0.0267  0.0350  367 ILE D CD1 
10731 N N   . ASP D 67  ? 0.8029 0.7736 0.7222 -0.1602 0.0234  0.0259  368 ASP D N   
10732 C CA  . ASP D 67  ? 0.7975 0.7414 0.6978 -0.1733 0.0241  0.0239  368 ASP D CA  
10733 C C   . ASP D 67  ? 0.7896 0.7024 0.6825 -0.1588 0.0210  0.0242  368 ASP D C   
10734 O O   . ASP D 67  ? 0.8013 0.6748 0.6711 -0.1620 0.0229  0.0251  368 ASP D O   
10735 C CB  . ASP D 67  ? 0.7207 0.6942 0.6308 -0.1863 0.0228  0.0190  368 ASP D CB  
10736 C CG  . ASP D 67  ? 0.7468 0.7467 0.6583 -0.2057 0.0268  0.0180  368 ASP D CG  
10737 O OD1 . ASP D 67  ? 0.8144 0.8017 0.7135 -0.2131 0.0315  0.0210  368 ASP D OD1 
10738 O OD2 . ASP D 67  ? 0.8417 0.8766 0.7666 -0.2139 0.0252  0.0143  368 ASP D OD2 
10739 N N   . GLN D 68  ? 0.6674 0.5967 0.5785 -0.1426 0.0164  0.0233  369 GLN D N   
10740 C CA  . GLN D 68  ? 0.7260 0.6290 0.6304 -0.1300 0.0140  0.0231  369 GLN D CA  
10741 C C   . GLN D 68  ? 0.7800 0.6582 0.6755 -0.1172 0.0148  0.0275  369 GLN D C   
10742 O O   . GLN D 68  ? 0.7421 0.5893 0.6232 -0.1107 0.0146  0.0278  369 GLN D O   
10743 C CB  . GLN D 68  ? 0.8030 0.7288 0.7269 -0.1182 0.0091  0.0212  369 GLN D CB  
10744 C CG  . GLN D 68  ? 0.9175 0.8734 0.8629 -0.1068 0.0068  0.0231  369 GLN D CG  
10745 C CD  . GLN D 68  ? 0.9732 0.9341 0.9301 -0.0910 0.0022  0.0229  369 GLN D CD  
10746 O OE1 . GLN D 68  ? 0.9709 0.9089 0.9200 -0.0823 0.0016  0.0234  369 GLN D OE1 
10747 N NE2 . GLN D 68  ? 0.8763 0.8673 0.8510 -0.0871 -0.0009 0.0222  369 GLN D NE2 
10748 N N   . TYR D 69  ? 0.8021 0.6934 0.7048 -0.1136 0.0159  0.0308  370 TYR D N   
10749 C CA  . TYR D 69  ? 0.7874 0.6550 0.6791 -0.1035 0.0167  0.0352  370 TYR D CA  
10750 C C   . TYR D 69  ? 0.7411 0.5722 0.6053 -0.1143 0.0204  0.0371  370 TYR D C   
10751 O O   . TYR D 69  ? 0.7596 0.5589 0.6086 -0.1053 0.0198  0.0389  370 TYR D O   
10752 C CB  . TYR D 69  ? 0.7246 0.6124 0.6271 -0.0992 0.0176  0.0380  370 TYR D CB  
10753 C CG  . TYR D 69  ? 0.7803 0.6419 0.6679 -0.0914 0.0184  0.0427  370 TYR D CG  
10754 C CD1 . TYR D 69  ? 0.8393 0.6879 0.7271 -0.0746 0.0150  0.0439  370 TYR D CD1 
10755 C CD2 . TYR D 69  ? 0.7501 0.6004 0.6227 -0.1012 0.0224  0.0461  370 TYR D CD2 
10756 C CE1 . TYR D 69  ? 0.8251 0.6516 0.6994 -0.0665 0.0151  0.0483  370 TYR D CE1 
10757 C CE2 . TYR D 69  ? 0.7487 0.5743 0.6063 -0.0934 0.0226  0.0511  370 TYR D CE2 
10758 C CZ  . TYR D 69  ? 0.7783 0.5926 0.6372 -0.0755 0.0186  0.0522  370 TYR D CZ  
10759 O OH  . TYR D 69  ? 0.7800 0.5721 0.6243 -0.0667 0.0182  0.0572  370 TYR D OH  
10760 N N   . TYR D 70  ? 0.6473 0.4823 0.5039 -0.1335 0.0242  0.0368  371 TYR D N   
10761 C CA  . TYR D 70  ? 0.7872 0.5838 0.6147 -0.1447 0.0278  0.0392  371 TYR D CA  
10762 C C   . TYR D 70  ? 0.7866 0.5526 0.5977 -0.1470 0.0273  0.0360  371 TYR D C   
10763 O O   . TYR D 70  ? 0.9233 0.6479 0.7093 -0.1456 0.0286  0.0384  371 TYR D O   
10764 C CB  . TYR D 70  ? 0.8000 0.6087 0.6220 -0.1669 0.0325  0.0395  371 TYR D CB  
10765 C CG  . TYR D 70  ? 0.7080 0.5240 0.5313 -0.1634 0.0345  0.0444  371 TYR D CG  
10766 C CD1 . TYR D 70  ? 0.6809 0.5365 0.5297 -0.1548 0.0332  0.0437  371 TYR D CD1 
10767 C CD2 . TYR D 70  ? 0.5864 0.3675 0.3841 -0.1668 0.0373  0.0497  371 TYR D CD2 
10768 C CE1 . TYR D 70  ? 0.7239 0.5861 0.5734 -0.1511 0.0351  0.0475  371 TYR D CE1 
10769 C CE2 . TYR D 70  ? 0.7646 0.5530 0.5628 -0.1633 0.0389  0.0543  371 TYR D CE2 
10770 C CZ  . TYR D 70  ? 0.7978 0.6274 0.6222 -0.1558 0.0380  0.0528  371 TYR D CZ  
10771 O OH  . TYR D 70  ? 0.8972 0.7344 0.7215 -0.1527 0.0398  0.0566  371 TYR D OH  
10772 N N   . SER D 71  ? 0.8538 0.6383 0.6778 -0.1488 0.0250  0.0307  372 SER D N   
10773 C CA  . SER D 71  ? 0.9148 0.6709 0.7234 -0.1495 0.0245  0.0270  372 SER D CA  
10774 C C   . SER D 71  ? 0.8814 0.6149 0.6861 -0.1271 0.0221  0.0285  372 SER D C   
10775 O O   . SER D 71  ? 0.9653 0.6586 0.7461 -0.1247 0.0234  0.0286  372 SER D O   
10776 C CB  . SER D 71  ? 0.7689 0.5531 0.5932 -0.1557 0.0223  0.0211  372 SER D CB  
10777 O OG  . SER D 71  ? 1.0840 0.8506 0.9035 -0.1457 0.0202  0.0178  372 SER D OG  
10778 N N   . SER D 72  ? 0.7577 0.5165 0.5849 -0.1103 0.0187  0.0299  373 SER D N   
10779 C CA  . SER D 72  ? 0.7120 0.4570 0.5389 -0.0895 0.0162  0.0309  373 SER D CA  
10780 C C   . SER D 72  ? 0.8418 0.5497 0.6455 -0.0832 0.0178  0.0356  373 SER D C   
10781 O O   . SER D 72  ? 0.8534 0.5373 0.6463 -0.0700 0.0168  0.0351  373 SER D O   
10782 C CB  . SER D 72  ? 0.8273 0.6052 0.6797 -0.0761 0.0129  0.0325  373 SER D CB  
10783 O OG  . SER D 72  ? 1.0009 0.7833 0.8537 -0.0760 0.0140  0.0374  373 SER D OG  
10784 N N   . ILE D 73  ? 0.9296 0.6334 0.7253 -0.0917 0.0202  0.0401  374 ILE D N   
10785 C CA  . ILE D 73  ? 0.9230 0.5920 0.6956 -0.0858 0.0213  0.0457  374 ILE D CA  
10786 C C   . ILE D 73  ? 0.8933 0.5237 0.6350 -0.1026 0.0254  0.0461  374 ILE D C   
10787 O O   . ILE D 73  ? 0.9425 0.5456 0.6631 -0.1036 0.0271  0.0517  374 ILE D O   
10788 C CB  . ILE D 73  ? 0.8764 0.5621 0.6569 -0.0827 0.0212  0.0513  374 ILE D CB  
10789 C CG1 . ILE D 73  ? 0.8152 0.5143 0.5948 -0.1043 0.0252  0.0520  374 ILE D CG1 
10790 C CG2 . ILE D 73  ? 0.7922 0.5137 0.6013 -0.0675 0.0173  0.0503  374 ILE D CG2 
10791 C CD1 . ILE D 73  ? 0.8170 0.5381 0.6067 -0.1023 0.0257  0.0562  374 ILE D CD1 
10792 N N   . LYS D 74  ? 0.9267 0.5531 0.6637 -0.1164 0.0269  0.0404  375 LYS D N   
10793 C CA  . LYS D 74  ? 1.0992 0.6847 0.8042 -0.1331 0.0307  0.0398  375 LYS D CA  
10794 C C   . LYS D 74  ? 1.1991 0.7812 0.8921 -0.1516 0.0345  0.0446  375 LYS D C   
10795 O O   . LYS D 74  ? 1.2822 0.8221 0.9445 -0.1567 0.0370  0.0487  375 LYS D O   
10796 C CB  . LYS D 74  ? 1.2169 0.7534 0.8954 -0.1180 0.0303  0.0414  375 LYS D CB  
10797 C CG  . LYS D 74  ? 1.3032 0.8233 0.9753 -0.1133 0.0298  0.0344  375 LYS D CG  
10798 C CD  . LYS D 74  ? 1.3891 0.8603 1.0246 -0.1297 0.0337  0.0325  375 LYS D CD  
10799 C CE  . LYS D 74  ? 1.4059 0.8519 1.0298 -0.1200 0.0333  0.0258  375 LYS D CE  
10800 N NZ  . LYS D 74  ? 1.3836 0.8714 1.0394 -0.1086 0.0300  0.0207  375 LYS D NZ  
10801 N N   . ARG D 75  ? 1.1823 0.8088 0.8987 -0.1610 0.0350  0.0443  376 ARG D N   
10802 C CA  . ARG D 75  ? 1.1749 0.8066 0.8835 -0.1794 0.0390  0.0481  376 ARG D CA  
10803 C C   . ARG D 75  ? 1.2099 0.8808 0.9346 -0.2002 0.0409  0.0432  376 ARG D C   
10804 O O   . ARG D 75  ? 1.2270 0.9230 0.9588 -0.2114 0.0436  0.0452  376 ARG D O   
10805 C CB  . ARG D 75  ? 1.1362 0.7851 0.8565 -0.1667 0.0381  0.0539  376 ARG D CB  
10806 C CG  . ARG D 75  ? 1.1301 0.7413 0.8311 -0.1492 0.0365  0.0600  376 ARG D CG  
10807 C CD  . ARG D 75  ? 1.1172 0.6807 0.7802 -0.1629 0.0404  0.0645  376 ARG D CD  
10808 N NE  . ARG D 75  ? 1.2375 0.7692 0.8829 -0.1453 0.0385  0.0716  376 ARG D NE  
10809 C CZ  . ARG D 75  ? 1.3699 0.8681 1.0015 -0.1273 0.0357  0.0720  376 ARG D CZ  
10810 N NH1 . ARG D 75  ? 1.3164 0.7900 0.9329 -0.1110 0.0337  0.0790  376 ARG D NH1 
10811 N NH2 . ARG D 75  ? 1.4592 0.9498 1.0921 -0.1249 0.0348  0.0654  376 ARG D NH2 
10812 N N   . PHE D 76  ? 1.1237 0.8022 0.8545 -0.2050 0.0395  0.0367  377 PHE D N   
10813 C CA  . PHE D 76  ? 1.0107 0.7320 0.7601 -0.2219 0.0401  0.0319  377 PHE D CA  
10814 C C   . PHE D 76  ? 1.0622 0.7741 0.7907 -0.2509 0.0454  0.0320  377 PHE D C   
10815 O O   . PHE D 76  ? 1.2698 0.9365 0.9669 -0.2624 0.0479  0.0319  377 PHE D O   
10816 C CB  . PHE D 76  ? 1.1125 0.8419 0.8708 -0.2201 0.0368  0.0252  377 PHE D CB  
10817 C CG  . PHE D 76  ? 1.0649 0.8402 0.8427 -0.2357 0.0365  0.0204  377 PHE D CG  
10818 C CD1 . PHE D 76  ? 0.9244 0.7484 0.7348 -0.2250 0.0334  0.0203  377 PHE D CD1 
10819 C CD2 . PHE D 76  ? 1.0406 0.8107 0.8034 -0.2612 0.0391  0.0162  377 PHE D CD2 
10820 C CE1 . PHE D 76  ? 0.8092 0.6764 0.6373 -0.2374 0.0327  0.0164  377 PHE D CE1 
10821 C CE2 . PHE D 76  ? 1.0120 0.8281 0.7934 -0.2752 0.0383  0.0120  377 PHE D CE2 
10822 C CZ  . PHE D 76  ? 0.9285 0.7939 0.7431 -0.2623 0.0350  0.0122  377 PHE D CZ  
10823 N N   . GLY D 77  ? 0.9246 0.6790 0.6698 -0.2631 0.0474  0.0319  378 GLY D N   
10824 C CA  . GLY D 77  ? 0.8218 0.5735 0.5491 -0.2922 0.0529  0.0319  378 GLY D CA  
10825 C C   . GLY D 77  ? 1.0462 0.7628 0.7471 -0.2972 0.0571  0.0390  378 GLY D C   
10826 O O   . GLY D 77  ? 1.1666 0.8726 0.8472 -0.3208 0.0616  0.0391  378 GLY D O   
10827 N N   . SER D 78  ? 1.0767 0.7771 0.7778 -0.2741 0.0551  0.0444  379 SER D N   
10828 C CA  . SER D 78  ? 1.1716 0.8381 0.8472 -0.2760 0.0583  0.0520  379 SER D CA  
10829 C C   . SER D 78  ? 1.2169 0.9216 0.9048 -0.2857 0.0619  0.0544  379 SER D C   
10830 O O   . SER D 78  ? 1.1456 0.9036 0.8638 -0.2867 0.0616  0.0503  379 SER D O   
10831 C CB  . SER D 78  ? 1.1535 0.7940 0.8265 -0.2470 0.0542  0.0566  379 SER D CB  
10832 O OG  . SER D 78  ? 1.0727 0.7543 0.7762 -0.2297 0.0517  0.0575  379 SER D OG  
10833 N N   . LYS D 79  ? 1.2516 0.9278 0.9143 -0.2922 0.0656  0.0614  380 LYS D N   
10834 C CA  . LYS D 79  ? 1.2354 0.9449 0.9077 -0.2990 0.0693  0.0642  380 LYS D CA  
10835 C C   . LYS D 79  ? 1.0845 0.8326 0.7903 -0.2736 0.0655  0.0636  380 LYS D C   
10836 O O   . LYS D 79  ? 1.0859 0.8843 0.8169 -0.2766 0.0670  0.0604  380 LYS D O   
10837 C CB  . LYS D 79  ? 1.4079 1.0805 1.0501 -0.3012 0.0713  0.0705  380 LYS D CB  
10838 C CG  . LYS D 79  ? 1.5141 1.1593 1.1289 -0.3189 0.0728  0.0677  380 LYS D CG  
10839 C CD  . LYS D 79  ? 1.5553 1.1610 1.1408 -0.3156 0.0734  0.0746  380 LYS D CD  
10840 C CE  . LYS D 79  ? 1.5381 1.1099 1.0924 -0.3322 0.0748  0.0724  380 LYS D CE  
10841 N NZ  . LYS D 79  ? 1.5104 1.1115 1.0642 -0.3568 0.0795  0.0700  380 LYS D NZ  
10842 N N   . ALA D 80  ? 0.8957 0.6211 0.6017 -0.2482 0.0604  0.0663  381 ALA D N   
10843 C CA  . ALA D 80  ? 0.8907 0.6485 0.6256 -0.2250 0.0567  0.0657  381 ALA D CA  
10844 C C   . ALA D 80  ? 0.9552 0.7576 0.7232 -0.2205 0.0540  0.0583  381 ALA D C   
10845 O O   . ALA D 80  ? 0.8876 0.7300 0.6812 -0.2113 0.0533  0.0565  381 ALA D O   
10846 C CB  . ALA D 80  ? 0.8804 0.6055 0.6079 -0.2006 0.0516  0.0696  381 ALA D CB  
10847 N N   . HIS D 81  ? 0.9361 0.7303 0.7026 -0.2262 0.0524  0.0539  382 HIS D N   
10848 C CA  . HIS D 81  ? 0.9277 0.7634 0.7234 -0.2233 0.0497  0.0473  382 HIS D CA  
10849 C C   . HIS D 81  ? 0.8595 0.7394 0.6683 -0.2416 0.0537  0.0443  382 HIS D C   
10850 O O   . HIS D 81  ? 0.7838 0.7073 0.6202 -0.2326 0.0524  0.0417  382 HIS D O   
10851 C CB  . HIS D 81  ? 0.9324 0.7472 0.7202 -0.2268 0.0473  0.0434  382 HIS D CB  
10852 C CG  . HIS D 81  ? 0.8492 0.7039 0.6633 -0.2261 0.0442  0.0371  382 HIS D CG  
10853 N ND1 . HIS D 81  ? 0.8947 0.7405 0.7035 -0.2345 0.0427  0.0325  382 HIS D ND1 
10854 C CD2 . HIS D 81  ? 0.8226 0.7248 0.6670 -0.2174 0.0422  0.0347  382 HIS D CD2 
10855 C CE1 . HIS D 81  ? 0.8339 0.7215 0.6690 -0.2312 0.0396  0.0280  382 HIS D CE1 
10856 N NE2 . HIS D 81  ? 0.8507 0.7721 0.7075 -0.2204 0.0392  0.0294  382 HIS D NE2 
10857 N N   . MET D 82  ? 0.9357 0.8046 0.7239 -0.2675 0.0587  0.0445  383 MET D N   
10858 C CA  . MET D 82  ? 0.9114 0.8252 0.7115 -0.2871 0.0628  0.0411  383 MET D CA  
10859 C C   . MET D 82  ? 0.9789 0.9257 0.7945 -0.2798 0.0653  0.0429  383 MET D C   
10860 O O   . MET D 82  ? 0.9889 0.9868 0.8299 -0.2803 0.0659  0.0386  383 MET D O   
10861 C CB  . MET D 82  ? 0.9334 0.8240 0.7040 -0.3177 0.0684  0.0419  383 MET D CB  
10862 C CG  . MET D 82  ? 1.1451 1.0548 0.9199 -0.3370 0.0681  0.0352  383 MET D CG  
10863 S SD  . MET D 82  ? 1.2788 1.2054 1.0796 -0.3161 0.0601  0.0296  383 MET D SD  
10864 C CE  . MET D 82  ? 1.2229 1.2197 1.0522 -0.3307 0.0604  0.0228  383 MET D CE  
10865 N N   . GLU D 83  ? 0.9931 0.9115 0.7937 -0.2712 0.0664  0.0490  384 GLU D N   
10866 C CA  . GLU D 83  ? 0.9415 0.8880 0.7538 -0.2647 0.0691  0.0505  384 GLU D CA  
10867 C C   . GLU D 83  ? 0.8435 0.8171 0.6854 -0.2381 0.0641  0.0479  384 GLU D C   
10868 O O   . GLU D 83  ? 0.8307 0.8458 0.6926 -0.2341 0.0659  0.0453  384 GLU D O   
10869 C CB  . GLU D 83  ? 1.0470 0.9540 0.8319 -0.2650 0.0716  0.0582  384 GLU D CB  
10870 C CG  . GLU D 83  ? 1.1400 1.0306 0.8968 -0.2940 0.0784  0.0612  384 GLU D CG  
10871 C CD  . GLU D 83  ? 1.0614 0.9075 0.7875 -0.2937 0.0802  0.0697  384 GLU D CD  
10872 O OE1 . GLU D 83  ? 0.9608 0.7901 0.6883 -0.2702 0.0758  0.0732  384 GLU D OE1 
10873 O OE2 . GLU D 83  ? 1.0042 0.8329 0.7043 -0.3178 0.0858  0.0731  384 GLU D OE2 
10874 N N   . ARG D 84  ? 0.7677 0.7181 0.6116 -0.2199 0.0580  0.0484  385 ARG D N   
10875 C CA  . ARG D 84  ? 0.7253 0.6976 0.5946 -0.1959 0.0533  0.0462  385 ARG D CA  
10876 C C   . ARG D 84  ? 0.8465 0.8659 0.7428 -0.1962 0.0522  0.0399  385 ARG D C   
10877 O O   . ARG D 84  ? 0.8061 0.8578 0.7229 -0.1839 0.0517  0.0377  385 ARG D O   
10878 C CB  . ARG D 84  ? 0.5788 0.5183 0.4438 -0.1791 0.0474  0.0477  385 ARG D CB  
10879 C CG  . ARG D 84  ? 0.6447 0.6050 0.5346 -0.1572 0.0422  0.0451  385 ARG D CG  
10880 C CD  . ARG D 84  ? 0.7126 0.6847 0.6097 -0.1446 0.0427  0.0467  385 ARG D CD  
10881 N NE  . ARG D 84  ? 0.7261 0.7145 0.6444 -0.1250 0.0378  0.0441  385 ARG D NE  
10882 C CZ  . ARG D 84  ? 0.7252 0.7357 0.6569 -0.1143 0.0380  0.0429  385 ARG D CZ  
10883 N NH1 . ARG D 84  ? 0.8840 0.9051 0.8112 -0.1207 0.0430  0.0438  385 ARG D NH1 
10884 N NH2 . ARG D 84  ? 0.6681 0.6889 0.6162 -0.0977 0.0334  0.0406  385 ARG D NH2 
10885 N N   . LEU D 85  ? 0.9248 0.9481 0.8201 -0.2100 0.0517  0.0368  386 LEU D N   
10886 C CA  . LEU D 85  ? 0.8598 0.9297 0.7791 -0.2123 0.0505  0.0311  386 LEU D CA  
10887 C C   . LEU D 85  ? 0.8752 0.9868 0.8053 -0.2202 0.0558  0.0293  386 LEU D C   
10888 O O   . LEU D 85  ? 0.8066 0.9561 0.7606 -0.2069 0.0543  0.0262  386 LEU D O   
10889 C CB  . LEU D 85  ? 0.8081 0.8737 0.7195 -0.2307 0.0501  0.0284  386 LEU D CB  
10890 C CG  . LEU D 85  ? 0.7453 0.7907 0.6569 -0.2220 0.0442  0.0270  386 LEU D CG  
10891 C CD1 . LEU D 85  ? 0.8206 0.8470 0.7129 -0.2446 0.0457  0.0253  386 LEU D CD1 
10892 C CD2 . LEU D 85  ? 0.6271 0.7129 0.5671 -0.2088 0.0394  0.0231  386 LEU D CD2 
10893 N N   . GLU D 86  ? 0.8914 0.9962 0.8029 -0.2420 0.0620  0.0312  387 GLU D N   
10894 C CA  . GLU D 86  ? 0.9000 1.0427 0.8188 -0.2510 0.0681  0.0298  387 GLU D CA  
10895 C C   . GLU D 86  ? 0.8351 0.9916 0.7679 -0.2287 0.0678  0.0301  387 GLU D C   
10896 O O   . GLU D 86  ? 0.8478 1.0499 0.8014 -0.2239 0.0696  0.0259  387 GLU D O   
10897 C CB  . GLU D 86  ? 1.0322 1.1502 0.9222 -0.2751 0.0747  0.0338  387 GLU D CB  
10898 C CG  . GLU D 86  ? 1.1586 1.3044 1.0505 -0.2813 0.0815  0.0341  387 GLU D CG  
10899 C CD  . GLU D 86  ? 1.3501 1.5435 1.2511 -0.3032 0.0866  0.0293  387 GLU D CD  
10900 O OE1 . GLU D 86  ? 1.4639 1.6634 1.3657 -0.3166 0.0849  0.0264  387 GLU D OE1 
10901 O OE2 . GLU D 86  ? 1.3980 1.6242 1.3053 -0.3073 0.0924  0.0281  387 GLU D OE2 
10902 N N   . GLU D 87  ? 0.7086 0.8268 0.6301 -0.2145 0.0653  0.0346  388 GLU D N   
10903 C CA  . GLU D 87  ? 0.7319 0.8588 0.6636 -0.1946 0.0649  0.0349  388 GLU D CA  
10904 C C   . GLU D 87  ? 0.7525 0.9079 0.7116 -0.1742 0.0598  0.0301  388 GLU D C   
10905 O O   . GLU D 87  ? 0.8239 1.0098 0.7982 -0.1640 0.0615  0.0270  388 GLU D O   
10906 C CB  . GLU D 87  ? 0.7094 0.7888 0.6221 -0.1850 0.0626  0.0408  388 GLU D CB  
10907 C CG  . GLU D 87  ? 0.5904 0.6711 0.5024 -0.1734 0.0643  0.0426  388 GLU D CG  
10908 C CD  . GLU D 87  ? 0.7376 0.7750 0.6338 -0.1613 0.0603  0.0481  388 GLU D CD  
10909 O OE1 . GLU D 87  ? 0.7334 0.7429 0.6231 -0.1582 0.0558  0.0498  388 GLU D OE1 
10910 O OE2 . GLU D 87  ? 0.7911 0.8240 0.6816 -0.1545 0.0616  0.0504  388 GLU D OE2 
10911 N N   . VAL D 88  ? 0.6295 0.7744 0.5940 -0.1679 0.0538  0.0293  389 VAL D N   
10912 C CA  . VAL D 88  ? 0.6133 0.7808 0.6010 -0.1486 0.0486  0.0257  389 VAL D CA  
10913 C C   . VAL D 88  ? 0.6920 0.9103 0.6992 -0.1523 0.0505  0.0205  389 VAL D C   
10914 O O   . VAL D 88  ? 0.7592 1.0033 0.7845 -0.1356 0.0490  0.0175  389 VAL D O   
10915 C CB  . VAL D 88  ? 0.5980 0.7438 0.5856 -0.1429 0.0421  0.0263  389 VAL D CB  
10916 C CG1 . VAL D 88  ? 0.5747 0.7444 0.5847 -0.1247 0.0369  0.0230  389 VAL D CG1 
10917 C CG2 . VAL D 88  ? 0.5830 0.6829 0.5540 -0.1356 0.0399  0.0308  389 VAL D CG2 
10918 N N   . ASN D 89  ? 0.8003 1.0337 0.8034 -0.1740 0.0538  0.0193  390 ASN D N   
10919 C CA  . ASN D 89  ? 0.8713 1.1578 0.8932 -0.1788 0.0558  0.0142  390 ASN D CA  
10920 C C   . ASN D 89  ? 0.8400 1.1542 0.8691 -0.1738 0.0614  0.0123  390 ASN D C   
10921 O O   . ASN D 89  ? 0.8872 1.2379 0.9371 -0.1589 0.0604  0.0081  390 ASN D O   
10922 C CB  . ASN D 89  ? 1.0363 1.3319 1.0494 -0.2064 0.0589  0.0133  390 ASN D CB  
10923 C CG  . ASN D 89  ? 1.0976 1.3991 1.1178 -0.2084 0.0530  0.0112  390 ASN D CG  
10924 O OD1 . ASN D 89  ? 1.1639 1.4926 1.1868 -0.2268 0.0543  0.0083  390 ASN D OD1 
10925 N ND2 . ASN D 89  ? 1.0305 1.3079 1.0534 -0.1902 0.0463  0.0126  390 ASN D ND2 
10926 N N   . LYS D 90  ? 0.8109 1.1075 0.8217 -0.1861 0.0675  0.0153  391 LYS D N   
10927 C CA  . LYS D 90  ? 0.7851 1.1014 0.7990 -0.1810 0.0731  0.0139  391 LYS D CA  
10928 C C   . LYS D 90  ? 0.6528 0.9742 0.6820 -0.1527 0.0693  0.0117  391 LYS D C   
10929 O O   . LYS D 90  ? 0.6912 1.0509 0.7368 -0.1428 0.0716  0.0068  391 LYS D O   
10930 C CB  . LYS D 90  ? 0.9062 1.1854 0.8941 -0.1919 0.0775  0.0195  391 LYS D CB  
10931 C CG  . LYS D 90  ? 0.9658 1.2484 0.9370 -0.2210 0.0846  0.0211  391 LYS D CG  
10932 C CD  . LYS D 90  ? 1.0666 1.3012 1.0089 -0.2280 0.0869  0.0281  391 LYS D CD  
10933 C CE  . LYS D 90  ? 1.1880 1.4309 1.1135 -0.2537 0.0956  0.0298  391 LYS D CE  
10934 N NZ  . LYS D 90  ? 1.2216 1.4767 1.1427 -0.2794 0.0979  0.0284  391 LYS D NZ  
10935 N N   . GLU D 91  ? 0.5086 0.7908 0.5315 -0.1397 0.0635  0.0150  392 GLU D N   
10936 C CA  . GLU D 91  ? 0.5125 0.7908 0.5444 -0.1153 0.0602  0.0137  392 GLU D CA  
10937 C C   . GLU D 91  ? 0.6963 1.0033 0.7506 -0.0997 0.0556  0.0092  392 GLU D C   
10938 O O   . GLU D 91  ? 0.8368 1.1600 0.9023 -0.0822 0.0555  0.0056  392 GLU D O   
10939 C CB  . GLU D 91  ? 0.4691 0.6990 0.4869 -0.1085 0.0555  0.0187  392 GLU D CB  
10940 C CG  . GLU D 91  ? 0.4357 0.6527 0.4538 -0.0897 0.0540  0.0185  392 GLU D CG  
10941 C CD  . GLU D 91  ? 0.6526 0.8246 0.6533 -0.0884 0.0509  0.0241  392 GLU D CD  
10942 O OE1 . GLU D 91  ? 0.7665 0.9242 0.7685 -0.0728 0.0473  0.0242  392 GLU D OE1 
10943 O OE2 . GLU D 91  ? 0.7121 0.8631 0.6973 -0.1031 0.0520  0.0283  392 GLU D OE2 
10944 N N   . ILE D 92  ? 0.6572 0.9695 0.7169 -0.1053 0.0515  0.0092  393 ILE D N   
10945 C CA  . ILE D 92  ? 0.6413 0.9821 0.7213 -0.0907 0.0467  0.0056  393 ILE D CA  
10946 C C   . ILE D 92  ? 0.8719 1.2653 0.9670 -0.0926 0.0511  0.0004  393 ILE D C   
10947 O O   . ILE D 92  ? 0.9584 1.3781 1.0701 -0.0743 0.0488  -0.0033 393 ILE D O   
10948 C CB  . ILE D 92  ? 0.5540 0.8860 0.6346 -0.0963 0.0407  0.0071  393 ILE D CB  
10949 C CG1 . ILE D 92  ? 0.5744 0.8561 0.6396 -0.0944 0.0371  0.0118  393 ILE D CG1 
10950 C CG2 . ILE D 92  ? 0.5455 0.9033 0.6450 -0.0794 0.0350  0.0044  393 ILE D CG2 
10951 C CD1 . ILE D 92  ? 0.4723 0.7424 0.5365 -0.0990 0.0315  0.0130  393 ILE D CD1 
10952 N N   . ASP D 93  ? 0.9736 1.3832 1.0626 -0.1143 0.0577  -0.0001 394 ASP D N   
10953 C CA  . ASP D 93  ? 0.8889 1.3515 0.9918 -0.1173 0.0631  -0.0053 394 ASP D CA  
10954 C C   . ASP D 93  ? 0.6945 1.1651 0.8003 -0.1019 0.0675  -0.0081 394 ASP D C   
10955 O O   . ASP D 93  ? 0.6780 1.1858 0.8012 -0.0862 0.0679  -0.0133 394 ASP D O   
10956 C CB  . ASP D 93  ? 0.9808 1.4555 1.0735 -0.1471 0.0696  -0.0047 394 ASP D CB  
10957 C CG  . ASP D 93  ? 1.0232 1.5311 1.1261 -0.1604 0.0676  -0.0070 394 ASP D CG  
10958 O OD1 . ASP D 93  ? 1.0549 1.5632 1.1679 -0.1489 0.0600  -0.0072 394 ASP D OD1 
10959 O OD2 . ASP D 93  ? 0.9627 1.4968 1.0629 -0.1833 0.0736  -0.0085 394 ASP D OD2 
10960 N N   . THR D 94  ? 0.5974 1.0334 0.6853 -0.1056 0.0707  -0.0048 395 THR D N   
10961 C CA  . THR D 94  ? 0.7016 1.1448 0.7897 -0.0937 0.0756  -0.0077 395 THR D CA  
10962 C C   . THR D 94  ? 0.8199 1.2457 0.9135 -0.0667 0.0702  -0.0090 395 THR D C   
10963 O O   . THR D 94  ? 0.9694 1.4121 1.0690 -0.0524 0.0734  -0.0138 395 THR D O   
10964 C CB  . THR D 94  ? 0.6744 1.0885 0.7402 -0.1083 0.0809  -0.0035 395 THR D CB  
10965 O OG1 . THR D 94  ? 0.7032 1.0659 0.7544 -0.1057 0.0754  0.0024  395 THR D OG1 
10966 C CG2 . THR D 94  ? 0.6673 1.0950 0.7245 -0.1367 0.0865  -0.0018 395 THR D CG2 
10967 N N   . THR D 95  ? 0.7724 1.1646 0.8629 -0.0598 0.0626  -0.0053 396 THR D N   
10968 C CA  . THR D 95  ? 0.6573 1.0273 0.7491 -0.0372 0.0579  -0.0059 396 THR D CA  
10969 C C   . THR D 95  ? 0.7300 1.1006 0.8336 -0.0235 0.0499  -0.0061 396 THR D C   
10970 O O   . THR D 95  ? 0.8400 1.1940 0.9446 -0.0048 0.0460  -0.0069 396 THR D O   
10971 C CB  . THR D 95  ? 0.6869 1.0086 0.7600 -0.0398 0.0563  -0.0008 396 THR D CB  
10972 O OG1 . THR D 95  ? 0.7808 1.0778 0.8480 -0.0486 0.0512  0.0042  396 THR D OG1 
10973 C CG2 . THR D 95  ? 0.5729 0.8894 0.6312 -0.0539 0.0634  0.0007  396 THR D CG2 
10974 N N   . SER D 96  ? 0.5692 0.9568 0.6800 -0.0329 0.0474  -0.0053 397 SER D N   
10975 C CA  . SER D 96  ? 0.6053 0.9925 0.7254 -0.0218 0.0395  -0.0046 397 SER D CA  
10976 C C   . SER D 96  ? 0.5644 0.9047 0.6734 -0.0176 0.0338  0.0000  397 SER D C   
10977 O O   . SER D 96  ? 0.5731 0.9066 0.6877 -0.0035 0.0275  0.0005  397 SER D O   
10978 C CB  . SER D 96  ? 0.7140 1.1273 0.8490 0.0011  0.0378  -0.0093 397 SER D CB  
10979 O OG  . SER D 96  ? 0.8351 1.2876 0.9778 0.0002  0.0447  -0.0143 397 SER D OG  
10980 N N   . THR D 97  ? 0.5284 0.8373 0.6214 -0.0293 0.0360  0.0036  398 THR D N   
10981 C CA  . THR D 97  ? 0.5320 0.7984 0.6136 -0.0275 0.0314  0.0079  398 THR D CA  
10982 C C   . THR D 97  ? 0.5687 0.8127 0.6336 -0.0446 0.0353  0.0115  398 THR D C   
10983 O O   . THR D 97  ? 0.6643 0.9243 0.7260 -0.0575 0.0414  0.0107  398 THR D O   
10984 C CB  . THR D 97  ? 0.5798 0.8275 0.6600 -0.0091 0.0292  0.0073  398 THR D CB  
10985 O OG1 . THR D 97  ? 0.6201 0.8305 0.6894 -0.0096 0.0252  0.0115  398 THR D OG1 
10986 C CG2 . THR D 97  ? 0.6155 0.8668 0.6905 -0.0079 0.0353  0.0050  398 THR D CG2 
10987 N N   . TYR D 98  ? 0.4739 0.6810 0.5274 -0.0444 0.0319  0.0155  399 TYR D N   
10988 C CA  . TYR D 98  ? 0.4622 0.6441 0.4979 -0.0573 0.0350  0.0194  399 TYR D CA  
10989 C C   . TYR D 98  ? 0.5389 0.6858 0.5651 -0.0481 0.0313  0.0225  399 TYR D C   
10990 O O   . TYR D 98  ? 0.6733 0.8158 0.7064 -0.0338 0.0269  0.0215  399 TYR D O   
10991 C CB  . TYR D 98  ? 0.4388 0.6169 0.4679 -0.0754 0.0356  0.0213  399 TYR D CB  
10992 C CG  . TYR D 98  ? 0.5274 0.6849 0.5548 -0.0740 0.0298  0.0231  399 TYR D CG  
10993 C CD1 . TYR D 98  ? 0.5651 0.6867 0.5757 -0.0795 0.0290  0.0271  399 TYR D CD1 
10994 C CD2 . TYR D 98  ? 0.5443 0.7187 0.5858 -0.0672 0.0252  0.0209  399 TYR D CD2 
10995 C CE1 . TYR D 98  ? 0.5687 0.6728 0.5775 -0.0781 0.0243  0.0281  399 TYR D CE1 
10996 C CE2 . TYR D 98  ? 0.5689 0.7252 0.6079 -0.0670 0.0203  0.0223  399 TYR D CE2 
10997 C CZ  . TYR D 98  ? 0.5563 0.6779 0.5791 -0.0725 0.0202  0.0256  399 TYR D CZ  
10998 O OH  . TYR D 98  ? 0.6084 0.7125 0.6281 -0.0718 0.0159  0.0265  399 TYR D OH  
10999 N N   . GLN D 99  ? 0.4254 0.5476 0.4348 -0.0566 0.0333  0.0265  400 GLN D N   
11000 C CA  . GLN D 99  ? 0.4961 0.5888 0.4956 -0.0485 0.0304  0.0295  400 GLN D CA  
11001 C C   . GLN D 99  ? 0.5851 0.6491 0.5710 -0.0560 0.0286  0.0340  400 GLN D C   
11002 O O   . GLN D 99  ? 0.6013 0.6582 0.5752 -0.0700 0.0321  0.0362  400 GLN D O   
11003 C CB  . GLN D 99  ? 0.6097 0.7002 0.6002 -0.0483 0.0345  0.0302  400 GLN D CB  
11004 C CG  . GLN D 99  ? 0.5304 0.6435 0.5319 -0.0380 0.0361  0.0253  400 GLN D CG  
11005 C CD  . GLN D 99  ? 0.6320 0.7361 0.6395 -0.0223 0.0307  0.0238  400 GLN D CD  
11006 O OE1 . GLN D 99  ? 0.8036 0.8846 0.8024 -0.0185 0.0279  0.0264  400 GLN D OE1 
11007 N NE2 . GLN D 99  ? 0.5906 0.7132 0.6124 -0.0131 0.0293  0.0196  400 GLN D NE2 
11008 N N   . LEU D 100 ? 0.5515 0.5978 0.5378 -0.0468 0.0233  0.0351  401 LEU D N   
11009 C CA  . LEU D 100 ? 0.5184 0.5375 0.4920 -0.0511 0.0215  0.0386  401 LEU D CA  
11010 C C   . LEU D 100 ? 0.6206 0.6166 0.5772 -0.0511 0.0226  0.0429  401 LEU D C   
11011 O O   . LEU D 100 ? 0.6611 0.6564 0.6182 -0.0417 0.0215  0.0431  401 LEU D O   
11012 C CB  . LEU D 100 ? 0.4317 0.4429 0.4119 -0.0408 0.0158  0.0380  401 LEU D CB  
11013 C CG  . LEU D 100 ? 0.4215 0.4494 0.4155 -0.0404 0.0134  0.0349  401 LEU D CG  
11014 C CD1 . LEU D 100 ? 0.3099 0.3259 0.3065 -0.0312 0.0083  0.0352  401 LEU D CD1 
11015 C CD2 . LEU D 100 ? 0.4590 0.4892 0.4490 -0.0547 0.0154  0.0346  401 LEU D CD2 
11016 N N   . LYS D 101 ? 0.5561 0.5322 0.4963 -0.0616 0.0246  0.0463  402 LYS D N   
11017 C CA  . LYS D 101 ? 0.3865 0.3355 0.3089 -0.0588 0.0241  0.0512  402 LYS D CA  
11018 C C   . LYS D 101 ? 0.5400 0.4776 0.4657 -0.0443 0.0185  0.0516  402 LYS D C   
11019 O O   . LYS D 101 ? 0.8909 0.8361 0.8292 -0.0391 0.0154  0.0487  402 LYS D O   
11020 C CB  . LYS D 101 ? 0.5152 0.4392 0.4177 -0.0710 0.0263  0.0548  402 LYS D CB  
11021 C CG  . LYS D 101 ? 0.6646 0.5991 0.5621 -0.0888 0.0322  0.0544  402 LYS D CG  
11022 C CD  . LYS D 101 ? 0.8066 0.7479 0.6974 -0.0920 0.0362  0.0566  402 LYS D CD  
11023 C CE  . LYS D 101 ? 0.8287 0.7606 0.7008 -0.1113 0.0419  0.0595  402 LYS D CE  
11024 N NZ  . LYS D 101 ? 0.9095 0.8704 0.7872 -0.1189 0.0473  0.0577  402 LYS D NZ  
11025 N N   . ASP D 102 ? 0.6678 0.5885 0.5816 -0.0380 0.0170  0.0555  403 ASP D N   
11026 C CA  . ASP D 102 ? 0.5947 0.5074 0.5113 -0.0249 0.0119  0.0559  403 ASP D CA  
11027 C C   . ASP D 102 ? 0.6293 0.5253 0.5418 -0.0245 0.0100  0.0561  403 ASP D C   
11028 O O   . ASP D 102 ? 0.7239 0.6235 0.6461 -0.0163 0.0064  0.0540  403 ASP D O   
11029 C CB  . ASP D 102 ? 0.7191 0.6188 0.6227 -0.0186 0.0106  0.0603  403 ASP D CB  
11030 C CG  . ASP D 102 ? 0.8976 0.8136 0.8050 -0.0178 0.0120  0.0593  403 ASP D CG  
11031 O OD1 . ASP D 102 ? 0.8912 0.8277 0.8107 -0.0215 0.0145  0.0551  403 ASP D OD1 
11032 O OD2 . ASP D 102 ? 0.9841 0.8925 0.8817 -0.0126 0.0105  0.0626  403 ASP D OD2 
11033 N N   . THR D 103 ? 0.5649 0.4413 0.4613 -0.0336 0.0126  0.0586  404 THR D N   
11034 C CA  . THR D 103 ? 0.5208 0.3799 0.4116 -0.0338 0.0114  0.0580  404 THR D CA  
11035 C C   . THR D 103 ? 0.6633 0.5415 0.5713 -0.0366 0.0106  0.0528  404 THR D C   
11036 O O   . THR D 103 ? 0.5610 0.4382 0.4753 -0.0292 0.0074  0.0509  404 THR D O   
11037 C CB  . THR D 103 ? 0.6322 0.4659 0.5012 -0.0458 0.0149  0.0609  404 THR D CB  
11038 O OG1 . THR D 103 ? 0.6743 0.5194 0.5415 -0.0594 0.0195  0.0614  404 THR D OG1 
11039 C CG2 . THR D 103 ? 0.5494 0.3527 0.3978 -0.0378 0.0136  0.0663  404 THR D CG2 
11040 N N   . GLU D 104 ? 0.7711 0.6691 0.6872 -0.0468 0.0135  0.0506  405 GLU D N   
11041 C CA  . GLU D 104 ? 0.6322 0.5505 0.5642 -0.0493 0.0124  0.0462  405 GLU D CA  
11042 C C   . GLU D 104 ? 0.5735 0.5055 0.5215 -0.0360 0.0082  0.0443  405 GLU D C   
11043 O O   . GLU D 104 ? 0.5700 0.5043 0.5247 -0.0332 0.0055  0.0422  405 GLU D O   
11044 C CB  . GLU D 104 ? 0.5583 0.4996 0.4968 -0.0607 0.0161  0.0444  405 GLU D CB  
11045 C CG  . GLU D 104 ? 0.4298 0.3571 0.3503 -0.0767 0.0208  0.0465  405 GLU D CG  
11046 C CD  . GLU D 104 ? 0.5531 0.5055 0.4788 -0.0884 0.0253  0.0451  405 GLU D CD  
11047 O OE1 . GLU D 104 ? 0.5229 0.4675 0.4352 -0.1044 0.0292  0.0461  405 GLU D OE1 
11048 O OE2 . GLU D 104 ? 0.6234 0.6026 0.5654 -0.0819 0.0251  0.0429  405 GLU D OE2 
11049 N N   . LEU D 105 ? 0.6594 0.5987 0.6115 -0.0284 0.0076  0.0451  406 LEU D N   
11050 C CA  . LEU D 105 ? 0.5915 0.5428 0.5572 -0.0178 0.0039  0.0431  406 LEU D CA  
11051 C C   . LEU D 105 ? 0.6763 0.6141 0.6394 -0.0101 0.0003  0.0437  406 LEU D C   
11052 O O   . LEU D 105 ? 0.6466 0.5922 0.6196 -0.0057 -0.0025 0.0416  406 LEU D O   
11053 C CB  . LEU D 105 ? 0.4755 0.4352 0.4436 -0.0124 0.0043  0.0432  406 LEU D CB  
11054 C CG  . LEU D 105 ? 0.5019 0.4718 0.4817 -0.0029 0.0008  0.0409  406 LEU D CG  
11055 C CD1 . LEU D 105 ? 0.3726 0.3617 0.3654 -0.0032 0.0010  0.0375  406 LEU D CD1 
11056 C CD2 . LEU D 105 ? 0.5625 0.5320 0.5386 0.0020  0.0009  0.0416  406 LEU D CD2 
11057 N N   . ILE D 106 ? 0.7200 0.6382 0.6694 -0.0080 0.0004  0.0467  407 ILE D N   
11058 C CA  . ILE D 106 ? 0.5502 0.4582 0.4975 0.0004  -0.0027 0.0469  407 ILE D CA  
11059 C C   . ILE D 106 ? 0.6785 0.5811 0.6258 -0.0033 -0.0027 0.0447  407 ILE D C   
11060 O O   . ILE D 106 ? 0.5513 0.4574 0.5049 0.0022  -0.0053 0.0429  407 ILE D O   
11061 C CB  . ILE D 106 ? 0.5034 0.3921 0.4352 0.0053  -0.0028 0.0508  407 ILE D CB  
11062 C CG1 . ILE D 106 ? 0.4946 0.3911 0.4275 0.0104  -0.0038 0.0526  407 ILE D CG1 
11063 C CG2 . ILE D 106 ? 0.3596 0.2379 0.2882 0.0140  -0.0053 0.0506  407 ILE D CG2 
11064 C CD1 . ILE D 106 ? 0.5270 0.4056 0.4427 0.0125  -0.0033 0.0574  407 ILE D CD1 
11065 N N   . TYR D 107 ? 0.6723 0.5664 0.6112 -0.0139 0.0003  0.0447  408 TYR D N   
11066 C CA  . TYR D 107 ? 0.6142 0.5031 0.5515 -0.0194 0.0005  0.0421  408 TYR D CA  
11067 C C   . TYR D 107 ? 0.6172 0.5292 0.5715 -0.0204 -0.0014 0.0389  408 TYR D C   
11068 O O   . TYR D 107 ? 0.7525 0.6645 0.7099 -0.0181 -0.0033 0.0367  408 TYR D O   
11069 C CB  . TYR D 107 ? 0.5244 0.4014 0.4488 -0.0330 0.0043  0.0425  408 TYR D CB  
11070 C CG  . TYR D 107 ? 0.5330 0.4099 0.4572 -0.0419 0.0047  0.0389  408 TYR D CG  
11071 C CD1 . TYR D 107 ? 0.5807 0.4328 0.4902 -0.0425 0.0051  0.0379  408 TYR D CD1 
11072 C CD2 . TYR D 107 ? 0.5423 0.4440 0.4801 -0.0491 0.0044  0.0363  408 TYR D CD2 
11073 C CE1 . TYR D 107 ? 0.5859 0.4377 0.4941 -0.0514 0.0055  0.0341  408 TYR D CE1 
11074 C CE2 . TYR D 107 ? 0.6920 0.5956 0.6295 -0.0575 0.0043  0.0330  408 TYR D CE2 
11075 C CZ  . TYR D 107 ? 0.6763 0.5546 0.5986 -0.0595 0.0049  0.0318  408 TYR D CZ  
11076 O OH  . TYR D 107 ? 0.7303 0.6102 0.6509 -0.0690 0.0048  0.0280  408 TYR D OH  
11077 N N   . GLY D 108 ? 0.5737 0.5052 0.5381 -0.0234 -0.0008 0.0386  409 GLY D N   
11078 C CA  . GLY D 108 ? 0.5622 0.5145 0.5413 -0.0231 -0.0029 0.0361  409 GLY D CA  
11079 C C   . GLY D 108 ? 0.5450 0.5009 0.5318 -0.0126 -0.0066 0.0358  409 GLY D C   
11080 O O   . GLY D 108 ? 0.7788 0.7419 0.7720 -0.0121 -0.0089 0.0342  409 GLY D O   
11081 N N   . ALA D 109 ? 0.5078 0.4592 0.4931 -0.0051 -0.0073 0.0374  410 ALA D N   
11082 C CA  . ALA D 109 ? 0.5220 0.4779 0.5139 0.0030  -0.0106 0.0369  410 ALA D CA  
11083 C C   . ALA D 109 ? 0.5310 0.4772 0.5187 0.0058  -0.0119 0.0364  410 ALA D C   
11084 O O   . ALA D 109 ? 0.4934 0.4459 0.4871 0.0089  -0.0143 0.0354  410 ALA D O   
11085 C CB  . ALA D 109 ? 0.4880 0.4439 0.4791 0.0089  -0.0109 0.0383  410 ALA D CB  
11086 N N   . LYS D 110 ? 0.5104 0.4406 0.4866 0.0050  -0.0101 0.0371  411 LYS D N   
11087 C CA  . LYS D 110 ? 0.4845 0.4053 0.4558 0.0086  -0.0108 0.0359  411 LYS D CA  
11088 C C   . LYS D 110 ? 0.6472 0.5708 0.6206 0.0022  -0.0108 0.0332  411 LYS D C   
11089 O O   . LYS D 110 ? 0.5357 0.4615 0.5114 0.0052  -0.0122 0.0313  411 LYS D O   
11090 C CB  . LYS D 110 ? 0.3280 0.2278 0.2843 0.0106  -0.0089 0.0374  411 LYS D CB  
11091 C CG  . LYS D 110 ? 0.4759 0.3731 0.4292 0.0198  -0.0100 0.0400  411 LYS D CG  
11092 C CD  . LYS D 110 ? 0.4883 0.3625 0.4251 0.0233  -0.0086 0.0416  411 LYS D CD  
11093 C CE  . LYS D 110 ? 0.6076 0.4792 0.5396 0.0319  -0.0099 0.0451  411 LYS D CE  
11094 N NZ  . LYS D 110 ? 0.6491 0.4945 0.5623 0.0355  -0.0086 0.0475  411 LYS D NZ  
11095 N N   . HIS D 111 ? 0.6010 0.5265 0.5736 -0.0071 -0.0092 0.0327  412 HIS D N   
11096 C CA  . HIS D 111 ? 0.6497 0.5789 0.6234 -0.0139 -0.0095 0.0301  412 HIS D CA  
11097 C C   . HIS D 111 ? 0.6307 0.5803 0.6180 -0.0128 -0.0126 0.0296  412 HIS D C   
11098 O O   . HIS D 111 ? 0.6865 0.6392 0.6751 -0.0142 -0.0140 0.0278  412 HIS D O   
11099 C CB  . HIS D 111 ? 0.5687 0.4937 0.5356 -0.0255 -0.0068 0.0295  412 HIS D CB  
11100 C CG  . HIS D 111 ? 0.5729 0.4719 0.5222 -0.0281 -0.0041 0.0291  412 HIS D CG  
11101 N ND1 . HIS D 111 ? 0.5678 0.4503 0.5077 -0.0218 -0.0029 0.0318  412 HIS D ND1 
11102 C CD2 . HIS D 111 ? 0.5813 0.4661 0.5193 -0.0354 -0.0027 0.0264  412 HIS D CD2 
11103 C CE1 . HIS D 111 ? 0.6470 0.5047 0.5699 -0.0243 -0.0009 0.0310  412 HIS D CE1 
11104 N NE2 . HIS D 111 ? 0.6213 0.4791 0.5423 -0.0330 -0.0004 0.0274  412 HIS D NE2 
11105 N N   . ALA D 112 ? 0.4942 0.4559 0.4902 -0.0095 -0.0136 0.0312  413 ALA D N   
11106 C CA  . ALA D 112 ? 0.5404 0.5166 0.5465 -0.0066 -0.0168 0.0312  413 ALA D CA  
11107 C C   . ALA D 112 ? 0.5720 0.5446 0.5778 -0.0013 -0.0188 0.0311  413 ALA D C   
11108 O O   . ALA D 112 ? 0.5613 0.5409 0.5709 -0.0017 -0.0211 0.0307  413 ALA D O   
11109 C CB  . ALA D 112 ? 0.4876 0.4735 0.5007 -0.0027 -0.0173 0.0325  413 ALA D CB  
11110 N N   . TRP D 113 ? 0.5436 0.5068 0.5447 0.0036  -0.0179 0.0314  414 TRP D N   
11111 C CA  . TRP D 113 ? 0.5589 0.5216 0.5597 0.0078  -0.0192 0.0307  414 TRP D CA  
11112 C C   . TRP D 113 ? 0.5849 0.5420 0.5801 0.0049  -0.0183 0.0282  414 TRP D C   
11113 O O   . TRP D 113 ? 0.7652 0.7280 0.7625 0.0046  -0.0197 0.0272  414 TRP D O   
11114 C CB  . TRP D 113 ? 0.4423 0.3999 0.4400 0.0144  -0.0186 0.0314  414 TRP D CB  
11115 C CG  . TRP D 113 ? 0.5799 0.5416 0.5786 0.0187  -0.0198 0.0304  414 TRP D CG  
11116 C CD1 . TRP D 113 ? 0.4168 0.3862 0.4190 0.0167  -0.0212 0.0294  414 TRP D CD1 
11117 C CD2 . TRP D 113 ? 0.7042 0.6649 0.7003 0.0255  -0.0196 0.0304  414 TRP D CD2 
11118 N NE1 . TRP D 113 ? 0.5655 0.5394 0.5676 0.0209  -0.0214 0.0285  414 TRP D NE1 
11119 C CE2 . TRP D 113 ? 0.7170 0.6869 0.7161 0.0267  -0.0205 0.0289  414 TRP D CE2 
11120 C CE3 . TRP D 113 ? 0.6452 0.5993 0.6364 0.0307  -0.0189 0.0317  414 TRP D CE3 
11121 C CZ2 . TRP D 113 ? 0.7505 0.7260 0.7492 0.0332  -0.0207 0.0281  414 TRP D CZ2 
11122 C CZ3 . TRP D 113 ? 0.4649 0.4233 0.4552 0.0381  -0.0196 0.0314  414 TRP D CZ3 
11123 C CH2 . TRP D 113 ? 0.6177 0.5881 0.6126 0.0393  -0.0204 0.0293  414 TRP D CH2 
11124 N N   . ARG D 114 ? 0.5192 0.4641 0.5060 0.0019  -0.0158 0.0272  415 ARG D N   
11125 C CA  . ARG D 114 ? 0.4115 0.3474 0.3904 -0.0012 -0.0145 0.0241  415 ARG D CA  
11126 C C   . ARG D 114 ? 0.5654 0.5122 0.5485 -0.0084 -0.0161 0.0228  415 ARG D C   
11127 O O   . ARG D 114 ? 0.6156 0.5613 0.5953 -0.0097 -0.0162 0.0201  415 ARG D O   
11128 C CB  . ARG D 114 ? 0.4355 0.3531 0.4022 -0.0047 -0.0115 0.0235  415 ARG D CB  
11129 C CG  . ARG D 114 ? 0.5285 0.4299 0.4826 -0.0075 -0.0095 0.0197  415 ARG D CG  
11130 C CD  . ARG D 114 ? 0.4617 0.3421 0.4017 -0.0131 -0.0065 0.0199  415 ARG D CD  
11131 N NE  . ARG D 114 ? 0.4986 0.3567 0.4228 -0.0131 -0.0042 0.0163  415 ARG D NE  
11132 C CZ  . ARG D 114 ? 0.5764 0.4100 0.4839 -0.0176 -0.0014 0.0161  415 ARG D CZ  
11133 N NH1 . ARG D 114 ? 0.6305 0.4412 0.5221 -0.0167 0.0006  0.0123  415 ARG D NH1 
11134 N NH2 . ARG D 114 ? 0.7706 0.6010 0.6758 -0.0232 -0.0005 0.0196  415 ARG D NH2 
11135 N N   . ASN D 115 ? 0.4581 0.4164 0.4484 -0.0125 -0.0175 0.0245  416 ASN D N   
11136 C CA  . ASN D 115 ? 0.4014 0.3724 0.3961 -0.0186 -0.0197 0.0239  416 ASN D CA  
11137 C C   . ASN D 115 ? 0.5492 0.5324 0.5519 -0.0143 -0.0232 0.0257  416 ASN D C   
11138 O O   . ASN D 115 ? 0.5585 0.5518 0.5638 -0.0180 -0.0257 0.0257  416 ASN D O   
11139 C CB  . ASN D 115 ? 0.3362 0.3161 0.3349 -0.0242 -0.0194 0.0247  416 ASN D CB  
11140 C CG  . ASN D 115 ? 0.3851 0.3524 0.3739 -0.0316 -0.0158 0.0231  416 ASN D CG  
11141 O OD1 . ASN D 115 ? 0.5463 0.4975 0.5242 -0.0337 -0.0139 0.0208  416 ASN D OD1 
11142 N ND2 . ASN D 115 ? 0.3995 0.3734 0.3909 -0.0358 -0.0145 0.0242  416 ASN D ND2 
11143 N N   . ALA D 116 ? 0.4566 0.4387 0.4620 -0.0072 -0.0237 0.0275  417 ALA D N   
11144 C CA  . ALA D 116 ? 0.5375 0.5273 0.5474 -0.0044 -0.0268 0.0294  417 ALA D CA  
11145 C C   . ALA D 116 ? 0.5193 0.5099 0.5254 -0.0068 -0.0275 0.0279  417 ALA D C   
11146 O O   . ALA D 116 ? 0.4962 0.4823 0.4987 -0.0046 -0.0259 0.0264  417 ALA D O   
11147 C CB  . ALA D 116 ? 0.3379 0.3252 0.3494 0.0014  -0.0268 0.0308  417 ALA D CB  
11148 N N   . SER D 117 ? 0.4685 0.4670 0.4755 -0.0109 -0.0301 0.0284  418 SER D N   
11149 C CA  A SER D 117 ? 0.4857 0.4851 0.4877 -0.0144 -0.0304 0.0266  418 SER D CA  
11150 C CA  B SER D 117 ? 0.4863 0.4857 0.4882 -0.0144 -0.0304 0.0266  418 SER D CA  
11151 C C   . SER D 117 ? 0.5320 0.5328 0.5334 -0.0117 -0.0315 0.0282  418 SER D C   
11152 O O   . SER D 117 ? 0.6254 0.6252 0.6221 -0.0128 -0.0299 0.0258  418 SER D O   
11153 C CB  A SER D 117 ? 0.4765 0.4853 0.4790 -0.0198 -0.0334 0.0270  418 SER D CB  
11154 C CB  B SER D 117 ? 0.4690 0.4781 0.4716 -0.0197 -0.0335 0.0271  418 SER D CB  
11155 O OG  A SER D 117 ? 0.4245 0.4421 0.4331 -0.0168 -0.0372 0.0311  418 SER D OG  
11156 O OG  B SER D 117 ? 0.4272 0.4367 0.4294 -0.0245 -0.0321 0.0249  418 SER D OG  
11157 N N   . ARG D 118 ? 0.4866 0.4894 0.4919 -0.0085 -0.0337 0.0319  419 ARG D N   
11158 C CA  . ARG D 118 ? 0.4438 0.4470 0.4471 -0.0081 -0.0347 0.0337  419 ARG D CA  
11159 C C   . ARG D 118 ? 0.4225 0.4234 0.4256 -0.0055 -0.0318 0.0319  419 ARG D C   
11160 O O   . ARG D 118 ? 0.4982 0.5015 0.4997 -0.0066 -0.0322 0.0331  419 ARG D O   
11161 C CB  . ARG D 118 ? 0.4786 0.4811 0.4835 -0.0060 -0.0381 0.0381  419 ARG D CB  
11162 C CG  . ARG D 118 ? 0.5695 0.5766 0.5751 -0.0063 -0.0418 0.0404  419 ARG D CG  
11163 C CD  . ARG D 118 ? 0.5322 0.5360 0.5369 -0.0026 -0.0455 0.0449  419 ARG D CD  
11164 N NE  . ARG D 118 ? 0.6393 0.6486 0.6422 -0.0029 -0.0496 0.0476  419 ARG D NE  
11165 C CZ  . ARG D 118 ? 0.6338 0.6412 0.6352 0.0020  -0.0537 0.0517  419 ARG D CZ  
11166 N NH1 . ARG D 118 ? 0.5401 0.5381 0.5407 0.0071  -0.0539 0.0533  419 ARG D NH1 
11167 N NH2 . ARG D 118 ? 0.5588 0.5734 0.5584 0.0022  -0.0578 0.0542  419 ARG D NH2 
11168 N N   . CYS D 119 ? 0.4079 0.4049 0.4118 -0.0024 -0.0290 0.0294  420 CYS D N   
11169 C CA  . CYS D 119 ? 0.4342 0.4308 0.4385 0.0017  -0.0270 0.0283  420 CYS D CA  
11170 C C   . CYS D 119 ? 0.4330 0.4295 0.4335 0.0034  -0.0241 0.0243  420 CYS D C   
11171 O O   . CYS D 119 ? 0.3816 0.3708 0.3786 0.0040  -0.0223 0.0220  420 CYS D O   
11172 C CB  . CYS D 119 ? 0.5587 0.5501 0.5655 0.0056  -0.0264 0.0290  420 CYS D CB  
11173 S SG  . CYS D 119 ? 0.5861 0.5786 0.5927 0.0117  -0.0245 0.0277  420 CYS D SG  
11174 N N   . VAL D 120 ? 0.3707 0.3753 0.3712 0.0042  -0.0233 0.0234  421 VAL D N   
11175 C CA  . VAL D 120 ? 0.4443 0.4522 0.4417 0.0075  -0.0203 0.0191  421 VAL D CA  
11176 C C   . VAL D 120 ? 0.4567 0.4630 0.4547 0.0159  -0.0185 0.0176  421 VAL D C   
11177 O O   . VAL D 120 ? 0.5105 0.5188 0.5056 0.0213  -0.0159 0.0138  421 VAL D O   
11178 C CB  . VAL D 120 ? 0.5777 0.5990 0.5752 0.0036  -0.0202 0.0189  421 VAL D CB  
11179 C CG1 . VAL D 120 ? 0.4098 0.4399 0.4116 0.0045  -0.0208 0.0204  421 VAL D CG1 
11180 C CG2 . VAL D 120 ? 0.6017 0.6281 0.5952 0.0057  -0.0169 0.0139  421 VAL D CG2 
11181 N N   . GLY D 121 ? 0.5010 0.5039 0.5019 0.0181  -0.0198 0.0203  422 GLY D N   
11182 C CA  . GLY D 121 ? 0.4043 0.4068 0.4052 0.0262  -0.0188 0.0197  422 GLY D CA  
11183 C C   . GLY D 121 ? 0.5292 0.5154 0.5246 0.0305  -0.0176 0.0195  422 GLY D C   
11184 O O   . GLY D 121 ? 0.5744 0.5579 0.5684 0.0376  -0.0173 0.0200  422 GLY D O   
11185 N N   . ARG D 122 ? 0.5018 0.4771 0.4930 0.0258  -0.0169 0.0189  423 ARG D N   
11186 C CA  . ARG D 122 ? 0.4120 0.3708 0.3969 0.0264  -0.0157 0.0193  423 ARG D CA  
11187 C C   . ARG D 122 ? 0.5149 0.4608 0.4904 0.0343  -0.0132 0.0167  423 ARG D C   
11188 O O   . ARG D 122 ? 0.5692 0.4981 0.5367 0.0342  -0.0121 0.0174  423 ARG D O   
11189 C CB  . ARG D 122 ? 0.4680 0.4216 0.4508 0.0175  -0.0157 0.0188  423 ARG D CB  
11190 C CG  . ARG D 122 ? 0.4972 0.4614 0.4881 0.0116  -0.0185 0.0217  423 ARG D CG  
11191 C CD  . ARG D 122 ? 0.6135 0.5757 0.6025 0.0039  -0.0188 0.0209  423 ARG D CD  
11192 N NE  . ARG D 122 ? 0.5574 0.5274 0.5468 0.0000  -0.0200 0.0196  423 ARG D NE  
11193 C CZ  . ARG D 122 ? 0.6076 0.5770 0.5938 -0.0066 -0.0203 0.0180  423 ARG D CZ  
11194 N NH1 . ARG D 122 ? 0.4381 0.3998 0.4206 -0.0108 -0.0192 0.0173  423 ARG D NH1 
11195 N NH2 . ARG D 122 ? 0.6910 0.6681 0.6768 -0.0100 -0.0217 0.0172  423 ARG D NH2 
11196 N N   . ILE D 123 ? 0.4910 0.4438 0.4660 0.0414  -0.0122 0.0138  424 ILE D N   
11197 C CA  . ILE D 123 ? 0.5444 0.4825 0.5091 0.0512  -0.0100 0.0115  424 ILE D CA  
11198 C C   . ILE D 123 ? 0.6060 0.5383 0.5691 0.0579  -0.0111 0.0153  424 ILE D C   
11199 O O   . ILE D 123 ? 0.6693 0.5814 0.6208 0.0635  -0.0098 0.0154  424 ILE D O   
11200 C CB  . ILE D 123 ? 0.4807 0.4298 0.4456 0.0596  -0.0085 0.0072  424 ILE D CB  
11201 C CG1 . ILE D 123 ? 0.5123 0.4417 0.4640 0.0713  -0.0061 0.0045  424 ILE D CG1 
11202 C CG2 . ILE D 123 ? 0.5612 0.5345 0.5371 0.0637  -0.0103 0.0087  424 ILE D CG2 
11203 C CD1 . ILE D 123 ? 0.4200 0.3564 0.3693 0.0804  -0.0037 -0.0011 424 ILE D CD1 
11204 N N   . GLN D 124 ? 0.6546 0.6026 0.6277 0.0565  -0.0135 0.0184  425 GLN D N   
11205 C CA  . GLN D 124 ? 0.6765 0.6231 0.6493 0.0616  -0.0150 0.0221  425 GLN D CA  
11206 C C   . GLN D 124 ? 0.7069 0.6397 0.6760 0.0547  -0.0150 0.0254  425 GLN D C   
11207 O O   . GLN D 124 ? 0.8545 0.7853 0.8223 0.0578  -0.0161 0.0285  425 GLN D O   
11208 C CB  . GLN D 124 ? 0.6428 0.6125 0.6270 0.0610  -0.0175 0.0234  425 GLN D CB  
11209 C CG  . GLN D 124 ? 0.6898 0.6788 0.6788 0.0674  -0.0177 0.0207  425 GLN D CG  
11210 C CD  . GLN D 124 ? 0.7854 0.7747 0.7702 0.0809  -0.0181 0.0209  425 GLN D CD  
11211 O OE1 . GLN D 124 ? 0.8992 0.8705 0.8753 0.0856  -0.0182 0.0233  425 GLN D OE1 
11212 N NE2 . GLN D 124 ? 0.9026 0.9136 0.8930 0.0873  -0.0185 0.0185  425 GLN D NE2 
11213 N N   . TRP D 125 ? 0.6778 0.6032 0.6454 0.0452  -0.0139 0.0245  426 TRP D N   
11214 C CA  . TRP D 125 ? 0.6391 0.5621 0.6085 0.0368  -0.0142 0.0272  426 TRP D CA  
11215 C C   . TRP D 125 ? 0.7502 0.6588 0.7111 0.0389  -0.0134 0.0302  426 TRP D C   
11216 O O   . TRP D 125 ? 0.6824 0.5951 0.6468 0.0353  -0.0140 0.0328  426 TRP D O   
11217 C CB  . TRP D 125 ? 0.5489 0.4670 0.5166 0.0272  -0.0131 0.0253  426 TRP D CB  
11218 C CG  . TRP D 125 ? 0.6180 0.5144 0.5717 0.0255  -0.0104 0.0239  426 TRP D CG  
11219 C CD1 . TRP D 125 ? 0.6970 0.5824 0.6419 0.0281  -0.0088 0.0202  426 TRP D CD1 
11220 C CD2 . TRP D 125 ? 0.6455 0.5270 0.5906 0.0198  -0.0088 0.0259  426 TRP D CD2 
11221 N NE1 . TRP D 125 ? 0.6344 0.4961 0.5645 0.0244  -0.0064 0.0197  426 TRP D NE1 
11222 C CE2 . TRP D 125 ? 0.6199 0.4793 0.5498 0.0185  -0.0064 0.0234  426 TRP D CE2 
11223 C CE3 . TRP D 125 ? 0.5794 0.4640 0.5271 0.0152  -0.0089 0.0292  426 TRP D CE3 
11224 C CZ2 . TRP D 125 ? 0.6075 0.4467 0.5241 0.0115  -0.0041 0.0246  426 TRP D CZ2 
11225 C CZ3 . TRP D 125 ? 0.5758 0.4434 0.5117 0.0086  -0.0065 0.0304  426 TRP D CZ3 
11226 C CH2 . TRP D 125 ? 0.5909 0.4355 0.5110 0.0061  -0.0042 0.0283  426 TRP D CH2 
11227 N N   . SER D 126 ? 0.6414 0.5317 0.5895 0.0450  -0.0119 0.0299  427 SER D N   
11228 C CA  . SER D 126 ? 0.6362 0.5094 0.5731 0.0458  -0.0110 0.0334  427 SER D CA  
11229 C C   . SER D 126 ? 0.7272 0.6069 0.6654 0.0553  -0.0131 0.0366  427 SER D C   
11230 O O   . SER D 126 ? 0.7742 0.6425 0.7040 0.0555  -0.0129 0.0402  427 SER D O   
11231 C CB  . SER D 126 ? 0.6866 0.5326 0.6058 0.0481  -0.0086 0.0324  427 SER D CB  
11232 O OG  . SER D 126 ? 0.8719 0.7163 0.7879 0.0616  -0.0092 0.0306  427 SER D OG  
11233 N N   . LYS D 127 ? 0.6980 0.5963 0.6457 0.0624  -0.0153 0.0352  428 LYS D N   
11234 C CA  . LYS D 127 ? 0.5480 0.4583 0.4991 0.0697  -0.0179 0.0377  428 LYS D CA  
11235 C C   . LYS D 127 ? 0.6549 0.5835 0.6184 0.0620  -0.0193 0.0381  428 LYS D C   
11236 O O   . LYS D 127 ? 0.8218 0.7694 0.7950 0.0630  -0.0212 0.0366  428 LYS D O   
11237 C CB  . LYS D 127 ? 0.5755 0.4983 0.5298 0.0811  -0.0193 0.0355  428 LYS D CB  
11238 C CG  . LYS D 127 ? 0.7020 0.6086 0.6430 0.0942  -0.0189 0.0362  428 LYS D CG  
11239 C CD  . LYS D 127 ? 0.9206 0.8488 0.8678 0.1071  -0.0215 0.0352  428 LYS D CD  
11240 C CE  . LYS D 127 ? 0.9596 0.8805 0.8968 0.1201  -0.0238 0.0394  428 LYS D CE  
11241 N NZ  . LYS D 127 ? 0.7504 0.6731 0.6872 0.1153  -0.0259 0.0441  428 LYS D NZ  
11242 N N   . LEU D 128 ? 0.5805 0.5025 0.5426 0.0539  -0.0182 0.0398  429 LEU D N   
11243 C CA  . LEU D 128 ? 0.5048 0.4404 0.4761 0.0480  -0.0192 0.0401  429 LEU D CA  
11244 C C   . LEU D 128 ? 0.5963 0.5281 0.5620 0.0493  -0.0194 0.0433  429 LEU D C   
11245 O O   . LEU D 128 ? 0.6401 0.5558 0.5948 0.0494  -0.0177 0.0457  429 LEU D O   
11246 C CB  . LEU D 128 ? 0.3002 0.2355 0.2758 0.0385  -0.0176 0.0388  429 LEU D CB  
11247 C CG  . LEU D 128 ? 0.3884 0.3361 0.3728 0.0342  -0.0187 0.0387  429 LEU D CG  
11248 C CD1 . LEU D 128 ? 0.3228 0.2840 0.3150 0.0356  -0.0211 0.0371  429 LEU D CD1 
11249 C CD2 . LEU D 128 ? 0.2824 0.2302 0.2700 0.0268  -0.0172 0.0380  429 LEU D CD2 
11250 N N   . GLN D 129 ? 0.4511 0.3967 0.4229 0.0495  -0.0214 0.0433  430 GLN D N   
11251 C CA  . GLN D 129 ? 0.4710 0.4155 0.4376 0.0504  -0.0218 0.0459  430 GLN D CA  
11252 C C   . GLN D 129 ? 0.5255 0.4736 0.4964 0.0426  -0.0203 0.0450  430 GLN D C   
11253 O O   . GLN D 129 ? 0.4979 0.4574 0.4771 0.0403  -0.0216 0.0427  430 GLN D O   
11254 C CB  . GLN D 129 ? 0.4631 0.4211 0.4317 0.0564  -0.0252 0.0460  430 GLN D CB  
11255 C CG  . GLN D 129 ? 0.5812 0.5382 0.5429 0.0577  -0.0260 0.0487  430 GLN D CG  
11256 C CD  . GLN D 129 ? 0.6669 0.6056 0.6149 0.0616  -0.0247 0.0529  430 GLN D CD  
11257 O OE1 . GLN D 129 ? 0.7018 0.6330 0.6437 0.0696  -0.0256 0.0544  430 GLN D OE1 
11258 N NE2 . GLN D 129 ? 0.6873 0.6178 0.6291 0.0559  -0.0224 0.0548  430 GLN D NE2 
11259 N N   . VAL D 130 ? 0.5591 0.4972 0.5237 0.0384  -0.0176 0.0467  431 VAL D N   
11260 C CA  . VAL D 130 ? 0.5009 0.4443 0.4703 0.0318  -0.0156 0.0453  431 VAL D CA  
11261 C C   . VAL D 130 ? 0.6010 0.5479 0.5668 0.0323  -0.0155 0.0463  431 VAL D C   
11262 O O   . VAL D 130 ? 0.6864 0.6255 0.6419 0.0343  -0.0152 0.0495  431 VAL D O   
11263 C CB  . VAL D 130 ? 0.5165 0.4518 0.4824 0.0253  -0.0122 0.0459  431 VAL D CB  
11264 C CG1 . VAL D 130 ? 0.4465 0.3923 0.4195 0.0199  -0.0103 0.0439  431 VAL D CG1 
11265 C CG2 . VAL D 130 ? 0.6198 0.5508 0.5876 0.0245  -0.0124 0.0445  431 VAL D CG2 
11266 N N   . PHE D 131 ? 0.5116 0.4688 0.4844 0.0308  -0.0159 0.0435  432 PHE D N   
11267 C CA  . PHE D 131 ? 0.4381 0.3995 0.4077 0.0308  -0.0157 0.0431  432 PHE D CA  
11268 C C   . PHE D 131 ? 0.5135 0.4780 0.4855 0.0264  -0.0121 0.0414  432 PHE D C   
11269 O O   . PHE D 131 ? 0.5352 0.5058 0.5150 0.0260  -0.0121 0.0381  432 PHE D O   
11270 C CB  . PHE D 131 ? 0.5520 0.5217 0.5259 0.0328  -0.0189 0.0406  432 PHE D CB  
11271 C CG  . PHE D 131 ? 0.5004 0.4725 0.4719 0.0372  -0.0223 0.0421  432 PHE D CG  
11272 C CD1 . PHE D 131 ? 0.5176 0.4879 0.4803 0.0407  -0.0233 0.0451  432 PHE D CD1 
11273 C CD2 . PHE D 131 ? 0.4086 0.3865 0.3864 0.0381  -0.0247 0.0405  432 PHE D CD2 
11274 C CE1 . PHE D 131 ? 0.4531 0.4287 0.4145 0.0463  -0.0268 0.0464  432 PHE D CE1 
11275 C CE2 . PHE D 131 ? 0.3863 0.3707 0.3631 0.0426  -0.0276 0.0415  432 PHE D CE2 
11276 C CZ  . PHE D 131 ? 0.4282 0.4121 0.3972 0.0473  -0.0288 0.0443  432 PHE D CZ  
11277 N N   . ASP D 132 ? 0.5115 0.4719 0.4759 0.0234  -0.0090 0.0435  433 ASP D N   
11278 C CA  . ASP D 132 ? 0.4641 0.4309 0.4307 0.0189  -0.0049 0.0417  433 ASP D CA  
11279 C C   . ASP D 132 ? 0.4739 0.4485 0.4417 0.0211  -0.0047 0.0384  433 ASP D C   
11280 O O   . ASP D 132 ? 0.6642 0.6374 0.6238 0.0216  -0.0046 0.0394  433 ASP D O   
11281 C CB  . ASP D 132 ? 0.4334 0.3937 0.3895 0.0137  -0.0014 0.0451  433 ASP D CB  
11282 C CG  . ASP D 132 ? 0.5095 0.4796 0.4692 0.0076  0.0032  0.0431  433 ASP D CG  
11283 O OD1 . ASP D 132 ? 0.5668 0.5318 0.5186 0.0008  0.0064  0.0458  433 ASP D OD1 
11284 O OD2 . ASP D 132 ? 0.4550 0.4378 0.4246 0.0097  0.0036  0.0389  433 ASP D OD2 
11285 N N   . ALA D 133 ? 0.3818 0.3634 0.3585 0.0226  -0.0048 0.0344  434 ALA D N   
11286 C CA  . ALA D 133 ? 0.4574 0.4434 0.4340 0.0252  -0.0043 0.0304  434 ALA D CA  
11287 C C   . ALA D 133 ? 0.5049 0.5004 0.4861 0.0250  -0.0002 0.0274  434 ALA D C   
11288 O O   . ALA D 133 ? 0.3706 0.3693 0.3544 0.0290  0.0002  0.0230  434 ALA D O   
11289 C CB  . ALA D 133 ? 0.6295 0.6131 0.6099 0.0284  -0.0081 0.0280  434 ALA D CB  
11290 N N   . ARG D 134 ? 0.4331 0.4331 0.4145 0.0203  0.0031  0.0293  435 ARG D N   
11291 C CA  . ARG D 134 ? 0.4001 0.4139 0.3874 0.0197  0.0072  0.0263  435 ARG D CA  
11292 C C   . ARG D 134 ? 0.5282 0.5483 0.5105 0.0207  0.0110  0.0233  435 ARG D C   
11293 O O   . ARG D 134 ? 0.5693 0.6035 0.5572 0.0219  0.0145  0.0198  435 ARG D O   
11294 C CB  . ARG D 134 ? 0.3767 0.3945 0.3648 0.0121  0.0097  0.0292  435 ARG D CB  
11295 C CG  . ARG D 134 ? 0.4386 0.4543 0.4340 0.0121  0.0064  0.0302  435 ARG D CG  
11296 C CD  . ARG D 134 ? 0.4767 0.4930 0.4704 0.0033  0.0084  0.0327  435 ARG D CD  
11297 N NE  . ARG D 134 ? 0.5277 0.5295 0.5081 -0.0016 0.0095  0.0368  435 ARG D NE  
11298 C CZ  . ARG D 134 ? 0.5161 0.5149 0.4898 -0.0110 0.0126  0.0392  435 ARG D CZ  
11299 N NH1 . ARG D 134 ? 0.6048 0.6174 0.5853 -0.0172 0.0149  0.0373  435 ARG D NH1 
11300 N NH2 . ARG D 134 ? 0.4942 0.4762 0.4533 -0.0143 0.0132  0.0434  435 ARG D NH2 
11301 N N   . ASP D 135 ? 0.6168 0.6287 0.5890 0.0207  0.0102  0.0242  436 ASP D N   
11302 C CA  . ASP D 135 ? 0.6153 0.6326 0.5813 0.0215  0.0137  0.0209  436 ASP D CA  
11303 C C   . ASP D 135 ? 0.5894 0.6038 0.5556 0.0282  0.0119  0.0155  436 ASP D C   
11304 O O   . ASP D 135 ? 0.5873 0.6051 0.5476 0.0295  0.0147  0.0116  436 ASP D O   
11305 C CB  . ASP D 135 ? 0.4924 0.5033 0.4451 0.0168  0.0141  0.0250  436 ASP D CB  
11306 C CG  . ASP D 135 ? 0.5712 0.5700 0.5186 0.0188  0.0084  0.0276  436 ASP D CG  
11307 O OD1 . ASP D 135 ? 0.6554 0.6499 0.5916 0.0171  0.0079  0.0305  436 ASP D OD1 
11308 O OD2 . ASP D 135 ? 0.6887 0.6835 0.6427 0.0221  0.0044  0.0270  436 ASP D OD2 
11309 N N   . CYS D 136 ? 0.6146 0.6223 0.5862 0.0319  0.0076  0.0148  437 CYS D N   
11310 C CA  . CYS D 136 ? 0.5042 0.5052 0.4736 0.0370  0.0057  0.0100  437 CYS D CA  
11311 C C   . CYS D 136 ? 0.6652 0.6734 0.6384 0.0433  0.0093  0.0043  437 CYS D C   
11312 O O   . CYS D 136 ? 0.7519 0.7712 0.7341 0.0449  0.0113  0.0047  437 CYS D O   
11313 C CB  . CYS D 136 ? 0.3329 0.3247 0.3061 0.0379  0.0004  0.0115  437 CYS D CB  
11314 S SG  . CYS D 136 ? 0.4713 0.4495 0.4374 0.0401  -0.0029 0.0071  437 CYS D SG  
11315 N N   . THR D 137 ? 0.5982 0.6009 0.5639 0.0471  0.0103  -0.0012 438 THR D N   
11316 C CA  . THR D 137 ? 0.4837 0.4921 0.4514 0.0552  0.0140  -0.0073 438 THR D CA  
11317 C C   . THR D 137 ? 0.4539 0.4461 0.4161 0.0619  0.0116  -0.0122 438 THR D C   
11318 O O   . THR D 137 ? 0.4529 0.4472 0.4169 0.0711  0.0139  -0.0170 438 THR D O   
11319 C CB  . THR D 137 ? 0.5832 0.6026 0.5453 0.0545  0.0199  -0.0108 438 THR D CB  
11320 O OG1 . THR D 137 ? 0.4106 0.4184 0.3595 0.0532  0.0194  -0.0143 438 THR D OG1 
11321 C CG2 . THR D 137 ? 0.5070 0.5383 0.4705 0.0458  0.0222  -0.0053 438 THR D CG2 
11322 N N   . THR D 138 ? 0.4786 0.4549 0.4335 0.0576  0.0072  -0.0113 439 THR D N   
11323 C CA  . THR D 138 ? 0.5104 0.4679 0.4559 0.0612  0.0052  -0.0162 439 THR D CA  
11324 C C   . THR D 138 ? 0.5527 0.4978 0.4973 0.0558  -0.0006 -0.0124 439 THR D C   
11325 O O   . THR D 138 ? 0.4345 0.3851 0.3827 0.0488  -0.0030 -0.0071 439 THR D O   
11326 C CB  . THR D 138 ? 0.5874 0.5379 0.5188 0.0586  0.0069  -0.0216 439 THR D CB  
11327 O OG1 . THR D 138 ? 0.6253 0.5769 0.5530 0.0488  0.0039  -0.0178 439 THR D OG1 
11328 C CG2 . THR D 138 ? 0.4400 0.4038 0.3706 0.0627  0.0131  -0.0257 439 THR D CG2 
11329 N N   . ALA D 139 ? 0.5542 0.4814 0.4923 0.0593  -0.0026 -0.0154 440 ALA D N   
11330 C CA  . ALA D 139 ? 0.5817 0.4965 0.5171 0.0532  -0.0076 -0.0124 440 ALA D CA  
11331 C C   . ALA D 139 ? 0.6812 0.5978 0.6112 0.0426  -0.0097 -0.0114 440 ALA D C   
11332 O O   . ALA D 139 ? 0.7120 0.6329 0.6469 0.0367  -0.0130 -0.0065 440 ALA D O   
11333 C CB  . ALA D 139 ? 0.6104 0.5017 0.5343 0.0570  -0.0089 -0.0166 440 ALA D CB  
11334 N N   . HIS D 140 ? 0.6151 0.5299 0.5349 0.0405  -0.0078 -0.0161 441 HIS D N   
11335 C CA  . HIS D 140 ? 0.4894 0.4090 0.4039 0.0312  -0.0101 -0.0152 441 HIS D CA  
11336 C C   . HIS D 140 ? 0.4907 0.4282 0.4156 0.0294  -0.0108 -0.0086 441 HIS D C   
11337 O O   . HIS D 140 ? 0.5450 0.4871 0.4712 0.0235  -0.0146 -0.0050 441 HIS D O   
11338 C CB  . HIS D 140 ? 0.5257 0.4432 0.4278 0.0301  -0.0075 -0.0213 441 HIS D CB  
11339 C CG  . HIS D 140 ? 0.4495 0.3465 0.3367 0.0274  -0.0083 -0.0281 441 HIS D CG  
11340 N ND1 . HIS D 140 ? 0.5626 0.4433 0.4434 0.0354  -0.0055 -0.0336 441 HIS D ND1 
11341 C CD2 . HIS D 140 ? 0.4870 0.3760 0.3632 0.0173  -0.0117 -0.0302 441 HIS D CD2 
11342 C CE1 . HIS D 140 ? 0.6215 0.4816 0.4864 0.0302  -0.0069 -0.0389 441 HIS D CE1 
11343 N NE2 . HIS D 140 ? 0.5057 0.3713 0.3677 0.0181  -0.0106 -0.0371 441 HIS D NE2 
11344 N N   . GLY D 141 ? 0.5334 0.4812 0.4650 0.0344  -0.0071 -0.0070 442 GLY D N   
11345 C CA  . GLY D 141 ? 0.5696 0.5301 0.5090 0.0326  -0.0075 -0.0005 442 GLY D CA  
11346 C C   . GLY D 141 ? 0.6263 0.5865 0.5744 0.0316  -0.0109 0.0042  442 GLY D C   
11347 O O   . GLY D 141 ? 0.5506 0.5161 0.5005 0.0282  -0.0135 0.0086  442 GLY D O   
11348 N N   . MET D 142 ? 0.6211 0.5748 0.5737 0.0352  -0.0111 0.0032  443 MET D N   
11349 C CA  . MET D 142 ? 0.4946 0.4477 0.4545 0.0340  -0.0142 0.0072  443 MET D CA  
11350 C C   . MET D 142 ? 0.5096 0.4586 0.4650 0.0276  -0.0183 0.0078  443 MET D C   
11351 O O   . MET D 142 ? 0.4210 0.3765 0.3816 0.0251  -0.0205 0.0119  443 MET D O   
11352 C CB  . MET D 142 ? 0.5313 0.4773 0.4945 0.0393  -0.0140 0.0059  443 MET D CB  
11353 C CG  . MET D 142 ? 0.3790 0.3352 0.3512 0.0450  -0.0109 0.0068  443 MET D CG  
11354 S SD  . MET D 142 ? 0.5998 0.5487 0.5733 0.0543  -0.0108 0.0040  443 MET D SD  
11355 C CE  . MET D 142 ? 0.3186 0.2623 0.2967 0.0517  -0.0156 0.0089  443 MET D CE  
11356 N N   . PHE D 143 ? 0.4985 0.4373 0.4437 0.0247  -0.0192 0.0033  444 PHE D N   
11357 C CA  . PHE D 143 ? 0.4601 0.3980 0.4003 0.0167  -0.0229 0.0032  444 PHE D CA  
11358 C C   . PHE D 143 ? 0.5721 0.5255 0.5144 0.0140  -0.0243 0.0061  444 PHE D C   
11359 O O   . PHE D 143 ? 0.6975 0.6587 0.6437 0.0105  -0.0273 0.0089  444 PHE D O   
11360 C CB  . PHE D 143 ? 0.5561 0.4802 0.4825 0.0126  -0.0230 -0.0029 444 PHE D CB  
11361 C CG  . PHE D 143 ? 0.6403 0.5665 0.5606 0.0023  -0.0266 -0.0037 444 PHE D CG  
11362 C CD1 . PHE D 143 ? 0.7333 0.6664 0.6465 -0.0024 -0.0273 -0.0063 444 PHE D CD1 
11363 C CD2 . PHE D 143 ? 0.5464 0.4698 0.4679 -0.0033 -0.0292 -0.0019 444 PHE D CD2 
11364 C CE1 . PHE D 143 ? 0.6831 0.6220 0.5913 -0.0126 -0.0308 -0.0074 444 PHE D CE1 
11365 C CE2 . PHE D 143 ? 0.6024 0.5313 0.5189 -0.0139 -0.0322 -0.0029 444 PHE D CE2 
11366 C CZ  . PHE D 143 ? 0.7327 0.6703 0.6430 -0.0185 -0.0331 -0.0058 444 PHE D CZ  
11367 N N   . ASN D 144 ? 0.5556 0.5142 0.4951 0.0163  -0.0222 0.0056  445 ASN D N   
11368 C CA  . ASN D 144 ? 0.4828 0.4541 0.4225 0.0154  -0.0237 0.0091  445 ASN D CA  
11369 C C   . ASN D 144 ? 0.4871 0.4647 0.4367 0.0187  -0.0243 0.0150  445 ASN D C   
11370 O O   . ASN D 144 ? 0.5223 0.5079 0.4743 0.0176  -0.0274 0.0178  445 ASN D O   
11371 C CB  . ASN D 144 ? 0.6169 0.5901 0.5503 0.0174  -0.0207 0.0079  445 ASN D CB  
11372 C CG  . ASN D 144 ? 0.6251 0.6092 0.5554 0.0170  -0.0227 0.0119  445 ASN D CG  
11373 O OD1 . ASN D 144 ? 0.5520 0.5431 0.4798 0.0136  -0.0268 0.0122  445 ASN D OD1 
11374 N ND2 . ASN D 144 ? 0.6754 0.6615 0.6051 0.0203  -0.0198 0.0151  445 ASN D ND2 
11375 N N   . TYR D 145 ? 0.4990 0.4736 0.4540 0.0228  -0.0211 0.0165  446 TYR D N   
11376 C CA  . TYR D 145 ? 0.5922 0.5702 0.5549 0.0250  -0.0213 0.0213  446 TYR D CA  
11377 C C   . TYR D 145 ? 0.5702 0.5488 0.5383 0.0234  -0.0243 0.0222  446 TYR D C   
11378 O O   . TYR D 145 ? 0.4160 0.3997 0.3878 0.0245  -0.0258 0.0257  446 TYR D O   
11379 C CB  . TYR D 145 ? 0.5949 0.5706 0.5625 0.0278  -0.0175 0.0216  446 TYR D CB  
11380 C CG  . TYR D 145 ? 0.5206 0.4995 0.4855 0.0285  -0.0144 0.0239  446 TYR D CG  
11381 C CD1 . TYR D 145 ? 0.3659 0.3460 0.3282 0.0292  -0.0104 0.0211  446 TYR D CD1 
11382 C CD2 . TYR D 145 ? 0.4504 0.4303 0.4141 0.0285  -0.0151 0.0288  446 TYR D CD2 
11383 C CE1 . TYR D 145 ? 0.3150 0.2986 0.2738 0.0282  -0.0072 0.0234  446 TYR D CE1 
11384 C CE2 . TYR D 145 ? 0.4644 0.4442 0.4232 0.0280  -0.0122 0.0314  446 TYR D CE2 
11385 C CZ  . TYR D 145 ? 0.4246 0.4068 0.3809 0.0270  -0.0082 0.0289  446 TYR D CZ  
11386 O OH  . TYR D 145 ? 0.5587 0.5412 0.5090 0.0248  -0.0049 0.0318  446 TYR D OH  
11387 N N   . ILE D 146 ? 0.4945 0.4667 0.4619 0.0209  -0.0251 0.0191  447 ILE D N   
11388 C CA  . ILE D 146 ? 0.5987 0.5714 0.5704 0.0184  -0.0275 0.0202  447 ILE D CA  
11389 C C   . ILE D 146 ? 0.5577 0.5394 0.5270 0.0138  -0.0307 0.0201  447 ILE D C   
11390 O O   . ILE D 146 ? 0.4883 0.4776 0.4628 0.0133  -0.0323 0.0223  447 ILE D O   
11391 C CB  . ILE D 146 ? 0.5335 0.4942 0.5033 0.0172  -0.0274 0.0178  447 ILE D CB  
11392 C CG1 . ILE D 146 ? 0.4446 0.4025 0.4205 0.0227  -0.0252 0.0192  447 ILE D CG1 
11393 C CG2 . ILE D 146 ? 0.3843 0.3445 0.3541 0.0117  -0.0301 0.0183  447 ILE D CG2 
11394 C CD1 . ILE D 146 ? 0.4938 0.4395 0.4668 0.0245  -0.0252 0.0170  447 ILE D CD1 
11395 N N   . CYS D 147 ? 0.6258 0.6088 0.5875 0.0105  -0.0316 0.0173  448 CYS D N   
11396 C CA  . CYS D 147 ? 0.5201 0.5157 0.4800 0.0056  -0.0349 0.0168  448 CYS D CA  
11397 C C   . CYS D 147 ? 0.5926 0.6022 0.5573 0.0110  -0.0362 0.0210  448 CYS D C   
11398 O O   . CYS D 147 ? 0.5803 0.6035 0.5481 0.0097  -0.0389 0.0217  448 CYS D O   
11399 C CB  . CYS D 147 ? 0.4679 0.4627 0.4177 0.0009  -0.0356 0.0128  448 CYS D CB  
11400 S SG  . CYS D 147 ? 0.6030 0.5835 0.5431 -0.0089 -0.0359 0.0071  448 CYS D SG  
11401 N N   . ASN D 148 ? 0.6125 0.6189 0.5767 0.0173  -0.0342 0.0235  449 ASN D N   
11402 C CA  . ASN D 148 ? 0.5228 0.5377 0.4888 0.0232  -0.0355 0.0278  449 ASN D CA  
11403 C C   . ASN D 148 ? 0.4704 0.4842 0.4439 0.0266  -0.0349 0.0303  449 ASN D C   
11404 O O   . ASN D 148 ? 0.4682 0.4910 0.4440 0.0309  -0.0368 0.0325  449 ASN D O   
11405 C CB  . ASN D 148 ? 0.5932 0.6025 0.5532 0.0272  -0.0334 0.0302  449 ASN D CB  
11406 C CG  . ASN D 148 ? 0.5806 0.5923 0.5320 0.0240  -0.0340 0.0276  449 ASN D CG  
11407 O OD1 . ASN D 148 ? 0.5602 0.5813 0.5094 0.0200  -0.0372 0.0252  449 ASN D OD1 
11408 N ND2 . ASN D 148 ? 0.5158 0.5201 0.4619 0.0251  -0.0308 0.0278  449 ASN D ND2 
11409 N N   . HIS D 149 ? 0.5474 0.5510 0.5243 0.0252  -0.0324 0.0295  450 HIS D N   
11410 C CA  . HIS D 149 ? 0.4124 0.4154 0.3958 0.0266  -0.0321 0.0308  450 HIS D CA  
11411 C C   . HIS D 149 ? 0.4806 0.4950 0.4672 0.0235  -0.0347 0.0297  450 HIS D C   
11412 O O   . HIS D 149 ? 0.5466 0.5697 0.5365 0.0275  -0.0357 0.0312  450 HIS D O   
11413 C CB  . HIS D 149 ? 0.4601 0.4526 0.4461 0.0247  -0.0298 0.0298  450 HIS D CB  
11414 C CG  . HIS D 149 ? 0.5603 0.5519 0.5521 0.0256  -0.0294 0.0312  450 HIS D CG  
11415 N ND1 . HIS D 149 ? 0.5349 0.5197 0.5292 0.0267  -0.0271 0.0320  450 HIS D ND1 
11416 C CD2 . HIS D 149 ? 0.6007 0.5987 0.5959 0.0250  -0.0308 0.0315  450 HIS D CD2 
11417 C CE1 . HIS D 149 ? 0.5960 0.5816 0.5943 0.0266  -0.0275 0.0328  450 HIS D CE1 
11418 N NE2 . HIS D 149 ? 0.5136 0.5069 0.5125 0.0259  -0.0295 0.0325  450 HIS D NE2 
11419 N N   . VAL D 150 ? 0.4096 0.4240 0.3941 0.0163  -0.0357 0.0266  451 VAL D N   
11420 C CA  . VAL D 150 ? 0.3374 0.3632 0.3238 0.0107  -0.0378 0.0253  451 VAL D CA  
11421 C C   . VAL D 150 ? 0.5075 0.5526 0.4956 0.0137  -0.0403 0.0260  451 VAL D C   
11422 O O   . VAL D 150 ? 0.6599 0.7175 0.6534 0.0156  -0.0410 0.0266  451 VAL D O   
11423 C CB  . VAL D 150 ? 0.3940 0.4137 0.3740 0.0012  -0.0385 0.0218  451 VAL D CB  
11424 C CG1 . VAL D 150 ? 0.3134 0.3481 0.2938 -0.0069 -0.0408 0.0203  451 VAL D CG1 
11425 C CG2 . VAL D 150 ? 0.3347 0.3361 0.3133 0.0003  -0.0367 0.0216  451 VAL D CG2 
11426 N N   . LYS D 151 ? 0.5950 0.6436 0.5782 0.0152  -0.0415 0.0259  452 LYS D N   
11427 C CA  . LYS D 151 ? 0.5541 0.6230 0.5381 0.0185  -0.0446 0.0266  452 LYS D CA  
11428 C C   . LYS D 151 ? 0.4531 0.5253 0.4409 0.0300  -0.0445 0.0303  452 LYS D C   
11429 O O   . LYS D 151 ? 0.5129 0.6035 0.5050 0.0339  -0.0467 0.0305  452 LYS D O   
11430 C CB  . LYS D 151 ? 0.5732 0.6430 0.5495 0.0179  -0.0461 0.0261  452 LYS D CB  
11431 C CG  . LYS D 151 ? 0.5156 0.6079 0.4917 0.0219  -0.0502 0.0272  452 LYS D CG  
11432 C CD  . LYS D 151 ? 0.4570 0.5517 0.4246 0.0163  -0.0519 0.0250  452 LYS D CD  
11433 C CE  . LYS D 151 ? 0.5674 0.6888 0.5350 0.0170  -0.0568 0.0250  452 LYS D CE  
11434 N NZ  . LYS D 151 ? 0.5945 0.7194 0.5535 0.0075  -0.0585 0.0213  452 LYS D NZ  
11435 N N   . TYR D 152 ? 0.4539 0.5087 0.4395 0.0356  -0.0420 0.0329  453 TYR D N   
11436 C CA  . TYR D 152 ? 0.5122 0.5646 0.4984 0.0458  -0.0415 0.0363  453 TYR D CA  
11437 C C   . TYR D 152 ? 0.6258 0.6811 0.6189 0.0462  -0.0405 0.0352  453 TYR D C   
11438 O O   . TYR D 152 ? 0.5889 0.6544 0.5844 0.0538  -0.0415 0.0359  453 TYR D O   
11439 C CB  . TYR D 152 ? 0.5321 0.5639 0.5125 0.0486  -0.0386 0.0390  453 TYR D CB  
11440 C CG  . TYR D 152 ? 0.5874 0.6100 0.5665 0.0566  -0.0373 0.0419  453 TYR D CG  
11441 C CD1 . TYR D 152 ? 0.6306 0.6522 0.6030 0.0661  -0.0389 0.0454  453 TYR D CD1 
11442 C CD2 . TYR D 152 ? 0.5909 0.6047 0.5739 0.0549  -0.0347 0.0411  453 TYR D CD2 
11443 C CE1 . TYR D 152 ? 0.6597 0.6690 0.6282 0.0736  -0.0376 0.0478  453 TYR D CE1 
11444 C CE2 . TYR D 152 ? 0.6087 0.6123 0.5886 0.0614  -0.0334 0.0430  453 TYR D CE2 
11445 C CZ  . TYR D 152 ? 0.6203 0.6205 0.5925 0.0707  -0.0347 0.0462  453 TYR D CZ  
11446 O OH  . TYR D 152 ? 0.7863 0.7725 0.7528 0.0775  -0.0333 0.0479  453 TYR D OH  
11447 N N   . ALA D 153 ? 0.6031 0.6498 0.5989 0.0388  -0.0384 0.0335  454 ALA D N   
11448 C CA  . ALA D 153 ? 0.4454 0.4938 0.4465 0.0381  -0.0372 0.0325  454 ALA D CA  
11449 C C   . ALA D 153 ? 0.4791 0.5497 0.4849 0.0359  -0.0392 0.0304  454 ALA D C   
11450 O O   . ALA D 153 ? 0.5217 0.6013 0.5312 0.0414  -0.0389 0.0302  454 ALA D O   
11451 C CB  . ALA D 153 ? 0.3022 0.3379 0.3040 0.0305  -0.0354 0.0315  454 ALA D CB  
11452 N N   . THR D 154 ? 0.5403 0.6205 0.5451 0.0277  -0.0411 0.0285  455 THR D N   
11453 C CA  . THR D 154 ? 0.4804 0.5837 0.4893 0.0226  -0.0427 0.0261  455 THR D CA  
11454 C C   . THR D 154 ? 0.6759 0.8010 0.6882 0.0327  -0.0448 0.0266  455 THR D C   
11455 O O   . THR D 154 ? 0.8057 0.9500 0.8239 0.0341  -0.0448 0.0251  455 THR D O   
11456 C CB  . THR D 154 ? 0.3755 0.4816 0.3803 0.0100  -0.0442 0.0237  455 THR D CB  
11457 O OG1 . THR D 154 ? 0.3901 0.4746 0.3908 0.0025  -0.0423 0.0233  455 THR D OG1 
11458 C CG2 . THR D 154 ? 0.2631 0.3948 0.2715 0.0023  -0.0457 0.0211  455 THR D CG2 
11459 N N   . ASN D 155 ? 0.6329 0.7561 0.6411 0.0404  -0.0465 0.0288  456 ASN D N   
11460 C CA  . ASN D 155 ? 0.3540 0.4933 0.3632 0.0534  -0.0490 0.0304  456 ASN D CA  
11461 C C   . ASN D 155 ? 0.4252 0.5980 0.4418 0.0518  -0.0511 0.0276  456 ASN D C   
11462 O O   . ASN D 155 ? 0.4964 0.6843 0.5173 0.0632  -0.0517 0.0277  456 ASN D O   
11463 C CB  . ASN D 155 ? 0.3558 0.4800 0.3638 0.0659  -0.0468 0.0328  456 ASN D CB  
11464 C CG  . ASN D 155 ? 0.4780 0.6108 0.4836 0.0815  -0.0493 0.0353  456 ASN D CG  
11465 O OD1 . ASN D 155 ? 0.6746 0.8150 0.6764 0.0842  -0.0525 0.0371  456 ASN D OD1 
11466 N ND2 . ASN D 155 ? 0.4646 0.5948 0.4709 0.0924  -0.0478 0.0355  456 ASN D ND2 
11467 N N   . LYS D 156 ? 0.4885 0.6733 0.5059 0.0374  -0.0522 0.0246  457 LYS D N   
11468 C CA  . LYS D 156 ? 0.5235 0.7432 0.5471 0.0323  -0.0544 0.0216  457 LYS D CA  
11469 C C   . LYS D 156 ? 0.5156 0.7483 0.5469 0.0336  -0.0519 0.0198  457 LYS D C   
11470 O O   . LYS D 156 ? 0.4041 0.6682 0.4424 0.0388  -0.0533 0.0182  457 LYS D O   
11471 C CB  . LYS D 156 ? 0.6444 0.8884 0.6692 0.0429  -0.0588 0.0226  457 LYS D CB  
11472 C CG  . LYS D 156 ? 0.7366 0.9788 0.7543 0.0366  -0.0618 0.0229  457 LYS D CG  
11473 C CD  . LYS D 156 ? 0.9075 1.1842 0.9278 0.0424  -0.0669 0.0228  457 LYS D CD  
11474 C CE  . LYS D 156 ? 0.9897 1.2663 1.0095 0.0645  -0.0687 0.0273  457 LYS D CE  
11475 N NZ  . LYS D 156 ? 0.8763 1.1491 0.8874 0.0703  -0.0726 0.0307  457 LYS D NZ  
11476 N N   . GLY D 157 ? 0.5794 0.7898 0.6093 0.0286  -0.0483 0.0199  458 GLY D N   
11477 C CA  . GLY D 157 ? 0.4965 0.7160 0.5319 0.0282  -0.0456 0.0182  458 GLY D CA  
11478 C C   . GLY D 157 ? 0.6002 0.8052 0.6361 0.0428  -0.0433 0.0197  458 GLY D C   
11479 O O   . GLY D 157 ? 0.5938 0.7964 0.6318 0.0410  -0.0403 0.0184  458 GLY D O   
11480 N N   . ASN D 158 ? 0.3768 0.5703 0.4091 0.0563  -0.0446 0.0225  459 ASN D N   
11481 C CA  . ASN D 158 ? 0.5251 0.7026 0.5554 0.0699  -0.0424 0.0237  459 ASN D CA  
11482 C C   . ASN D 158 ? 0.6568 0.7989 0.6802 0.0665  -0.0404 0.0262  459 ASN D C   
11483 O O   . ASN D 158 ? 0.6221 0.7470 0.6392 0.0733  -0.0410 0.0292  459 ASN D O   
11484 C CB  . ASN D 158 ? 0.3308 0.5163 0.3593 0.0872  -0.0449 0.0255  459 ASN D CB  
11485 C CG  . ASN D 158 ? 0.5071 0.6750 0.5314 0.1013  -0.0425 0.0262  459 ASN D CG  
11486 O OD1 . ASN D 158 ? 0.6998 0.8511 0.7231 0.0975  -0.0390 0.0251  459 ASN D OD1 
11487 N ND2 . ASN D 158 ? 0.4553 0.6259 0.4758 0.1179  -0.0447 0.0281  459 ASN D ND2 
11488 N N   . LEU D 159 ? 0.7075 0.8400 0.7319 0.0561  -0.0379 0.0250  460 LEU D N   
11489 C CA  . LEU D 159 ? 0.5216 0.6267 0.5412 0.0503  -0.0366 0.0269  460 LEU D CA  
11490 C C   . LEU D 159 ? 0.5214 0.6046 0.5359 0.0598  -0.0349 0.0289  460 LEU D C   
11491 O O   . LEU D 159 ? 0.5601 0.6436 0.5745 0.0684  -0.0335 0.0281  460 LEU D O   
11492 C CB  . LEU D 159 ? 0.4796 0.5805 0.5007 0.0388  -0.0349 0.0255  460 LEU D CB  
11493 C CG  . LEU D 159 ? 0.6220 0.7434 0.6462 0.0280  -0.0360 0.0233  460 LEU D CG  
11494 C CD1 . LEU D 159 ? 0.8191 0.9306 0.8420 0.0174  -0.0344 0.0231  460 LEU D CD1 
11495 C CD2 . LEU D 159 ? 0.4973 0.6214 0.5189 0.0221  -0.0385 0.0235  460 LEU D CD2 
11496 N N   . ARG D 160 ? 0.4538 0.5178 0.4633 0.0575  -0.0346 0.0313  461 ARG D N   
11497 C CA  . ARG D 160 ? 0.5601 0.6018 0.5633 0.0629  -0.0328 0.0335  461 ARG D CA  
11498 C C   . ARG D 160 ? 0.6699 0.6960 0.6726 0.0540  -0.0310 0.0338  461 ARG D C   
11499 O O   . ARG D 160 ? 0.6736 0.7010 0.6777 0.0465  -0.0318 0.0336  461 ARG D O   
11500 C CB  . ARG D 160 ? 0.6161 0.6519 0.6125 0.0697  -0.0342 0.0365  461 ARG D CB  
11501 C CG  . ARG D 160 ? 0.5688 0.6229 0.5657 0.0791  -0.0371 0.0367  461 ARG D CG  
11502 C CD  . ARG D 160 ? 0.5707 0.6159 0.5587 0.0862  -0.0388 0.0407  461 ARG D CD  
11503 N NE  . ARG D 160 ? 0.4791 0.5360 0.4679 0.0810  -0.0414 0.0410  461 ARG D NE  
11504 C CZ  . ARG D 160 ? 0.6061 0.6639 0.5881 0.0873  -0.0440 0.0441  461 ARG D CZ  
11505 N NH1 . ARG D 160 ? 0.6763 0.7221 0.6500 0.0993  -0.0442 0.0475  461 ARG D NH1 
11506 N NH2 . ARG D 160 ? 0.5316 0.6000 0.5135 0.0815  -0.0462 0.0438  461 ARG D NH2 
11507 N N   . SER D 161 ? 0.6219 0.6333 0.6218 0.0551  -0.0287 0.0341  462 SER D N   
11508 C CA  . SER D 161 ? 0.6063 0.6056 0.6063 0.0477  -0.0272 0.0344  462 SER D CA  
11509 C C   . SER D 161 ? 0.4601 0.4504 0.4560 0.0467  -0.0269 0.0366  462 SER D C   
11510 O O   . SER D 161 ? 0.4087 0.3925 0.3981 0.0523  -0.0268 0.0386  462 SER D O   
11511 C CB  . SER D 161 ? 0.6583 0.6456 0.6554 0.0484  -0.0249 0.0339  462 SER D CB  
11512 O OG  . SER D 161 ? 0.7362 0.7292 0.7335 0.0536  -0.0245 0.0319  462 SER D OG  
11513 N N   . ALA D 162 ? 0.3260 0.3152 0.3245 0.0401  -0.0268 0.0362  463 ALA D N   
11514 C CA  . ALA D 162 ? 0.3541 0.3366 0.3490 0.0390  -0.0259 0.0376  463 ALA D CA  
11515 C C   . ALA D 162 ? 0.4025 0.3831 0.4011 0.0332  -0.0251 0.0365  463 ALA D C   
11516 O O   . ALA D 162 ? 0.4780 0.4632 0.4805 0.0301  -0.0263 0.0351  463 ALA D O   
11517 C CB  . ALA D 162 ? 0.3991 0.3887 0.3917 0.0409  -0.0278 0.0379  463 ALA D CB  
11518 N N   . ILE D 163 ? 0.5703 0.5444 0.5665 0.0321  -0.0231 0.0374  464 ILE D N   
11519 C CA  . ILE D 163 ? 0.4218 0.3958 0.4212 0.0287  -0.0221 0.0363  464 ILE D CA  
11520 C C   . ILE D 163 ? 0.4325 0.4057 0.4282 0.0290  -0.0207 0.0365  464 ILE D C   
11521 O O   . ILE D 163 ? 0.4250 0.3945 0.4148 0.0304  -0.0196 0.0384  464 ILE D O   
11522 C CB  . ILE D 163 ? 0.3793 0.3503 0.3806 0.0262  -0.0203 0.0366  464 ILE D CB  
11523 C CG1 . ILE D 163 ? 0.3285 0.3032 0.3344 0.0243  -0.0196 0.0355  464 ILE D CG1 
11524 C CG2 . ILE D 163 ? 0.2678 0.2317 0.2629 0.0259  -0.0179 0.0384  464 ILE D CG2 
11525 C CD1 . ILE D 163 ? 0.3989 0.3749 0.4079 0.0212  -0.0186 0.0355  464 ILE D CD1 
11526 N N   . THR D 164 ? 0.4301 0.4055 0.4279 0.0280  -0.0205 0.0346  465 THR D N   
11527 C CA  . THR D 164 ? 0.5675 0.5430 0.5619 0.0282  -0.0185 0.0338  465 THR D CA  
11528 C C   . THR D 164 ? 0.4951 0.4731 0.4939 0.0277  -0.0164 0.0323  465 THR D C   
11529 O O   . THR D 164 ? 0.4615 0.4400 0.4641 0.0287  -0.0178 0.0306  465 THR D O   
11530 C CB  . THR D 164 ? 0.5286 0.5051 0.5196 0.0287  -0.0202 0.0319  465 THR D CB  
11531 O OG1 . THR D 164 ? 0.5301 0.5086 0.5178 0.0295  -0.0223 0.0334  465 THR D OG1 
11532 C CG2 . THR D 164 ? 0.4069 0.3837 0.3937 0.0290  -0.0177 0.0307  465 THR D CG2 
11533 N N   . ILE D 165 ? 0.5361 0.5160 0.5337 0.0262  -0.0132 0.0330  466 ILE D N   
11534 C CA  . ILE D 165 ? 0.5080 0.4947 0.5110 0.0252  -0.0109 0.0318  466 ILE D CA  
11535 C C   . ILE D 165 ? 0.5899 0.5818 0.5915 0.0267  -0.0082 0.0294  466 ILE D C   
11536 O O   . ILE D 165 ? 0.5886 0.5800 0.5841 0.0247  -0.0058 0.0303  466 ILE D O   
11537 C CB  . ILE D 165 ? 0.4909 0.4777 0.4930 0.0202  -0.0088 0.0339  466 ILE D CB  
11538 C CG1 . ILE D 165 ? 0.4624 0.4429 0.4646 0.0194  -0.0112 0.0355  466 ILE D CG1 
11539 C CG2 . ILE D 165 ? 0.5124 0.5105 0.5207 0.0180  -0.0065 0.0325  466 ILE D CG2 
11540 C CD1 . ILE D 165 ? 0.4639 0.4402 0.4623 0.0140  -0.0091 0.0372  466 ILE D CD1 
11541 N N   . PHE D 166 ? 0.6142 0.6102 0.6203 0.0308  -0.0084 0.0264  467 PHE D N   
11542 C CA  . PHE D 166 ? 0.4936 0.4941 0.4983 0.0342  -0.0058 0.0230  467 PHE D CA  
11543 C C   . PHE D 166 ? 0.4601 0.4750 0.4710 0.0342  -0.0023 0.0218  467 PHE D C   
11544 O O   . PHE D 166 ? 0.5335 0.5539 0.5493 0.0306  -0.0024 0.0238  467 PHE D O   
11545 C CB  . PHE D 166 ? 0.5199 0.5136 0.5238 0.0398  -0.0084 0.0201  467 PHE D CB  
11546 C CG  . PHE D 166 ? 0.6111 0.5938 0.6078 0.0381  -0.0110 0.0202  467 PHE D CG  
11547 C CD1 . PHE D 166 ? 0.5321 0.5123 0.5213 0.0378  -0.0098 0.0181  467 PHE D CD1 
11548 C CD2 . PHE D 166 ? 0.6765 0.6535 0.6739 0.0362  -0.0147 0.0223  467 PHE D CD2 
11549 C CE1 . PHE D 166 ? 0.5444 0.5175 0.5273 0.0354  -0.0126 0.0179  467 PHE D CE1 
11550 C CE2 . PHE D 166 ? 0.6534 0.6241 0.6449 0.0338  -0.0171 0.0221  467 PHE D CE2 
11551 C CZ  . PHE D 166 ? 0.5608 0.5301 0.5453 0.0332  -0.0163 0.0199  467 PHE D CZ  
11552 N N   . PRO D 167 ? 0.6011 0.6241 0.6119 0.0376  0.0010  0.0183  468 PRO D N   
11553 C CA  . PRO D 167 ? 0.6163 0.6575 0.6336 0.0364  0.0049  0.0172  468 PRO D CA  
11554 C C   . PRO D 167 ? 0.5531 0.6040 0.5804 0.0391  0.0029  0.0172  468 PRO D C   
11555 O O   . PRO D 167 ? 0.5367 0.5827 0.5663 0.0465  -0.0005 0.0161  468 PRO D O   
11556 C CB  . PRO D 167 ? 0.5953 0.6429 0.6107 0.0424  0.0083  0.0123  468 PRO D CB  
11557 C CG  . PRO D 167 ? 0.4264 0.4592 0.4314 0.0417  0.0076  0.0122  468 PRO D CG  
11558 C CD  . PRO D 167 ? 0.5653 0.5829 0.5688 0.0411  0.0022  0.0151  468 PRO D CD  
11559 N N   . GLN D 168 ? 0.4961 0.5607 0.5283 0.0324  0.0049  0.0185  469 GLN D N   
11560 C CA  . GLN D 168 ? 0.3993 0.4758 0.4409 0.0336  0.0027  0.0186  469 GLN D CA  
11561 C C   . GLN D 168 ? 0.4630 0.5552 0.5121 0.0442  0.0031  0.0148  469 GLN D C   
11562 O O   . GLN D 168 ? 0.5323 0.6283 0.5796 0.0495  0.0062  0.0114  469 GLN D O   
11563 C CB  . GLN D 168 ? 0.3842 0.4735 0.4283 0.0225  0.0052  0.0201  469 GLN D CB  
11564 C CG  . GLN D 168 ? 0.4014 0.5115 0.4482 0.0200  0.0107  0.0174  469 GLN D CG  
11565 C CD  . GLN D 168 ? 0.4592 0.5696 0.4997 0.0057  0.0145  0.0197  469 GLN D CD  
11566 O OE1 . GLN D 168 ? 0.7425 0.8319 0.7726 0.0006  0.0140  0.0230  469 GLN D OE1 
11567 N NE2 . GLN D 168 ? 0.4024 0.5366 0.4483 -0.0008 0.0183  0.0181  469 GLN D NE2 
11568 N N   . ARG D 169 ? 0.6199 0.7216 0.6769 0.0480  -0.0002 0.0152  470 ARG D N   
11569 C CA  . ARG D 169 ? 0.5105 0.6282 0.5747 0.0600  -0.0004 0.0120  470 ARG D CA  
11570 C C   . ARG D 169 ? 0.4213 0.5669 0.4921 0.0572  0.0050  0.0090  470 ARG D C   
11571 O O   . ARG D 169 ? 0.5014 0.6561 0.5728 0.0443  0.0077  0.0104  470 ARG D O   
11572 C CB  . ARG D 169 ? 0.4835 0.6060 0.5539 0.0640  -0.0058 0.0140  470 ARG D CB  
11573 C CG  . ARG D 169 ? 0.6418 0.7763 0.7179 0.0795  -0.0075 0.0115  470 ARG D CG  
11574 C CD  . ARG D 169 ? 0.6317 0.7671 0.7114 0.0833  -0.0137 0.0146  470 ARG D CD  
11575 N NE  . ARG D 169 ? 0.6110 0.7166 0.6808 0.0879  -0.0179 0.0169  470 ARG D NE  
11576 C CZ  . ARG D 169 ? 0.9000 0.9974 0.9685 0.0864  -0.0229 0.0208  470 ARG D CZ  
11577 N NH1 . ARG D 169 ? 1.0174 1.1337 1.0937 0.0806  -0.0246 0.0225  470 ARG D NH1 
11578 N NH2 . ARG D 169 ? 0.9714 1.0420 1.0299 0.0892  -0.0262 0.0228  470 ARG D NH2 
11579 N N   . THR D 170 ? 0.4341 0.5925 0.5085 0.0692  0.0071  0.0046  471 THR D N   
11580 C CA  . THR D 170 ? 0.4622 0.6520 0.5441 0.0675  0.0127  0.0011  471 THR D CA  
11581 C C   . THR D 170 ? 0.5642 0.7806 0.6584 0.0798  0.0110  -0.0015 471 THR D C   
11582 O O   . THR D 170 ? 0.6433 0.8865 0.7473 0.0735  0.0112  -0.0010 471 THR D O   
11583 C CB  . THR D 170 ? 0.5232 0.7111 0.5987 0.0699  0.0184  -0.0029 471 THR D CB  
11584 O OG1 . THR D 170 ? 0.5877 0.7664 0.6606 0.0868  0.0173  -0.0068 471 THR D OG1 
11585 C CG2 . THR D 170 ? 0.4451 0.6084 0.5080 0.0587  0.0195  0.0000  471 THR D CG2 
11586 N N   . ASP D 171 ? 0.5274 0.7366 0.6204 0.0975  0.0092  -0.0043 472 ASP D N   
11587 C CA  . ASP D 171 ? 0.5291 0.7612 0.6324 0.1124  0.0068  -0.0063 472 ASP D CA  
11588 C C   . ASP D 171 ? 0.6143 0.8208 0.7117 0.1262  0.0001  -0.0043 472 ASP D C   
11589 O O   . ASP D 171 ? 0.7306 0.9466 0.8318 0.1435  -0.0018 -0.0066 472 ASP D O   
11590 C CB  . ASP D 171 ? 0.6161 0.8711 0.7237 0.1235  0.0125  -0.0130 472 ASP D CB  
11591 C CG  . ASP D 171 ? 0.7114 0.9390 0.8060 0.1309  0.0150  -0.0164 472 ASP D CG  
11592 O OD1 . ASP D 171 ? 0.7804 0.9800 0.8640 0.1204  0.0149  -0.0139 472 ASP D OD1 
11593 O OD2 . ASP D 171 ? 0.7571 0.9922 0.8522 0.1473  0.0172  -0.0219 472 ASP D OD2 
11594 N N   . GLY D 172 ? 0.5491 0.7235 0.6366 0.1190  -0.0035 -0.0001 473 GLY D N   
11595 C CA  . GLY D 172 ? 0.5786 0.7265 0.6584 0.1290  -0.0095 0.0024  473 GLY D CA  
11596 C C   . GLY D 172 ? 0.7242 0.8484 0.7925 0.1419  -0.0085 -0.0014 473 GLY D C   
11597 O O   . GLY D 172 ? 0.7711 0.8642 0.8279 0.1453  -0.0126 0.0007  473 GLY D O   
11598 N N   . LYS D 173 ? 0.6967 0.8347 0.7667 0.1481  -0.0029 -0.0072 474 LYS D N   
11599 C CA  . LYS D 173 ? 0.6908 0.8066 0.7488 0.1606  -0.0014 -0.0119 474 LYS D CA  
11600 C C   . LYS D 173 ? 0.6742 0.7664 0.7201 0.1495  0.0016  -0.0131 474 LYS D C   
11601 O O   . LYS D 173 ? 0.6744 0.7428 0.7076 0.1570  0.0022  -0.0168 474 LYS D O   
11602 C CB  . LYS D 173 ? 0.7332 0.8757 0.7980 0.1748  0.0034  -0.0186 474 LYS D CB  
11603 C CG  . LYS D 173 ? 0.8580 1.0371 0.9388 0.1836  0.0016  -0.0180 474 LYS D CG  
11604 C CD  . LYS D 173 ? 1.0017 1.1665 1.0798 0.1959  -0.0063 -0.0138 474 LYS D CD  
11605 C CE  . LYS D 173 ? 1.1477 1.2805 1.2106 0.2143  -0.0076 -0.0169 474 LYS D CE  
11606 N NZ  . LYS D 173 ? 1.2178 1.3708 1.2844 0.2318  -0.0026 -0.0247 474 LYS D NZ  
11607 N N   . HIS D 174 ? 0.7321 0.8297 0.7806 0.1322  0.0032  -0.0101 475 HIS D N   
11608 C CA  . HIS D 174 ? 0.6560 0.7359 0.6941 0.1218  0.0058  -0.0108 475 HIS D CA  
11609 C C   . HIS D 174 ? 0.6245 0.6905 0.6602 0.1078  0.0022  -0.0047 475 HIS D C   
11610 O O   . HIS D 174 ? 0.5859 0.6548 0.6209 0.0955  0.0046  -0.0031 475 HIS D O   
11611 C CB  . HIS D 174 ? 0.6933 0.7956 0.7350 0.1159  0.0127  -0.0140 475 HIS D CB  
11612 C CG  . HIS D 174 ? 0.7441 0.8650 0.7893 0.1295  0.0171  -0.0207 475 HIS D CG  
11613 N ND1 . HIS D 174 ? 0.7476 0.8957 0.8056 0.1392  0.0170  -0.0218 475 HIS D ND1 
11614 C CD2 . HIS D 174 ? 0.7853 0.9023 0.8226 0.1358  0.0218  -0.0271 475 HIS D CD2 
11615 C CE1 . HIS D 174 ? 0.7938 0.9550 0.8523 0.1518  0.0216  -0.0287 475 HIS D CE1 
11616 N NE2 . HIS D 174 ? 0.8322 0.9739 0.8778 0.1499  0.0248  -0.0321 475 HIS D NE2 
11617 N N   . ASP D 175 ? 0.6511 0.7022 0.6850 0.1101  -0.0035 -0.0012 476 ASP D N   
11618 C CA  . ASP D 175 ? 0.5864 0.6262 0.6187 0.0982  -0.0069 0.0042  476 ASP D CA  
11619 C C   . ASP D 175 ? 0.5921 0.6070 0.6117 0.0928  -0.0072 0.0038  476 ASP D C   
11620 O O   . ASP D 175 ? 0.6052 0.6028 0.6150 0.0997  -0.0075 0.0005  476 ASP D O   
11621 C CB  . ASP D 175 ? 0.7209 0.7543 0.7547 0.1022  -0.0127 0.0080  476 ASP D CB  
11622 C CG  . ASP D 175 ? 0.8584 0.9188 0.9053 0.1055  -0.0135 0.0092  476 ASP D CG  
11623 O OD1 . ASP D 175 ? 0.9878 1.0730 1.0433 0.1032  -0.0093 0.0071  476 ASP D OD1 
11624 O OD2 . ASP D 175 ? 0.8426 0.9002 0.8907 0.1096  -0.0184 0.0124  476 ASP D OD2 
11625 N N   . PHE D 176 ? 0.4620 0.4752 0.4811 0.0806  -0.0072 0.0070  477 PHE D N   
11626 C CA  . PHE D 176 ? 0.4085 0.4010 0.4175 0.0746  -0.0092 0.0079  477 PHE D CA  
11627 C C   . PHE D 176 ? 0.6567 0.6379 0.6650 0.0728  -0.0143 0.0118  477 PHE D C   
11628 O O   . PHE D 176 ? 0.5879 0.5793 0.6041 0.0708  -0.0159 0.0151  477 PHE D O   
11629 C CB  . PHE D 176 ? 0.4794 0.4765 0.4879 0.0643  -0.0072 0.0097  477 PHE D CB  
11630 C CG  . PHE D 176 ? 0.6684 0.6733 0.6743 0.0643  -0.0023 0.0063  477 PHE D CG  
11631 C CD1 . PHE D 176 ? 0.7638 0.7881 0.7767 0.0676  0.0017  0.0043  477 PHE D CD1 
11632 C CD2 . PHE D 176 ? 0.6706 0.6657 0.6669 0.0602  -0.0017 0.0051  477 PHE D CD2 
11633 C CE1 . PHE D 176 ? 0.7987 0.8312 0.8085 0.0667  0.0066  0.0013  477 PHE D CE1 
11634 C CE2 . PHE D 176 ? 0.6228 0.6251 0.6155 0.0598  0.0028  0.0022  477 PHE D CE2 
11635 C CZ  . PHE D 176 ? 0.7283 0.7487 0.7274 0.0629  0.0072  0.0003  477 PHE D CZ  
11636 N N   . ARG D 177 ? 0.6555 0.6159 0.6532 0.0722  -0.0168 0.0113  478 ARG D N   
11637 C CA  . ARG D 177 ? 0.4353 0.3841 0.4305 0.0701  -0.0213 0.0149  478 ARG D CA  
11638 C C   . ARG D 177 ? 0.5510 0.4825 0.5354 0.0626  -0.0228 0.0147  478 ARG D C   
11639 O O   . ARG D 177 ? 0.5970 0.5156 0.5713 0.0640  -0.0219 0.0110  478 ARG D O   
11640 C CB  . ARG D 177 ? 0.5874 0.5279 0.5796 0.0809  -0.0234 0.0145  478 ARG D CB  
11641 C CG  . ARG D 177 ? 0.6376 0.5979 0.6417 0.0875  -0.0237 0.0160  478 ARG D CG  
11642 C CD  . ARG D 177 ? 0.5699 0.5421 0.5823 0.0789  -0.0253 0.0204  478 ARG D CD  
11643 N NE  . ARG D 177 ? 0.6887 0.6481 0.6964 0.0764  -0.0298 0.0243  478 ARG D NE  
11644 C CZ  . ARG D 177 ? 0.7023 0.6616 0.7106 0.0830  -0.0333 0.0267  478 ARG D CZ  
11645 N NH1 . ARG D 177 ? 0.7464 0.7189 0.7607 0.0937  -0.0330 0.0254  478 ARG D NH1 
11646 N NH2 . ARG D 177 ? 0.6682 0.6154 0.6707 0.0791  -0.0370 0.0305  478 ARG D NH2 
11647 N N   . VAL D 178 ? 0.5284 0.4600 0.5142 0.0546  -0.0252 0.0184  479 VAL D N   
11648 C CA  . VAL D 178 ? 0.4648 0.3813 0.4406 0.0476  -0.0275 0.0186  479 VAL D CA  
11649 C C   . VAL D 178 ? 0.5452 0.4472 0.5151 0.0503  -0.0306 0.0206  479 VAL D C   
11650 O O   . VAL D 178 ? 0.7335 0.6412 0.7090 0.0500  -0.0325 0.0244  479 VAL D O   
11651 C CB  . VAL D 178 ? 0.5256 0.4510 0.5055 0.0386  -0.0282 0.0212  479 VAL D CB  
11652 C CG1 . VAL D 178 ? 0.5640 0.4785 0.5339 0.0307  -0.0299 0.0203  479 VAL D CG1 
11653 C CG2 . VAL D 178 ? 0.5334 0.4732 0.5194 0.0379  -0.0254 0.0206  479 VAL D CG2 
11654 N N   . TRP D 179 ? 0.5674 0.4489 0.5242 0.0530  -0.0312 0.0181  480 TRP D N   
11655 C CA  . TRP D 179 ? 0.5555 0.4188 0.5034 0.0558  -0.0344 0.0206  480 TRP D CA  
11656 C C   . TRP D 179 ? 0.6203 0.4779 0.5636 0.0441  -0.0370 0.0242  480 TRP D C   
11657 O O   . TRP D 179 ? 0.8457 0.6949 0.7850 0.0449  -0.0398 0.0280  480 TRP D O   
11658 C CB  . TRP D 179 ? 0.5089 0.3474 0.4410 0.0615  -0.0342 0.0168  480 TRP D CB  
11659 C CG  . TRP D 179 ? 0.4603 0.3034 0.3963 0.0761  -0.0322 0.0138  480 TRP D CG  
11660 C CD1 . TRP D 179 ? 0.4225 0.2906 0.3729 0.0806  -0.0291 0.0121  480 TRP D CD1 
11661 C CD2 . TRP D 179 ? 0.4641 0.2872 0.3888 0.0886  -0.0330 0.0120  480 TRP D CD2 
11662 N NE1 . TRP D 179 ? 0.4866 0.3547 0.4369 0.0949  -0.0277 0.0090  480 TRP D NE1 
11663 C CE2 . TRP D 179 ? 0.4870 0.3276 0.4219 0.1012  -0.0302 0.0088  480 TRP D CE2 
11664 C CE3 . TRP D 179 ? 0.5227 0.3139 0.4287 0.0906  -0.0358 0.0129  480 TRP D CE3 
11665 C CZ2 . TRP D 179 ? 0.6310 0.4605 0.5593 0.1171  -0.0301 0.0062  480 TRP D CZ2 
11666 C CZ3 . TRP D 179 ? 0.5840 0.3602 0.4817 0.1067  -0.0360 0.0106  480 TRP D CZ3 
11667 C CH2 . TRP D 179 ? 0.6142 0.4105 0.5237 0.1206  -0.0332 0.0071  480 TRP D CH2 
11668 N N   . ASN D 180 ? 0.6519 0.5153 0.5952 0.0335  -0.0362 0.0230  481 ASN D N   
11669 C CA  . ASN D 180 ? 0.6222 0.4871 0.5639 0.0224  -0.0380 0.0260  481 ASN D CA  
11670 C C   . ASN D 180 ? 0.6725 0.5542 0.6267 0.0238  -0.0387 0.0299  481 ASN D C   
11671 O O   . ASN D 180 ? 0.6855 0.5841 0.6518 0.0283  -0.0369 0.0296  481 ASN D O   
11672 C CB  . ASN D 180 ? 0.5286 0.4035 0.4712 0.0129  -0.0369 0.0238  481 ASN D CB  
11673 C CG  . ASN D 180 ? 0.6043 0.4660 0.5352 0.0106  -0.0361 0.0192  481 ASN D CG  
11674 O OD1 . ASN D 180 ? 0.6975 0.5607 0.6301 0.0175  -0.0340 0.0161  481 ASN D OD1 
11675 N ND2 . ASN D 180 ? 0.5688 0.4175 0.4870 -0.0001 -0.0374 0.0185  481 ASN D ND2 
11676 N N   . SER D 181 ? 0.6220 0.4985 0.5720 0.0187  -0.0410 0.0335  482 SER D N   
11677 C CA  . SER D 181 ? 0.5971 0.4894 0.5574 0.0182  -0.0416 0.0367  482 SER D CA  
11678 C C   . SER D 181 ? 0.6062 0.5160 0.5744 0.0114  -0.0399 0.0357  482 SER D C   
11679 O O   . SER D 181 ? 0.6657 0.5906 0.6445 0.0137  -0.0389 0.0363  482 SER D O   
11680 C CB  . SER D 181 ? 0.6699 0.5517 0.6221 0.0147  -0.0444 0.0408  482 SER D CB  
11681 O OG  . SER D 181 ? 0.7233 0.5949 0.6642 0.0034  -0.0449 0.0409  482 SER D OG  
11682 N N   . GLN D 182 ? 0.6403 0.5483 0.6027 0.0035  -0.0395 0.0338  483 GLN D N   
11683 C CA  . GLN D 182 ? 0.6598 0.5853 0.6294 -0.0004 -0.0381 0.0323  483 GLN D CA  
11684 C C   . GLN D 182 ? 0.6064 0.5293 0.5709 -0.0027 -0.0374 0.0289  483 GLN D C   
11685 O O   . GLN D 182 ? 0.7315 0.6373 0.6852 -0.0040 -0.0380 0.0273  483 GLN D O   
11686 C CB  . GLN D 182 ? 0.6391 0.5731 0.6084 -0.0091 -0.0387 0.0336  483 GLN D CB  
11687 C CG  . GLN D 182 ? 0.6630 0.5998 0.6357 -0.0081 -0.0394 0.0367  483 GLN D CG  
11688 C CD  . GLN D 182 ? 0.6897 0.6322 0.6589 -0.0178 -0.0398 0.0377  483 GLN D CD  
11689 O OE1 . GLN D 182 ? 0.5621 0.5187 0.5342 -0.0226 -0.0387 0.0358  483 GLN D OE1 
11690 N NE2 . GLN D 182 ? 0.6798 0.6124 0.6422 -0.0207 -0.0413 0.0408  483 GLN D NE2 
11691 N N   . LEU D 183 ? 0.6309 0.5696 0.6019 -0.0032 -0.0364 0.0275  484 LEU D N   
11692 C CA  . LEU D 183 ? 0.6353 0.5736 0.6015 -0.0052 -0.0360 0.0243  484 LEU D CA  
11693 C C   . LEU D 183 ? 0.6285 0.5652 0.5858 -0.0168 -0.0375 0.0228  484 LEU D C   
11694 O O   . LEU D 183 ? 0.6108 0.5338 0.5571 -0.0208 -0.0378 0.0201  484 LEU D O   
11695 C CB  . LEU D 183 ? 0.4353 0.3902 0.4097 -0.0011 -0.0349 0.0240  484 LEU D CB  
11696 C CG  . LEU D 183 ? 0.4406 0.3985 0.4227 0.0079  -0.0331 0.0254  484 LEU D CG  
11697 C CD1 . LEU D 183 ? 0.2963 0.2674 0.2830 0.0105  -0.0323 0.0258  484 LEU D CD1 
11698 C CD2 . LEU D 183 ? 0.3319 0.2791 0.3110 0.0128  -0.0317 0.0239  484 LEU D CD2 
11699 N N   . ILE D 184 ? 0.6459 0.5963 0.6069 -0.0228 -0.0381 0.0241  485 ILE D N   
11700 C CA  . ILE D 184 ? 0.5931 0.5441 0.5457 -0.0356 -0.0393 0.0229  485 ILE D CA  
11701 C C   . ILE D 184 ? 0.6302 0.5700 0.5774 -0.0404 -0.0398 0.0257  485 ILE D C   
11702 O O   . ILE D 184 ? 0.5702 0.5182 0.5252 -0.0366 -0.0394 0.0283  485 ILE D O   
11703 C CB  . ILE D 184 ? 0.4746 0.4528 0.4349 -0.0395 -0.0395 0.0220  485 ILE D CB  
11704 C CG1 . ILE D 184 ? 0.6424 0.6311 0.6080 -0.0323 -0.0394 0.0204  485 ILE D CG1 
11705 C CG2 . ILE D 184 ? 0.4911 0.4726 0.4426 -0.0543 -0.0405 0.0201  485 ILE D CG2 
11706 C CD1 . ILE D 184 ? 0.7515 0.7666 0.7275 -0.0293 -0.0397 0.0208  485 ILE D CD1 
11707 N N   . ARG D 185 ? 0.5772 0.4971 0.5093 -0.0492 -0.0406 0.0252  486 ARG D N   
11708 C CA  . ARG D 185 ? 0.6890 0.5916 0.6109 -0.0545 -0.0415 0.0283  486 ARG D CA  
11709 C C   . ARG D 185 ? 0.7096 0.5922 0.6126 -0.0675 -0.0422 0.0266  486 ARG D C   
11710 O O   . ARG D 185 ? 0.5899 0.4627 0.4863 -0.0676 -0.0421 0.0229  486 ARG D O   
11711 C CB  . ARG D 185 ? 0.7850 0.6695 0.7061 -0.0424 -0.0420 0.0310  486 ARG D CB  
11712 C CG  . ARG D 185 ? 0.7923 0.6916 0.7273 -0.0341 -0.0417 0.0337  486 ARG D CG  
11713 C CD  . ARG D 185 ? 0.8446 0.7263 0.7738 -0.0288 -0.0432 0.0374  486 ARG D CD  
11714 N NE  . ARG D 185 ? 1.0190 0.8995 0.9421 -0.0379 -0.0441 0.0408  486 ARG D NE  
11715 C CZ  . ARG D 185 ? 1.0214 0.8943 0.9422 -0.0340 -0.0457 0.0449  486 ARG D CZ  
11716 N NH1 . ARG D 185 ? 0.9857 0.8531 0.9106 -0.0211 -0.0467 0.0460  486 ARG D NH1 
11717 N NH2 . ARG D 185 ? 1.0000 0.8723 0.9140 -0.0434 -0.0463 0.0480  486 ARG D NH2 
11718 N N   . TYR D 186 ? 0.6356 0.5108 0.5284 -0.0791 -0.0427 0.0291  487 TYR D N   
11719 C CA  . TYR D 186 ? 0.5385 0.3927 0.4108 -0.0941 -0.0433 0.0276  487 TYR D CA  
11720 C C   . TYR D 186 ? 0.6720 0.4861 0.5257 -0.0904 -0.0445 0.0300  487 TYR D C   
11721 O O   . TYR D 186 ? 0.7988 0.6045 0.6549 -0.0796 -0.0453 0.0341  487 TYR D O   
11722 C CB  . TYR D 186 ? 0.4431 0.3115 0.3119 -0.1114 -0.0429 0.0288  487 TYR D CB  
11723 C CG  . TYR D 186 ? 0.5187 0.4278 0.4045 -0.1147 -0.0419 0.0261  487 TYR D CG  
11724 C CD1 . TYR D 186 ? 0.6255 0.5600 0.5244 -0.1135 -0.0409 0.0281  487 TYR D CD1 
11725 C CD2 . TYR D 186 ? 0.6892 0.6114 0.5771 -0.1185 -0.0420 0.0213  487 TYR D CD2 
11726 C CE1 . TYR D 186 ? 0.6592 0.6303 0.5729 -0.1144 -0.0401 0.0255  487 TYR D CE1 
11727 C CE2 . TYR D 186 ? 0.7025 0.6630 0.6057 -0.1199 -0.0416 0.0192  487 TYR D CE2 
11728 C CZ  . TYR D 186 ? 0.6511 0.6357 0.5673 -0.1171 -0.0406 0.0213  487 TYR D CZ  
11729 O OH  . TYR D 186 ? 0.4805 0.5028 0.4113 -0.1161 -0.0402 0.0191  487 TYR D OH  
11730 N N   . ALA D 187 ? 0.7327 0.5218 0.5670 -0.0992 -0.0447 0.0271  488 ALA D N   
11731 C CA  . ALA D 187 ? 0.7978 0.5456 0.6123 -0.0938 -0.0458 0.0285  488 ALA D CA  
11732 C C   . ALA D 187 ? 0.8807 0.6088 0.6791 -0.1033 -0.0470 0.0341  488 ALA D C   
11733 O O   . ALA D 187 ? 0.8924 0.6368 0.6915 -0.1184 -0.0466 0.0357  488 ALA D O   
11734 C CB  . ALA D 187 ? 0.8146 0.5389 0.6111 -0.1003 -0.0453 0.0228  488 ALA D CB  
11735 N N   . GLY D 188 ? 0.9378 0.6306 0.7208 -0.0939 -0.0487 0.0372  489 GLY D N   
11736 C CA  . GLY D 188 ? 0.9567 0.6241 0.7202 -0.1016 -0.0503 0.0432  489 GLY D CA  
11737 C C   . GLY D 188 ? 1.0422 0.6601 0.7760 -0.1018 -0.0515 0.0429  489 GLY D C   
11738 O O   . GLY D 188 ? 1.1021 0.7031 0.8342 -0.0845 -0.0520 0.0409  489 GLY D O   
11739 N N   . TYR D 189 ? 1.0035 0.5970 0.7124 -0.1215 -0.0516 0.0447  490 TYR D N   
11740 C CA  . TYR D 189 ? 0.9792 0.5205 0.6555 -0.1239 -0.0526 0.0443  490 TYR D CA  
11741 C C   . TYR D 189 ? 1.0757 0.5879 0.7291 -0.1321 -0.0546 0.0524  490 TYR D C   
11742 O O   . TYR D 189 ? 1.0704 0.5900 0.7166 -0.1545 -0.0536 0.0544  490 TYR D O   
11743 C CB  . TYR D 189 ? 0.9068 0.4401 0.5690 -0.1436 -0.0506 0.0373  490 TYR D CB  
11744 C CG  . TYR D 189 ? 0.9483 0.5193 0.6339 -0.1420 -0.0486 0.0299  490 TYR D CG  
11745 C CD1 . TYR D 189 ? 0.9491 0.5657 0.6546 -0.1549 -0.0474 0.0286  490 TYR D CD1 
11746 C CD2 . TYR D 189 ? 0.9622 0.5231 0.6488 -0.1275 -0.0480 0.0240  490 TYR D CD2 
11747 C CE1 . TYR D 189 ? 0.9852 0.6346 0.7102 -0.1526 -0.0461 0.0224  490 TYR D CE1 
11748 C CE2 . TYR D 189 ? 0.9806 0.5746 0.6865 -0.1266 -0.0464 0.0178  490 TYR D CE2 
11749 C CZ  . TYR D 189 ? 0.9854 0.6226 0.7099 -0.1390 -0.0457 0.0173  490 TYR D CZ  
11750 O OH  . TYR D 189 ? 1.0014 0.6701 0.7435 -0.1372 -0.0446 0.0117  490 TYR D OH  
11751 N N   . LYS D 190 ? 1.0470 0.5271 0.6882 -0.1142 -0.0574 0.0572  491 LYS D N   
11752 C CA  . LYS D 190 ? 1.0682 0.5117 0.6815 -0.1210 -0.0598 0.0654  491 LYS D CA  
11753 C C   . LYS D 190 ? 1.1896 0.5858 0.7671 -0.1354 -0.0591 0.0629  491 LYS D C   
11754 O O   . LYS D 190 ? 1.2731 0.6511 0.8438 -0.1275 -0.0582 0.0562  491 LYS D O   
11755 C CB  . LYS D 190 ? 1.1280 0.5568 0.7417 -0.0950 -0.0636 0.0716  491 LYS D CB  
11756 C CG  . LYS D 190 ? 1.2668 0.6931 0.8734 -0.0985 -0.0664 0.0818  491 LYS D CG  
11757 C CD  . LYS D 190 ? 1.3433 0.7768 0.9634 -0.0712 -0.0701 0.0866  491 LYS D CD  
11758 C CE  . LYS D 190 ? 1.3401 0.7507 0.9407 -0.0684 -0.0736 0.0953  491 LYS D CE  
11759 N NZ  . LYS D 190 ? 1.2548 0.6651 0.8634 -0.0397 -0.0776 0.0987  491 LYS D NZ  
11760 N N   . GLN D 191 ? 1.1826 0.5716 0.7427 -0.1546 -0.0586 0.0661  492 GLN D N   
11761 C CA  . GLN D 191 ? 1.2092 0.5685 0.7403 -0.1697 -0.0571 0.0625  492 GLN D CA  
11762 C C   . GLN D 191 ? 1.1652 0.4844 0.6724 -0.1562 -0.0595 0.0671  492 GLN D C   
11763 O O   . GLN D 191 ? 1.2971 0.6169 0.8110 -0.1389 -0.0625 0.0737  492 GLN D O   
11764 C CB  . GLN D 191 ? 1.2104 0.5897 0.7371 -0.2003 -0.0549 0.0630  492 GLN D CB  
11765 C CG  . GLN D 191 ? 1.2358 0.6630 0.7906 -0.2118 -0.0530 0.0605  492 GLN D CG  
11766 C CD  . GLN D 191 ? 1.3278 0.7646 0.8823 -0.2273 -0.0504 0.0513  492 GLN D CD  
11767 O OE1 . GLN D 191 ? 1.3482 0.7814 0.9100 -0.2158 -0.0504 0.0458  492 GLN D OE1 
11768 N NE2 . GLN D 191 ? 1.3126 0.7642 0.8588 -0.2537 -0.0481 0.0494  492 GLN D NE2 
11769 N N   . PRO D 192 ? 1.0534 0.3372 0.5319 -0.1635 -0.0586 0.0636  493 PRO D N   
11770 C CA  . PRO D 192 ? 1.2118 0.4558 0.6659 -0.1507 -0.0611 0.0682  493 PRO D CA  
11771 C C   . PRO D 192 ? 1.3638 0.6085 0.8099 -0.1596 -0.0629 0.0769  493 PRO D C   
11772 O O   . PRO D 192 ? 1.4020 0.6247 0.8376 -0.1435 -0.0661 0.0828  493 PRO D O   
11773 C CB  . PRO D 192 ? 1.1946 0.4032 0.6183 -0.1626 -0.0590 0.0621  493 PRO D CB  
11774 C CG  . PRO D 192 ? 1.1667 0.4020 0.5960 -0.1909 -0.0557 0.0570  493 PRO D CG  
11775 C CD  . PRO D 192 ? 1.0532 0.3301 0.5187 -0.1824 -0.0555 0.0554  493 PRO D CD  
11776 N N   . ASP D 193 ? 1.3272 0.5978 0.7774 -0.1851 -0.0610 0.0777  494 ASP D N   
11777 C CA  . ASP D 193 ? 1.2002 0.4746 0.6424 -0.1969 -0.0620 0.0851  494 ASP D CA  
11778 C C   . ASP D 193 ? 1.1813 0.4896 0.6510 -0.1861 -0.0637 0.0911  494 ASP D C   
11779 O O   . ASP D 193 ? 1.3516 0.6737 0.8203 -0.1982 -0.0639 0.0966  494 ASP D O   
11780 C CB  . ASP D 193 ? 1.2304 0.5193 0.6634 -0.2299 -0.0586 0.0824  494 ASP D CB  
11781 C CG  . ASP D 193 ? 1.3528 0.6900 0.8149 -0.2411 -0.0558 0.0778  494 ASP D CG  
11782 O OD1 . ASP D 193 ? 1.3360 0.7074 0.8113 -0.2540 -0.0547 0.0808  494 ASP D OD1 
11783 O OD2 . ASP D 193 ? 1.4842 0.8257 0.9557 -0.2367 -0.0546 0.0710  494 ASP D OD2 
11784 N N   . GLY D 194 ? 1.1182 0.4405 0.6115 -0.1641 -0.0649 0.0899  495 GLY D N   
11785 C CA  . GLY D 194 ? 1.1172 0.4705 0.6360 -0.1526 -0.0667 0.0953  495 GLY D CA  
11786 C C   . GLY D 194 ? 1.1329 0.5305 0.6759 -0.1675 -0.0640 0.0936  495 GLY D C   
11787 O O   . GLY D 194 ? 1.1691 0.5931 0.7358 -0.1555 -0.0653 0.0965  495 GLY D O   
11788 N N   . SER D 195 ? 1.1299 0.5384 0.6678 -0.1932 -0.0604 0.0891  496 SER D N   
11789 C CA  . SER D 195 ? 1.0896 0.5433 0.6519 -0.2068 -0.0576 0.0867  496 SER D CA  
11790 C C   . SER D 195 ? 1.1363 0.6032 0.7209 -0.1921 -0.0577 0.0823  496 SER D C   
11791 O O   . SER D 195 ? 1.1120 0.5536 0.6915 -0.1746 -0.0592 0.0795  496 SER D O   
11792 C CB  . SER D 195 ? 1.1120 0.5764 0.6647 -0.2357 -0.0539 0.0815  496 SER D CB  
11793 O OG  . SER D 195 ? 1.1607 0.5935 0.6929 -0.2385 -0.0535 0.0758  496 SER D OG  
11794 N N   . THR D 196 ? 1.1890 0.7070 0.8043 -0.1948 -0.0555 0.0793  497 THR D N   
11795 C CA  . THR D 196 ? 1.1599 0.7082 0.8056 -0.1764 -0.0549 0.0725  497 THR D CA  
11796 C C   . THR D 196 ? 1.1497 0.7400 0.8139 -0.1913 -0.0513 0.0651  497 THR D C   
11797 O O   . THR D 196 ? 1.1401 0.7646 0.8154 -0.2043 -0.0494 0.0658  497 THR D O   
11798 C CB  . THR D 196 ? 1.1845 0.7593 0.8558 -0.1545 -0.0565 0.0758  497 THR D CB  
11799 O OG1 . THR D 196 ? 1.2547 0.7927 0.9102 -0.1379 -0.0604 0.0821  497 THR D OG1 
11800 C CG2 . THR D 196 ? 1.2020 0.8093 0.9036 -0.1387 -0.0553 0.0688  497 THR D CG2 
11801 N N   . LEU D 197 ? 1.1665 0.7550 0.8337 -0.1882 -0.0505 0.0578  498 LEU D N   
11802 C CA  . LEU D 197 ? 0.9606 0.5875 0.6446 -0.1997 -0.0479 0.0506  498 LEU D CA  
11803 C C   . LEU D 197 ? 0.8636 0.5279 0.5814 -0.1788 -0.0477 0.0473  498 LEU D C   
11804 O O   . LEU D 197 ? 0.9079 0.5581 0.6300 -0.1577 -0.0491 0.0472  498 LEU D O   
11805 C CB  . LEU D 197 ? 0.9403 0.5412 0.6041 -0.2115 -0.0474 0.0445  498 LEU D CB  
11806 C CG  . LEU D 197 ? 1.0263 0.6669 0.7043 -0.2262 -0.0452 0.0373  498 LEU D CG  
11807 C CD1 . LEU D 197 ? 0.8955 0.5695 0.5793 -0.2459 -0.0436 0.0394  498 LEU D CD1 
11808 C CD2 . LEU D 197 ? 1.1214 0.7331 0.7755 -0.2405 -0.0449 0.0312  498 LEU D CD2 
11809 N N   . GLY D 198 ? 0.8496 0.5613 0.5903 -0.1846 -0.0458 0.0447  499 GLY D N   
11810 C CA  . GLY D 198 ? 0.8800 0.6259 0.6512 -0.1654 -0.0456 0.0425  499 GLY D CA  
11811 C C   . GLY D 198 ? 0.8029 0.5575 0.5865 -0.1512 -0.0464 0.0481  499 GLY D C   
11812 O O   . GLY D 198 ? 0.9646 0.7182 0.7410 -0.1597 -0.0464 0.0531  499 GLY D O   
11813 N N   . ASP D 199 ? 0.7752 0.5381 0.5763 -0.1302 -0.0470 0.0473  500 ASP D N   
11814 C CA  . ASP D 199 ? 0.7027 0.4821 0.5205 -0.1161 -0.0476 0.0509  500 ASP D CA  
11815 C C   . ASP D 199 ? 0.8427 0.5894 0.6491 -0.1026 -0.0504 0.0556  500 ASP D C   
11816 O O   . ASP D 199 ? 0.9060 0.6405 0.7143 -0.0882 -0.0512 0.0535  500 ASP D O   
11817 C CB  . ASP D 199 ? 0.7926 0.6033 0.6365 -0.1029 -0.0464 0.0467  500 ASP D CB  
11818 C CG  . ASP D 199 ? 0.9050 0.7345 0.7660 -0.0904 -0.0466 0.0495  500 ASP D CG  
11819 O OD1 . ASP D 199 ? 0.9883 0.8004 0.8443 -0.0812 -0.0487 0.0538  500 ASP D OD1 
11820 O OD2 . ASP D 199 ? 0.9178 0.7796 0.7970 -0.0894 -0.0448 0.0471  500 ASP D OD2 
11821 N N   . PRO D 200 ? 0.8609 0.5939 0.6553 -0.1060 -0.0520 0.0620  501 PRO D N   
11822 C CA  . PRO D 200 ? 0.8175 0.5162 0.5972 -0.0933 -0.0554 0.0670  501 PRO D CA  
11823 C C   . PRO D 200 ? 0.8393 0.5494 0.6375 -0.0707 -0.0568 0.0669  501 PRO D C   
11824 O O   . PRO D 200 ? 0.7041 0.3887 0.4925 -0.0572 -0.0595 0.0695  501 PRO D O   
11825 C CB  . PRO D 200 ? 0.6899 0.3813 0.4564 -0.1031 -0.0568 0.0741  501 PRO D CB  
11826 C CG  . PRO D 200 ? 0.7068 0.4133 0.4699 -0.1262 -0.0536 0.0719  501 PRO D CG  
11827 C CD  . PRO D 200 ? 0.6880 0.4316 0.4761 -0.1245 -0.0508 0.0647  501 PRO D CD  
11828 N N   . ALA D 201 ? 0.8748 0.6223 0.6987 -0.0661 -0.0549 0.0638  502 ALA D N   
11829 C CA  . ALA D 201 ? 0.8429 0.6028 0.6843 -0.0469 -0.0557 0.0631  502 ALA D CA  
11830 C C   . ALA D 201 ? 0.8808 0.6290 0.7223 -0.0363 -0.0553 0.0587  502 ALA D C   
11831 O O   . ALA D 201 ? 0.9968 0.7386 0.8413 -0.0201 -0.0570 0.0594  502 ALA D O   
11832 C CB  . ALA D 201 ? 0.7935 0.5924 0.6592 -0.0465 -0.0534 0.0605  502 ALA D CB  
11833 N N   . ASN D 202 ? 0.8860 0.6334 0.7245 -0.0453 -0.0531 0.0537  503 ASN D N   
11834 C CA  . ASN D 202 ? 0.8593 0.6025 0.7009 -0.0362 -0.0519 0.0483  503 ASN D CA  
11835 C C   . ASN D 202 ? 0.8582 0.5611 0.6757 -0.0343 -0.0531 0.0478  503 ASN D C   
11836 O O   . ASN D 202 ? 0.9001 0.5959 0.7165 -0.0282 -0.0518 0.0427  503 ASN D O   
11837 C CB  . ASN D 202 ? 0.7782 0.5446 0.6300 -0.0458 -0.0491 0.0430  503 ASN D CB  
11838 C CG  . ASN D 202 ? 0.8521 0.6554 0.7260 -0.0458 -0.0479 0.0434  503 ASN D CG  
11839 O OD1 . ASN D 202 ? 0.8426 0.6578 0.7299 -0.0337 -0.0483 0.0450  503 ASN D OD1 
11840 N ND2 . ASN D 202 ? 0.8598 0.6816 0.7369 -0.0594 -0.0465 0.0418  503 ASN D ND2 
11841 N N   . VAL D 203 ? 0.8827 0.5577 0.6797 -0.0387 -0.0555 0.0531  504 VAL D N   
11842 C CA  . VAL D 203 ? 0.9038 0.5353 0.6735 -0.0389 -0.0566 0.0527  504 VAL D CA  
11843 C C   . VAL D 203 ? 0.9853 0.6045 0.7563 -0.0168 -0.0572 0.0504  504 VAL D C   
11844 O O   . VAL D 203 ? 1.0150 0.6097 0.7719 -0.0146 -0.0562 0.0457  504 VAL D O   
11845 C CB  . VAL D 203 ? 0.8888 0.4922 0.6357 -0.0465 -0.0593 0.0601  504 VAL D CB  
11846 C CG1 . VAL D 203 ? 0.9384 0.4913 0.6545 -0.0439 -0.0608 0.0604  504 VAL D CG1 
11847 C CG2 . VAL D 203 ? 0.9462 0.5629 0.6905 -0.0706 -0.0578 0.0610  504 VAL D CG2 
11848 N N   . GLN D 204 ? 1.0089 0.6465 0.7968 -0.0003 -0.0587 0.0532  505 GLN D N   
11849 C CA  . GLN D 204 ? 0.9896 0.6204 0.7802 0.0210  -0.0591 0.0508  505 GLN D CA  
11850 C C   . GLN D 204 ? 0.8880 0.5358 0.6917 0.0234  -0.0552 0.0428  505 GLN D C   
11851 O O   . GLN D 204 ? 0.7725 0.4008 0.5665 0.0327  -0.0542 0.0383  505 GLN D O   
11852 C CB  . GLN D 204 ? 1.0493 0.7013 0.8565 0.0362  -0.0615 0.0553  505 GLN D CB  
11853 C CG  . GLN D 204 ? 1.2009 0.8321 0.9990 0.0576  -0.0642 0.0565  505 GLN D CG  
11854 C CD  . GLN D 204 ? 1.2117 0.8754 1.0344 0.0751  -0.0639 0.0547  505 GLN D CD  
11855 O OE1 . GLN D 204 ? 1.1643 0.8555 1.0035 0.0765  -0.0653 0.0583  505 GLN D OE1 
11856 N NE2 . GLN D 204 ? 1.1851 0.8459 1.0093 0.0878  -0.0616 0.0487  505 GLN D NE2 
11857 N N   . PHE D 205 ? 0.7635 0.4468 0.5881 0.0153  -0.0530 0.0410  506 PHE D N   
11858 C CA  . PHE D 205 ? 0.7229 0.4233 0.5591 0.0165  -0.0496 0.0342  506 PHE D CA  
11859 C C   . PHE D 205 ? 0.8257 0.5050 0.6440 0.0041  -0.0481 0.0293  506 PHE D C   
11860 O O   . PHE D 205 ? 0.8463 0.5191 0.6616 0.0100  -0.0461 0.0235  506 PHE D O   
11861 C CB  . PHE D 205 ? 0.6031 0.3428 0.4629 0.0109  -0.0481 0.0344  506 PHE D CB  
11862 C CG  . PHE D 205 ? 0.7648 0.5236 0.6375 0.0146  -0.0450 0.0287  506 PHE D CG  
11863 C CD1 . PHE D 205 ? 0.8481 0.6213 0.7347 0.0297  -0.0439 0.0277  506 PHE D CD1 
11864 C CD2 . PHE D 205 ? 0.7605 0.5244 0.6312 0.0027  -0.0433 0.0246  506 PHE D CD2 
11865 C CE1 . PHE D 205 ? 0.7667 0.5570 0.6638 0.0323  -0.0408 0.0229  506 PHE D CE1 
11866 C CE2 . PHE D 205 ? 0.7398 0.5210 0.6212 0.0063  -0.0407 0.0201  506 PHE D CE2 
11867 C CZ  . PHE D 205 ? 0.7024 0.4956 0.5963 0.0209  -0.0393 0.0193  506 PHE D CZ  
11868 N N   . THR D 206 ? 0.8015 0.4713 0.6073 -0.0140 -0.0490 0.0313  507 THR D N   
11869 C CA  . THR D 206 ? 0.7837 0.4307 0.5691 -0.0278 -0.0480 0.0268  507 THR D CA  
11870 C C   . THR D 206 ? 0.9928 0.5981 0.7553 -0.0180 -0.0483 0.0244  507 THR D C   
11871 O O   . THR D 206 ? 1.1221 0.7141 0.8741 -0.0207 -0.0465 0.0178  507 THR D O   
11872 C CB  . THR D 206 ? 0.7022 0.3429 0.4753 -0.0487 -0.0490 0.0303  507 THR D CB  
11873 O OG1 . THR D 206 ? 0.6460 0.3272 0.4407 -0.0565 -0.0482 0.0315  507 THR D OG1 
11874 C CG2 . THR D 206 ? 0.6278 0.2460 0.3792 -0.0650 -0.0480 0.0255  507 THR D CG2 
11875 N N   . GLU D 207 ? 1.1186 0.7029 0.8726 -0.0056 -0.0509 0.0295  508 GLU D N   
11876 C CA  . GLU D 207 ? 1.1958 0.7410 0.9287 0.0078  -0.0513 0.0271  508 GLU D CA  
11877 C C   . GLU D 207 ? 1.0428 0.6025 0.7895 0.0247  -0.0486 0.0206  508 GLU D C   
11878 O O   . GLU D 207 ? 1.0342 0.5687 0.7647 0.0285  -0.0469 0.0143  508 GLU D O   
11879 C CB  . GLU D 207 ? 1.2929 0.8170 1.0159 0.0203  -0.0551 0.0346  508 GLU D CB  
11880 C CG  . GLU D 207 ? 1.4169 0.9102 1.1148 0.0038  -0.0575 0.0405  508 GLU D CG  
11881 C CD  . GLU D 207 ? 1.5751 1.0524 1.2650 0.0159  -0.0618 0.0492  508 GLU D CD  
11882 O OE1 . GLU D 207 ? 1.6044 1.1093 1.3161 0.0322  -0.0632 0.0518  508 GLU D OE1 
11883 O OE2 . GLU D 207 ? 1.5736 1.0106 1.2343 0.0084  -0.0640 0.0537  508 GLU D OE2 
11884 N N   . ILE D 208 ? 0.8992 0.4993 0.6746 0.0338  -0.0479 0.0215  509 ILE D N   
11885 C CA  . ILE D 208 ? 0.8309 0.4463 0.6190 0.0492  -0.0451 0.0157  509 ILE D CA  
11886 C C   . ILE D 208 ? 0.8275 0.4462 0.6132 0.0384  -0.0418 0.0082  509 ILE D C   
11887 O O   . ILE D 208 ? 0.9676 0.5680 0.7416 0.0456  -0.0397 0.0018  509 ILE D O   
11888 C CB  . ILE D 208 ? 0.7584 0.4160 0.5762 0.0582  -0.0449 0.0184  509 ILE D CB  
11889 C CG1 . ILE D 208 ? 0.8568 0.5140 0.6769 0.0657  -0.0487 0.0260  509 ILE D CG1 
11890 C CG2 . ILE D 208 ? 0.7316 0.4012 0.5593 0.0753  -0.0421 0.0131  509 ILE D CG2 
11891 C CD1 . ILE D 208 ? 0.7796 0.4714 0.6245 0.0798  -0.0486 0.0274  509 ILE D CD1 
11892 N N   . CYS D 209 ? 0.8049 0.4469 0.6006 0.0213  -0.0414 0.0088  510 CYS D N   
11893 C CA  . CYS D 209 ? 0.8744 0.5229 0.6679 0.0095  -0.0390 0.0024  510 CYS D CA  
11894 C C   . CYS D 209 ? 0.9951 0.6028 0.7593 0.0036  -0.0385 -0.0028 510 CYS D C   
11895 O O   . CYS D 209 ? 1.0256 0.6260 0.7838 0.0088  -0.0360 -0.0098 510 CYS D O   
11896 C CB  . CYS D 209 ? 0.7873 0.4598 0.5898 -0.0092 -0.0397 0.0049  510 CYS D CB  
11897 S SG  . CYS D 209 ? 0.7689 0.4852 0.6023 -0.0046 -0.0401 0.0104  510 CYS D SG  
11898 N N   . ILE D 210 ? 0.9724 0.5522 0.7166 -0.0082 -0.0408 0.0005  511 ILE D N   
11899 C CA  . ILE D 210 ? 1.0089 0.5457 0.7217 -0.0166 -0.0405 -0.0041 511 ILE D CA  
11900 C C   . ILE D 210 ? 1.0521 0.5620 0.7533 0.0039  -0.0391 -0.0088 511 ILE D C   
11901 O O   . ILE D 210 ? 1.1311 0.6206 0.8158 0.0016  -0.0369 -0.0166 511 ILE D O   
11902 C CB  . ILE D 210 ? 0.9931 0.5014 0.6854 -0.0296 -0.0433 0.0019  511 ILE D CB  
11903 C CG1 . ILE D 210 ? 0.9086 0.4443 0.6099 -0.0526 -0.0438 0.0042  511 ILE D CG1 
11904 C CG2 . ILE D 210 ? 0.9490 0.4049 0.6056 -0.0346 -0.0431 -0.0023 511 ILE D CG2 
11905 C CD1 . ILE D 210 ? 0.8962 0.4105 0.5802 -0.0663 -0.0461 0.0107  511 ILE D CD1 
11906 N N   . GLN D 211 ? 1.1079 0.6202 0.8184 0.0247  -0.0402 -0.0047 512 GLN D N   
11907 C CA  . GLN D 211 ? 1.1526 0.6452 0.8551 0.0470  -0.0387 -0.0092 512 GLN D CA  
11908 C C   . GLN D 211 ? 1.0442 0.5609 0.7601 0.0528  -0.0345 -0.0173 512 GLN D C   
11909 O O   . GLN D 211 ? 0.9631 0.4570 0.6641 0.0627  -0.0321 -0.0246 512 GLN D O   
11910 C CB  . GLN D 211 ? 1.2019 0.7034 0.9169 0.0677  -0.0410 -0.0028 512 GLN D CB  
11911 C CG  . GLN D 211 ? 1.2683 0.7566 0.9786 0.0928  -0.0396 -0.0073 512 GLN D CG  
11912 C CD  . GLN D 211 ? 1.4897 0.9495 1.1861 0.1076  -0.0435 -0.0013 512 GLN D CD  
11913 O OE1 . GLN D 211 ? 1.6149 1.0328 1.2856 0.1187  -0.0436 -0.0044 512 GLN D OE1 
11914 N NE2 . GLN D 211 ? 1.5127 0.9932 1.2241 0.1082  -0.0470 0.0075  512 GLN D NE2 
11915 N N   . GLN D 212 ? 0.9626 0.5238 0.7051 0.0470  -0.0336 -0.0162 513 GLN D N   
11916 C CA  . GLN D 212 ? 0.9564 0.5437 0.7127 0.0516  -0.0298 -0.0225 513 GLN D CA  
11917 C C   . GLN D 212 ? 0.9793 0.5634 0.7249 0.0335  -0.0282 -0.0286 513 GLN D C   
11918 O O   . GLN D 212 ? 1.0681 0.6785 0.8263 0.0334  -0.0256 -0.0326 513 GLN D O   
11919 C CB  . GLN D 212 ? 1.0311 0.6654 0.8191 0.0545  -0.0296 -0.0179 513 GLN D CB  
11920 C CG  . GLN D 212 ? 1.0595 0.7033 0.8604 0.0691  -0.0316 -0.0114 513 GLN D CG  
11921 C CD  . GLN D 212 ? 1.1983 0.8306 0.9952 0.0916  -0.0301 -0.0147 513 GLN D CD  
11922 O OE1 . GLN D 212 ? 1.2521 0.8778 1.0420 0.0977  -0.0266 -0.0224 513 GLN D OE1 
11923 N NE2 . GLN D 212 ? 1.2632 0.8943 1.0642 0.1045  -0.0329 -0.0091 513 GLN D NE2 
11924 N N   . GLY D 213 ? 0.9305 0.4843 0.6528 0.0172  -0.0299 -0.0292 514 GLY D N   
11925 C CA  . GLY D 213 ? 0.9687 0.5160 0.6771 -0.0002 -0.0287 -0.0360 514 GLY D CA  
11926 C C   . GLY D 213 ? 1.0114 0.5806 0.7263 -0.0230 -0.0308 -0.0328 514 GLY D C   
11927 O O   . GLY D 213 ? 1.0560 0.6225 0.7594 -0.0391 -0.0304 -0.0383 514 GLY D O   
11928 N N   . TRP D 214 ? 0.9479 0.5403 0.6808 -0.0247 -0.0330 -0.0247 515 TRP D N   
11929 C CA  . TRP D 214 ? 0.8772 0.4922 0.6167 -0.0451 -0.0348 -0.0220 515 TRP D CA  
11930 C C   . TRP D 214 ? 1.0192 0.6019 0.7311 -0.0649 -0.0361 -0.0233 515 TRP D C   
11931 O O   . TRP D 214 ? 1.0183 0.5635 0.7106 -0.0628 -0.0370 -0.0212 515 TRP D O   
11932 C CB  . TRP D 214 ? 1.0062 0.6475 0.7675 -0.0417 -0.0365 -0.0134 515 TRP D CB  
11933 C CG  . TRP D 214 ? 1.0456 0.7179 0.8184 -0.0588 -0.0378 -0.0112 515 TRP D CG  
11934 C CD1 . TRP D 214 ? 0.9871 0.6891 0.7709 -0.0655 -0.0372 -0.0145 515 TRP D CD1 
11935 C CD2 . TRP D 214 ? 0.9646 0.6429 0.7390 -0.0703 -0.0398 -0.0052 515 TRP D CD2 
11936 N NE1 . TRP D 214 ? 0.9845 0.7113 0.7772 -0.0793 -0.0389 -0.0111 515 TRP D NE1 
11937 C CE2 . TRP D 214 ? 0.9382 0.6517 0.7257 -0.0830 -0.0401 -0.0057 515 TRP D CE2 
11938 C CE3 . TRP D 214 ? 0.9183 0.5763 0.6838 -0.0708 -0.0413 0.0005  515 TRP D CE3 
11939 C CZ2 . TRP D 214 ? 0.8244 0.5544 0.6169 -0.0958 -0.0415 -0.0014 515 TRP D CZ2 
11940 C CZ3 . TRP D 214 ? 0.9666 0.6401 0.7363 -0.0848 -0.0426 0.0052  515 TRP D CZ3 
11941 C CH2 . TRP D 214 ? 0.8885 0.5984 0.6721 -0.0970 -0.0424 0.0039  515 TRP D CH2 
11942 N N   . LYS D 215 ? 1.1352 0.7328 0.8448 -0.0845 -0.0364 -0.0268 516 LYS D N   
11943 C CA  . LYS D 215 ? 1.1376 0.7105 0.8219 -0.1073 -0.0374 -0.0286 516 LYS D CA  
11944 C C   . LYS D 215 ? 1.0650 0.6650 0.7613 -0.1220 -0.0394 -0.0222 516 LYS D C   
11945 O O   . LYS D 215 ? 1.1103 0.7513 0.8249 -0.1295 -0.0398 -0.0227 516 LYS D O   
11946 C CB  . LYS D 215 ? 1.2324 0.8061 0.9052 -0.1207 -0.0365 -0.0375 516 LYS D CB  
11947 C CG  . LYS D 215 ? 1.3411 0.8885 1.0009 -0.1065 -0.0340 -0.0449 516 LYS D CG  
11948 C CD  . LYS D 215 ? 1.3626 0.8538 0.9849 -0.1145 -0.0335 -0.0495 516 LYS D CD  
11949 C CE  . LYS D 215 ? 1.3414 0.8015 0.9523 -0.0925 -0.0309 -0.0545 516 LYS D CE  
11950 N NZ  . LYS D 215 ? 1.2446 0.7024 0.8682 -0.0694 -0.0313 -0.0475 516 LYS D NZ  
11951 N N   . PRO D 216 ? 1.1347 0.7148 0.8215 -0.1255 -0.0406 -0.0161 517 PRO D N   
11952 C CA  . PRO D 216 ? 1.0171 0.6275 0.7196 -0.1348 -0.0420 -0.0096 517 PRO D CA  
11953 C C   . PRO D 216 ? 1.0157 0.6295 0.7048 -0.1631 -0.0425 -0.0112 517 PRO D C   
11954 O O   . PRO D 216 ? 1.1284 0.7029 0.7875 -0.1770 -0.0424 -0.0137 517 PRO D O   
11955 C CB  . PRO D 216 ? 1.0430 0.6275 0.7389 -0.1245 -0.0430 -0.0023 517 PRO D CB  
11956 C CG  . PRO D 216 ? 1.0868 0.6174 0.7512 -0.1222 -0.0427 -0.0054 517 PRO D CG  
11957 C CD  . PRO D 216 ? 1.1602 0.6906 0.8237 -0.1162 -0.0409 -0.0143 517 PRO D CD  
11958 N N   . PRO D 217 ? 0.9176 0.5778 0.6275 -0.1726 -0.0429 -0.0101 518 PRO D N   
11959 C CA  . PRO D 217 ? 0.9059 0.5753 0.6053 -0.2001 -0.0434 -0.0110 518 PRO D CA  
11960 C C   . PRO D 217 ? 0.9985 0.6405 0.6795 -0.2114 -0.0436 -0.0053 518 PRO D C   
11961 O O   . PRO D 217 ? 1.0547 0.6885 0.7169 -0.2363 -0.0435 -0.0068 518 PRO D O   
11962 C CB  . PRO D 217 ? 0.8086 0.5365 0.5388 -0.2004 -0.0438 -0.0096 518 PRO D CB  
11963 C CG  . PRO D 217 ? 0.7429 0.4873 0.4941 -0.1767 -0.0436 -0.0103 518 PRO D CG  
11964 C CD  . PRO D 217 ? 0.7184 0.4244 0.4610 -0.1585 -0.0430 -0.0083 518 PRO D CD  
11965 N N   . ARG D 218 ? 1.1789 0.8075 0.8641 -0.1948 -0.0440 0.0013  519 ARG D N   
11966 C CA  . ARG D 218 ? 1.2176 0.8252 0.8882 -0.2036 -0.0445 0.0081  519 ARG D CA  
11967 C C   . ARG D 218 ? 1.1989 0.8431 0.8776 -0.2254 -0.0441 0.0097  519 ARG D C   
11968 O O   . ARG D 218 ? 1.2702 0.8997 0.9269 -0.2497 -0.0437 0.0094  519 ARG D O   
11969 C CB  . ARG D 218 ? 1.1763 0.7237 0.8081 -0.2125 -0.0447 0.0074  519 ARG D CB  
11970 C CG  . ARG D 218 ? 1.1890 0.7018 0.8111 -0.1918 -0.0447 0.0037  519 ARG D CG  
11971 C CD  . ARG D 218 ? 1.3002 0.7506 0.8862 -0.1924 -0.0455 0.0064  519 ARG D CD  
11972 N NE  . ARG D 218 ? 1.4604 0.9034 1.0507 -0.1777 -0.0472 0.0155  519 ARG D NE  
11973 C CZ  . ARG D 218 ? 1.5114 0.9358 1.1036 -0.1510 -0.0482 0.0176  519 ARG D CZ  
11974 N NH1 . ARG D 218 ? 1.4992 0.9207 1.0956 -0.1394 -0.0503 0.0261  519 ARG D NH1 
11975 N NH2 . ARG D 218 ? 1.4681 0.8783 1.0577 -0.1362 -0.0472 0.0110  519 ARG D NH2 
11976 N N   . GLY D 219 ? 1.0643 0.7572 0.7747 -0.2163 -0.0439 0.0111  520 GLY D N   
11977 C CA  . GLY D 219 ? 1.0287 0.7619 0.7513 -0.2318 -0.0432 0.0126  520 GLY D CA  
11978 C C   . GLY D 219 ? 1.1102 0.8613 0.8513 -0.2185 -0.0432 0.0192  520 GLY D C   
11979 O O   . GLY D 219 ? 1.1233 0.8514 0.8640 -0.2001 -0.0440 0.0232  520 GLY D O   
11980 N N   . ARG D 220 ? 1.0888 0.8822 0.8461 -0.2270 -0.0422 0.0200  521 ARG D N   
11981 C CA  . ARG D 220 ? 0.9222 0.7330 0.6961 -0.2153 -0.0419 0.0256  521 ARG D CA  
11982 C C   . ARG D 220 ? 0.8381 0.6782 0.6408 -0.1924 -0.0420 0.0246  521 ARG D C   
11983 O O   . ARG D 220 ? 0.8182 0.6561 0.6303 -0.1766 -0.0423 0.0288  521 ARG D O   
11984 C CB  . ARG D 220 ? 0.9672 0.8094 0.7446 -0.2337 -0.0402 0.0268  521 ARG D CB  
11985 C CG  . ARG D 220 ? 1.0896 0.9468 0.8803 -0.2238 -0.0395 0.0322  521 ARG D CG  
11986 C CD  . ARG D 220 ? 1.1834 1.0071 0.9507 -0.2341 -0.0396 0.0385  521 ARG D CD  
11987 N NE  . ARG D 220 ? 1.1720 1.0216 0.9509 -0.2338 -0.0381 0.0423  521 ARG D NE  
11988 C CZ  . ARG D 220 ? 1.1606 1.0375 0.9393 -0.2529 -0.0357 0.0419  521 ARG D CZ  
11989 N NH1 . ARG D 220 ? 1.1506 1.0327 0.9179 -0.2751 -0.0347 0.0382  521 ARG D NH1 
11990 N NH2 . ARG D 220 ? 1.1306 1.0305 0.9200 -0.2506 -0.0341 0.0449  521 ARG D NH2 
11991 N N   . PHE D 221 ? 0.9545 0.8216 0.7705 -0.1907 -0.0420 0.0192  522 PHE D N   
11992 C CA  . PHE D 221 ? 0.8528 0.7491 0.6949 -0.1709 -0.0420 0.0186  522 PHE D CA  
11993 C C   . PHE D 221 ? 0.8464 0.7368 0.6900 -0.1617 -0.0429 0.0142  522 PHE D C   
11994 O O   . PHE D 221 ? 0.9179 0.8390 0.7768 -0.1575 -0.0431 0.0111  522 PHE D O   
11995 C CB  . PHE D 221 ? 0.8352 0.7795 0.6957 -0.1757 -0.0411 0.0176  522 PHE D CB  
11996 C CG  . PHE D 221 ? 0.8556 0.8079 0.7158 -0.1831 -0.0398 0.0216  522 PHE D CG  
11997 C CD1 . PHE D 221 ? 0.9027 0.8776 0.7593 -0.2034 -0.0385 0.0203  522 PHE D CD1 
11998 C CD2 . PHE D 221 ? 0.7750 0.7132 0.6380 -0.1704 -0.0396 0.0265  522 PHE D CD2 
11999 C CE1 . PHE D 221 ? 0.7523 0.7348 0.6077 -0.2108 -0.0368 0.0239  522 PHE D CE1 
12000 C CE2 . PHE D 221 ? 0.7196 0.6646 0.5810 -0.1774 -0.0384 0.0302  522 PHE D CE2 
12001 C CZ  . PHE D 221 ? 0.7164 0.6830 0.5737 -0.1975 -0.0368 0.0288  522 PHE D CZ  
12002 N N   . ASP D 222 ? 0.7373 0.5873 0.5641 -0.1574 -0.0433 0.0140  523 ASP D N   
12003 C CA  . ASP D 222 ? 0.6781 0.5187 0.5059 -0.1456 -0.0435 0.0101  523 ASP D CA  
12004 C C   . ASP D 222 ? 0.7755 0.6302 0.6244 -0.1233 -0.0432 0.0124  523 ASP D C   
12005 O O   . ASP D 222 ? 0.8807 0.7235 0.7318 -0.1133 -0.0432 0.0168  523 ASP D O   
12006 C CB  . ASP D 222 ? 0.5788 0.3709 0.3818 -0.1456 -0.0437 0.0093  523 ASP D CB  
12007 C CG  . ASP D 222 ? 0.8376 0.6081 0.6153 -0.1690 -0.0439 0.0078  523 ASP D CG  
12008 O OD1 . ASP D 222 ? 0.9109 0.7066 0.6909 -0.1866 -0.0437 0.0075  523 ASP D OD1 
12009 O OD2 . ASP D 222 ? 0.9725 0.7001 0.7270 -0.1699 -0.0440 0.0068  523 ASP D OD2 
12010 N N   . VAL D 223 ? 0.8312 0.7111 0.6949 -0.1160 -0.0431 0.0096  524 VAL D N   
12011 C CA  . VAL D 223 ? 0.6716 0.5593 0.5517 -0.0960 -0.0426 0.0113  524 VAL D CA  
12012 C C   . VAL D 223 ? 0.7044 0.5606 0.5745 -0.0857 -0.0421 0.0101  524 VAL D C   
12013 O O   . VAL D 223 ? 0.7257 0.5666 0.5827 -0.0903 -0.0420 0.0055  524 VAL D O   
12014 C CB  . VAL D 223 ? 0.5233 0.4435 0.4191 -0.0913 -0.0427 0.0092  524 VAL D CB  
12015 C CG1 . VAL D 223 ? 0.4565 0.3784 0.3649 -0.0725 -0.0418 0.0110  524 VAL D CG1 
12016 C CG2 . VAL D 223 ? 0.3897 0.3436 0.2970 -0.0978 -0.0431 0.0104  524 VAL D CG2 
12017 N N   . LEU D 224 ? 0.5878 0.4353 0.4638 -0.0718 -0.0417 0.0136  525 LEU D N   
12018 C CA  . LEU D 224 ? 0.6171 0.4373 0.4843 -0.0610 -0.0412 0.0123  525 LEU D CA  
12019 C C   . LEU D 224 ? 0.6567 0.4877 0.5319 -0.0517 -0.0398 0.0084  525 LEU D C   
12020 O O   . LEU D 224 ? 0.7751 0.6344 0.6649 -0.0506 -0.0396 0.0084  525 LEU D O   
12021 C CB  . LEU D 224 ? 0.6399 0.4524 0.5123 -0.0484 -0.0415 0.0171  525 LEU D CB  
12022 C CG  . LEU D 224 ? 0.6582 0.4482 0.5164 -0.0545 -0.0430 0.0210  525 LEU D CG  
12023 C CD1 . LEU D 224 ? 0.4470 0.2488 0.3190 -0.0447 -0.0436 0.0261  525 LEU D CD1 
12024 C CD2 . LEU D 224 ? 0.5686 0.3197 0.4059 -0.0507 -0.0435 0.0196  525 LEU D CD2 
12025 N N   . PRO D 225 ? 0.6010 0.4095 0.4659 -0.0444 -0.0388 0.0052  526 PRO D N   
12026 C CA  . PRO D 225 ? 0.6927 0.5116 0.5649 -0.0350 -0.0370 0.0017  526 PRO D CA  
12027 C C   . PRO D 225 ? 0.6810 0.5109 0.5693 -0.0194 -0.0359 0.0050  526 PRO D C   
12028 O O   . PRO D 225 ? 0.7312 0.5538 0.6215 -0.0139 -0.0366 0.0088  526 PRO D O   
12029 C CB  . PRO D 225 ? 0.6654 0.4537 0.5182 -0.0337 -0.0360 -0.0036 526 PRO D CB  
12030 C CG  . PRO D 225 ? 0.6967 0.4566 0.5370 -0.0327 -0.0372 -0.0008 526 PRO D CG  
12031 C CD  . PRO D 225 ? 0.7155 0.4864 0.5593 -0.0449 -0.0391 0.0040  526 PRO D CD  
12032 N N   . LEU D 226 ? 0.5200 0.3680 0.4190 -0.0131 -0.0343 0.0036  527 LEU D N   
12033 C CA  . LEU D 226 ? 0.5371 0.3934 0.4487 0.0004  -0.0327 0.0057  527 LEU D CA  
12034 C C   . LEU D 226 ? 0.6580 0.4937 0.5610 0.0104  -0.0312 0.0027  527 LEU D C   
12035 O O   . LEU D 226 ? 0.8667 0.6856 0.7555 0.0085  -0.0304 -0.0023 527 LEU D O   
12036 C CB  . LEU D 226 ? 0.6483 0.5276 0.5713 0.0031  -0.0311 0.0053  527 LEU D CB  
12037 C CG  . LEU D 226 ? 0.6364 0.5369 0.5695 -0.0026 -0.0326 0.0088  527 LEU D CG  
12038 C CD1 . LEU D 226 ? 0.5691 0.4892 0.5114 0.0012  -0.0314 0.0093  527 LEU D CD1 
12039 C CD2 . LEU D 226 ? 0.5328 0.4351 0.4737 -0.0001 -0.0334 0.0134  527 LEU D CD2 
12040 N N   . LEU D 227 ? 0.7902 0.6275 0.7013 0.0213  -0.0308 0.0055  528 LEU D N   
12041 C CA  . LEU D 227 ? 0.7611 0.5847 0.6674 0.0340  -0.0293 0.0029  528 LEU D CA  
12042 C C   . LEU D 227 ? 0.7291 0.5764 0.6526 0.0432  -0.0271 0.0040  528 LEU D C   
12043 O O   . LEU D 227 ? 0.7402 0.5989 0.6748 0.0463  -0.0281 0.0085  528 LEU D O   
12044 C CB  . LEU D 227 ? 0.7608 0.5637 0.6589 0.0381  -0.0318 0.0058  528 LEU D CB  
12045 C CG  . LEU D 227 ? 0.7130 0.4857 0.5928 0.0453  -0.0314 0.0017  528 LEU D CG  
12046 C CD1 . LEU D 227 ? 0.6431 0.4070 0.5231 0.0578  -0.0333 0.0052  528 LEU D CD1 
12047 C CD2 . LEU D 227 ? 0.6490 0.4258 0.5289 0.0526  -0.0277 -0.0047 528 LEU D CD2 
12048 N N   . LEU D 228 ? 0.6133 0.4686 0.5380 0.0462  -0.0239 -0.0001 529 LEU D N   
12049 C CA  . LEU D 228 ? 0.6409 0.5201 0.5804 0.0510  -0.0214 0.0010  529 LEU D CA  
12050 C C   . LEU D 228 ? 0.6760 0.5559 0.6161 0.0634  -0.0182 -0.0028 529 LEU D C   
12051 O O   . LEU D 228 ? 0.6580 0.5229 0.5861 0.0670  -0.0167 -0.0082 529 LEU D O   
12052 C CB  . LEU D 228 ? 0.7111 0.6033 0.6524 0.0437  -0.0201 0.0003  529 LEU D CB  
12053 C CG  . LEU D 228 ? 0.6644 0.5595 0.6060 0.0328  -0.0232 0.0035  529 LEU D CG  
12054 C CD1 . LEU D 228 ? 0.7489 0.6562 0.6906 0.0276  -0.0223 0.0026  529 LEU D CD1 
12055 C CD2 . LEU D 228 ? 0.5430 0.4492 0.4966 0.0332  -0.0245 0.0090  529 LEU D CD2 
12056 N N   . GLN D 229 ? 0.6203 0.5187 0.5741 0.0695  -0.0170 -0.0004 530 GLN D N   
12057 C CA  . GLN D 229 ? 0.6275 0.5336 0.5851 0.0814  -0.0138 -0.0037 530 GLN D CA  
12058 C C   . GLN D 229 ? 0.5694 0.5018 0.5396 0.0795  -0.0105 -0.0028 530 GLN D C   
12059 O O   . GLN D 229 ? 0.5929 0.5371 0.5722 0.0735  -0.0117 0.0020  530 GLN D O   
12060 C CB  . GLN D 229 ? 0.6867 0.5899 0.6475 0.0912  -0.0163 -0.0015 530 GLN D CB  
12061 C CG  . GLN D 229 ? 0.5579 0.4827 0.5306 0.1023  -0.0137 -0.0027 530 GLN D CG  
12062 C CD  . GLN D 229 ? 0.6211 0.5430 0.5959 0.1128  -0.0172 -0.0002 530 GLN D CD  
12063 O OE1 . GLN D 229 ? 0.6510 0.5701 0.6279 0.1082  -0.0213 0.0052  530 GLN D OE1 
12064 N NE2 . GLN D 229 ? 0.5632 0.4867 0.5371 0.1276  -0.0157 -0.0041 530 GLN D NE2 
12065 N N   . ALA D 230 ? 0.6167 0.5567 0.5859 0.0843  -0.0060 -0.0076 531 ALA D N   
12066 C CA  . ALA D 230 ? 0.6462 0.6095 0.6245 0.0815  -0.0021 -0.0071 531 ALA D CA  
12067 C C   . ALA D 230 ? 0.6043 0.5822 0.5881 0.0926  0.0019  -0.0112 531 ALA D C   
12068 O O   . ALA D 230 ? 0.7032 0.6715 0.6789 0.1015  0.0035  -0.0168 531 ALA D O   
12069 C CB  . ALA D 230 ? 0.6557 0.6172 0.6259 0.0739  0.0000  -0.0089 531 ALA D CB  
12070 N N   . ASN D 231 ? 0.5462 0.5474 0.5430 0.0920  0.0034  -0.0087 532 ASN D N   
12071 C CA  . ASN D 231 ? 0.5550 0.5776 0.5591 0.1007  0.0078  -0.0126 532 ASN D CA  
12072 C C   . ASN D 231 ? 0.5720 0.5880 0.5747 0.1163  0.0064  -0.0161 532 ASN D C   
12073 O O   . ASN D 231 ? 0.6293 0.6513 0.6303 0.1267  0.0102  -0.0221 532 ASN D O   
12074 C CB  . ASN D 231 ? 0.5511 0.5804 0.5498 0.0985  0.0136  -0.0171 532 ASN D CB  
12075 C CG  . ASN D 231 ? 0.7403 0.8004 0.7497 0.0978  0.0188  -0.0180 532 ASN D CG  
12076 O OD1 . ASN D 231 ? 0.9695 1.0432 0.9813 0.1078  0.0227  -0.0235 532 ASN D OD1 
12077 N ND2 . ASN D 231 ? 0.7929 0.8640 0.8078 0.0858  0.0191  -0.0128 532 ASN D ND2 
12078 N N   . GLY D 232 ? 0.6649 0.6677 0.6673 0.1185  0.0009  -0.0122 533 GLY D N   
12079 C CA  . GLY D 232 ? 0.6267 0.6201 0.6262 0.1336  -0.0016 -0.0138 533 GLY D CA  
12080 C C   . GLY D 232 ? 0.6045 0.5708 0.5874 0.1417  -0.0010 -0.0194 533 GLY D C   
12081 O O   . GLY D 232 ? 0.5470 0.5065 0.5262 0.1572  -0.0016 -0.0222 533 GLY D O   
12082 N N   . ASN D 233 ? 0.7134 0.6637 0.6852 0.1322  0.0003  -0.0213 534 ASN D N   
12083 C CA  . ASN D 233 ? 0.6847 0.6069 0.6387 0.1383  0.0008  -0.0270 534 ASN D CA  
12084 C C   . ASN D 233 ? 0.7479 0.6389 0.6898 0.1352  -0.0049 -0.0236 534 ASN D C   
12085 O O   . ASN D 233 ? 0.6150 0.5080 0.5626 0.1264  -0.0088 -0.0170 534 ASN D O   
12086 C CB  . ASN D 233 ? 0.8207 0.7414 0.7670 0.1294  0.0047  -0.0313 534 ASN D CB  
12087 C CG  . ASN D 233 ? 0.9209 0.8697 0.8758 0.1339  0.0110  -0.0356 534 ASN D CG  
12088 O OD1 . ASN D 233 ? 0.9679 0.9265 0.9265 0.1485  0.0136  -0.0397 534 ASN D OD1 
12089 N ND2 . ASN D 233 ? 0.8650 0.8278 0.8228 0.1216  0.0136  -0.0344 534 ASN D ND2 
12090 N N   . ASP D 234 ? 0.8550 0.7165 0.7791 0.1428  -0.0052 -0.0282 535 ASP D N   
12091 C CA  . ASP D 234 ? 0.8181 0.6469 0.7272 0.1371  -0.0101 -0.0253 535 ASP D CA  
12092 C C   . ASP D 234 ? 0.7329 0.5627 0.6419 0.1173  -0.0113 -0.0223 535 ASP D C   
12093 O O   . ASP D 234 ? 0.7601 0.6030 0.6717 0.1103  -0.0081 -0.0251 535 ASP D O   
12094 C CB  . ASP D 234 ? 0.9350 0.7281 0.8209 0.1443  -0.0093 -0.0319 535 ASP D CB  
12095 C CG  . ASP D 234 ? 0.9920 0.7812 0.8758 0.1668  -0.0083 -0.0353 535 ASP D CG  
12096 O OD1 . ASP D 234 ? 1.0442 0.8054 0.9090 0.1752  -0.0067 -0.0419 535 ASP D OD1 
12097 O OD2 . ASP D 234 ? 0.9964 0.8110 0.8970 0.1763  -0.0090 -0.0319 535 ASP D OD2 
12098 N N   . PRO D 235 ? 0.7528 0.5721 0.6597 0.1083  -0.0159 -0.0165 536 PRO D N   
12099 C CA  . PRO D 235 ? 0.7418 0.5669 0.6507 0.0910  -0.0171 -0.0137 536 PRO D CA  
12100 C C   . PRO D 235 ? 0.6814 0.4829 0.5714 0.0819  -0.0170 -0.0183 536 PRO D C   
12101 O O   . PRO D 235 ? 0.6305 0.4057 0.5037 0.0879  -0.0165 -0.0230 536 PRO D O   
12102 C CB  . PRO D 235 ? 0.6924 0.5153 0.6053 0.0865  -0.0217 -0.0064 536 PRO D CB  
12103 C CG  . PRO D 235 ? 0.5831 0.3808 0.4836 0.0973  -0.0237 -0.0066 536 PRO D CG  
12104 C CD  . PRO D 235 ? 0.6125 0.4158 0.5151 0.1140  -0.0203 -0.0119 536 PRO D CD  
12105 N N   . GLU D 236 ? 0.7294 0.5407 0.6216 0.0675  -0.0175 -0.0170 537 GLU D N   
12106 C CA  . GLU D 236 ? 0.7782 0.5748 0.6547 0.0569  -0.0174 -0.0217 537 GLU D CA  
12107 C C   . GLU D 236 ? 0.7392 0.5374 0.6152 0.0410  -0.0210 -0.0176 537 GLU D C   
12108 O O   . GLU D 236 ? 0.6312 0.4516 0.5224 0.0375  -0.0221 -0.0123 537 GLU D O   
12109 C CB  . GLU D 236 ? 0.7127 0.5259 0.5920 0.0568  -0.0135 -0.0263 537 GLU D CB  
12110 C CG  . GLU D 236 ? 0.7240 0.5381 0.6031 0.0718  -0.0091 -0.0315 537 GLU D CG  
12111 C CD  . GLU D 236 ? 0.8703 0.7097 0.7581 0.0720  -0.0050 -0.0334 537 GLU D CD  
12112 O OE1 . GLU D 236 ? 0.9247 0.7657 0.8056 0.0625  -0.0046 -0.0359 537 GLU D OE1 
12113 O OE2 . GLU D 236 ? 0.8410 0.6996 0.7421 0.0813  -0.0024 -0.0323 537 GLU D OE2 
12114 N N   . LEU D 237 ? 0.6556 0.4307 0.5133 0.0311  -0.0225 -0.0205 538 LEU D N   
12115 C CA  . LEU D 237 ? 0.6326 0.4105 0.4887 0.0152  -0.0258 -0.0173 538 LEU D CA  
12116 C C   . LEU D 237 ? 0.8050 0.6061 0.6669 0.0060  -0.0255 -0.0186 538 LEU D C   
12117 O O   . LEU D 237 ? 0.8431 0.6476 0.7018 0.0085  -0.0231 -0.0234 538 LEU D O   
12118 C CB  . LEU D 237 ? 0.5338 0.2787 0.3668 0.0061  -0.0274 -0.0201 538 LEU D CB  
12119 C CG  . LEU D 237 ? 0.7528 0.4685 0.5748 0.0142  -0.0284 -0.0183 538 LEU D CG  
12120 C CD1 . LEU D 237 ? 0.8966 0.5761 0.6919 0.0034  -0.0295 -0.0217 538 LEU D CD1 
12121 C CD2 . LEU D 237 ? 0.7467 0.4735 0.5816 0.0149  -0.0310 -0.0102 538 LEU D CD2 
12122 N N   . PHE D 238 ? 0.8465 0.6643 0.7166 -0.0038 -0.0281 -0.0141 539 PHE D N   
12123 C CA  . PHE D 238 ? 0.7723 0.6107 0.6455 -0.0133 -0.0290 -0.0149 539 PHE D CA  
12124 C C   . PHE D 238 ? 0.8532 0.6988 0.7275 -0.0261 -0.0323 -0.0117 539 PHE D C   
12125 O O   . PHE D 238 ? 0.8395 0.6850 0.7201 -0.0251 -0.0333 -0.0070 539 PHE D O   
12126 C CB  . PHE D 238 ? 0.6189 0.4842 0.5093 -0.0060 -0.0278 -0.0119 539 PHE D CB  
12127 C CG  . PHE D 238 ? 0.6345 0.4978 0.5262 0.0058  -0.0241 -0.0144 539 PHE D CG  
12128 C CD1 . PHE D 238 ? 0.5514 0.4164 0.4531 0.0168  -0.0226 -0.0115 539 PHE D CD1 
12129 C CD2 . PHE D 238 ? 0.7314 0.5927 0.6137 0.0052  -0.0222 -0.0200 539 PHE D CD2 
12130 C CE1 . PHE D 238 ? 0.6609 0.5276 0.5645 0.0272  -0.0189 -0.0142 539 PHE D CE1 
12131 C CE2 . PHE D 238 ? 0.6851 0.5462 0.5683 0.0158  -0.0182 -0.0228 539 PHE D CE2 
12132 C CZ  . PHE D 238 ? 0.6996 0.5645 0.5940 0.0269  -0.0165 -0.0198 539 PHE D CZ  
12133 N N   . GLN D 239 ? 0.8242 0.6783 0.6924 -0.0385 -0.0338 -0.0145 540 GLN D N   
12134 C CA  . GLN D 239 ? 0.8596 0.7270 0.7300 -0.0513 -0.0367 -0.0121 540 GLN D CA  
12135 C C   . GLN D 239 ? 0.7825 0.6839 0.6704 -0.0485 -0.0377 -0.0086 540 GLN D C   
12136 O O   . GLN D 239 ? 0.8104 0.7256 0.6986 -0.0491 -0.0381 -0.0108 540 GLN D O   
12137 C CB  . GLN D 239 ? 0.9636 0.8223 0.8165 -0.0676 -0.0380 -0.0174 540 GLN D CB  
12138 C CG  . GLN D 239 ? 1.0180 0.8940 0.8729 -0.0828 -0.0407 -0.0156 540 GLN D CG  
12139 C CD  . GLN D 239 ? 1.1060 0.9981 0.9545 -0.0964 -0.0426 -0.0203 540 GLN D CD  
12140 O OE1 . GLN D 239 ? 1.1134 1.0264 0.9693 -0.0916 -0.0432 -0.0211 540 GLN D OE1 
12141 N NE2 . GLN D 239 ? 1.0426 0.9249 0.8763 -0.1142 -0.0438 -0.0232 540 GLN D NE2 
12142 N N   . ILE D 240 ? 0.7974 0.7109 0.6986 -0.0449 -0.0382 -0.0032 541 ILE D N   
12143 C CA  . ILE D 240 ? 0.7589 0.7024 0.6747 -0.0428 -0.0395 0.0001  541 ILE D CA  
12144 C C   . ILE D 240 ? 0.7728 0.7334 0.6846 -0.0553 -0.0421 -0.0024 541 ILE D C   
12145 O O   . ILE D 240 ? 0.8601 0.8171 0.7647 -0.0678 -0.0432 -0.0037 541 ILE D O   
12146 C CB  . ILE D 240 ? 0.5859 0.5368 0.5128 -0.0402 -0.0397 0.0051  541 ILE D CB  
12147 C CG1 . ILE D 240 ? 0.6731 0.6084 0.6034 -0.0296 -0.0377 0.0075  541 ILE D CG1 
12148 C CG2 . ILE D 240 ? 0.4759 0.4547 0.4164 -0.0357 -0.0407 0.0079  541 ILE D CG2 
12149 C CD1 . ILE D 240 ? 0.6714 0.6160 0.6131 -0.0265 -0.0379 0.0122  541 ILE D CD1 
12150 N N   . PRO D 241 ? 0.7541 0.7342 0.6697 -0.0530 -0.0433 -0.0029 542 PRO D N   
12151 C CA  . PRO D 241 ? 0.7264 0.7250 0.6378 -0.0649 -0.0463 -0.0058 542 PRO D CA  
12152 C C   . PRO D 241 ? 0.6657 0.6845 0.5853 -0.0713 -0.0480 -0.0035 542 PRO D C   
12153 O O   . PRO D 241 ? 0.5710 0.6034 0.5041 -0.0621 -0.0478 0.0009  542 PRO D O   
12154 C CB  . PRO D 241 ? 0.5953 0.6127 0.5117 -0.0569 -0.0474 -0.0049 542 PRO D CB  
12155 C CG  . PRO D 241 ? 0.6212 0.6210 0.5381 -0.0446 -0.0442 -0.0037 542 PRO D CG  
12156 C CD  . PRO D 241 ? 0.6754 0.6629 0.5986 -0.0400 -0.0423 -0.0006 542 PRO D CD  
12157 N N   . PRO D 242 ? 0.5472 0.5678 0.4579 -0.0875 -0.0493 -0.0067 543 PRO D N   
12158 C CA  . PRO D 242 ? 0.6036 0.6402 0.5204 -0.0952 -0.0500 -0.0049 543 PRO D CA  
12159 C C   . PRO D 242 ? 0.6766 0.7510 0.6096 -0.0886 -0.0518 -0.0024 543 PRO D C   
12160 O O   . PRO D 242 ? 0.7409 0.8283 0.6832 -0.0877 -0.0514 0.0002  543 PRO D O   
12161 C CB  . PRO D 242 ? 0.6093 0.6423 0.5110 -0.1160 -0.0511 -0.0097 543 PRO D CB  
12162 C CG  . PRO D 242 ? 0.5737 0.5777 0.4593 -0.1175 -0.0503 -0.0139 543 PRO D CG  
12163 C CD  . PRO D 242 ? 0.4664 0.4756 0.3602 -0.1008 -0.0500 -0.0126 543 PRO D CD  
12164 N N   . GLU D 243 ? 0.6011 0.6929 0.5371 -0.0829 -0.0539 -0.0030 544 GLU D N   
12165 C CA  . GLU D 243 ? 0.5392 0.6652 0.4894 -0.0742 -0.0561 -0.0003 544 GLU D CA  
12166 C C   . GLU D 243 ? 0.4858 0.6069 0.4468 -0.0568 -0.0542 0.0047  544 GLU D C   
12167 O O   . GLU D 243 ? 0.4608 0.6057 0.4326 -0.0479 -0.0555 0.0072  544 GLU D O   
12168 C CB  . GLU D 243 ? 0.5468 0.6913 0.4953 -0.0721 -0.0594 -0.0017 544 GLU D CB  
12169 C CG  . GLU D 243 ? 0.6333 0.7594 0.5773 -0.0609 -0.0586 -0.0004 544 GLU D CG  
12170 C CD  . GLU D 243 ? 0.6936 0.7952 0.6217 -0.0703 -0.0575 -0.0052 544 GLU D CD  
12171 O OE1 . GLU D 243 ? 0.6630 0.7556 0.5820 -0.0854 -0.0572 -0.0093 544 GLU D OE1 
12172 O OE2 . GLU D 243 ? 0.7702 0.8607 0.6938 -0.0626 -0.0567 -0.0051 544 GLU D OE2 
12173 N N   . LEU D 244 ? 0.4403 0.5315 0.3979 -0.0517 -0.0513 0.0061  545 LEU D N   
12174 C CA  . LEU D 244 ? 0.4133 0.4987 0.3798 -0.0374 -0.0493 0.0104  545 LEU D CA  
12175 C C   . LEU D 244 ? 0.4247 0.5028 0.3950 -0.0394 -0.0474 0.0118  545 LEU D C   
12176 O O   . LEU D 244 ? 0.5096 0.5861 0.4876 -0.0289 -0.0460 0.0150  545 LEU D O   
12177 C CB  . LEU D 244 ? 0.3160 0.3775 0.2779 -0.0297 -0.0473 0.0111  545 LEU D CB  
12178 C CG  . LEU D 244 ? 0.4633 0.5269 0.4212 -0.0246 -0.0481 0.0109  545 LEU D CG  
12179 C CD1 . LEU D 244 ? 0.4665 0.5083 0.4229 -0.0165 -0.0449 0.0123  545 LEU D CD1 
12180 C CD2 . LEU D 244 ? 0.5554 0.6433 0.5204 -0.0162 -0.0506 0.0139  545 LEU D CD2 
12181 N N   . VAL D 245 ? 0.4046 0.4768 0.3681 -0.0531 -0.0473 0.0096  546 VAL D N   
12182 C CA  . VAL D 245 ? 0.4797 0.5449 0.4447 -0.0566 -0.0456 0.0113  546 VAL D CA  
12183 C C   . VAL D 245 ? 0.5344 0.6302 0.5066 -0.0623 -0.0466 0.0108  546 VAL D C   
12184 O O   . VAL D 245 ? 0.5064 0.6116 0.4728 -0.0773 -0.0475 0.0082  546 VAL D O   
12185 C CB  . VAL D 245 ? 0.5454 0.5834 0.4964 -0.0682 -0.0449 0.0097  546 VAL D CB  
12186 C CG1 . VAL D 245 ? 0.6321 0.6612 0.5838 -0.0700 -0.0435 0.0125  546 VAL D CG1 
12187 C CG2 . VAL D 245 ? 0.4992 0.5106 0.4427 -0.0621 -0.0440 0.0089  546 VAL D CG2 
12188 N N   . LEU D 246 ? 0.4521 0.5637 0.4361 -0.0507 -0.0460 0.0131  547 LEU D N   
12189 C CA  . LEU D 246 ? 0.4715 0.6138 0.4635 -0.0535 -0.0464 0.0124  547 LEU D CA  
12190 C C   . LEU D 246 ? 0.5814 0.7168 0.5707 -0.0633 -0.0443 0.0129  547 LEU D C   
12191 O O   . LEU D 246 ? 0.5817 0.6944 0.5694 -0.0590 -0.0425 0.0153  547 LEU D O   
12192 C CB  . LEU D 246 ? 0.4312 0.5885 0.4346 -0.0363 -0.0462 0.0144  547 LEU D CB  
12193 C CG  . LEU D 246 ? 0.3867 0.5735 0.3991 -0.0356 -0.0456 0.0135  547 LEU D CG  
12194 C CD1 . LEU D 246 ? 0.4360 0.6546 0.4498 -0.0450 -0.0480 0.0104  547 LEU D CD1 
12195 C CD2 . LEU D 246 ? 0.4267 0.6208 0.4475 -0.0170 -0.0452 0.0153  547 LEU D CD2 
12196 N N   . GLU D 247 ? 0.4895 0.6461 0.4779 -0.0771 -0.0446 0.0106  548 GLU D N   
12197 C CA  . GLU D 247 ? 0.4389 0.5896 0.4222 -0.0893 -0.0426 0.0112  548 GLU D CA  
12198 C C   . GLU D 247 ? 0.5491 0.7380 0.5415 -0.0934 -0.0418 0.0095  548 GLU D C   
12199 O O   . GLU D 247 ? 0.5826 0.8032 0.5822 -0.0924 -0.0435 0.0071  548 GLU D O   
12200 C CB  . GLU D 247 ? 0.3874 0.5175 0.3542 -0.1077 -0.0431 0.0098  548 GLU D CB  
12201 C CG  . GLU D 247 ? 0.3806 0.4705 0.3369 -0.1037 -0.0432 0.0112  548 GLU D CG  
12202 C CD  . GLU D 247 ? 0.5265 0.5944 0.4644 -0.1212 -0.0437 0.0093  548 GLU D CD  
12203 O OE1 . GLU D 247 ? 0.5046 0.5890 0.4384 -0.1342 -0.0450 0.0058  548 GLU D OE1 
12204 O OE2 . GLU D 247 ? 0.5529 0.5865 0.4792 -0.1222 -0.0430 0.0112  548 GLU D OE2 
12205 N N   . VAL D 248 ? 0.4951 0.6825 0.4870 -0.0979 -0.0394 0.0108  549 VAL D N   
12206 C CA  . VAL D 248 ? 0.5347 0.7583 0.5351 -0.1017 -0.0377 0.0090  549 VAL D CA  
12207 C C   . VAL D 248 ? 0.4661 0.6876 0.4553 -0.1242 -0.0363 0.0087  549 VAL D C   
12208 O O   . VAL D 248 ? 0.4330 0.6257 0.4125 -0.1288 -0.0349 0.0116  549 VAL D O   
12209 C CB  . VAL D 248 ? 0.4478 0.6750 0.4577 -0.0862 -0.0354 0.0104  549 VAL D CB  
12210 C CG1 . VAL D 248 ? 0.4103 0.6765 0.4286 -0.0893 -0.0333 0.0077  549 VAL D CG1 
12211 C CG2 . VAL D 248 ? 0.3990 0.6220 0.4167 -0.0649 -0.0367 0.0112  549 VAL D CG2 
12212 N N   . PRO D 249 ? 0.4087 0.6593 0.3974 -0.1394 -0.0366 0.0054  550 PRO D N   
12213 C CA  . PRO D 249 ? 0.5056 0.7573 0.4835 -0.1619 -0.0345 0.0053  550 PRO D CA  
12214 C C   . PRO D 249 ? 0.6288 0.9005 0.6151 -0.1581 -0.0311 0.0058  550 PRO D C   
12215 O O   . PRO D 249 ? 0.6841 0.9875 0.6864 -0.1435 -0.0305 0.0038  550 PRO D O   
12216 C CB  . PRO D 249 ? 0.3409 0.6260 0.3190 -0.1777 -0.0358 0.0010  550 PRO D CB  
12217 C CG  . PRO D 249 ? 0.4225 0.7417 0.4189 -0.1587 -0.0378 -0.0013 550 PRO D CG  
12218 C CD  . PRO D 249 ? 0.4367 0.7250 0.4357 -0.1365 -0.0389 0.0018  550 PRO D CD  
12219 N N   . ILE D 250 ? 0.6570 0.9086 0.6312 -0.1705 -0.0289 0.0085  551 ILE D N   
12220 C CA  . ILE D 250 ? 0.5585 0.8231 0.5382 -0.1670 -0.0255 0.0094  551 ILE D CA  
12221 C C   . ILE D 250 ? 0.4538 0.7527 0.4318 -0.1875 -0.0227 0.0068  551 ILE D C   
12222 O O   . ILE D 250 ? 0.5532 0.8372 0.5144 -0.2099 -0.0224 0.0082  551 ILE D O   
12223 C CB  . ILE D 250 ? 0.4659 0.6882 0.4338 -0.1656 -0.0250 0.0145  551 ILE D CB  
12224 C CG1 . ILE D 250 ? 0.4647 0.6547 0.4335 -0.1479 -0.0277 0.0166  551 ILE D CG1 
12225 C CG2 . ILE D 250 ? 0.4688 0.7053 0.4434 -0.1591 -0.0217 0.0148  551 ILE D CG2 
12226 C CD1 . ILE D 250 ? 0.3337 0.5428 0.3203 -0.1259 -0.0281 0.0145  551 ILE D CD1 
12227 N N   . ARG D 251 ? 0.4327 0.7778 0.4274 -0.1798 -0.0207 0.0029  552 ARG D N   
12228 C CA  . ARG D 251 ? 0.5383 0.9231 0.5348 -0.1964 -0.0172 0.0000  552 ARG D CA  
12229 C C   . ARG D 251 ? 0.5030 0.9068 0.5097 -0.1837 -0.0132 -0.0010 552 ARG D C   
12230 O O   . ARG D 251 ? 0.5113 0.9004 0.5247 -0.1618 -0.0136 0.0000  552 ARG D O   
12231 C CB  . ARG D 251 ? 0.5101 0.9421 0.5177 -0.2005 -0.0184 -0.0052 552 ARG D CB  
12232 C CG  . ARG D 251 ? 0.5655 1.0235 0.5928 -0.1737 -0.0201 -0.0079 552 ARG D CG  
12233 C CD  . ARG D 251 ? 0.5236 0.9599 0.5499 -0.1646 -0.0251 -0.0068 552 ARG D CD  
12234 N NE  . ARG D 251 ? 0.5368 0.9960 0.5797 -0.1393 -0.0270 -0.0087 552 ARG D NE  
12235 C CZ  . ARG D 251 ? 0.5956 1.0312 0.6392 -0.1232 -0.0305 -0.0067 552 ARG D CZ  
12236 N NH1 . ARG D 251 ? 0.6376 1.0934 0.6944 -0.1006 -0.0320 -0.0079 552 ARG D NH1 
12237 N NH2 . ARG D 251 ? 0.6105 1.0019 0.6408 -0.1293 -0.0323 -0.0035 552 ARG D NH2 
12238 N N   . HIS D 252 ? 0.5210 0.9581 0.5281 -0.1985 -0.0091 -0.0033 553 HIS D N   
12239 C CA  . HIS D 252 ? 0.5679 1.0216 0.5816 -0.1896 -0.0046 -0.0046 553 HIS D CA  
12240 C C   . HIS D 252 ? 0.5998 1.1156 0.6309 -0.1857 -0.0018 -0.0113 553 HIS D C   
12241 O O   . HIS D 252 ? 0.6936 1.2412 0.7261 -0.2021 -0.0019 -0.0140 553 HIS D O   
12242 C CB  . HIS D 252 ? 0.5483 0.9835 0.5446 -0.2106 -0.0015 -0.0010 553 HIS D CB  
12243 C CG  . HIS D 252 ? 0.5354 0.9761 0.5348 -0.2011 0.0027  -0.0014 553 HIS D CG  
12244 N ND1 . HIS D 252 ? 0.5447 1.0333 0.5539 -0.2026 0.0078  -0.0066 553 HIS D ND1 
12245 C CD2 . HIS D 252 ? 0.5140 0.9189 0.5070 -0.1912 0.0026  0.0024  553 HIS D CD2 
12246 C CE1 . HIS D 252 ? 0.4385 0.9190 0.4467 -0.1935 0.0108  -0.0062 553 HIS D CE1 
12247 N NE2 . HIS D 252 ? 0.5345 0.9647 0.5330 -0.1869 0.0075  -0.0007 553 HIS D NE2 
12248 N N   . PRO D 253 ? 0.5698 1.1045 0.6140 -0.1640 0.0008  -0.0144 554 PRO D N   
12249 C CA  . PRO D 253 ? 0.5083 1.1032 0.5699 -0.1561 0.0032  -0.0212 554 PRO D CA  
12250 C C   . PRO D 253 ? 0.5455 1.1800 0.6056 -0.1786 0.0084  -0.0242 554 PRO D C   
12251 O O   . PRO D 253 ? 0.7111 1.3915 0.7797 -0.1809 0.0090  -0.0291 554 PRO D O   
12252 C CB  . PRO D 253 ? 0.3559 0.9498 0.4272 -0.1271 0.0051  -0.0234 554 PRO D CB  
12253 C CG  . PRO D 253 ? 0.3989 0.9399 0.4566 -0.1274 0.0053  -0.0183 554 PRO D CG  
12254 C CD  . PRO D 253 ? 0.4267 0.9279 0.4704 -0.1434 0.0010  -0.0124 554 PRO D CD  
12255 N N   . LYS D 254 ? 0.6159 1.2293 0.6620 -0.1937 0.0119  -0.0212 555 LYS D N   
12256 C CA  . LYS D 254 ? 0.6805 1.3253 0.7211 -0.2151 0.0173  -0.0235 555 LYS D CA  
12257 C C   . LYS D 254 ? 0.6082 1.2295 0.6263 -0.2446 0.0158  -0.0197 555 LYS D C   
12258 O O   . LYS D 254 ? 0.6409 1.2860 0.6511 -0.2578 0.0174  -0.0229 555 LYS D O   
12259 C CB  . LYS D 254 ? 0.8916 1.5268 0.9273 -0.2141 0.0224  -0.0225 555 LYS D CB  
12260 C CG  . LYS D 254 ? 1.0003 1.6253 1.0462 -0.1821 0.0226  -0.0245 555 LYS D CG  
12261 C CD  . LYS D 254 ? 1.0339 1.7147 1.1004 -0.1632 0.0255  -0.0329 555 LYS D CD  
12262 C CE  . LYS D 254 ? 1.0613 1.7273 1.1343 -0.1328 0.0263  -0.0351 555 LYS D CE  
12263 N NZ  . LYS D 254 ? 1.0872 1.8056 1.1779 -0.1133 0.0298  -0.0435 555 LYS D NZ  
12264 N N   . PHE D 255 ? 0.5789 1.1528 0.5852 -0.2549 0.0126  -0.0130 556 PHE D N   
12265 C CA  . PHE D 255 ? 0.6660 1.2082 0.6466 -0.2819 0.0115  -0.0087 556 PHE D CA  
12266 C C   . PHE D 255 ? 0.7469 1.2827 0.7267 -0.2850 0.0066  -0.0093 556 PHE D C   
12267 O O   . PHE D 255 ? 0.7839 1.2943 0.7689 -0.2748 0.0020  -0.0069 556 PHE D O   
12268 C CB  . PHE D 255 ? 0.7423 1.2311 0.7059 -0.2901 0.0109  -0.0009 556 PHE D CB  
12269 C CG  . PHE D 255 ? 0.7181 1.2075 0.6807 -0.2842 0.0153  0.0002  556 PHE D CG  
12270 C CD1 . PHE D 255 ? 0.6244 1.0636 0.5753 -0.2757 0.0134  0.0062  556 PHE D CD1 
12271 C CD2 . PHE D 255 ? 0.8237 1.3600 0.7945 -0.2842 0.0206  -0.0054 556 PHE D CD2 
12272 C CE1 . PHE D 255 ? 0.6156 1.0555 0.5647 -0.2708 0.0171  0.0069  556 PHE D CE1 
12273 C CE2 . PHE D 255 ? 0.8015 1.3404 0.7715 -0.2804 0.0251  -0.0049 556 PHE D CE2 
12274 C CZ  . PHE D 255 ? 0.7221 1.2117 0.6806 -0.2740 0.0232  0.0013  556 PHE D CZ  
12275 N N   . GLU D 256 ? 0.7405 1.2985 0.7125 -0.2982 0.0074  -0.0128 557 GLU D N   
12276 C CA  . GLU D 256 ? 0.6926 1.2448 0.6612 -0.3034 0.0034  -0.0136 557 GLU D CA  
12277 C C   . GLU D 256 ? 0.7536 1.2500 0.6970 -0.3231 0.0009  -0.0081 557 GLU D C   
12278 O O   . GLU D 256 ? 0.9212 1.3997 0.8629 -0.3231 -0.0033 -0.0077 557 GLU D O   
12279 C CB  . GLU D 256 ? 0.8476 1.4430 0.8150 -0.3118 0.0054  -0.0193 557 GLU D CB  
12280 C CG  . GLU D 256 ? 1.0107 1.6569 0.9949 -0.2976 0.0092  -0.0245 557 GLU D CG  
12281 C CD  . GLU D 256 ? 1.2450 1.9143 1.2148 -0.3175 0.0133  -0.0273 557 GLU D CD  
12282 O OE1 . GLU D 256 ? 1.3884 2.0585 1.3435 -0.3366 0.0127  -0.0281 557 GLU D OE1 
12283 O OE2 . GLU D 256 ? 1.2551 1.9413 1.2274 -0.3146 0.0171  -0.0289 557 GLU D OE2 
12284 N N   . TRP D 257 ? 0.7628 1.2297 0.6856 -0.3386 0.0032  -0.0037 558 TRP D N   
12285 C CA  . TRP D 257 ? 0.7287 1.1372 0.6258 -0.3539 0.0006  0.0020  558 TRP D CA  
12286 C C   . TRP D 257 ? 0.7663 1.1385 0.6697 -0.3402 -0.0037 0.0061  558 TRP D C   
12287 O O   . TRP D 257 ? 0.8733 1.1962 0.7568 -0.3493 -0.0065 0.0102  558 TRP D O   
12288 C CB  . TRP D 257 ? 0.8142 1.1963 0.6869 -0.3705 0.0033  0.0066  558 TRP D CB  
12289 C CG  . TRP D 257 ? 0.6937 1.0859 0.5761 -0.3603 0.0063  0.0085  558 TRP D CG  
12290 C CD1 . TRP D 257 ? 0.7297 1.1647 0.6200 -0.3596 0.0108  0.0045  558 TRP D CD1 
12291 C CD2 . TRP D 257 ? 0.7792 1.1379 0.6628 -0.3500 0.0052  0.0145  558 TRP D CD2 
12292 N NE1 . TRP D 257 ? 0.8255 1.2555 0.7219 -0.3493 0.0128  0.0073  558 TRP D NE1 
12293 C CE2 . TRP D 257 ? 0.8166 1.2006 0.7090 -0.3437 0.0095  0.0137  558 TRP D CE2 
12294 C CE3 . TRP D 257 ? 0.8012 1.1114 0.6786 -0.3453 0.0011  0.0202  558 TRP D CE3 
12295 C CZ2 . TRP D 257 ? 0.7006 1.0629 0.5951 -0.3334 0.0100  0.0188  558 TRP D CZ2 
12296 C CZ3 . TRP D 257 ? 0.7503 1.0335 0.6276 -0.3272 0.0005  0.0246  558 TRP D CZ3 
12297 C CH2 . TRP D 257 ? 0.6595 0.9684 0.5450 -0.3217 0.0048  0.0239  558 TRP D CH2 
12298 N N   . PHE D 258 ? 0.6662 1.0593 0.5949 -0.3170 -0.0042 0.0047  559 PHE D N   
12299 C CA  . PHE D 258 ? 0.6495 0.9952 0.5765 -0.2948 -0.0077 0.0089  559 PHE D CA  
12300 C C   . PHE D 258 ? 0.7329 1.0546 0.6568 -0.2909 -0.0126 0.0085  559 PHE D C   
12301 O O   . PHE D 258 ? 0.7168 0.9867 0.6257 -0.2882 -0.0153 0.0130  559 PHE D O   
12302 C CB  . PHE D 258 ? 0.5569 0.9228 0.5061 -0.2657 -0.0068 0.0070  559 PHE D CB  
12303 C CG  . PHE D 258 ? 0.5964 0.9168 0.5404 -0.2491 -0.0083 0.0122  559 PHE D CG  
12304 C CD1 . PHE D 258 ? 0.6359 0.9505 0.5756 -0.2484 -0.0053 0.0149  559 PHE D CD1 
12305 C CD2 . PHE D 258 ? 0.6095 0.8939 0.5521 -0.2353 -0.0128 0.0143  559 PHE D CD2 
12306 C CE1 . PHE D 258 ? 0.6103 0.8857 0.5452 -0.2340 -0.0071 0.0195  559 PHE D CE1 
12307 C CE2 . PHE D 258 ? 0.6017 0.8478 0.5401 -0.2208 -0.0142 0.0188  559 PHE D CE2 
12308 C CZ  . PHE D 258 ? 0.6259 0.8678 0.5605 -0.2203 -0.0116 0.0215  559 PHE D CZ  
12309 N N   . LYS D 259 ? 0.6541 1.0142 0.5918 -0.2900 -0.0139 0.0029  560 LYS D N   
12310 C CA  . LYS D 259 ? 0.7056 1.0468 0.6396 -0.2884 -0.0184 0.0019  560 LYS D CA  
12311 C C   . LYS D 259 ? 0.7262 1.0249 0.6321 -0.3134 -0.0194 0.0043  560 LYS D C   
12312 O O   . LYS D 259 ? 0.7697 1.0321 0.6664 -0.3093 -0.0228 0.0051  560 LYS D O   
12313 C CB  . LYS D 259 ? 0.5941 0.9891 0.5456 -0.2877 -0.0196 -0.0044 560 LYS D CB  
12314 C CG  . LYS D 259 ? 0.5218 0.9588 0.4713 -0.3080 -0.0158 -0.0079 560 LYS D CG  
12315 C CD  . LYS D 259 ? 0.7166 1.1909 0.6749 -0.3050 -0.0172 -0.0132 560 LYS D CD  
12316 C CE  . LYS D 259 ? 0.7686 1.2699 0.7154 -0.3237 -0.0125 -0.0160 560 LYS D CE  
12317 N NZ  . LYS D 259 ? 0.7495 1.2831 0.7036 -0.3210 -0.0076 -0.0170 560 LYS D NZ  
12318 N N   . ASP D 260 ? 0.6933 0.9940 0.5837 -0.3393 -0.0162 0.0055  561 ASP D N   
12319 C CA  . ASP D 260 ? 0.7140 0.9674 0.5726 -0.3593 -0.0165 0.0082  561 ASP D CA  
12320 C C   . ASP D 260 ? 0.6696 0.8621 0.5120 -0.3548 -0.0184 0.0148  561 ASP D C   
12321 O O   . ASP D 260 ? 0.6738 0.8203 0.4895 -0.3685 -0.0196 0.0171  561 ASP D O   
12322 C CB  . ASP D 260 ? 0.8381 1.1027 0.6793 -0.3785 -0.0118 0.0081  561 ASP D CB  
12323 C CG  . ASP D 260 ? 0.9328 1.2596 0.7895 -0.3798 -0.0092 0.0018  561 ASP D CG  
12324 O OD1 . ASP D 260 ? 1.0283 1.3859 0.9071 -0.3659 -0.0113 -0.0023 561 ASP D OD1 
12325 O OD2 . ASP D 260 ? 0.9295 1.2745 0.7756 -0.3941 -0.0053 0.0009  561 ASP D OD2 
12326 N N   . LEU D 261 ? 0.6463 0.8333 0.5015 -0.3301 -0.0184 0.0178  562 LEU D N   
12327 C CA  . LEU D 261 ? 0.6717 0.8012 0.5117 -0.3196 -0.0206 0.0238  562 LEU D CA  
12328 C C   . LEU D 261 ? 0.8048 0.9054 0.6430 -0.3075 -0.0246 0.0225  562 LEU D C   
12329 O O   . LEU D 261 ? 0.8489 0.8982 0.6684 -0.3051 -0.0266 0.0265  562 LEU D O   
12330 C CB  . LEU D 261 ? 0.6084 0.7426 0.4627 -0.2977 -0.0196 0.0268  562 LEU D CB  
12331 C CG  . LEU D 261 ? 0.6374 0.8054 0.4945 -0.3096 -0.0151 0.0270  562 LEU D CG  
12332 C CD1 . LEU D 261 ? 0.7164 0.8998 0.5919 -0.2869 -0.0139 0.0276  562 LEU D CD1 
12333 C CD2 . LEU D 261 ? 0.7034 0.8384 0.5314 -0.3328 -0.0140 0.0327  562 LEU D CD2 
12334 N N   . GLY D 262 ? 0.8242 0.9571 0.6802 -0.3003 -0.0258 0.0168  563 GLY D N   
12335 C CA  . GLY D 262 ? 0.7818 0.8920 0.6364 -0.2899 -0.0292 0.0150  563 GLY D CA  
12336 C C   . GLY D 262 ? 0.8056 0.9026 0.6743 -0.2601 -0.0308 0.0169  563 GLY D C   
12337 O O   . GLY D 262 ? 0.8201 0.8884 0.6838 -0.2507 -0.0333 0.0166  563 GLY D O   
12338 N N   . LEU D 263 ? 0.7535 0.8707 0.6387 -0.2455 -0.0293 0.0186  564 LEU D N   
12339 C CA  . LEU D 263 ? 0.7244 0.8249 0.6197 -0.2198 -0.0305 0.0210  564 LEU D CA  
12340 C C   . LEU D 263 ? 0.6671 0.7948 0.5837 -0.2018 -0.0318 0.0171  564 LEU D C   
12341 O O   . LEU D 263 ? 0.4589 0.6288 0.3880 -0.2046 -0.0312 0.0131  564 LEU D O   
12342 C CB  . LEU D 263 ? 0.6493 0.7541 0.5498 -0.2129 -0.0284 0.0245  564 LEU D CB  
12343 C CG  . LEU D 263 ? 0.7388 0.8186 0.6181 -0.2298 -0.0272 0.0293  564 LEU D CG  
12344 C CD1 . LEU D 263 ? 0.5565 0.6541 0.4439 -0.2248 -0.0245 0.0314  564 LEU D CD1 
12345 C CD2 . LEU D 263 ? 0.7749 0.8000 0.6346 -0.2270 -0.0299 0.0340  564 LEU D CD2 
12346 N N   . LYS D 264 ? 0.6218 0.7251 0.5416 -0.1830 -0.0336 0.0187  565 LYS D N   
12347 C CA  . LYS D 264 ? 0.5557 0.6763 0.4934 -0.1634 -0.0347 0.0165  565 LYS D CA  
12348 C C   . LYS D 264 ? 0.6462 0.7374 0.5855 -0.1449 -0.0353 0.0200  565 LYS D C   
12349 O O   . LYS D 264 ? 0.7906 0.8488 0.7170 -0.1474 -0.0355 0.0235  565 LYS D O   
12350 C CB  . LYS D 264 ? 0.5630 0.6868 0.4984 -0.1672 -0.0370 0.0129  565 LYS D CB  
12351 C CG  . LYS D 264 ? 0.5776 0.6571 0.4948 -0.1711 -0.0386 0.0137  565 LYS D CG  
12352 C CD  . LYS D 264 ? 0.6324 0.7196 0.5493 -0.1730 -0.0406 0.0094  565 LYS D CD  
12353 C CE  . LYS D 264 ? 0.7366 0.7856 0.6314 -0.1845 -0.0417 0.0082  565 LYS D CE  
12354 N NZ  . LYS D 264 ? 0.8205 0.8797 0.7172 -0.1833 -0.0437 0.0037  565 LYS D NZ  
12355 N N   . TRP D 265 ? 0.5544 0.6586 0.5092 -0.1264 -0.0357 0.0190  566 TRP D N   
12356 C CA  . TRP D 265 ? 0.6134 0.6928 0.5704 -0.1100 -0.0362 0.0218  566 TRP D CA  
12357 C C   . TRP D 265 ? 0.7286 0.8155 0.6956 -0.0959 -0.0375 0.0199  566 TRP D C   
12358 O O   . TRP D 265 ? 0.8368 0.9534 0.8130 -0.0942 -0.0378 0.0171  566 TRP D O   
12359 C CB  . TRP D 265 ? 0.4215 0.5052 0.3854 -0.1020 -0.0344 0.0241  566 TRP D CB  
12360 C CG  . TRP D 265 ? 0.3703 0.4236 0.3310 -0.0917 -0.0351 0.0275  566 TRP D CG  
12361 C CD1 . TRP D 265 ? 0.3626 0.4147 0.3334 -0.0753 -0.0350 0.0281  566 TRP D CD1 
12362 C CD2 . TRP D 265 ? 0.3976 0.4177 0.3432 -0.0970 -0.0363 0.0308  566 TRP D CD2 
12363 N NE1 . TRP D 265 ? 0.3424 0.3663 0.3070 -0.0707 -0.0360 0.0312  566 TRP D NE1 
12364 C CE2 . TRP D 265 ? 0.4011 0.4052 0.3505 -0.0826 -0.0369 0.0330  566 TRP D CE2 
12365 C CE3 . TRP D 265 ? 0.4723 0.4742 0.4006 -0.1126 -0.0369 0.0321  566 TRP D CE3 
12366 C CZ2 . TRP D 265 ? 0.5154 0.4893 0.4536 -0.0817 -0.0384 0.0365  566 TRP D CZ2 
12367 C CZ3 . TRP D 265 ? 0.5542 0.5213 0.4692 -0.1112 -0.0384 0.0359  566 TRP D CZ3 
12368 C CH2 . TRP D 265 ? 0.6232 0.5781 0.5441 -0.0949 -0.0393 0.0380  566 TRP D CH2 
12369 N N   . TYR D 266 ? 0.5585 0.6191 0.5229 -0.0861 -0.0383 0.0214  567 TYR D N   
12370 C CA  . TYR D 266 ? 0.4522 0.5179 0.4251 -0.0725 -0.0390 0.0204  567 TYR D CA  
12371 C C   . TYR D 266 ? 0.5049 0.5866 0.4912 -0.0588 -0.0378 0.0212  567 TYR D C   
12372 O O   . TYR D 266 ? 0.6467 0.7264 0.6346 -0.0575 -0.0364 0.0229  567 TYR D O   
12373 C CB  . TYR D 266 ? 0.4613 0.4964 0.4277 -0.0664 -0.0396 0.0215  567 TYR D CB  
12374 C CG  . TYR D 266 ? 0.5014 0.5159 0.4656 -0.0617 -0.0389 0.0248  567 TYR D CG  
12375 C CD1 . TYR D 266 ? 0.6410 0.6576 0.6150 -0.0485 -0.0380 0.0264  567 TYR D CD1 
12376 C CD2 . TYR D 266 ? 0.4852 0.4775 0.4362 -0.0706 -0.0393 0.0265  567 TYR D CD2 
12377 C CE1 . TYR D 266 ? 0.5593 0.5599 0.5316 -0.0447 -0.0378 0.0293  567 TYR D CE1 
12378 C CE2 . TYR D 266 ? 0.5447 0.5198 0.4936 -0.0652 -0.0393 0.0299  567 TYR D CE2 
12379 C CZ  . TYR D 266 ? 0.5995 0.5809 0.5600 -0.0524 -0.0386 0.0311  567 TYR D CZ  
12380 O OH  . TYR D 266 ? 0.7766 0.7441 0.7357 -0.0475 -0.0389 0.0343  567 TYR D OH  
12381 N N   . GLY D 267 ? 0.5313 0.6274 0.5255 -0.0487 -0.0385 0.0201  568 GLY D N   
12382 C CA  . GLY D 267 ? 0.3609 0.4720 0.3656 -0.0360 -0.0374 0.0204  568 GLY D CA  
12383 C C   . GLY D 267 ? 0.4059 0.4984 0.4126 -0.0233 -0.0367 0.0226  568 GLY D C   
12384 O O   . GLY D 267 ? 0.4740 0.5737 0.4870 -0.0132 -0.0355 0.0228  568 GLY D O   
12385 N N   . LEU D 268 ? 0.4068 0.4755 0.4077 -0.0234 -0.0371 0.0238  569 LEU D N   
12386 C CA  . LEU D 268 ? 0.4914 0.5467 0.4944 -0.0121 -0.0365 0.0254  569 LEU D CA  
12387 C C   . LEU D 268 ? 0.6024 0.6360 0.6017 -0.0130 -0.0358 0.0272  569 LEU D C   
12388 O O   . LEU D 268 ? 0.6746 0.6927 0.6671 -0.0171 -0.0365 0.0273  569 LEU D O   
12389 C CB  . LEU D 268 ? 0.4389 0.4913 0.4396 -0.0092 -0.0376 0.0248  569 LEU D CB  
12390 C CG  . LEU D 268 ? 0.4805 0.5191 0.4823 0.0007  -0.0365 0.0265  569 LEU D CG  
12391 C CD1 . LEU D 268 ? 0.4729 0.5204 0.4801 0.0105  -0.0357 0.0275  569 LEU D CD1 
12392 C CD2 . LEU D 268 ? 0.4012 0.4314 0.3983 0.0013  -0.0370 0.0260  569 LEU D CD2 
12393 N N   . PRO D 269 ? 0.4935 0.5256 0.4963 -0.0090 -0.0346 0.0285  570 PRO D N   
12394 C CA  . PRO D 269 ? 0.3358 0.3502 0.3357 -0.0091 -0.0345 0.0304  570 PRO D CA  
12395 C C   . PRO D 269 ? 0.3759 0.3803 0.3775 -0.0011 -0.0340 0.0310  570 PRO D C   
12396 O O   . PRO D 269 ? 0.4052 0.4141 0.4113 0.0056  -0.0329 0.0310  570 PRO D O   
12397 C CB  . PRO D 269 ? 0.4034 0.4239 0.4065 -0.0085 -0.0334 0.0310  570 PRO D CB  
12398 C CG  . PRO D 269 ? 0.4903 0.5266 0.4995 -0.0018 -0.0322 0.0292  570 PRO D CG  
12399 C CD  . PRO D 269 ? 0.4644 0.5112 0.4733 -0.0036 -0.0333 0.0278  570 PRO D CD  
12400 N N   . ALA D 270 ? 0.4134 0.4038 0.4106 -0.0017 -0.0347 0.0314  571 ALA D N   
12401 C CA  . ALA D 270 ? 0.4628 0.4469 0.4618 0.0051  -0.0337 0.0315  571 ALA D CA  
12402 C C   . ALA D 270 ? 0.4912 0.4622 0.4878 0.0064  -0.0342 0.0325  571 ALA D C   
12403 O O   . ALA D 270 ? 0.6414 0.6019 0.6316 0.0046  -0.0350 0.0319  571 ALA D O   
12404 C CB  . ALA D 270 ? 0.3768 0.3619 0.3730 0.0053  -0.0338 0.0298  571 ALA D CB  
12405 N N   . VAL D 271 ? 0.4356 0.4070 0.4366 0.0098  -0.0336 0.0339  572 VAL D N   
12406 C CA  . VAL D 271 ? 0.4065 0.3697 0.4067 0.0123  -0.0345 0.0351  572 VAL D CA  
12407 C C   . VAL D 271 ? 0.3675 0.3280 0.3688 0.0177  -0.0332 0.0339  572 VAL D C   
12408 O O   . VAL D 271 ? 0.4900 0.4568 0.4957 0.0201  -0.0313 0.0334  572 VAL D O   
12409 C CB  . VAL D 271 ? 0.4532 0.4212 0.4579 0.0132  -0.0345 0.0367  572 VAL D CB  
12410 C CG1 . VAL D 271 ? 0.3338 0.2975 0.3392 0.0173  -0.0356 0.0378  572 VAL D CG1 
12411 C CG2 . VAL D 271 ? 0.3784 0.3483 0.3807 0.0079  -0.0356 0.0377  572 VAL D CG2 
12412 N N   . SER D 272 ? 0.3354 0.2858 0.3319 0.0198  -0.0341 0.0335  573 SER D N   
12413 C CA  . SER D 272 ? 0.4568 0.4056 0.4537 0.0252  -0.0325 0.0315  573 SER D CA  
12414 C C   . SER D 272 ? 0.6288 0.5748 0.6270 0.0318  -0.0330 0.0319  573 SER D C   
12415 O O   . SER D 272 ? 0.5831 0.5302 0.5823 0.0371  -0.0312 0.0298  573 SER D O   
12416 C CB  . SER D 272 ? 0.4860 0.4259 0.4746 0.0233  -0.0325 0.0291  573 SER D CB  
12417 O OG  . SER D 272 ? 0.5037 0.4303 0.4834 0.0199  -0.0347 0.0295  573 SER D OG  
12418 N N   . ASN D 273 ? 0.5767 0.5208 0.5748 0.0322  -0.0354 0.0344  574 ASN D N   
12419 C CA  . ASN D 273 ? 0.4842 0.4254 0.4823 0.0399  -0.0368 0.0351  574 ASN D CA  
12420 C C   . ASN D 273 ? 0.5076 0.4645 0.5156 0.0424  -0.0367 0.0362  574 ASN D C   
12421 O O   . ASN D 273 ? 0.6052 0.5643 0.6147 0.0494  -0.0382 0.0369  574 ASN D O   
12422 C CB  . ASN D 273 ? 0.4413 0.3673 0.4297 0.0394  -0.0402 0.0377  574 ASN D CB  
12423 C CG  . ASN D 273 ? 0.5783 0.5085 0.5675 0.0324  -0.0418 0.0407  574 ASN D CG  
12424 O OD1 . ASN D 273 ? 0.6670 0.6110 0.6642 0.0292  -0.0405 0.0405  574 ASN D OD1 
12425 N ND2 . ASN D 273 ? 0.5079 0.4246 0.4870 0.0296  -0.0445 0.0433  574 ASN D ND2 
12426 N N   . MET D 274 ? 0.4571 0.4248 0.4710 0.0372  -0.0350 0.0363  575 MET D N   
12427 C CA  . MET D 274 ? 0.4569 0.4383 0.4784 0.0371  -0.0349 0.0370  575 MET D CA  
12428 C C   . MET D 274 ? 0.5873 0.5797 0.6147 0.0395  -0.0318 0.0348  575 MET D C   
12429 O O   . MET D 274 ? 0.7625 0.7519 0.7882 0.0429  -0.0299 0.0328  575 MET D O   
12430 C CB  . MET D 274 ? 0.4147 0.3988 0.4368 0.0300  -0.0347 0.0378  575 MET D CB  
12431 C CG  . MET D 274 ? 0.5489 0.5272 0.5665 0.0279  -0.0379 0.0402  575 MET D CG  
12432 S SD  . MET D 274 ? 0.6056 0.5880 0.6234 0.0205  -0.0373 0.0404  575 MET D SD  
12433 C CE  . MET D 274 ? 0.5608 0.5557 0.5848 0.0201  -0.0375 0.0403  575 MET D CE  
12434 N N   . LEU D 275 ? 0.5023 0.5079 0.5359 0.0369  -0.0310 0.0350  576 LEU D N   
12435 C CA  . LEU D 275 ? 0.4114 0.4297 0.4504 0.0375  -0.0278 0.0331  576 LEU D CA  
12436 C C   . LEU D 275 ? 0.4878 0.5115 0.5282 0.0290  -0.0258 0.0331  576 LEU D C   
12437 O O   . LEU D 275 ? 0.6967 0.7215 0.7374 0.0250  -0.0276 0.0342  576 LEU D O   
12438 C CB  . LEU D 275 ? 0.4850 0.5172 0.5301 0.0441  -0.0293 0.0327  576 LEU D CB  
12439 C CG  . LEU D 275 ? 0.4927 0.5410 0.5438 0.0460  -0.0257 0.0301  576 LEU D CG  
12440 C CD1 . LEU D 275 ? 0.4475 0.5026 0.5015 0.0578  -0.0271 0.0289  576 LEU D CD1 
12441 C CD2 . LEU D 275 ? 0.4885 0.5543 0.5456 0.0382  -0.0244 0.0300  576 LEU D CD2 
12442 N N   . LEU D 276 ? 0.5570 0.5817 0.5965 0.0259  -0.0219 0.0320  577 LEU D N   
12443 C CA  . LEU D 276 ? 0.4647 0.4887 0.5018 0.0178  -0.0196 0.0323  577 LEU D CA  
12444 C C   . LEU D 276 ? 0.6271 0.6671 0.6690 0.0137  -0.0172 0.0311  577 LEU D C   
12445 O O   . LEU D 276 ? 0.6405 0.6891 0.6851 0.0163  -0.0149 0.0298  577 LEU D O   
12446 C CB  . LEU D 276 ? 0.4755 0.4877 0.5059 0.0167  -0.0173 0.0325  577 LEU D CB  
12447 C CG  . LEU D 276 ? 0.4876 0.4955 0.5128 0.0095  -0.0143 0.0331  577 LEU D CG  
12448 C CD1 . LEU D 276 ? 0.3000 0.3002 0.3220 0.0063  -0.0157 0.0336  577 LEU D CD1 
12449 C CD2 . LEU D 276 ? 0.3654 0.3638 0.3836 0.0105  -0.0121 0.0338  577 LEU D CD2 
12450 N N   . GLU D 277 ? 0.5623 0.6075 0.6049 0.0065  -0.0175 0.0312  578 GLU D N   
12451 C CA  . GLU D 277 ? 0.4483 0.5115 0.4955 0.0005  -0.0156 0.0298  578 GLU D CA  
12452 C C   . GLU D 277 ? 0.4918 0.5464 0.5310 -0.0107 -0.0121 0.0298  578 GLU D C   
12453 O O   . GLU D 277 ? 0.4853 0.5290 0.5189 -0.0155 -0.0130 0.0301  578 GLU D O   
12454 C CB  . GLU D 277 ? 0.4391 0.5170 0.4927 0.0003  -0.0192 0.0297  578 GLU D CB  
12455 C CG  . GLU D 277 ? 0.5272 0.6313 0.5889 -0.0029 -0.0181 0.0280  578 GLU D CG  
12456 C CD  . GLU D 277 ? 0.7581 0.8676 0.8167 -0.0175 -0.0162 0.0269  578 GLU D CD  
12457 O OE1 . GLU D 277 ? 0.8439 0.9340 0.8925 -0.0249 -0.0138 0.0272  578 GLU D OE1 
12458 O OE2 . GLU D 277 ? 0.8381 0.9715 0.9038 -0.0216 -0.0170 0.0255  578 GLU D OE2 
12459 N N   . ILE D 278 ? 0.5027 0.5612 0.5399 -0.0148 -0.0079 0.0294  579 ILE D N   
12460 C CA  . ILE D 278 ? 0.4735 0.5221 0.5007 -0.0262 -0.0043 0.0298  579 ILE D CA  
12461 C C   . ILE D 278 ? 0.4988 0.5686 0.5299 -0.0347 -0.0009 0.0282  579 ILE D C   
12462 O O   . ILE D 278 ? 0.5002 0.5826 0.5360 -0.0310 0.0012  0.0276  579 ILE D O   
12463 C CB  . ILE D 278 ? 0.3658 0.3941 0.3828 -0.0239 -0.0022 0.0317  579 ILE D CB  
12464 C CG1 . ILE D 278 ? 0.4665 0.4813 0.4828 -0.0141 -0.0056 0.0327  579 ILE D CG1 
12465 C CG2 . ILE D 278 ? 0.4301 0.4413 0.4337 -0.0341 0.0006  0.0329  579 ILE D CG2 
12466 C CD1 . ILE D 278 ? 0.4695 0.4678 0.4770 -0.0107 -0.0046 0.0346  579 ILE D CD1 
12467 N N   . GLY D 279 ? 0.4896 0.5649 0.5186 -0.0466 -0.0004 0.0272  580 GLY D N   
12468 C CA  . GLY D 279 ? 0.3763 0.4723 0.4075 -0.0578 0.0033  0.0256  580 GLY D CA  
12469 C C   . GLY D 279 ? 0.5463 0.6756 0.5934 -0.0512 0.0025  0.0237  580 GLY D C   
12470 O O   . GLY D 279 ? 0.6378 0.7860 0.6879 -0.0565 0.0066  0.0223  580 GLY D O   
12471 N N   . GLY D 280 ? 0.6293 0.7665 0.6859 -0.0396 -0.0024 0.0234  581 GLY D N   
12472 C CA  . GLY D 280 ? 0.5908 0.7557 0.6610 -0.0296 -0.0036 0.0218  581 GLY D CA  
12473 C C   . GLY D 280 ? 0.5655 0.7237 0.6367 -0.0161 -0.0028 0.0220  581 GLY D C   
12474 O O   . GLY D 280 ? 0.6846 0.8598 0.7654 -0.0043 -0.0044 0.0206  581 GLY D O   
12475 N N   . LEU D 281 ? 0.4782 0.6120 0.5392 -0.0169 -0.0005 0.0234  582 LEU D N   
12476 C CA  . LEU D 281 ? 0.5064 0.6334 0.5670 -0.0054 0.0002  0.0231  582 LEU D CA  
12477 C C   . LEU D 281 ? 0.6078 0.7176 0.6676 0.0053  -0.0048 0.0244  582 LEU D C   
12478 O O   . LEU D 281 ? 0.7232 0.8168 0.7780 0.0021  -0.0073 0.0264  582 LEU D O   
12479 C CB  . LEU D 281 ? 0.5505 0.6611 0.5999 -0.0114 0.0045  0.0243  582 LEU D CB  
12480 C CG  . LEU D 281 ? 0.4800 0.6051 0.5273 -0.0237 0.0101  0.0235  582 LEU D CG  
12481 C CD1 . LEU D 281 ? 0.5389 0.6424 0.5721 -0.0296 0.0134  0.0258  582 LEU D CD1 
12482 C CD2 . LEU D 281 ? 0.4891 0.6427 0.5467 -0.0182 0.0127  0.0201  582 LEU D CD2 
12483 N N   . GLU D 282 ? 0.5812 0.6942 0.6451 0.0177  -0.0060 0.0231  583 GLU D N   
12484 C CA  . GLU D 282 ? 0.5919 0.6892 0.6541 0.0271  -0.0106 0.0243  583 GLU D CA  
12485 C C   . GLU D 282 ? 0.6492 0.7283 0.7039 0.0317  -0.0094 0.0240  583 GLU D C   
12486 O O   . GLU D 282 ? 0.5749 0.6598 0.6304 0.0375  -0.0069 0.0215  583 GLU D O   
12487 C CB  . GLU D 282 ? 0.5236 0.6355 0.5938 0.0382  -0.0138 0.0233  583 GLU D CB  
12488 C CG  . GLU D 282 ? 0.5533 0.6879 0.6317 0.0341  -0.0155 0.0234  583 GLU D CG  
12489 C CD  . GLU D 282 ? 0.5733 0.7218 0.6588 0.0472  -0.0194 0.0230  583 GLU D CD  
12490 O OE1 . GLU D 282 ? 0.7511 0.9009 0.8380 0.0478  -0.0242 0.0252  583 GLU D OE1 
12491 O OE2 . GLU D 282 ? 0.4777 0.6349 0.5664 0.0575  -0.0177 0.0205  583 GLU D OE2 
12492 N N   . PHE D 283 ? 0.5261 0.5850 0.5737 0.0291  -0.0112 0.0261  584 PHE D N   
12493 C CA  . PHE D 283 ? 0.2807 0.3234 0.3210 0.0324  -0.0109 0.0259  584 PHE D CA  
12494 C C   . PHE D 283 ? 0.3533 0.3854 0.3923 0.0397  -0.0151 0.0261  584 PHE D C   
12495 O O   . PHE D 283 ? 0.4157 0.4364 0.4515 0.0375  -0.0179 0.0281  584 PHE D O   
12496 C CB  . PHE D 283 ? 0.3109 0.3411 0.3440 0.0251  -0.0100 0.0281  584 PHE D CB  
12497 C CG  . PHE D 283 ? 0.4681 0.5040 0.4989 0.0176  -0.0057 0.0283  584 PHE D CG  
12498 C CD1 . PHE D 283 ? 0.3642 0.4028 0.3949 0.0092  -0.0049 0.0295  584 PHE D CD1 
12499 C CD2 . PHE D 283 ? 0.4948 0.5328 0.5221 0.0180  -0.0021 0.0272  584 PHE D CD2 
12500 C CE1 . PHE D 283 ? 0.3960 0.4377 0.4223 0.0007  -0.0007 0.0300  584 PHE D CE1 
12501 C CE2 . PHE D 283 ? 0.4843 0.5269 0.5077 0.0099  0.0021  0.0279  584 PHE D CE2 
12502 C CZ  . PHE D 283 ? 0.4054 0.4490 0.4279 0.0009  0.0029  0.0295  584 PHE D CZ  
12503 N N   . SER D 284 ? 0.3215 0.3568 0.3620 0.0486  -0.0153 0.0239  585 SER D N   
12504 C CA  . SER D 284 ? 0.4194 0.4424 0.4566 0.0555  -0.0194 0.0243  585 SER D CA  
12505 C C   . SER D 284 ? 0.4255 0.4286 0.4534 0.0536  -0.0204 0.0246  585 SER D C   
12506 O O   . SER D 284 ? 0.4287 0.4190 0.4516 0.0566  -0.0237 0.0253  585 SER D O   
12507 C CB  . SER D 284 ? 0.3563 0.3845 0.3951 0.0668  -0.0191 0.0215  585 SER D CB  
12508 O OG  . SER D 284 ? 0.4928 0.5265 0.5310 0.0683  -0.0145 0.0180  585 SER D OG  
12509 N N   . ALA D 285 ? 0.4935 0.4938 0.5178 0.0484  -0.0180 0.0241  586 ALA D N   
12510 C CA  . ALA D 285 ? 0.4672 0.4526 0.4835 0.0462  -0.0193 0.0241  586 ALA D CA  
12511 C C   . ALA D 285 ? 0.5532 0.5398 0.5687 0.0392  -0.0182 0.0259  586 ALA D C   
12512 O O   . ALA D 285 ? 0.5667 0.5575 0.5809 0.0377  -0.0152 0.0252  586 ALA D O   
12513 C CB  . ALA D 285 ? 0.3992 0.3781 0.4092 0.0504  -0.0178 0.0205  586 ALA D CB  
12514 N N   . CYS D 286 ? 0.4126 0.3951 0.4278 0.0355  -0.0207 0.0282  587 CYS D N   
12515 C CA  . CYS D 286 ? 0.4194 0.4030 0.4342 0.0308  -0.0200 0.0301  587 CYS D CA  
12516 C C   . CYS D 286 ? 0.4753 0.4531 0.4872 0.0286  -0.0226 0.0311  587 CYS D C   
12517 O O   . CYS D 286 ? 0.6086 0.5876 0.6220 0.0263  -0.0231 0.0326  587 CYS D O   
12518 C CB  . CYS D 286 ? 0.4474 0.4378 0.4673 0.0284  -0.0194 0.0313  587 CYS D CB  
12519 S SG  . CYS D 286 ? 0.5233 0.5150 0.5473 0.0294  -0.0229 0.0322  587 CYS D SG  
12520 N N   . PRO D 287 ? 0.4461 0.4186 0.4534 0.0287  -0.0240 0.0300  588 PRO D N   
12521 C CA  . PRO D 287 ? 0.3448 0.3153 0.3502 0.0256  -0.0264 0.0307  588 PRO D CA  
12522 C C   . PRO D 287 ? 0.3955 0.3706 0.4021 0.0244  -0.0261 0.0322  588 PRO D C   
12523 O O   . PRO D 287 ? 0.5668 0.5433 0.5719 0.0256  -0.0245 0.0326  588 PRO D O   
12524 C CB  . PRO D 287 ? 0.2854 0.2516 0.2846 0.0244  -0.0272 0.0288  588 PRO D CB  
12525 C CG  . PRO D 287 ? 0.5674 0.5336 0.5650 0.0273  -0.0250 0.0272  588 PRO D CG  
12526 C CD  . PRO D 287 ? 0.5737 0.5429 0.5764 0.0306  -0.0231 0.0276  588 PRO D CD  
12527 N N   . PHE D 288 ? 0.4283 0.4050 0.4365 0.0225  -0.0275 0.0329  589 PHE D N   
12528 C CA  . PHE D 288 ? 0.3898 0.3703 0.3985 0.0227  -0.0271 0.0337  589 PHE D CA  
12529 C C   . PHE D 288 ? 0.4276 0.4127 0.4359 0.0203  -0.0289 0.0332  589 PHE D C   
12530 O O   . PHE D 288 ? 0.4524 0.4360 0.4597 0.0168  -0.0304 0.0330  589 PHE D O   
12531 C CB  . PHE D 288 ? 0.5921 0.5717 0.6031 0.0227  -0.0259 0.0344  589 PHE D CB  
12532 C CG  . PHE D 288 ? 0.6206 0.6006 0.6341 0.0204  -0.0272 0.0346  589 PHE D CG  
12533 C CD1 . PHE D 288 ? 0.5589 0.5411 0.5724 0.0183  -0.0283 0.0346  589 PHE D CD1 
12534 C CD2 . PHE D 288 ? 0.6527 0.6321 0.6682 0.0210  -0.0273 0.0347  589 PHE D CD2 
12535 C CE1 . PHE D 288 ? 0.5362 0.5183 0.5506 0.0162  -0.0298 0.0353  589 PHE D CE1 
12536 C CE2 . PHE D 288 ? 0.5450 0.5251 0.5621 0.0201  -0.0291 0.0355  589 PHE D CE2 
12537 C CZ  . PHE D 288 ? 0.4509 0.4315 0.4669 0.0173  -0.0305 0.0360  589 PHE D CZ  
12538 N N   . SER D 289 ? 0.3465 0.3374 0.3549 0.0223  -0.0287 0.0332  590 SER D N   
12539 C CA  . SER D 289 ? 0.3884 0.3884 0.3972 0.0201  -0.0300 0.0323  590 SER D CA  
12540 C C   . SER D 289 ? 0.5407 0.5469 0.5507 0.0246  -0.0292 0.0321  590 SER D C   
12541 O O   . SER D 289 ? 0.6127 0.6145 0.6208 0.0299  -0.0281 0.0328  590 SER D O   
12542 C CB  . SER D 289 ? 0.4869 0.4919 0.4935 0.0185  -0.0314 0.0314  590 SER D CB  
12543 O OG  . SER D 289 ? 0.5571 0.5643 0.5626 0.0240  -0.0311 0.0320  590 SER D OG  
12544 N N   . GLY D 290 ? 0.5234 0.5391 0.5351 0.0225  -0.0296 0.0310  591 GLY D N   
12545 C CA  . GLY D 290 ? 0.4791 0.5034 0.4919 0.0280  -0.0288 0.0299  591 GLY D CA  
12546 C C   . GLY D 290 ? 0.5474 0.5898 0.5626 0.0254  -0.0298 0.0282  591 GLY D C   
12547 O O   . GLY D 290 ? 0.7618 0.8127 0.7772 0.0244  -0.0314 0.0281  591 GLY D O   
12548 N N   . TRP D 291 ? 0.4316 0.4815 0.4485 0.0234  -0.0288 0.0268  592 TRP D N   
12549 C CA  . TRP D 291 ? 0.4816 0.5510 0.5008 0.0186  -0.0292 0.0251  592 TRP D CA  
12550 C C   . TRP D 291 ? 0.5543 0.6244 0.5729 0.0115  -0.0281 0.0246  592 TRP D C   
12551 O O   . TRP D 291 ? 0.4363 0.4951 0.4535 0.0130  -0.0270 0.0251  592 TRP D O   
12552 C CB  . TRP D 291 ? 0.5165 0.6038 0.5391 0.0276  -0.0288 0.0231  592 TRP D CB  
12553 C CG  . TRP D 291 ? 0.5873 0.6702 0.6093 0.0365  -0.0266 0.0218  592 TRP D CG  
12554 C CD1 . TRP D 291 ? 0.6435 0.7317 0.6661 0.0352  -0.0244 0.0196  592 TRP D CD1 
12555 C CD2 . TRP D 291 ? 0.5710 0.6410 0.5895 0.0474  -0.0260 0.0225  592 TRP D CD2 
12556 N NE1 . TRP D 291 ? 0.6166 0.6954 0.6363 0.0450  -0.0226 0.0183  592 TRP D NE1 
12557 C CE2 . TRP D 291 ? 0.6630 0.7293 0.6796 0.0524  -0.0235 0.0203  592 TRP D CE2 
12558 C CE3 . TRP D 291 ? 0.5921 0.6518 0.6075 0.0528  -0.0273 0.0249  592 TRP D CE3 
12559 C CZ2 . TRP D 291 ? 0.7260 0.7767 0.7368 0.0623  -0.0223 0.0203  592 TRP D CZ2 
12560 C CZ3 . TRP D 291 ? 0.5443 0.5896 0.5540 0.0623  -0.0261 0.0255  592 TRP D CZ3 
12561 C CH2 . TRP D 291 ? 0.7178 0.7574 0.7247 0.0669  -0.0237 0.0232  592 TRP D CH2 
12562 N N   . TYR D 292 ? 0.5515 0.6360 0.5703 0.0031  -0.0284 0.0237  593 TYR D N   
12563 C CA  . TYR D 292 ? 0.4873 0.5710 0.5031 -0.0063 -0.0278 0.0242  593 TYR D CA  
12564 C C   . TYR D 292 ? 0.4848 0.5810 0.5028 -0.0035 -0.0252 0.0218  593 TYR D C   
12565 O O   . TYR D 292 ? 0.5381 0.6530 0.5606 0.0026  -0.0239 0.0189  593 TYR D O   
12566 C CB  . TYR D 292 ? 0.5143 0.6073 0.5272 -0.0185 -0.0287 0.0242  593 TYR D CB  
12567 C CG  . TYR D 292 ? 0.6036 0.6764 0.6091 -0.0260 -0.0308 0.0269  593 TYR D CG  
12568 C CD1 . TYR D 292 ? 0.5280 0.6003 0.5309 -0.0304 -0.0324 0.0265  593 TYR D CD1 
12569 C CD2 . TYR D 292 ? 0.4875 0.5418 0.4879 -0.0282 -0.0312 0.0296  593 TYR D CD2 
12570 C CE1 . TYR D 292 ? 0.4972 0.5485 0.4916 -0.0365 -0.0340 0.0284  593 TYR D CE1 
12571 C CE2 . TYR D 292 ? 0.5612 0.5961 0.5541 -0.0329 -0.0331 0.0319  593 TYR D CE2 
12572 C CZ  . TYR D 292 ? 0.5454 0.5777 0.5349 -0.0368 -0.0343 0.0311  593 TYR D CZ  
12573 O OH  . TYR D 292 ? 0.6973 0.7078 0.6777 -0.0405 -0.0359 0.0329  593 TYR D OH  
12574 N N   . MET D 293 ? 0.4489 0.5356 0.4632 -0.0077 -0.0245 0.0229  594 MET D N   
12575 C CA  . MET D 293 ? 0.3321 0.4319 0.3460 -0.0106 -0.0221 0.0207  594 MET D CA  
12576 C C   . MET D 293 ? 0.3566 0.4660 0.3669 -0.0242 -0.0224 0.0218  594 MET D C   
12577 O O   . MET D 293 ? 0.3736 0.4684 0.3781 -0.0321 -0.0247 0.0252  594 MET D O   
12578 C CB  . MET D 293 ? 0.4290 0.5141 0.4390 -0.0102 -0.0217 0.0216  594 MET D CB  
12579 C CG  . MET D 293 ? 0.4360 0.5330 0.4446 -0.0118 -0.0188 0.0188  594 MET D CG  
12580 S SD  . MET D 293 ? 0.5270 0.6055 0.5316 -0.0084 -0.0187 0.0189  594 MET D SD  
12581 C CE  . MET D 293 ? 0.4645 0.5292 0.4631 -0.0193 -0.0223 0.0248  594 MET D CE  
12582 N N   . GLY D 294 ? 0.4188 0.5523 0.4316 -0.0270 -0.0200 0.0187  595 GLY D N   
12583 C CA  . GLY D 294 ? 0.5436 0.6889 0.5524 -0.0418 -0.0199 0.0194  595 GLY D CA  
12584 C C   . GLY D 294 ? 0.6496 0.7754 0.6477 -0.0533 -0.0211 0.0237  595 GLY D C   
12585 O O   . GLY D 294 ? 0.7127 0.8316 0.7038 -0.0647 -0.0227 0.0263  595 GLY D O   
12586 N N   . THR D 295 ? 0.5417 0.6569 0.5370 -0.0503 -0.0205 0.0247  596 THR D N   
12587 C CA  . THR D 295 ? 0.5098 0.6093 0.4941 -0.0604 -0.0218 0.0291  596 THR D CA  
12588 C C   . THR D 295 ? 0.4975 0.5714 0.4755 -0.0625 -0.0257 0.0337  596 THR D C   
12589 O O   . THR D 295 ? 0.5700 0.6306 0.5367 -0.0724 -0.0272 0.0378  596 THR D O   
12590 C CB  . THR D 295 ? 0.5059 0.5991 0.4888 -0.0555 -0.0212 0.0291  596 THR D CB  
12591 O OG1 . THR D 295 ? 0.4348 0.5151 0.4228 -0.0434 -0.0226 0.0288  596 THR D OG1 
12592 C CG2 . THR D 295 ? 0.2981 0.4145 0.2837 -0.0552 -0.0169 0.0244  596 THR D CG2 
12593 N N   . GLU D 296 ? 0.5228 0.5879 0.5064 -0.0528 -0.0272 0.0333  597 GLU D N   
12594 C CA  . GLU D 296 ? 0.4322 0.4739 0.4101 -0.0532 -0.0304 0.0369  597 GLU D CA  
12595 C C   . GLU D 296 ? 0.5296 0.5674 0.4990 -0.0649 -0.0313 0.0381  597 GLU D C   
12596 O O   . GLU D 296 ? 0.6290 0.6453 0.5872 -0.0701 -0.0336 0.0420  597 GLU D O   
12597 C CB  . GLU D 296 ? 0.5687 0.6060 0.5544 -0.0418 -0.0311 0.0354  597 GLU D CB  
12598 C CG  . GLU D 296 ? 0.6190 0.6591 0.6119 -0.0314 -0.0299 0.0337  597 GLU D CG  
12599 C CD  . GLU D 296 ? 0.6069 0.6386 0.6045 -0.0224 -0.0307 0.0334  597 GLU D CD  
12600 O OE1 . GLU D 296 ? 0.6837 0.7002 0.6777 -0.0227 -0.0329 0.0359  597 GLU D OE1 
12601 O OE2 . GLU D 296 ? 0.5762 0.6157 0.5799 -0.0148 -0.0291 0.0308  597 GLU D OE2 
12602 N N   . ILE D 297 ? 0.5820 0.6394 0.5558 -0.0688 -0.0298 0.0348  598 ILE D N   
12603 C CA  . ILE D 297 ? 0.5808 0.6369 0.5459 -0.0823 -0.0304 0.0352  598 ILE D CA  
12604 C C   . ILE D 297 ? 0.5476 0.6089 0.5035 -0.0966 -0.0290 0.0368  598 ILE D C   
12605 O O   . ILE D 297 ? 0.5442 0.5856 0.4853 -0.1078 -0.0304 0.0403  598 ILE D O   
12606 C CB  . ILE D 297 ? 0.5053 0.5848 0.4789 -0.0822 -0.0295 0.0308  598 ILE D CB  
12607 C CG1 . ILE D 297 ? 0.5116 0.5868 0.4933 -0.0683 -0.0308 0.0295  598 ILE D CG1 
12608 C CG2 . ILE D 297 ? 0.3724 0.4521 0.3361 -0.0987 -0.0301 0.0306  598 ILE D CG2 
12609 C CD1 . ILE D 297 ? 0.4224 0.5260 0.4165 -0.0607 -0.0295 0.0255  598 ILE D CD1 
12610 N N   . GLY D 298 ? 0.6359 0.7232 0.5991 -0.0962 -0.0259 0.0340  599 GLY D N   
12611 C CA  . GLY D 298 ? 0.8066 0.9071 0.7627 -0.1107 -0.0236 0.0344  599 GLY D CA  
12612 C C   . GLY D 298 ? 0.7535 0.8352 0.6975 -0.1156 -0.0242 0.0392  599 GLY D C   
12613 O O   . GLY D 298 ? 0.8996 0.9826 0.8321 -0.1310 -0.0231 0.0413  599 GLY D O   
12614 N N   . VAL D 299 ? 0.6748 0.7400 0.6205 -0.1037 -0.0261 0.0412  600 VAL D N   
12615 C CA  . VAL D 299 ? 0.6773 0.7257 0.6117 -0.1067 -0.0274 0.0461  600 VAL D CA  
12616 C C   . VAL D 299 ? 0.6865 0.7014 0.6108 -0.1042 -0.0319 0.0514  600 VAL D C   
12617 O O   . VAL D 299 ? 0.6418 0.6378 0.5498 -0.1135 -0.0337 0.0566  600 VAL D O   
12618 C CB  . VAL D 299 ? 0.6440 0.7024 0.5868 -0.0962 -0.0261 0.0441  600 VAL D CB  
12619 C CG1 . VAL D 299 ? 0.6242 0.6701 0.5548 -0.1011 -0.0275 0.0489  600 VAL D CG1 
12620 C CG2 . VAL D 299 ? 0.6458 0.7363 0.5987 -0.0956 -0.0215 0.0380  600 VAL D CG2 
12621 N N   . ARG D 300 ? 0.7243 0.7311 0.6572 -0.0912 -0.0337 0.0502  601 ARG D N   
12622 C CA  . ARG D 300 ? 0.6996 0.6774 0.6244 -0.0863 -0.0376 0.0546  601 ARG D CA  
12623 C C   . ARG D 300 ? 0.7785 0.7395 0.6935 -0.0929 -0.0389 0.0553  601 ARG D C   
12624 O O   . ARG D 300 ? 0.6760 0.6120 0.5744 -0.0984 -0.0413 0.0601  601 ARG D O   
12625 C CB  . ARG D 300 ? 0.5498 0.5275 0.4875 -0.0703 -0.0386 0.0529  601 ARG D CB  
12626 C CG  . ARG D 300 ? 0.4450 0.4386 0.3922 -0.0640 -0.0371 0.0509  601 ARG D CG  
12627 C CD  . ARG D 300 ? 0.6119 0.5995 0.5495 -0.0678 -0.0387 0.0552  601 ARG D CD  
12628 N NE  . ARG D 300 ? 0.5091 0.4719 0.4351 -0.0672 -0.0430 0.0610  601 ARG D NE  
12629 C CZ  . ARG D 300 ? 0.4822 0.4353 0.4116 -0.0562 -0.0460 0.0625  601 ARG D CZ  
12630 N NH1 . ARG D 300 ? 0.4552 0.4206 0.3984 -0.0473 -0.0449 0.0587  601 ARG D NH1 
12631 N NH2 . ARG D 300 ? 0.5078 0.4391 0.4262 -0.0542 -0.0499 0.0675  601 ARG D NH2 
12632 N N   . ASP D 301 ? 0.8138 0.7871 0.7372 -0.0926 -0.0373 0.0507  602 ASP D N   
12633 C CA  . ASP D 301 ? 0.8006 0.7584 0.7148 -0.0987 -0.0384 0.0504  602 ASP D CA  
12634 C C   . ASP D 301 ? 0.8323 0.7835 0.7296 -0.1175 -0.0379 0.0524  602 ASP D C   
12635 O O   . ASP D 301 ? 0.7175 0.6389 0.5971 -0.1231 -0.0400 0.0557  602 ASP D O   
12636 C CB  . ASP D 301 ? 0.6663 0.6435 0.5933 -0.0954 -0.0370 0.0449  602 ASP D CB  
12637 C CG  . ASP D 301 ? 0.6792 0.6553 0.6183 -0.0786 -0.0377 0.0436  602 ASP D CG  
12638 O OD1 . ASP D 301 ? 0.6792 0.6329 0.6137 -0.0715 -0.0399 0.0461  602 ASP D OD1 
12639 O OD2 . ASP D 301 ? 0.6917 0.6896 0.6445 -0.0724 -0.0361 0.0400  602 ASP D OD2 
12640 N N   . TYR D 302 ? 0.8054 0.7840 0.7068 -0.1276 -0.0349 0.0502  603 TYR D N   
12641 C CA  . TYR D 302 ? 0.8875 0.8647 0.7735 -0.1479 -0.0337 0.0514  603 TYR D CA  
12642 C C   . TYR D 302 ? 0.8643 0.8262 0.7345 -0.1560 -0.0341 0.0573  603 TYR D C   
12643 O O   . TYR D 302 ? 0.8158 0.7645 0.6674 -0.1734 -0.0339 0.0599  603 TYR D O   
12644 C CB  . TYR D 302 ? 0.9080 0.9251 0.8054 -0.1559 -0.0301 0.0463  603 TYR D CB  
12645 C CG  . TYR D 302 ? 0.7894 0.8214 0.6972 -0.1533 -0.0301 0.0411  603 TYR D CG  
12646 C CD1 . TYR D 302 ? 0.7257 0.7973 0.6496 -0.1519 -0.0276 0.0360  603 TYR D CD1 
12647 C CD2 . TYR D 302 ? 0.7460 0.7530 0.6468 -0.1515 -0.0327 0.0413  603 TYR D CD2 
12648 C CE1 . TYR D 302 ? 0.7045 0.7908 0.6373 -0.1491 -0.0281 0.0319  603 TYR D CE1 
12649 C CE2 . TYR D 302 ? 0.8178 0.8390 0.7270 -0.1498 -0.0328 0.0367  603 TYR D CE2 
12650 C CZ  . TYR D 302 ? 0.8237 0.8850 0.7489 -0.1487 -0.0308 0.0323  603 TYR D CZ  
12651 O OH  . TYR D 302 ? 0.8717 0.9488 0.8050 -0.1464 -0.0315 0.0281  603 TYR D OH  
12652 N N   . CYS D 303 ? 0.8239 0.7867 0.6996 -0.1449 -0.0348 0.0596  604 CYS D N   
12653 C CA  . CYS D 303 ? 0.7805 0.7383 0.6433 -0.1536 -0.0346 0.0644  604 CYS D CA  
12654 C C   . CYS D 303 ? 0.6806 0.6072 0.5318 -0.1454 -0.0389 0.0711  604 CYS D C   
12655 O O   . CYS D 303 ? 0.6073 0.5176 0.4395 -0.1559 -0.0399 0.0768  604 CYS D O   
12656 C CB  . CYS D 303 ? 0.7249 0.7179 0.6019 -0.1519 -0.0310 0.0609  604 CYS D CB  
12657 S SG  . CYS D 303 ? 0.7265 0.7553 0.6077 -0.1685 -0.0258 0.0555  604 CYS D SG  
12658 N N   . ASP D 304 ? 0.7540 0.6726 0.6150 -0.1276 -0.0416 0.0708  605 ASP D N   
12659 C CA  . ASP D 304 ? 0.7674 0.6562 0.6167 -0.1192 -0.0462 0.0770  605 ASP D CA  
12660 C C   . ASP D 304 ? 0.9052 0.7598 0.7296 -0.1296 -0.0483 0.0820  605 ASP D C   
12661 O O   . ASP D 304 ? 0.9190 0.7676 0.7390 -0.1373 -0.0470 0.0792  605 ASP D O   
12662 C CB  . ASP D 304 ? 0.5939 0.4790 0.4568 -0.1004 -0.0484 0.0750  605 ASP D CB  
12663 C CG  . ASP D 304 ? 0.7119 0.6213 0.5941 -0.0892 -0.0475 0.0721  605 ASP D CG  
12664 O OD1 . ASP D 304 ? 0.7878 0.7200 0.6757 -0.0947 -0.0446 0.0700  605 ASP D OD1 
12665 O OD2 . ASP D 304 ? 0.5894 0.4945 0.4801 -0.0751 -0.0497 0.0717  605 ASP D OD2 
12666 N N   . ASN D 305 ? 0.9495 0.7805 0.7559 -0.1300 -0.0517 0.0894  606 ASN D N   
12667 C CA  . ASN D 305 ? 1.0672 0.8610 0.8460 -0.1400 -0.0538 0.0948  606 ASN D CA  
12668 C C   . ASN D 305 ? 1.0883 0.8550 0.8631 -0.1289 -0.0564 0.0939  606 ASN D C   
12669 O O   . ASN D 305 ? 1.1716 0.9151 0.9297 -0.1391 -0.0560 0.0938  606 ASN D O   
12670 C CB  . ASN D 305 ? 1.2668 1.0410 1.0264 -0.1413 -0.0573 0.1036  606 ASN D CB  
12671 C CG  . ASN D 305 ? 1.3878 1.1823 1.1431 -0.1582 -0.0540 0.1050  606 ASN D CG  
12672 O OD1 . ASN D 305 ? 1.4269 1.2147 1.1658 -0.1779 -0.0516 0.1063  606 ASN D OD1 
12673 N ND2 . ASN D 305 ? 1.3717 1.1911 1.1409 -0.1512 -0.0538 0.1045  606 ASN D ND2 
12674 N N   . SER D 306 ? 1.0462 0.8163 0.8359 -0.1087 -0.0587 0.0928  607 SER D N   
12675 C CA  . SER D 306 ? 1.0914 0.8413 0.8804 -0.0964 -0.0605 0.0908  607 SER D CA  
12676 C C   . SER D 306 ? 1.1188 0.8837 0.9207 -0.0997 -0.0568 0.0829  607 SER D C   
12677 O O   . SER D 306 ? 1.1347 0.8863 0.9376 -0.0897 -0.0577 0.0802  607 SER D O   
12678 C CB  . SER D 306 ? 1.0653 0.8205 0.8683 -0.0747 -0.0635 0.0915  607 SER D CB  
12679 O OG  . SER D 306 ? 1.1307 0.8709 0.9210 -0.0696 -0.0679 0.0991  607 SER D OG  
12680 N N   . ARG D 307 ? 1.0744 0.8679 0.8861 -0.1125 -0.0529 0.0789  608 ARG D N   
12681 C CA  . ARG D 307 ? 1.0018 0.8136 0.8269 -0.1145 -0.0500 0.0717  608 ARG D CA  
12682 C C   . ARG D 307 ? 0.9614 0.7736 0.7740 -0.1361 -0.0476 0.0701  608 ARG D C   
12683 O O   . ARG D 307 ? 1.0621 0.8424 0.8502 -0.1466 -0.0489 0.0736  608 ARG D O   
12684 C CB  . ARG D 307 ? 0.8698 0.7205 0.7215 -0.1068 -0.0477 0.0674  608 ARG D CB  
12685 C CG  . ARG D 307 ? 0.7327 0.5856 0.5970 -0.0876 -0.0497 0.0684  608 ARG D CG  
12686 C CD  . ARG D 307 ? 0.7970 0.6380 0.6659 -0.0746 -0.0509 0.0658  608 ARG D CD  
12687 N NE  . ARG D 307 ? 0.7657 0.6204 0.6436 -0.0775 -0.0483 0.0598  608 ARG D NE  
12688 C CZ  . ARG D 307 ? 0.8501 0.7349 0.7470 -0.0746 -0.0459 0.0556  608 ARG D CZ  
12689 N NH1 . ARG D 307 ? 0.7911 0.6940 0.6995 -0.0695 -0.0453 0.0562  608 ARG D NH1 
12690 N NH2 . ARG D 307 ? 0.9374 0.8330 0.8405 -0.0768 -0.0442 0.0508  608 ARG D NH2 
12691 N N   . TYR D 308 ? 0.7444 0.5919 0.5724 -0.1432 -0.0442 0.0649  609 TYR D N   
12692 C CA  . TYR D 308 ? 0.8161 0.6676 0.6339 -0.1636 -0.0421 0.0624  609 TYR D CA  
12693 C C   . TYR D 308 ? 0.8894 0.7413 0.6921 -0.1822 -0.0407 0.0664  609 TYR D C   
12694 O O   . TYR D 308 ? 1.0700 0.9150 0.8570 -0.2017 -0.0394 0.0659  609 TYR D O   
12695 C CB  . TYR D 308 ? 0.8666 0.7574 0.7056 -0.1641 -0.0394 0.0554  609 TYR D CB  
12696 C CG  . TYR D 308 ? 0.8804 0.7623 0.7201 -0.1606 -0.0402 0.0511  609 TYR D CG  
12697 C CD1 . TYR D 308 ? 0.7575 0.6395 0.6114 -0.1410 -0.0414 0.0491  609 TYR D CD1 
12698 C CD2 . TYR D 308 ? 0.8429 0.7160 0.6677 -0.1781 -0.0397 0.0488  609 TYR D CD2 
12699 C CE1 . TYR D 308 ? 0.7771 0.6514 0.6305 -0.1382 -0.0419 0.0451  609 TYR D CE1 
12700 C CE2 . TYR D 308 ? 0.7623 0.6272 0.5865 -0.1755 -0.0405 0.0444  609 TYR D CE2 
12701 C CZ  . TYR D 308 ? 0.8763 0.7418 0.7149 -0.1551 -0.0416 0.0426  609 TYR D CZ  
12702 O OH  . TYR D 308 ? 1.0175 0.8756 0.8549 -0.1526 -0.0421 0.0382  609 TYR D OH  
12703 N N   . ASN D 309 ? 0.8075 0.6689 0.6144 -0.1778 -0.0406 0.0701  610 ASN D N   
12704 C CA  . ASN D 309 ? 0.9024 0.7553 0.6908 -0.1927 -0.0401 0.0758  610 ASN D CA  
12705 C C   . ASN D 309 ? 0.8877 0.7581 0.6687 -0.2173 -0.0363 0.0734  610 ASN D C   
12706 O O   . ASN D 309 ? 0.7355 0.5807 0.4911 -0.2353 -0.0364 0.0773  610 ASN D O   
12707 C CB  . ASN D 309 ? 0.8910 0.6946 0.6529 -0.1915 -0.0443 0.0833  610 ASN D CB  
12708 C CG  . ASN D 309 ? 0.9119 0.7046 0.6546 -0.2032 -0.0446 0.0905  610 ASN D CG  
12709 O OD1 . ASN D 309 ? 0.8479 0.6701 0.6010 -0.2054 -0.0423 0.0904  610 ASN D OD1 
12710 N ND2 . ASN D 309 ? 0.9185 0.6676 0.6314 -0.2109 -0.0472 0.0969  610 ASN D ND2 
12711 N N   . ILE D 310 ? 0.9402 0.8554 0.7433 -0.2179 -0.0327 0.0671  611 ILE D N   
12712 C CA  . ILE D 310 ? 1.0169 0.9581 0.8181 -0.2393 -0.0289 0.0635  611 ILE D CA  
12713 C C   . ILE D 310 ? 0.9805 0.9500 0.7836 -0.2490 -0.0253 0.0644  611 ILE D C   
12714 O O   . ILE D 310 ? 0.9626 0.9662 0.7710 -0.2636 -0.0214 0.0601  611 ILE D O   
12715 C CB  . ILE D 310 ? 0.9937 0.9682 0.8169 -0.2343 -0.0276 0.0555  611 ILE D CB  
12716 C CG1 . ILE D 310 ? 0.9369 0.9419 0.7868 -0.2135 -0.0267 0.0522  611 ILE D CG1 
12717 C CG2 . ILE D 310 ? 1.0009 0.9477 0.8190 -0.2286 -0.0307 0.0542  611 ILE D CG2 
12718 C CD1 . ILE D 310 ? 0.9567 1.0046 0.8274 -0.2118 -0.0243 0.0449  611 ILE D CD1 
12719 N N   . LEU D 311 ? 0.9846 0.9424 0.7832 -0.2415 -0.0264 0.0696  612 LEU D N   
12720 C CA  . LEU D 311 ? 0.8427 0.8275 0.6425 -0.2502 -0.0226 0.0700  612 LEU D CA  
12721 C C   . LEU D 311 ? 0.9026 0.8803 0.6780 -0.2780 -0.0204 0.0736  612 LEU D C   
12722 O O   . LEU D 311 ? 0.9362 0.9508 0.7167 -0.2920 -0.0155 0.0700  612 LEU D O   
12723 C CB  . LEU D 311 ? 0.7053 0.6786 0.5050 -0.2359 -0.0247 0.0746  612 LEU D CB  
12724 C CG  . LEU D 311 ? 0.6841 0.6790 0.5095 -0.2129 -0.0248 0.0701  612 LEU D CG  
12725 C CD1 . LEU D 311 ? 0.7021 0.6764 0.5214 -0.2018 -0.0281 0.0759  612 LEU D CD1 
12726 C CD2 . LEU D 311 ? 0.4600 0.5023 0.3037 -0.2139 -0.0194 0.0632  612 LEU D CD2 
12727 N N   . GLU D 312 ? 0.8618 0.7922 0.6095 -0.2866 -0.0237 0.0806  613 GLU D N   
12728 C CA  . GLU D 312 ? 1.0056 0.9250 0.7268 -0.3149 -0.0214 0.0844  613 GLU D CA  
12729 C C   . GLU D 312 ? 0.9542 0.9038 0.6814 -0.3328 -0.0176 0.0773  613 GLU D C   
12730 O O   . GLU D 312 ? 0.9291 0.9051 0.6515 -0.3541 -0.0130 0.0763  613 GLU D O   
12731 C CB  . GLU D 312 ? 1.2240 1.0825 0.9125 -0.3200 -0.0259 0.0925  613 GLU D CB  
12732 C CG  . GLU D 312 ? 1.3201 1.1466 1.0008 -0.3016 -0.0307 0.1001  613 GLU D CG  
12733 C CD  . GLU D 312 ? 1.3681 1.1706 1.0569 -0.2775 -0.0356 0.0992  613 GLU D CD  
12734 O OE1 . GLU D 312 ? 1.5340 1.2900 1.2011 -0.2717 -0.0402 0.1061  613 GLU D OE1 
12735 O OE2 . GLU D 312 ? 1.1140 0.9438 0.8299 -0.2643 -0.0347 0.0917  613 GLU D OE2 
12736 N N   . GLU D 313 ? 0.7856 0.7347 0.5239 -0.3245 -0.0194 0.0721  614 GLU D N   
12737 C CA  . GLU D 313 ? 0.9557 0.9337 0.6985 -0.3422 -0.0164 0.0656  614 GLU D CA  
12738 C C   . GLU D 313 ? 0.9444 0.9853 0.7148 -0.3403 -0.0119 0.0589  614 GLU D C   
12739 O O   . GLU D 313 ? 1.0713 1.1439 0.8403 -0.3619 -0.0078 0.0557  614 GLU D O   
12740 C CB  . GLU D 313 ? 0.9966 0.9611 0.7446 -0.3335 -0.0195 0.0615  614 GLU D CB  
12741 C CG  . GLU D 313 ? 1.1204 1.1013 0.8621 -0.3581 -0.0174 0.0564  614 GLU D CG  
12742 C CD  . GLU D 313 ? 1.2045 1.1735 0.9500 -0.3512 -0.0203 0.0519  614 GLU D CD  
12743 O OE1 . GLU D 313 ? 1.2025 1.2115 0.9643 -0.3559 -0.0189 0.0449  614 GLU D OE1 
12744 O OE2 . GLU D 313 ? 1.2688 1.1898 1.0006 -0.3407 -0.0241 0.0553  614 GLU D OE2 
12745 N N   . VAL D 314 ? 0.8118 0.8719 0.6067 -0.3149 -0.0123 0.0564  615 VAL D N   
12746 C CA  . VAL D 314 ? 0.7408 0.8582 0.5610 -0.3106 -0.0080 0.0495  615 VAL D CA  
12747 C C   . VAL D 314 ? 0.8127 0.9495 0.6257 -0.3249 -0.0035 0.0514  615 VAL D C   
12748 O O   . VAL D 314 ? 0.9789 1.1609 0.8005 -0.3372 0.0013  0.0463  615 VAL D O   
12749 C CB  . VAL D 314 ? 0.7591 0.8870 0.6043 -0.2802 -0.0096 0.0464  615 VAL D CB  
12750 C CG1 . VAL D 314 ? 0.6500 0.8320 0.5178 -0.2741 -0.0050 0.0399  615 VAL D CG1 
12751 C CG2 . VAL D 314 ? 0.8738 0.9918 0.7278 -0.2685 -0.0132 0.0435  615 VAL D CG2 
12752 N N   . ALA D 315 ? 0.8775 0.9816 0.6735 -0.3242 -0.0048 0.0587  616 ALA D N   
12753 C CA  . ALA D 315 ? 0.7399 0.8610 0.5274 -0.3378 -0.0004 0.0608  616 ALA D CA  
12754 C C   . ALA D 315 ? 0.7755 0.8991 0.5425 -0.3671 0.0019  0.0612  616 ALA D C   
12755 O O   . ALA D 315 ? 0.6718 0.8317 0.4417 -0.3756 0.0058  0.0567  616 ALA D O   
12756 C CB  . ALA D 315 ? 0.7618 0.8446 0.5337 -0.3300 -0.0035 0.0691  616 ALA D CB  
12757 N N   . LYS D 316 ? 0.8382 0.9211 0.5843 -0.3754 -0.0023 0.0637  617 LYS D N   
12758 C CA  . LYS D 316 ? 0.8507 0.9335 0.5770 -0.3962 -0.0020 0.0609  617 LYS D CA  
12759 C C   . LYS D 316 ? 0.9343 1.0737 0.6804 -0.4016 0.0018  0.0512  617 LYS D C   
12760 O O   . LYS D 316 ? 0.9989 1.1722 0.7445 -0.4124 0.0053  0.0472  617 LYS D O   
12761 C CB  . LYS D 316 ? 0.7960 0.8247 0.4967 -0.4023 -0.0067 0.0643  617 LYS D CB  
12762 C CG  . LYS D 316 ? 0.9312 0.9050 0.6056 -0.4002 -0.0106 0.0734  617 LYS D CG  
12763 C CD  . LYS D 316 ? 1.1131 1.0319 0.7664 -0.3987 -0.0155 0.0765  617 LYS D CD  
12764 C CE  . LYS D 316 ? 1.2329 1.0991 0.8605 -0.3939 -0.0197 0.0855  617 LYS D CE  
12765 N NZ  . LYS D 316 ? 1.3600 1.1719 0.9646 -0.3920 -0.0241 0.0877  617 LYS D NZ  
12766 N N   . LYS D 317 ? 0.9799 1.1328 0.7452 -0.3923 0.0011  0.0472  618 LYS D N   
12767 C CA  . LYS D 317 ? 0.9360 1.1449 0.7229 -0.3929 0.0040  0.0381  618 LYS D CA  
12768 C C   . LYS D 317 ? 0.9222 1.1835 0.7320 -0.3842 0.0087  0.0339  618 LYS D C   
12769 O O   . LYS D 317 ? 0.9446 1.2552 0.7700 -0.3846 0.0114  0.0262  618 LYS D O   
12770 C CB  . LYS D 317 ? 0.8350 1.0477 0.6404 -0.3807 0.0015  0.0353  618 LYS D CB  
12771 C CG  . LYS D 317 ? 0.8553 1.0272 0.6406 -0.3900 -0.0024 0.0365  618 LYS D CG  
12772 C CD  . LYS D 317 ? 0.8159 1.0214 0.6161 -0.3902 -0.0026 0.0290  618 LYS D CD  
12773 C CE  . LYS D 317 ? 0.9666 1.1772 0.7462 -0.4119 -0.0016 0.0258  618 LYS D CE  
12774 N NZ  . LYS D 317 ? 1.0861 1.2354 0.8317 -0.4245 -0.0045 0.0307  618 LYS D NZ  
12775 N N   . MET D 318 ? 0.8290 1.0810 0.6405 -0.3754 0.0099  0.0384  619 MET D N   
12776 C CA  . MET D 318 ? 0.7458 1.0441 0.5751 -0.3679 0.0149  0.0339  619 MET D CA  
12777 C C   . MET D 318 ? 0.8031 1.1057 0.6137 -0.3836 0.0172  0.0343  619 MET D C   
12778 O O   . MET D 318 ? 0.9397 1.2844 0.7634 -0.3797 0.0216  0.0291  619 MET D O   
12779 C CB  . MET D 318 ? 0.6152 0.9076 0.4588 -0.3484 0.0158  0.0373  619 MET D CB  
12780 C CG  . MET D 318 ? 0.6095 0.9070 0.4768 -0.3218 0.0123  0.0325  619 MET D CG  
12781 S SD  . MET D 318 ? 0.6571 0.9468 0.5415 -0.2871 0.0107  0.0315  619 MET D SD  
12782 C CE  . MET D 318 ? 0.6759 1.0191 0.5715 -0.2879 0.0183  0.0254  619 MET D CE  
12783 N N   . ASN D 319 ? 0.8187 1.0796 0.5990 -0.4010 0.0141  0.0397  620 ASN D N   
12784 C CA  . ASN D 319 ? 0.8378 1.0958 0.5968 -0.4176 0.0153  0.0412  620 ASN D CA  
12785 C C   . ASN D 319 ? 0.7378 0.9844 0.4949 -0.4095 0.0163  0.0463  620 ASN D C   
12786 O O   . ASN D 319 ? 0.8362 1.1089 0.5929 -0.4147 0.0196  0.0437  620 ASN D O   
12787 C CB  . ASN D 319 ? 0.9096 1.2231 0.6769 -0.4274 0.0195  0.0322  620 ASN D CB  
12788 C CG  . ASN D 319 ? 1.0902 1.4113 0.8515 -0.4403 0.0183  0.0281  620 ASN D CG  
12789 O OD1 . ASN D 319 ? 1.2508 1.5301 0.9866 -0.4544 0.0149  0.0323  620 ASN D OD1 
12790 N ND2 . ASN D 319 ? 1.0283 1.4028 0.8122 -0.4349 0.0210  0.0196  620 ASN D ND2 
12791 N N   . LEU D 320 ? 0.6979 0.9058 0.4529 -0.3967 0.0132  0.0535  621 LEU D N   
12792 C CA  . LEU D 320 ? 0.8422 1.0402 0.5967 -0.3866 0.0138  0.0585  621 LEU D CA  
12793 C C   . LEU D 320 ? 0.9628 1.1119 0.6852 -0.3972 0.0096  0.0673  621 LEU D C   
12794 O O   . LEU D 320 ? 1.0589 1.1691 0.7606 -0.4064 0.0053  0.0711  621 LEU D O   
12795 C CB  . LEU D 320 ? 0.7513 0.9376 0.5216 -0.3658 0.0126  0.0615  621 LEU D CB  
12796 C CG  . LEU D 320 ? 0.7061 0.9417 0.5091 -0.3531 0.0168  0.0529  621 LEU D CG  
12797 C CD1 . LEU D 320 ? 0.5995 0.8186 0.4186 -0.3225 0.0124  0.0522  621 LEU D CD1 
12798 C CD2 . LEU D 320 ? 0.6352 0.9228 0.4505 -0.3540 0.0228  0.0450  621 LEU D CD2 
12799 N N   . ASP D 321 ? 0.9332 1.0847 0.6511 -0.3952 0.0109  0.0701  622 ASP D N   
12800 C CA  . ASP D 321 ? 0.9842 1.0906 0.6730 -0.4025 0.0066  0.0789  622 ASP D CA  
12801 C C   . ASP D 321 ? 0.9619 1.0253 0.6466 -0.3857 0.0015  0.0873  622 ASP D C   
12802 O O   . ASP D 321 ? 1.0700 1.1429 0.7675 -0.3704 0.0025  0.0887  622 ASP D O   
12803 C CB  . ASP D 321 ? 1.1409 1.2680 0.8258 -0.4077 0.0097  0.0784  622 ASP D CB  
12804 C CG  . ASP D 321 ? 1.2763 1.3568 0.9326 -0.4122 0.0047  0.0882  622 ASP D CG  
12805 O OD1 . ASP D 321 ? 1.3201 1.4031 0.9763 -0.4052 0.0052  0.0912  622 ASP D OD1 
12806 O OD2 . ASP D 321 ? 1.2726 1.3133 0.9060 -0.4219 0.0003  0.0928  622 ASP D OD2 
12807 N N   . MET D 322 ? 1.0023 1.0190 0.6685 -0.3878 -0.0040 0.0925  623 MET D N   
12808 C CA  . MET D 322 ? 1.0777 1.0513 0.7384 -0.3711 -0.0096 0.1004  623 MET D CA  
12809 C C   . MET D 322 ? 1.2026 1.1307 0.8346 -0.3725 -0.0150 0.1094  623 MET D C   
12810 O O   . MET D 322 ? 1.3124 1.1956 0.9318 -0.3625 -0.0209 0.1158  623 MET D O   
12811 C CB  . MET D 322 ? 1.0750 1.0289 0.7375 -0.3683 -0.0120 0.0990  623 MET D CB  
12812 C CG  . MET D 322 ? 1.0276 1.0264 0.7200 -0.3642 -0.0073 0.0907  623 MET D CG  
12813 S SD  . MET D 322 ? 1.0062 0.9971 0.6981 -0.3719 -0.0085 0.0857  623 MET D SD  
12814 C CE  . MET D 322 ? 1.0338 0.9569 0.7065 -0.3594 -0.0160 0.0943  623 MET D CE  
12815 N N   . ARG D 323 ? 1.0522 0.9925 0.6741 -0.3841 -0.0131 0.1099  624 ARG D N   
12816 C CA  . ARG D 323 ? 1.2115 1.1157 0.8089 -0.3842 -0.0177 0.1185  624 ARG D CA  
12817 C C   . ARG D 323 ? 1.4083 1.3177 1.0147 -0.3669 -0.0190 0.1228  624 ARG D C   
12818 O O   . ARG D 323 ? 1.5746 1.4469 1.1701 -0.3535 -0.0253 0.1308  624 ARG D O   
12819 C CB  . ARG D 323 ? 1.2508 1.1663 0.8323 -0.4058 -0.0151 0.1170  624 ARG D CB  
12820 C CG  . ARG D 323 ? 1.3270 1.2271 0.8901 -0.4250 -0.0154 0.1147  624 ARG D CG  
12821 C CD  . ARG D 323 ? 1.4489 1.3732 1.0017 -0.4468 -0.0116 0.1116  624 ARG D CD  
12822 N NE  . ARG D 323 ? 1.5813 1.5639 1.1582 -0.4534 -0.0050 0.1011  624 ARG D NE  
12823 C CZ  . ARG D 323 ? 1.7132 1.7161 1.2857 -0.4726 -0.0022 0.0947  624 ARG D CZ  
12824 N NH1 . ARG D 323 ? 1.7466 1.7146 1.2897 -0.4891 -0.0051 0.0977  624 ARG D NH1 
12825 N NH2 . ARG D 323 ? 1.7470 1.8057 1.3435 -0.4750 0.0034  0.0852  624 ARG D NH2 
12826 N N   . LYS D 324 ? 1.3285 1.2846 0.9544 -0.3663 -0.0132 0.1171  625 LYS D N   
12827 C CA  . LYS D 324 ? 1.2261 1.1911 0.8588 -0.3523 -0.0137 0.1198  625 LYS D CA  
12828 C C   . LYS D 324 ? 1.1649 1.1473 0.8221 -0.3350 -0.0124 0.1167  625 LYS D C   
12829 O O   . LYS D 324 ? 1.1441 1.1638 0.8218 -0.3370 -0.0063 0.1083  625 LYS D O   
12830 C CB  . LYS D 324 ? 1.0769 1.0805 0.7130 -0.3622 -0.0080 0.1150  625 LYS D CB  
12831 C CG  . LYS D 324 ? 1.1819 1.1751 0.7953 -0.3823 -0.0082 0.1167  625 LYS D CG  
12832 C CD  . LYS D 324 ? 1.2589 1.3018 0.8829 -0.3970 -0.0004 0.1070  625 LYS D CD  
12833 C CE  . LYS D 324 ? 1.1486 1.2368 0.7980 -0.3852 0.0054  0.0999  625 LYS D CE  
12834 N NZ  . LYS D 324 ? 1.0806 1.2135 0.7532 -0.3876 0.0118  0.0890  625 LYS D NZ  
12835 N N   . THR D 325 ? 1.0681 1.0242 0.7230 -0.3178 -0.0183 0.1234  626 THR D N   
12836 C CA  . THR D 325 ? 0.9238 0.8970 0.6078 -0.2950 -0.0191 0.1164  626 THR D CA  
12837 C C   . THR D 325 ? 0.8798 0.9020 0.5856 -0.2918 -0.0124 0.1063  626 THR D C   
12838 O O   . THR D 325 ? 0.6553 0.7038 0.3876 -0.2806 -0.0096 0.0967  626 THR D O   
12839 C CB  . THR D 325 ? 0.9168 0.8605 0.5979 -0.2751 -0.0273 0.1225  626 THR D CB  
12840 O OG1 . THR D 325 ? 0.9047 0.8458 0.5694 -0.2789 -0.0287 0.1286  626 THR D OG1 
12841 C CG2 . THR D 325 ? 0.8587 0.7552 0.5217 -0.2737 -0.0337 0.1308  626 THR D CG2 
12842 N N   . SER D 326 ? 0.9098 0.9438 0.6034 -0.3014 -0.0098 0.1085  627 SER D N   
12843 C CA  . SER D 326 ? 0.8549 0.9316 0.5657 -0.2970 -0.0037 0.0991  627 SER D CA  
12844 C C   . SER D 326 ? 0.8251 0.9435 0.5499 -0.3075 0.0050  0.0896  627 SER D C   
12845 O O   . SER D 326 ? 0.8509 1.0064 0.5909 -0.3022 0.0107  0.0807  627 SER D O   
12846 C CB  . SER D 326 ? 0.8466 0.9225 0.5373 -0.3057 -0.0033 0.1045  627 SER D CB  
12847 O OG  . SER D 326 ? 0.8459 0.9117 0.5147 -0.3272 -0.0024 0.1095  627 SER D OG  
12848 N N   . SER D 327 ? 0.8129 0.9279 0.5328 -0.3219 0.0063  0.0907  628 SER D N   
12849 C CA  . SER D 327 ? 0.7670 0.9255 0.5070 -0.3260 0.0133  0.0803  628 SER D CA  
12850 C C   . SER D 327 ? 0.6421 0.8103 0.4108 -0.3027 0.0117  0.0724  628 SER D C   
12851 O O   . SER D 327 ? 0.6700 0.8773 0.4589 -0.3000 0.0171  0.0628  628 SER D O   
12852 C CB  . SER D 327 ? 0.7825 0.9365 0.5110 -0.3472 0.0139  0.0816  628 SER D CB  
12853 O OG  . SER D 327 ? 0.7359 0.8605 0.4631 -0.3442 0.0094  0.0854  628 SER D OG  
12854 N N   . LEU D 328 ? 0.5771 0.7114 0.3474 -0.2858 0.0045  0.0763  629 LEU D N   
12855 C CA  . LEU D 328 ? 0.6986 0.8377 0.4937 -0.2637 0.0026  0.0699  629 LEU D CA  
12856 C C   . LEU D 328 ? 0.8229 0.9714 0.6278 -0.2679 0.0037  0.0661  629 LEU D C   
12857 O O   . LEU D 328 ? 0.8872 1.0610 0.7153 -0.2551 0.0057  0.0578  629 LEU D O   
12858 C CB  . LEU D 328 ? 0.7664 0.9394 0.5817 -0.2489 0.0069  0.0604  629 LEU D CB  
12859 C CG  . LEU D 328 ? 0.7039 0.8702 0.5103 -0.2446 0.0059  0.0627  629 LEU D CG  
12860 C CD1 . LEU D 328 ? 0.5437 0.7348 0.3698 -0.2267 0.0091  0.0528  629 LEU D CD1 
12861 C CD2 . LEU D 328 ? 0.7704 0.8929 0.5639 -0.2384 -0.0026 0.0723  629 LEU D CD2 
12862 N N   . TRP D 329 ? 0.8751 1.0011 0.6608 -0.2861 0.0021  0.0725  630 TRP D N   
12863 C CA  . TRP D 329 ? 0.7839 0.9155 0.5767 -0.2912 0.0024  0.0692  630 TRP D CA  
12864 C C   . TRP D 329 ? 0.8185 0.9310 0.6252 -0.2699 -0.0029 0.0679  630 TRP D C   
12865 O O   . TRP D 329 ? 0.8513 0.9858 0.6772 -0.2629 -0.0015 0.0609  630 TRP D O   
12866 C CB  . TRP D 329 ? 0.7313 0.8372 0.4968 -0.3164 0.0017  0.0764  630 TRP D CB  
12867 C CG  . TRP D 329 ? 0.8061 0.8558 0.5479 -0.3151 -0.0052 0.0869  630 TRP D CG  
12868 C CD1 . TRP D 329 ? 0.8213 0.8454 0.5395 -0.3214 -0.0073 0.0958  630 TRP D CD1 
12869 C CD2 . TRP D 329 ? 0.8324 0.8454 0.5709 -0.3061 -0.0111 0.0896  630 TRP D CD2 
12870 N NE1 . TRP D 329 ? 0.8344 0.8082 0.5353 -0.3157 -0.0143 0.1039  630 TRP D NE1 
12871 C CE2 . TRP D 329 ? 0.8762 0.8425 0.5893 -0.3062 -0.0164 0.1000  630 TRP D CE2 
12872 C CE3 . TRP D 329 ? 0.8238 0.8393 0.5779 -0.2974 -0.0123 0.0842  630 TRP D CE3 
12873 C CZ2 . TRP D 329 ? 0.8156 0.7385 0.5192 -0.2969 -0.0226 0.1045  630 TRP D CZ2 
12874 C CZ3 . TRP D 329 ? 0.7900 0.7622 0.5341 -0.2897 -0.0181 0.0887  630 TRP D CZ3 
12875 C CH2 . TRP D 329 ? 0.8246 0.7514 0.5440 -0.2890 -0.0230 0.0984  630 TRP D CH2 
12876 N N   . LYS D 330 ? 0.8425 0.9155 0.6396 -0.2593 -0.0089 0.0746  631 LYS D N   
12877 C CA  . LYS D 330 ? 0.7388 0.7963 0.5498 -0.2386 -0.0135 0.0731  631 LYS D CA  
12878 C C   . LYS D 330 ? 0.7496 0.8406 0.5879 -0.2210 -0.0108 0.0642  631 LYS D C   
12879 O O   . LYS D 330 ? 0.8141 0.9136 0.6684 -0.2115 -0.0111 0.0592  631 LYS D O   
12880 C CB  . LYS D 330 ? 0.6635 0.6820 0.4623 -0.2282 -0.0198 0.0810  631 LYS D CB  
12881 C CG  . LYS D 330 ? 0.7425 0.7183 0.5168 -0.2373 -0.0242 0.0893  631 LYS D CG  
12882 C CD  . LYS D 330 ? 0.6805 0.6231 0.4474 -0.2220 -0.0308 0.0960  631 LYS D CD  
12883 C CE  . LYS D 330 ? 0.7329 0.6298 0.4749 -0.2276 -0.0355 0.1040  631 LYS D CE  
12884 N NZ  . LYS D 330 ? 0.8478 0.7203 0.5948 -0.2061 -0.0415 0.1059  631 LYS D NZ  
12885 N N   . ASP D 331 ? 0.7021 0.8110 0.5445 -0.2166 -0.0082 0.0620  632 ASP D N   
12886 C CA  . ASP D 331 ? 0.7090 0.8467 0.5743 -0.1999 -0.0053 0.0533  632 ASP D CA  
12887 C C   . ASP D 331 ? 0.6459 0.8208 0.5258 -0.2031 -0.0002 0.0455  632 ASP D C   
12888 O O   . ASP D 331 ? 0.6563 0.8443 0.5548 -0.1878 0.0001  0.0396  632 ASP D O   
12889 C CB  . ASP D 331 ? 0.6546 0.8044 0.5175 -0.1981 -0.0026 0.0520  632 ASP D CB  
12890 C CG  . ASP D 331 ? 0.6374 0.7542 0.4843 -0.1970 -0.0079 0.0603  632 ASP D CG  
12891 O OD1 . ASP D 331 ? 0.6338 0.7346 0.4596 -0.2126 -0.0091 0.0677  632 ASP D OD1 
12892 O OD2 . ASP D 331 ? 0.6500 0.7571 0.5047 -0.1808 -0.0111 0.0595  632 ASP D OD2 
12893 N N   . GLN D 332 ? 0.5552 0.7484 0.4262 -0.2231 0.0038  0.0456  633 GLN D N   
12894 C CA  . GLN D 332 ? 0.5889 0.8246 0.4742 -0.2268 0.0089  0.0378  633 GLN D CA  
12895 C C   . GLN D 332 ? 0.6616 0.8937 0.5541 -0.2257 0.0062  0.0368  633 GLN D C   
12896 O O   . GLN D 332 ? 0.7147 0.9746 0.6264 -0.2147 0.0078  0.0299  633 GLN D O   
12897 C CB  . GLN D 332 ? 0.5734 0.8298 0.4459 -0.2508 0.0139  0.0386  633 GLN D CB  
12898 C CG  . GLN D 332 ? 0.5743 0.8796 0.4592 -0.2502 0.0211  0.0303  633 GLN D CG  
12899 C CD  . GLN D 332 ? 0.7356 1.0561 0.6039 -0.2763 0.0258  0.0327  633 GLN D CD  
12900 O OE1 . GLN D 332 ? 0.7890 1.0822 0.6366 -0.2953 0.0234  0.0404  633 GLN D OE1 
12901 N NE2 . GLN D 332 ? 0.8276 1.1903 0.7035 -0.2776 0.0326  0.0259  633 GLN D NE2 
12902 N N   . ALA D 333 ? 0.6444 0.8413 0.5203 -0.2366 0.0020  0.0437  634 ALA D N   
12903 C CA  . ALA D 333 ? 0.6684 0.8595 0.5486 -0.2372 -0.0006 0.0426  634 ALA D CA  
12904 C C   . ALA D 333 ? 0.6798 0.8600 0.5758 -0.2129 -0.0043 0.0405  634 ALA D C   
12905 O O   . ALA D 333 ? 0.7475 0.9440 0.6574 -0.2066 -0.0044 0.0357  634 ALA D O   
12906 C CB  . ALA D 333 ? 0.6366 0.7885 0.4921 -0.2547 -0.0039 0.0502  634 ALA D CB  
12907 N N   . LEU D 334 ? 0.6580 0.8122 0.5517 -0.1996 -0.0072 0.0440  635 LEU D N   
12908 C CA  . LEU D 334 ? 0.5129 0.6572 0.4206 -0.1778 -0.0102 0.0421  635 LEU D CA  
12909 C C   . LEU D 334 ? 0.5642 0.7445 0.4935 -0.1645 -0.0069 0.0339  635 LEU D C   
12910 O O   . LEU D 334 ? 0.6959 0.8763 0.6369 -0.1524 -0.0088 0.0313  635 LEU D O   
12911 C CB  . LEU D 334 ? 0.4495 0.5689 0.3522 -0.1674 -0.0130 0.0463  635 LEU D CB  
12912 C CG  . LEU D 334 ? 0.4788 0.5903 0.3955 -0.1460 -0.0154 0.0441  635 LEU D CG  
12913 C CD1 . LEU D 334 ? 0.5990 0.6841 0.5134 -0.1423 -0.0199 0.0471  635 LEU D CD1 
12914 C CD2 . LEU D 334 ? 0.5922 0.6910 0.5051 -0.1387 -0.0169 0.0467  635 LEU D CD2 
12915 N N   . VAL D 335 ? 0.5725 0.7827 0.5065 -0.1656 -0.0021 0.0297  636 VAL D N   
12916 C CA  . VAL D 335 ? 0.5431 0.7858 0.4962 -0.1509 0.0010  0.0218  636 VAL D CA  
12917 C C   . VAL D 335 ? 0.5909 0.8579 0.5527 -0.1549 0.0015  0.0183  636 VAL D C   
12918 O O   . VAL D 335 ? 0.5908 0.8656 0.5662 -0.1398 0.0003  0.0148  636 VAL D O   
12919 C CB  . VAL D 335 ? 0.5076 0.7784 0.4628 -0.1512 0.0066  0.0173  636 VAL D CB  
12920 C CG1 . VAL D 335 ? 0.3434 0.6487 0.3173 -0.1352 0.0099  0.0087  636 VAL D CG1 
12921 C CG2 . VAL D 335 ? 0.5042 0.7522 0.4519 -0.1453 0.0057  0.0198  636 VAL D CG2 
12922 N N   . GLU D 336 ? 0.5872 0.8669 0.5405 -0.1760 0.0031  0.0194  637 GLU D N   
12923 C CA  . GLU D 336 ? 0.5590 0.8653 0.5199 -0.1824 0.0035  0.0159  637 GLU D CA  
12924 C C   . GLU D 336 ? 0.6998 0.9823 0.6627 -0.1752 -0.0018 0.0176  637 GLU D C   
12925 O O   . GLU D 336 ? 0.6326 0.9363 0.6093 -0.1659 -0.0024 0.0133  637 GLU D O   
12926 C CB  . GLU D 336 ? 0.5007 0.8167 0.4477 -0.2099 0.0056  0.0178  637 GLU D CB  
12927 C CG  . GLU D 336 ? 0.5334 0.8804 0.4791 -0.2193 0.0116  0.0153  637 GLU D CG  
12928 C CD  . GLU D 336 ? 0.5871 0.9859 0.5538 -0.2072 0.0159  0.0065  637 GLU D CD  
12929 O OE1 . GLU D 336 ? 0.5666 0.9764 0.5488 -0.1903 0.0139  0.0027  637 GLU D OE1 
12930 O OE2 . GLU D 336 ? 0.6769 1.1059 0.6439 -0.2142 0.0214  0.0033  637 GLU D OE2 
12931 N N   . ILE D 337 ? 0.7075 0.9463 0.6560 -0.1788 -0.0056 0.0240  638 ILE D N   
12932 C CA  . ILE D 337 ? 0.5539 0.7676 0.5028 -0.1717 -0.0102 0.0255  638 ILE D CA  
12933 C C   . ILE D 337 ? 0.6599 0.8805 0.6264 -0.1477 -0.0110 0.0220  638 ILE D C   
12934 O O   . ILE D 337 ? 0.7764 1.0040 0.7513 -0.1411 -0.0128 0.0196  638 ILE D O   
12935 C CB  . ILE D 337 ? 0.4895 0.6556 0.4207 -0.1755 -0.0137 0.0327  638 ILE D CB  
12936 C CG1 . ILE D 337 ? 0.5508 0.7050 0.4616 -0.2000 -0.0134 0.0364  638 ILE D CG1 
12937 C CG2 . ILE D 337 ? 0.4846 0.6257 0.4180 -0.1641 -0.0179 0.0335  638 ILE D CG2 
12938 C CD1 . ILE D 337 ? 0.6377 0.7457 0.5291 -0.2026 -0.0168 0.0439  638 ILE D CD1 
12939 N N   . ASN D 338 ? 0.6324 0.8508 0.6031 -0.1350 -0.0097 0.0216  639 ASN D N   
12940 C CA  . ASN D 338 ? 0.6056 0.8245 0.5897 -0.1132 -0.0105 0.0188  639 ASN D CA  
12941 C C   . ASN D 338 ? 0.5197 0.7777 0.5188 -0.1042 -0.0078 0.0123  639 ASN D C   
12942 O O   . ASN D 338 ? 0.4339 0.6915 0.4425 -0.0872 -0.0091 0.0103  639 ASN D O   
12943 C CB  . ASN D 338 ? 0.5070 0.7102 0.4890 -0.1042 -0.0099 0.0200  639 ASN D CB  
12944 C CG  . ASN D 338 ? 0.6042 0.7685 0.5765 -0.1040 -0.0139 0.0259  639 ASN D CG  
12945 O OD1 . ASN D 338 ? 0.7432 0.8920 0.7202 -0.0926 -0.0166 0.0264  639 ASN D OD1 
12946 N ND2 . ASN D 338 ? 0.5762 0.7251 0.5343 -0.1167 -0.0146 0.0306  639 ASN D ND2 
12947 N N   . ILE D 339 ? 0.5036 0.7951 0.5042 -0.1149 -0.0041 0.0091  640 ILE D N   
12948 C CA  . ILE D 339 ? 0.5055 0.8388 0.5204 -0.1072 -0.0020 0.0029  640 ILE D CA  
12949 C C   . ILE D 339 ? 0.5369 0.8769 0.5552 -0.1108 -0.0053 0.0029  640 ILE D C   
12950 O O   . ILE D 339 ? 0.5660 0.9208 0.5959 -0.0956 -0.0066 -0.0001 640 ILE D O   
12951 C CB  . ILE D 339 ? 0.3982 0.7685 0.4136 -0.1195 0.0031  -0.0006 640 ILE D CB  
12952 C CG1 . ILE D 339 ? 0.4122 0.7834 0.4272 -0.1109 0.0070  -0.0027 640 ILE D CG1 
12953 C CG2 . ILE D 339 ? 0.4603 0.8776 0.4898 -0.1157 0.0045  -0.0065 640 ILE D CG2 
12954 C CD1 . ILE D 339 ? 0.3351 0.7182 0.3403 -0.1302 0.0110  -0.0021 640 ILE D CD1 
12955 N N   . ALA D 340 ? 0.5275 0.8551 0.5340 -0.1313 -0.0068 0.0063  641 ALA D N   
12956 C CA  . ALA D 340 ? 0.7493 1.0788 0.7557 -0.1379 -0.0101 0.0063  641 ALA D CA  
12957 C C   . ALA D 340 ? 0.7196 1.0251 0.7302 -0.1204 -0.0140 0.0076  641 ALA D C   
12958 O O   . ALA D 340 ? 0.6152 0.9395 0.6358 -0.1116 -0.0157 0.0048  641 ALA D O   
12959 C CB  . ALA D 340 ? 0.8080 1.1150 0.7962 -0.1622 -0.0110 0.0103  641 ALA D CB  
12960 N N   . VAL D 341 ? 0.6402 0.9055 0.6431 -0.1152 -0.0156 0.0119  642 VAL D N   
12961 C CA  . VAL D 341 ? 0.4452 0.6868 0.4512 -0.0996 -0.0188 0.0132  642 VAL D CA  
12962 C C   . VAL D 341 ? 0.4853 0.7485 0.5059 -0.0794 -0.0182 0.0095  642 VAL D C   
12963 O O   . VAL D 341 ? 0.4136 0.6817 0.4399 -0.0712 -0.0206 0.0085  642 VAL D O   
12964 C CB  . VAL D 341 ? 0.3043 0.5069 0.3018 -0.0959 -0.0198 0.0177  642 VAL D CB  
12965 C CG1 . VAL D 341 ? 0.4633 0.6489 0.4667 -0.0778 -0.0219 0.0182  642 VAL D CG1 
12966 C CG2 . VAL D 341 ? 0.3769 0.5516 0.3584 -0.1122 -0.0217 0.0220  642 VAL D CG2 
12967 N N   . LEU D 342 ? 0.5347 0.8091 0.5600 -0.0709 -0.0150 0.0074  643 LEU D N   
12968 C CA  . LEU D 342 ? 0.5514 0.8400 0.5877 -0.0502 -0.0143 0.0040  643 LEU D CA  
12969 C C   . LEU D 342 ? 0.5872 0.9150 0.6333 -0.0479 -0.0146 0.0001  643 LEU D C   
12970 O O   . LEU D 342 ? 0.4800 0.8122 0.5326 -0.0327 -0.0167 -0.0008 643 LEU D O   
12971 C CB  . LEU D 342 ? 0.3673 0.6601 0.4048 -0.0426 -0.0104 0.0016  643 LEU D CB  
12972 C CG  . LEU D 342 ? 0.4276 0.6826 0.4573 -0.0400 -0.0109 0.0050  643 LEU D CG  
12973 C CD1 . LEU D 342 ? 0.4004 0.6578 0.4280 -0.0374 -0.0070 0.0027  643 LEU D CD1 
12974 C CD2 . LEU D 342 ? 0.2744 0.5081 0.3064 -0.0248 -0.0135 0.0062  643 LEU D CD2 
12975 N N   . TYR D 343 ? 0.6918 1.0493 0.7384 -0.0632 -0.0127 -0.0020 644 TYR D N   
12976 C CA  . TYR D 343 ? 0.4912 0.8922 0.5482 -0.0620 -0.0129 -0.0061 644 TYR D CA  
12977 C C   . TYR D 343 ? 0.5967 0.9941 0.6524 -0.0676 -0.0175 -0.0045 644 TYR D C   
12978 O O   . TYR D 343 ? 0.5092 0.9351 0.5741 -0.0594 -0.0194 -0.0070 644 TYR D O   
12979 C CB  . TYR D 343 ? 0.3029 0.7373 0.3599 -0.0796 -0.0091 -0.0089 644 TYR D CB  
12980 C CG  . TYR D 343 ? 0.3185 0.7983 0.3834 -0.0877 -0.0098 -0.0125 644 TYR D CG  
12981 C CD1 . TYR D 343 ? 0.2750 0.7979 0.3544 -0.0721 -0.0087 -0.0176 644 TYR D CD1 
12982 C CD2 . TYR D 343 ? 0.3223 0.8029 0.3793 -0.1116 -0.0114 -0.0111 644 TYR D CD2 
12983 C CE1 . TYR D 343 ? 0.4248 0.9936 0.5124 -0.0795 -0.0096 -0.0210 644 TYR D CE1 
12984 C CE2 . TYR D 343 ? 0.4981 1.0227 0.5620 -0.1210 -0.0120 -0.0147 644 TYR D CE2 
12985 C CZ  . TYR D 343 ? 0.5291 1.0999 0.6093 -0.1048 -0.0112 -0.0197 644 TYR D CZ  
12986 O OH  . TYR D 343 ? 0.6108 1.2302 0.6992 -0.1139 -0.0122 -0.0235 644 TYR D OH  
12987 N N   . SER D 344 ? 0.5678 0.9304 0.6115 -0.0808 -0.0194 -0.0004 645 SER D N   
12988 C CA  . SER D 344 ? 0.3448 0.7025 0.3853 -0.0880 -0.0233 0.0005  645 SER D CA  
12989 C C   . SER D 344 ? 0.4234 0.7637 0.4675 -0.0687 -0.0264 0.0019  645 SER D C   
12990 O O   . SER D 344 ? 0.4062 0.7627 0.4547 -0.0655 -0.0294 0.0006  645 SER D O   
12991 C CB  . SER D 344 ? 0.3501 0.6759 0.3747 -0.1084 -0.0238 0.0038  645 SER D CB  
12992 O OG  . SER D 344 ? 0.3549 0.7036 0.3754 -0.1292 -0.0215 0.0022  645 SER D OG  
12993 N N   . PHE D 345 ? 0.4049 0.7137 0.4467 -0.0563 -0.0259 0.0044  646 PHE D N   
12994 C CA  . PHE D 345 ? 0.4073 0.7004 0.4519 -0.0384 -0.0283 0.0058  646 PHE D CA  
12995 C C   . PHE D 345 ? 0.5585 0.8813 0.6142 -0.0203 -0.0283 0.0029  646 PHE D C   
12996 O O   . PHE D 345 ? 0.7610 1.0882 0.8196 -0.0105 -0.0314 0.0033  646 PHE D O   
12997 C CB  . PHE D 345 ? 0.2514 0.5069 0.2909 -0.0311 -0.0274 0.0088  646 PHE D CB  
12998 C CG  . PHE D 345 ? 0.4834 0.7051 0.5123 -0.0423 -0.0289 0.0123  646 PHE D CG  
12999 C CD1 . PHE D 345 ? 0.2660 0.4858 0.2868 -0.0616 -0.0287 0.0128  646 PHE D CD1 
13000 C CD2 . PHE D 345 ? 0.3587 0.5506 0.3848 -0.0334 -0.0303 0.0150  646 PHE D CD2 
13001 C CE1 . PHE D 345 ? 0.3379 0.5245 0.3475 -0.0698 -0.0302 0.0159  646 PHE D CE1 
13002 C CE2 . PHE D 345 ? 0.3479 0.5110 0.3647 -0.0416 -0.0315 0.0177  646 PHE D CE2 
13003 C CZ  . PHE D 345 ? 0.4253 0.5846 0.4337 -0.0588 -0.0316 0.0181  646 PHE D CZ  
13004 N N   . GLN D 346 ? 0.4287 0.7722 0.4898 -0.0151 -0.0249 0.0000  647 GLN D N   
13005 C CA  . GLN D 346 ? 0.4663 0.8347 0.5367 0.0049  -0.0247 -0.0028 647 GLN D CA  
13006 C C   . GLN D 346 ? 0.5515 0.9608 0.6296 0.0034  -0.0273 -0.0052 647 GLN D C   
13007 O O   . GLN D 346 ? 0.6156 1.0388 0.6993 0.0212  -0.0295 -0.0058 647 GLN D O   
13008 C CB  . GLN D 346 ? 0.4860 0.8671 0.5595 0.0107  -0.0200 -0.0063 647 GLN D CB  
13009 C CG  . GLN D 346 ? 0.5269 0.8712 0.5943 0.0208  -0.0182 -0.0048 647 GLN D CG  
13010 C CD  . GLN D 346 ? 0.6106 0.9603 0.6771 0.0177  -0.0134 -0.0076 647 GLN D CD  
13011 O OE1 . GLN D 346 ? 0.6068 0.9842 0.6758 0.0051  -0.0111 -0.0100 647 GLN D OE1 
13012 N NE2 . GLN D 346 ? 0.6067 0.9304 0.6686 0.0282  -0.0116 -0.0076 647 GLN D NE2 
13013 N N   . SER D 347 ? 0.5123 0.9406 0.5896 -0.0179 -0.0272 -0.0064 648 SER D N   
13014 C CA  . SER D 347 ? 0.4397 0.9097 0.5241 -0.0223 -0.0298 -0.0090 648 SER D CA  
13015 C C   . SER D 347 ? 0.5891 1.0456 0.6701 -0.0206 -0.0350 -0.0064 648 SER D C   
13016 O O   . SER D 347 ? 0.5716 1.0578 0.6595 -0.0123 -0.0383 -0.0078 648 SER D O   
13017 C CB  . SER D 347 ? 0.3498 0.8403 0.4317 -0.0485 -0.0278 -0.0110 648 SER D CB  
13018 O OG  . SER D 347 ? 0.5321 1.0378 0.6170 -0.0497 -0.0227 -0.0134 648 SER D OG  
13019 N N   . ASP D 348 ? 0.4392 0.8522 0.5094 -0.0276 -0.0358 -0.0027 649 ASP D N   
13020 C CA  . ASP D 348 ? 0.4121 0.8078 0.4775 -0.0259 -0.0400 -0.0004 649 ASP D CA  
13021 C C   . ASP D 348 ? 0.5399 0.9106 0.6050 -0.0037 -0.0410 0.0026  649 ASP D C   
13022 O O   . ASP D 348 ? 0.6404 0.9852 0.6990 -0.0030 -0.0434 0.0053  649 ASP D O   
13023 C CB  . ASP D 348 ? 0.2598 0.6236 0.3128 -0.0459 -0.0401 0.0013  649 ASP D CB  
13024 C CG  . ASP D 348 ? 0.4022 0.7884 0.4524 -0.0695 -0.0396 -0.0015 649 ASP D CG  
13025 O OD1 . ASP D 348 ? 0.4141 0.8437 0.4736 -0.0708 -0.0389 -0.0048 649 ASP D OD1 
13026 O OD2 . ASP D 348 ? 0.5358 0.8965 0.5739 -0.0869 -0.0397 -0.0005 649 ASP D OD2 
13027 N N   . LYS D 349 ? 0.5615 0.9390 0.6324 0.0137  -0.0390 0.0018  650 LYS D N   
13028 C CA  . LYS D 349 ? 0.5595 0.9118 0.6283 0.0342  -0.0393 0.0044  650 LYS D CA  
13029 C C   . LYS D 349 ? 0.5352 0.8427 0.5942 0.0304  -0.0397 0.0084  650 LYS D C   
13030 O O   . LYS D 349 ? 0.5464 0.8376 0.6019 0.0410  -0.0420 0.0112  650 LYS D O   
13031 C CB  . LYS D 349 ? 0.5695 0.9450 0.6430 0.0513  -0.0430 0.0045  650 LYS D CB  
13032 C CG  . LYS D 349 ? 0.5288 0.9465 0.6127 0.0613  -0.0417 0.0003  650 LYS D CG  
13033 C CD  . LYS D 349 ? 0.6649 1.1185 0.7551 0.0725  -0.0463 -0.0003 650 LYS D CD  
13034 C CE  . LYS D 349 ? 0.8299 1.2699 0.9174 0.0991  -0.0482 0.0023  650 LYS D CE  
13035 N NZ  . LYS D 349 ? 0.9183 1.3988 1.0128 0.1133  -0.0527 0.0016  650 LYS D NZ  
13036 N N   . VAL D 350 ? 0.3865 0.6750 0.4407 0.0154  -0.0375 0.0088  651 VAL D N   
13037 C CA  . VAL D 350 ? 0.4352 0.6832 0.4811 0.0124  -0.0371 0.0120  651 VAL D CA  
13038 C C   . VAL D 350 ? 0.5177 0.7481 0.5629 0.0191  -0.0337 0.0124  651 VAL D C   
13039 O O   . VAL D 350 ? 0.4191 0.6595 0.4660 0.0130  -0.0311 0.0105  651 VAL D O   
13040 C CB  . VAL D 350 ? 0.3967 0.6343 0.4363 -0.0078 -0.0374 0.0123  651 VAL D CB  
13041 C CG1 . VAL D 350 ? 0.3913 0.5897 0.4232 -0.0087 -0.0371 0.0153  651 VAL D CG1 
13042 C CG2 . VAL D 350 ? 0.4009 0.6567 0.4400 -0.0159 -0.0406 0.0110  651 VAL D CG2 
13043 N N   . THR D 351 ? 0.4890 0.6933 0.5307 0.0302  -0.0337 0.0148  652 THR D N   
13044 C CA  . THR D 351 ? 0.4601 0.6483 0.5003 0.0372  -0.0308 0.0147  652 THR D CA  
13045 C C   . THR D 351 ? 0.5067 0.6845 0.5443 0.0238  -0.0287 0.0148  652 THR D C   
13046 O O   . THR D 351 ? 0.4872 0.6503 0.5205 0.0126  -0.0298 0.0168  652 THR D O   
13047 C CB  . THR D 351 ? 0.4605 0.6194 0.4953 0.0466  -0.0311 0.0176  652 THR D CB  
13048 O OG1 . THR D 351 ? 0.5505 0.7167 0.5856 0.0601  -0.0331 0.0183  652 THR D OG1 
13049 C CG2 . THR D 351 ? 0.3895 0.5310 0.4215 0.0515  -0.0280 0.0170  652 THR D CG2 
13050 N N   . ILE D 352 ? 0.5310 0.7162 0.5703 0.0259  -0.0258 0.0125  653 ILE D N   
13051 C CA  . ILE D 352 ? 0.3963 0.5701 0.4318 0.0154  -0.0239 0.0129  653 ILE D CA  
13052 C C   . ILE D 352 ? 0.4806 0.6550 0.5166 0.0245  -0.0208 0.0103  653 ILE D C   
13053 O O   . ILE D 352 ? 0.5093 0.6989 0.5489 0.0370  -0.0198 0.0075  653 ILE D O   
13054 C CB  . ILE D 352 ? 0.3483 0.5408 0.3840 -0.0006 -0.0237 0.0121  653 ILE D CB  
13055 C CG1 . ILE D 352 ? 0.3359 0.5090 0.3644 -0.0128 -0.0231 0.0145  653 ILE D CG1 
13056 C CG2 . ILE D 352 ? 0.2640 0.4904 0.3061 0.0023  -0.0214 0.0080  653 ILE D CG2 
13057 C CD1 . ILE D 352 ? 0.2540 0.4357 0.2782 -0.0312 -0.0235 0.0151  653 ILE D CD1 
13058 N N   . VAL D 353 ? 0.5120 0.6696 0.5432 0.0188  -0.0194 0.0111  654 VAL D N   
13059 C CA  . VAL D 353 ? 0.5451 0.7033 0.5751 0.0245  -0.0161 0.0080  654 VAL D CA  
13060 C C   . VAL D 353 ? 0.5566 0.7189 0.5837 0.0111  -0.0146 0.0080  654 VAL D C   
13061 O O   . VAL D 353 ? 0.5415 0.6902 0.5645 -0.0002 -0.0164 0.0117  654 VAL D O   
13062 C CB  . VAL D 353 ? 0.4934 0.6236 0.5185 0.0329  -0.0159 0.0088  654 VAL D CB  
13063 C CG1 . VAL D 353 ? 0.4057 0.5140 0.4262 0.0230  -0.0172 0.0124  654 VAL D CG1 
13064 C CG2 . VAL D 353 ? 0.5151 0.6467 0.5380 0.0422  -0.0125 0.0044  654 VAL D CG2 
13065 N N   . ASP D 354 ? 0.5295 0.7111 0.5581 0.0127  -0.0112 0.0039  655 ASP D N   
13066 C CA  . ASP D 354 ? 0.5709 0.7562 0.5952 0.0005  -0.0094 0.0038  655 ASP D CA  
13067 C C   . ASP D 354 ? 0.5415 0.7019 0.5592 0.0016  -0.0090 0.0047  655 ASP D C   
13068 O O   . ASP D 354 ? 0.4928 0.6383 0.5097 0.0128  -0.0088 0.0034  655 ASP D O   
13069 C CB  . ASP D 354 ? 0.6083 0.8248 0.6362 0.0019  -0.0053 -0.0015 655 ASP D CB  
13070 C CG  . ASP D 354 ? 0.8026 1.0214 0.8323 0.0198  -0.0027 -0.0066 655 ASP D CG  
13071 O OD1 . ASP D 354 ? 0.9608 1.1836 0.9951 0.0326  -0.0038 -0.0075 655 ASP D OD1 
13072 O OD2 . ASP D 354 ? 0.8556 1.0702 0.8808 0.0213  0.0004  -0.0095 655 ASP D OD2 
13073 N N   . HIS D 355 ? 0.5885 0.7446 0.6004 -0.0107 -0.0090 0.0069  656 HIS D N   
13074 C CA  . HIS D 355 ? 0.4573 0.5921 0.4631 -0.0107 -0.0094 0.0079  656 HIS D CA  
13075 C C   . HIS D 355 ? 0.4130 0.5510 0.4176 -0.0014 -0.0057 0.0022  656 HIS D C   
13076 O O   . HIS D 355 ? 0.4154 0.5341 0.4159 0.0026  -0.0060 0.0018  656 HIS D O   
13077 C CB  . HIS D 355 ? 0.2953 0.4250 0.2939 -0.0249 -0.0106 0.0120  656 HIS D CB  
13078 C CG  . HIS D 355 ? 0.4607 0.6127 0.4572 -0.0341 -0.0077 0.0103  656 HIS D CG  
13079 N ND1 . HIS D 355 ? 0.4189 0.5885 0.4178 -0.0417 -0.0075 0.0108  656 HIS D ND1 
13080 C CD2 . HIS D 355 ? 0.4296 0.5893 0.4208 -0.0386 -0.0049 0.0082  656 HIS D CD2 
13081 C CE1 . HIS D 355 ? 0.4736 0.6618 0.4691 -0.0507 -0.0043 0.0092  656 HIS D CE1 
13082 N NE2 . HIS D 355 ? 0.4665 0.6491 0.4574 -0.0485 -0.0026 0.0076  656 HIS D NE2 
13083 N N   . HIS D 356 ? 0.3981 0.5602 0.4059 0.0027  -0.0020 -0.0029 657 HIS D N   
13084 C CA  . HIS D 356 ? 0.3959 0.5591 0.4012 0.0133  0.0018  -0.0091 657 HIS D CA  
13085 C C   . HIS D 356 ? 0.5230 0.6708 0.5289 0.0284  0.0013  -0.0107 657 HIS D C   
13086 O O   . HIS D 356 ? 0.5132 0.6396 0.5124 0.0327  0.0019  -0.0122 657 HIS D O   
13087 C CB  . HIS D 356 ? 0.4239 0.6190 0.4329 0.0151  0.0061  -0.0145 657 HIS D CB  
13088 C CG  . HIS D 356 ? 0.4871 0.6958 0.4929 -0.0008 0.0074  -0.0132 657 HIS D CG  
13089 N ND1 . HIS D 356 ? 0.5299 0.7310 0.5272 -0.0066 0.0091  -0.0143 657 HIS D ND1 
13090 C CD2 . HIS D 356 ? 0.4770 0.7040 0.4850 -0.0135 0.0068  -0.0104 657 HIS D CD2 
13091 C CE1 . HIS D 356 ? 0.5907 0.8053 0.5850 -0.0213 0.0097  -0.0119 657 HIS D CE1 
13092 N NE2 . HIS D 356 ? 0.5314 0.7609 0.5318 -0.0263 0.0085  -0.0095 657 HIS D NE2 
13093 N N   . SER D 357 ? 0.6083 0.7663 0.6209 0.0358  0.0001  -0.0101 658 SER D N   
13094 C CA  . SER D 357 ? 0.4777 0.6200 0.4893 0.0503  -0.0006 -0.0107 658 SER D CA  
13095 C C   . SER D 357 ? 0.4763 0.5873 0.4825 0.0466  -0.0033 -0.0064 658 SER D C   
13096 O O   . SER D 357 ? 0.4850 0.5752 0.4845 0.0540  -0.0024 -0.0082 658 SER D O   
13097 C CB  . SER D 357 ? 0.6086 0.7682 0.6280 0.0570  -0.0025 -0.0095 658 SER D CB  
13098 O OG  . SER D 357 ? 0.7833 0.9261 0.7999 0.0711  -0.0035 -0.0092 658 SER D OG  
13099 N N   . ALA D 358 ? 0.2780 0.3856 0.2864 0.0346  -0.0065 -0.0011 659 ALA D N   
13100 C CA  . ALA D 358 ? 0.3802 0.4628 0.3851 0.0311  -0.0091 0.0029  659 ALA D CA  
13101 C C   . ALA D 358 ? 0.5769 0.6439 0.5743 0.0289  -0.0077 0.0010  659 ALA D C   
13102 O O   . ALA D 358 ? 0.6198 0.6667 0.6125 0.0328  -0.0079 0.0009  659 ALA D O   
13103 C CB  . ALA D 358 ? 0.2651 0.3487 0.2726 0.0193  -0.0124 0.0082  659 ALA D CB  
13104 N N   . THR D 359 ? 0.5732 0.6492 0.5683 0.0214  -0.0064 -0.0005 660 THR D N   
13105 C CA  . THR D 359 ? 0.4839 0.5463 0.4716 0.0175  -0.0058 -0.0021 660 THR D CA  
13106 C C   . THR D 359 ? 0.4631 0.5164 0.4444 0.0276  -0.0022 -0.0083 660 THR D C   
13107 O O   . THR D 359 ? 0.4626 0.4962 0.4371 0.0270  -0.0023 -0.0092 660 THR D O   
13108 C CB  . THR D 359 ? 0.4273 0.5012 0.4124 0.0072  -0.0054 -0.0020 660 THR D CB  
13109 O OG1 . THR D 359 ? 0.5177 0.6139 0.5052 0.0092  -0.0021 -0.0056 660 THR D OG1 
13110 C CG2 . THR D 359 ? 0.4394 0.5125 0.4265 -0.0029 -0.0094 0.0048  660 THR D CG2 
13111 N N   . GLU D 360 ? 0.4944 0.5618 0.4772 0.0369  0.0009  -0.0128 661 GLU D N   
13112 C CA  . GLU D 360 ? 0.4836 0.5403 0.4589 0.0491  0.0044  -0.0189 661 GLU D CA  
13113 C C   . GLU D 360 ? 0.6103 0.6423 0.5815 0.0557  0.0028  -0.0169 661 GLU D C   
13114 O O   . GLU D 360 ? 0.5867 0.5958 0.5472 0.0575  0.0043  -0.0197 661 GLU D O   
13115 C CB  . GLU D 360 ? 0.4472 0.5269 0.4268 0.0600  0.0074  -0.0234 661 GLU D CB  
13116 C CG  . GLU D 360 ? 0.7175 0.7862 0.6891 0.0763  0.0108  -0.0297 661 GLU D CG  
13117 C CD  . GLU D 360 ? 1.0012 1.0975 0.9794 0.0892  0.0132  -0.0337 661 GLU D CD  
13118 O OE1 . GLU D 360 ? 1.0341 1.1575 1.0237 0.0845  0.0117  -0.0308 661 GLU D OE1 
13119 O OE2 . GLU D 360 ? 1.0926 1.1840 1.0641 0.1041  0.0166  -0.0399 661 GLU D OE2 
13120 N N   . SER D 361 ? 0.6492 0.6849 0.6276 0.0581  0.0000  -0.0121 662 SER D N   
13121 C CA  A SER D 361 ? 0.6025 0.6157 0.5764 0.0636  -0.0013 -0.0096 662 SER D CA  
13122 C CA  B SER D 361 ? 0.6014 0.6147 0.5754 0.0635  -0.0014 -0.0095 662 SER D CA  
13123 C C   . SER D 361 ? 0.5847 0.5777 0.5535 0.0528  -0.0027 -0.0072 662 SER D C   
13124 O O   . SER D 361 ? 0.6235 0.5931 0.5826 0.0553  -0.0018 -0.0082 662 SER D O   
13125 C CB  A SER D 361 ? 0.5515 0.5748 0.5340 0.0666  -0.0043 -0.0048 662 SER D CB  
13126 C CB  B SER D 361 ? 0.5525 0.5760 0.5352 0.0660  -0.0044 -0.0046 662 SER D CB  
13127 O OG  A SER D 361 ? 0.5264 0.5666 0.5122 0.0790  -0.0032 -0.0073 662 SER D OG  
13128 O OG  B SER D 361 ? 0.5345 0.5577 0.5223 0.0540  -0.0075 0.0006  662 SER D OG  
13129 N N   . PHE D 362 ? 0.5898 0.5917 0.5642 0.0407  -0.0049 -0.0041 663 PHE D N   
13130 C CA  . PHE D 362 ? 0.6110 0.5986 0.5820 0.0311  -0.0065 -0.0020 663 PHE D CA  
13131 C C   . PHE D 362 ? 0.6800 0.6541 0.6399 0.0289  -0.0041 -0.0071 663 PHE D C   
13132 O O   . PHE D 362 ? 0.7647 0.7204 0.7179 0.0254  -0.0042 -0.0070 663 PHE D O   
13133 C CB  . PHE D 362 ? 0.5923 0.5924 0.5701 0.0206  -0.0096 0.0021  663 PHE D CB  
13134 C CG  . PHE D 362 ? 0.4900 0.4801 0.4656 0.0120  -0.0116 0.0042  663 PHE D CG  
13135 C CD1 . PHE D 362 ? 0.3610 0.3421 0.3388 0.0113  -0.0134 0.0077  663 PHE D CD1 
13136 C CD2 . PHE D 362 ? 0.4632 0.4548 0.4343 0.0047  -0.0117 0.0023  663 PHE D CD2 
13137 C CE1 . PHE D 362 ? 0.4761 0.4519 0.4529 0.0036  -0.0153 0.0093  663 PHE D CE1 
13138 C CE2 . PHE D 362 ? 0.6286 0.6145 0.5983 -0.0030 -0.0141 0.0041  663 PHE D CE2 
13139 C CZ  . PHE D 362 ? 0.6852 0.6641 0.6583 -0.0034 -0.0158 0.0075  663 PHE D CZ  
13140 N N   . ILE D 363 ? 0.6359 0.6192 0.5929 0.0300  -0.0016 -0.0119 664 ILE D N   
13141 C CA  . ILE D 363 ? 0.5181 0.4875 0.4627 0.0284  0.0012  -0.0179 664 ILE D CA  
13142 C C   . ILE D 363 ? 0.6764 0.6215 0.6103 0.0376  0.0036  -0.0209 664 ILE D C   
13143 O O   . ILE D 363 ? 0.5680 0.4919 0.4913 0.0323  0.0040  -0.0225 664 ILE D O   
13144 C CB  . ILE D 363 ? 0.4830 0.4676 0.4258 0.0298  0.0042  -0.0232 664 ILE D CB  
13145 C CG1 . ILE D 363 ? 0.5330 0.5358 0.4818 0.0179  0.0018  -0.0199 664 ILE D CG1 
13146 C CG2 . ILE D 363 ? 0.4454 0.4132 0.3738 0.0302  0.0076  -0.0305 664 ILE D CG2 
13147 C CD1 . ILE D 363 ? 0.4337 0.4267 0.3781 0.0065  -0.0009 -0.0182 664 ILE D CD1 
13148 N N   . LYS D 364 ? 0.6839 0.6314 0.6195 0.0513  0.0048  -0.0214 665 LYS D N   
13149 C CA  . LYS D 364 ? 0.6883 0.6105 0.6124 0.0616  0.0064  -0.0230 665 LYS D CA  
13150 C C   . LYS D 364 ? 0.6915 0.5953 0.6129 0.0544  0.0041  -0.0178 665 LYS D C   
13151 O O   . LYS D 364 ? 0.7035 0.5799 0.6103 0.0533  0.0057  -0.0197 665 LYS D O   
13152 C CB  . LYS D 364 ? 0.6307 0.5631 0.5595 0.0777  0.0068  -0.0226 665 LYS D CB  
13153 C CG  . LYS D 364 ? 0.6972 0.6483 0.6276 0.0873  0.0099  -0.0287 665 LYS D CG  
13154 C CD  . LYS D 364 ? 0.9353 0.8631 0.8484 0.0963  0.0141  -0.0361 665 LYS D CD  
13155 C CE  . LYS D 364 ? 1.0116 0.9210 0.9158 0.1142  0.0147  -0.0363 665 LYS D CE  
13156 N NZ  . LYS D 364 ? 0.9911 0.9196 0.8982 0.1319  0.0171  -0.0413 665 LYS D NZ  
13157 N N   . HIS D 365 ? 0.5646 0.4826 0.4988 0.0488  0.0006  -0.0115 666 HIS D N   
13158 C CA  . HIS D 365 ? 0.6532 0.5579 0.5862 0.0420  -0.0013 -0.0068 666 HIS D CA  
13159 C C   . HIS D 365 ? 0.7147 0.6098 0.6415 0.0284  -0.0012 -0.0083 666 HIS D C   
13160 O O   . HIS D 365 ? 0.7235 0.5987 0.6412 0.0235  -0.0006 -0.0078 666 HIS D O   
13161 C CB  . HIS D 365 ? 0.4543 0.3779 0.4021 0.0394  -0.0047 -0.0008 666 HIS D CB  
13162 C CG  . HIS D 365 ? 0.4343 0.3513 0.3836 0.0302  -0.0066 0.0035  666 HIS D CG  
13163 N ND1 . HIS D 365 ? 0.5702 0.4681 0.5117 0.0313  -0.0059 0.0053  666 HIS D ND1 
13164 C CD2 . HIS D 365 ? 0.5552 0.4835 0.5128 0.0203  -0.0091 0.0063  666 HIS D CD2 
13165 C CE1 . HIS D 365 ? 0.6347 0.5347 0.5805 0.0218  -0.0075 0.0086  666 HIS D CE1 
13166 N NE2 . HIS D 365 ? 0.5532 0.4715 0.5090 0.0158  -0.0095 0.0091  666 HIS D NE2 
13167 N N   . MET D 366 ? 0.7268 0.6369 0.6580 0.0216  -0.0018 -0.0102 667 MET D N   
13168 C CA  . MET D 366 ? 0.6850 0.5905 0.6114 0.0087  -0.0024 -0.0116 667 MET D CA  
13169 C C   . MET D 366 ? 0.6326 0.5125 0.5409 0.0075  0.0010  -0.0175 667 MET D C   
13170 O O   . MET D 366 ? 0.6509 0.5164 0.5520 -0.0017 0.0009  -0.0173 667 MET D O   
13171 C CB  . MET D 366 ? 0.7521 0.6779 0.6845 0.0032  -0.0037 -0.0124 667 MET D CB  
13172 C CG  . MET D 366 ? 0.7227 0.6501 0.6533 -0.0101 -0.0059 -0.0123 667 MET D CG  
13173 S SD  . MET D 366 ? 0.6292 0.5807 0.5667 -0.0143 -0.0081 -0.0114 667 MET D SD  
13174 C CE  . MET D 366 ? 0.6955 0.6528 0.6352 -0.0275 -0.0126 -0.0082 667 MET D CE  
13175 N N   . GLU D 367 ? 0.6268 0.5004 0.5267 0.0164  0.0043  -0.0233 668 GLU D N   
13176 C CA  . GLU D 367 ? 0.8123 0.6576 0.6924 0.0158  0.0077  -0.0296 668 GLU D CA  
13177 C C   . GLU D 367 ? 0.8226 0.6414 0.6926 0.0170  0.0083  -0.0271 668 GLU D C   
13178 O O   . GLU D 367 ? 0.7519 0.5500 0.6088 0.0063  0.0092  -0.0288 668 GLU D O   
13179 C CB  . GLU D 367 ? 0.9042 0.7457 0.7764 0.0289  0.0115  -0.0364 668 GLU D CB  
13180 C CG  . GLU D 367 ? 1.0218 0.8945 0.9088 0.0357  0.0112  -0.0361 668 GLU D CG  
13181 C CD  . GLU D 367 ? 1.0528 0.9329 0.9342 0.0353  0.0141  -0.0435 668 GLU D CD  
13182 O OE1 . GLU D 367 ? 1.0610 0.9342 0.9341 0.0231  0.0142  -0.0466 668 GLU D OE1 
13183 O OE2 . GLU D 367 ? 1.0495 0.9443 0.9348 0.0467  0.0164  -0.0464 668 GLU D OE2 
13184 N N   . ASN D 368 ? 0.8857 0.7064 0.7617 0.0287  0.0076  -0.0226 669 ASN D N   
13185 C CA  . ASN D 368 ? 0.8008 0.5969 0.6666 0.0309  0.0080  -0.0193 669 ASN D CA  
13186 C C   . ASN D 368 ? 0.7861 0.5806 0.6535 0.0144  0.0063  -0.0155 669 ASN D C   
13187 O O   . ASN D 368 ? 0.7136 0.4816 0.5648 0.0072  0.0080  -0.0163 669 ASN D O   
13188 C CB  . ASN D 368 ? 0.9028 0.7087 0.7780 0.0451  0.0065  -0.0144 669 ASN D CB  
13189 C CG  . ASN D 368 ? 0.8715 0.6510 0.7343 0.0493  0.0068  -0.0108 669 ASN D CG  
13190 O OD1 . ASN D 368 ? 0.8635 0.6113 0.7057 0.0529  0.0095  -0.0139 669 ASN D OD1 
13191 N ND2 . ASN D 368 ? 0.8625 0.6528 0.7357 0.0480  0.0043  -0.0041 669 ASN D ND2 
13192 N N   . GLU D 369 ? 0.6890 0.5119 0.5750 0.0079  0.0030  -0.0116 670 GLU D N   
13193 C CA  . GLU D 369 ? 0.5523 0.3797 0.4422 -0.0067 0.0013  -0.0084 670 GLU D CA  
13194 C C   . GLU D 369 ? 0.6995 0.5174 0.5781 -0.0211 0.0024  -0.0132 670 GLU D C   
13195 O O   . GLU D 369 ? 0.7983 0.6091 0.6721 -0.0330 0.0025  -0.0120 670 GLU D O   
13196 C CB  . GLU D 369 ? 0.5641 0.4231 0.4747 -0.0086 -0.0024 -0.0042 670 GLU D CB  
13197 C CG  . GLU D 369 ? 0.7339 0.6016 0.6547 0.0017  -0.0037 0.0008  670 GLU D CG  
13198 C CD  . GLU D 369 ? 0.6326 0.4932 0.5529 -0.0018 -0.0039 0.0052  670 GLU D CD  
13199 O OE1 . GLU D 369 ? 0.6419 0.5200 0.5745 -0.0066 -0.0063 0.0088  670 GLU D OE1 
13200 O OE2 . GLU D 369 ? 0.6578 0.4946 0.5641 0.0005  -0.0017 0.0052  670 GLU D OE2 
13201 N N   . TYR D 370 ? 0.6914 0.5113 0.5658 -0.0214 0.0033  -0.0189 671 TYR D N   
13202 C CA  . TYR D 370 ? 0.7820 0.5919 0.6439 -0.0359 0.0043  -0.0239 671 TYR D CA  
13203 C C   . TYR D 370 ? 0.9597 0.7316 0.7979 -0.0373 0.0082  -0.0276 671 TYR D C   
13204 O O   . TYR D 370 ? 0.9757 0.7354 0.8033 -0.0523 0.0088  -0.0289 671 TYR D O   
13205 C CB  . TYR D 370 ? 0.7963 0.6181 0.6584 -0.0368 0.0042  -0.0292 671 TYR D CB  
13206 C CG  . TYR D 370 ? 0.7289 0.5831 0.6081 -0.0439 -0.0001 -0.0259 671 TYR D CG  
13207 C CD1 . TYR D 370 ? 0.6913 0.5679 0.5878 -0.0355 -0.0026 -0.0206 671 TYR D CD1 
13208 C CD2 . TYR D 370 ? 0.7605 0.6223 0.6372 -0.0589 -0.0019 -0.0279 671 TYR D CD2 
13209 C CE1 . TYR D 370 ? 0.7438 0.6459 0.6533 -0.0410 -0.0067 -0.0172 671 TYR D CE1 
13210 C CE2 . TYR D 370 ? 0.7018 0.5926 0.5931 -0.0636 -0.0064 -0.0243 671 TYR D CE2 
13211 C CZ  . TYR D 370 ? 0.6890 0.5981 0.5960 -0.0541 -0.0088 -0.0187 671 TYR D CZ  
13212 O OH  . TYR D 370 ? 0.5967 0.5305 0.5158 -0.0576 -0.0133 -0.0147 671 TYR D OH  
13213 N N   . ARG D 371 ? 1.0856 0.8384 0.9144 -0.0218 0.0108  -0.0294 672 ARG D N   
13214 C CA  . ARG D 371 ? 1.1389 0.8509 0.9425 -0.0207 0.0144  -0.0326 672 ARG D CA  
13215 C C   . ARG D 371 ? 1.1935 0.8913 0.9916 -0.0292 0.0142  -0.0270 672 ARG D C   
13216 O O   . ARG D 371 ? 1.3659 1.0413 1.1468 -0.0439 0.0160  -0.0293 672 ARG D O   
13217 C CB  . ARG D 371 ? 1.3244 1.0229 1.1217 0.0010  0.0164  -0.0341 672 ARG D CB  
13218 C CG  . ARG D 371 ? 1.5540 1.2082 1.3220 0.0050  0.0205  -0.0398 672 ARG D CG  
13219 C CD  . ARG D 371 ? 1.7118 1.3566 1.4753 0.0294  0.0221  -0.0412 672 ARG D CD  
13220 N NE  . ARG D 371 ? 1.7439 1.4211 1.5242 0.0392  0.0218  -0.0444 672 ARG D NE  
13221 C CZ  . ARG D 371 ? 1.6894 1.3946 1.4891 0.0524  0.0197  -0.0402 672 ARG D CZ  
13222 N NH1 . ARG D 371 ? 1.6702 1.3750 1.4751 0.0584  0.0176  -0.0329 672 ARG D NH1 
13223 N NH2 . ARG D 371 ? 1.6096 1.3433 1.4223 0.0588  0.0200  -0.0436 672 ARG D NH2 
13224 N N   . CYS D 372 ? 1.0471 0.7585 0.8593 -0.0215 0.0122  -0.0198 673 CYS D N   
13225 C CA  . CYS D 372 ? 1.0245 0.7198 0.8293 -0.0267 0.0126  -0.0145 673 CYS D CA  
13226 C C   . CYS D 372 ? 1.0010 0.7203 0.8198 -0.0427 0.0105  -0.0106 673 CYS D C   
13227 O O   . CYS D 372 ? 1.0392 0.7439 0.8478 -0.0537 0.0119  -0.0082 673 CYS D O   
13228 C CB  . CYS D 372 ? 0.9517 0.6454 0.7608 -0.0085 0.0118  -0.0091 673 CYS D CB  
13229 S SG  . CYS D 372 ? 0.9945 0.7327 0.8350 -0.0031 0.0076  -0.0030 673 CYS D SG  
13230 N N   . ARG D 373 ? 0.9145 0.6700 0.7556 -0.0440 0.0074  -0.0098 674 ARG D N   
13231 C CA  . ARG D 373 ? 0.7569 0.5375 0.6124 -0.0565 0.0052  -0.0063 674 ARG D CA  
13232 C C   . ARG D 373 ? 0.8040 0.6002 0.6622 -0.0711 0.0040  -0.0104 674 ARG D C   
13233 O O   . ARG D 373 ? 0.7314 0.5446 0.5971 -0.0836 0.0027  -0.0085 674 ARG D O   
13234 C CB  . ARG D 373 ? 0.5914 0.4016 0.4700 -0.0463 0.0020  -0.0012 674 ARG D CB  
13235 C CG  . ARG D 373 ? 0.5516 0.3831 0.4435 -0.0545 0.0003  0.0033  674 ARG D CG  
13236 C CD  . ARG D 373 ? 0.5479 0.4069 0.4610 -0.0449 -0.0031 0.0071  674 ARG D CD  
13237 N NE  . ARG D 373 ? 0.5275 0.4038 0.4517 -0.0500 -0.0042 0.0110  674 ARG D NE  
13238 C CZ  . ARG D 373 ? 0.6170 0.5178 0.5586 -0.0449 -0.0072 0.0139  674 ARG D CZ  
13239 N NH1 . ARG D 373 ? 0.7260 0.6361 0.6751 -0.0365 -0.0094 0.0136  674 ARG D NH1 
13240 N NH2 . ARG D 373 ? 0.6388 0.5540 0.5891 -0.0484 -0.0077 0.0168  674 ARG D NH2 
13241 N N   . GLY D 374 ? 0.7662 0.5593 0.6189 -0.0699 0.0043  -0.0159 675 GLY D N   
13242 C CA  . GLY D 374 ? 0.8491 0.6574 0.7033 -0.0838 0.0027  -0.0197 675 GLY D CA  
13243 C C   . GLY D 374 ? 0.8104 0.6545 0.6860 -0.0806 -0.0016 -0.0174 675 GLY D C   
13244 O O   . GLY D 374 ? 0.7890 0.6521 0.6694 -0.0922 -0.0041 -0.0185 675 GLY D O   
13245 N N   . GLY D 375 ? 0.7287 0.5824 0.6160 -0.0657 -0.0028 -0.0141 676 GLY D N   
13246 C CA  . GLY D 375 ? 0.7829 0.6662 0.6876 -0.0626 -0.0067 -0.0117 676 GLY D CA  
13247 C C   . GLY D 375 ? 0.7372 0.6302 0.6556 -0.0498 -0.0080 -0.0060 676 GLY D C   
13248 O O   . GLY D 375 ? 0.7772 0.6563 0.6925 -0.0430 -0.0060 -0.0041 676 GLY D O   
13249 N N   . CYS D 376 ? 0.5975 0.5140 0.5297 -0.0471 -0.0114 -0.0033 677 CYS D N   
13250 C CA  . CYS D 376 ? 0.5890 0.5161 0.5337 -0.0367 -0.0130 0.0016  677 CYS D CA  
13251 C C   . CYS D 376 ? 0.6774 0.6280 0.6340 -0.0381 -0.0173 0.0045  677 CYS D C   
13252 O O   . CYS D 376 ? 0.7378 0.6942 0.6934 -0.0372 -0.0180 0.0030  677 CYS D O   
13253 C CB  . CYS D 376 ? 0.5380 0.4555 0.4786 -0.0253 -0.0107 -0.0001 677 CYS D CB  
13254 S SG  . CYS D 376 ? 0.6334 0.5674 0.5886 -0.0153 -0.0129 0.0050  677 CYS D SG  
13255 N N   . PRO D 377 ? 0.5923 0.5562 0.5590 -0.0399 -0.0201 0.0087  678 PRO D N   
13256 C CA  . PRO D 377 ? 0.5765 0.5598 0.5524 -0.0398 -0.0245 0.0119  678 PRO D CA  
13257 C C   . PRO D 377 ? 0.6294 0.6153 0.6097 -0.0311 -0.0253 0.0145  678 PRO D C   
13258 O O   . PRO D 377 ? 0.6642 0.6457 0.6478 -0.0244 -0.0241 0.0163  678 PRO D O   
13259 C CB  . PRO D 377 ? 0.6419 0.6362 0.6267 -0.0413 -0.0265 0.0153  678 PRO D CB  
13260 C CG  . PRO D 377 ? 0.5240 0.5051 0.5068 -0.0387 -0.0229 0.0154  678 PRO D CG  
13261 C CD  . PRO D 377 ? 0.5619 0.5235 0.5311 -0.0416 -0.0192 0.0108  678 PRO D CD  
13262 N N   . ALA D 378 ? 0.6689 0.6629 0.6484 -0.0323 -0.0274 0.0146  679 ALA D N   
13263 C CA  . ALA D 378 ? 0.5471 0.5441 0.5287 -0.0267 -0.0278 0.0166  679 ALA D CA  
13264 C C   . ALA D 378 ? 0.5504 0.5594 0.5340 -0.0292 -0.0322 0.0202  679 ALA D C   
13265 O O   . ALA D 378 ? 0.5188 0.5341 0.4998 -0.0351 -0.0344 0.0196  679 ALA D O   
13266 C CB  . ALA D 378 ? 0.4598 0.4502 0.4340 -0.0248 -0.0240 0.0120  679 ALA D CB  
13267 N N   . ASP D 379 ? 0.5083 0.5199 0.4951 -0.0251 -0.0336 0.0241  680 ASP D N   
13268 C CA  . ASP D 379 ? 0.4917 0.5105 0.4791 -0.0260 -0.0381 0.0290  680 ASP D CA  
13269 C C   . ASP D 379 ? 0.6011 0.6204 0.5834 -0.0270 -0.0370 0.0291  680 ASP D C   
13270 O O   . ASP D 379 ? 0.6308 0.6481 0.6148 -0.0242 -0.0364 0.0311  680 ASP D O   
13271 C CB  . ASP D 379 ? 0.5035 0.5218 0.4976 -0.0208 -0.0405 0.0336  680 ASP D CB  
13272 C CG  . ASP D 379 ? 0.5338 0.5559 0.5268 -0.0201 -0.0456 0.0391  680 ASP D CG  
13273 O OD1 . ASP D 379 ? 0.5761 0.6005 0.5739 -0.0161 -0.0483 0.0417  680 ASP D OD1 
13274 O OD2 . ASP D 379 ? 0.6235 0.6459 0.6100 -0.0230 -0.0468 0.0408  680 ASP D OD2 
13275 N N   . TRP D 380 ? 0.6669 0.6897 0.6424 -0.0319 -0.0364 0.0264  681 TRP D N   
13276 C CA  . TRP D 380 ? 0.4399 0.4661 0.4095 -0.0344 -0.0348 0.0258  681 TRP D CA  
13277 C C   . TRP D 380 ? 0.3444 0.3714 0.3138 -0.0344 -0.0374 0.0319  681 TRP D C   
13278 O O   . TRP D 380 ? 0.4333 0.4622 0.4012 -0.0351 -0.0349 0.0315  681 TRP D O   
13279 C CB  . TRP D 380 ? 0.5078 0.5391 0.4696 -0.0407 -0.0358 0.0238  681 TRP D CB  
13280 C CG  . TRP D 380 ? 0.4222 0.4576 0.3768 -0.0437 -0.0324 0.0207  681 TRP D CG  
13281 C CD1 . TRP D 380 ? 0.3817 0.4163 0.3322 -0.0433 -0.0274 0.0133  681 TRP D CD1 
13282 C CD2 . TRP D 380 ? 0.3525 0.3935 0.3025 -0.0473 -0.0334 0.0246  681 TRP D CD2 
13283 N NE1 . TRP D 380 ? 0.4922 0.5345 0.4374 -0.0459 -0.0250 0.0120  681 TRP D NE1 
13284 C CE2 . TRP D 380 ? 0.3861 0.4326 0.3306 -0.0494 -0.0286 0.0191  681 TRP D CE2 
13285 C CE3 . TRP D 380 ? 0.3412 0.3815 0.2896 -0.0490 -0.0378 0.0323  681 TRP D CE3 
13286 C CZ2 . TRP D 380 ? 0.4048 0.4590 0.3433 -0.0544 -0.0278 0.0210  681 TRP D CZ2 
13287 C CZ3 . TRP D 380 ? 0.4274 0.4718 0.3681 -0.0544 -0.0372 0.0346  681 TRP D CZ3 
13288 C CH2 . TRP D 380 ? 0.4354 0.4880 0.3717 -0.0578 -0.0321 0.0291  681 TRP D CH2 
13289 N N   . VAL D 381 ? 0.3971 0.4229 0.3671 -0.0339 -0.0425 0.0375  682 VAL D N   
13290 C CA  . VAL D 381 ? 0.3533 0.3753 0.3197 -0.0342 -0.0454 0.0437  682 VAL D CA  
13291 C C   . VAL D 381 ? 0.5462 0.5630 0.5167 -0.0312 -0.0431 0.0438  682 VAL D C   
13292 O O   . VAL D 381 ? 0.6207 0.6340 0.5863 -0.0339 -0.0435 0.0470  682 VAL D O   
13293 C CB  . VAL D 381 ? 0.3576 0.3779 0.3240 -0.0313 -0.0514 0.0492  682 VAL D CB  
13294 C CG1 . VAL D 381 ? 0.3908 0.4018 0.3514 -0.0302 -0.0544 0.0557  682 VAL D CG1 
13295 C CG2 . VAL D 381 ? 0.4690 0.4972 0.4306 -0.0351 -0.0543 0.0495  682 VAL D CG2 
13296 N N   . TRP D 382 ? 0.6294 0.6453 0.6078 -0.0264 -0.0408 0.0403  683 TRP D N   
13297 C CA  . TRP D 382 ? 0.5810 0.5934 0.5636 -0.0231 -0.0388 0.0398  683 TRP D CA  
13298 C C   . TRP D 382 ? 0.6165 0.6338 0.6011 -0.0224 -0.0339 0.0345  683 TRP D C   
13299 O O   . TRP D 382 ? 0.5979 0.6173 0.5833 -0.0224 -0.0324 0.0344  683 TRP D O   
13300 C CB  . TRP D 382 ? 0.5770 0.5848 0.5663 -0.0174 -0.0399 0.0404  683 TRP D CB  
13301 C CG  . TRP D 382 ? 0.6545 0.6571 0.6427 -0.0154 -0.0442 0.0455  683 TRP D CG  
13302 C CD1 . TRP D 382 ? 0.6710 0.6746 0.6558 -0.0157 -0.0483 0.0490  683 TRP D CD1 
13303 C CD2 . TRP D 382 ? 0.6967 0.6917 0.6859 -0.0118 -0.0450 0.0476  683 TRP D CD2 
13304 N NE1 . TRP D 382 ? 0.6684 0.6645 0.6520 -0.0112 -0.0516 0.0533  683 TRP D NE1 
13305 C CE2 . TRP D 382 ? 0.6783 0.6681 0.6642 -0.0091 -0.0494 0.0522  683 TRP D CE2 
13306 C CE3 . TRP D 382 ? 0.6074 0.5993 0.5992 -0.0102 -0.0425 0.0459  683 TRP D CE3 
13307 C CZ2 . TRP D 382 ? 0.7178 0.6975 0.7022 -0.0047 -0.0510 0.0546  683 TRP D CZ2 
13308 C CZ3 . TRP D 382 ? 0.6308 0.6139 0.6214 -0.0073 -0.0442 0.0482  683 TRP D CZ3 
13309 C CH2 . TRP D 382 ? 0.7072 0.6832 0.6936 -0.0045 -0.0481 0.0523  683 TRP D CH2 
13310 N N   . ILE D 383 ? 0.4670 0.4862 0.4513 -0.0216 -0.0315 0.0299  684 ILE D N   
13311 C CA  . ILE D 383 ? 0.3532 0.3756 0.3381 -0.0186 -0.0269 0.0247  684 ILE D CA  
13312 C C   . ILE D 383 ? 0.4094 0.4418 0.3909 -0.0221 -0.0251 0.0237  684 ILE D C   
13313 O O   . ILE D 383 ? 0.5353 0.5743 0.5195 -0.0190 -0.0223 0.0212  684 ILE D O   
13314 C CB  . ILE D 383 ? 0.2899 0.3083 0.2719 -0.0174 -0.0248 0.0198  684 ILE D CB  
13315 C CG1 . ILE D 383 ? 0.3512 0.3611 0.3363 -0.0155 -0.0260 0.0205  684 ILE D CG1 
13316 C CG2 . ILE D 383 ? 0.2810 0.3004 0.2622 -0.0120 -0.0202 0.0144  684 ILE D CG2 
13317 C CD1 . ILE D 383 ? 0.4210 0.4279 0.4119 -0.0104 -0.0260 0.0226  684 ILE D CD1 
13318 N N   . VAL D 384 ? 0.4831 0.5186 0.4585 -0.0287 -0.0266 0.0257  685 VAL D N   
13319 C CA  . VAL D 384 ? 0.4723 0.5188 0.4433 -0.0336 -0.0242 0.0245  685 VAL D CA  
13320 C C   . VAL D 384 ? 0.5098 0.5592 0.4820 -0.0365 -0.0249 0.0282  685 VAL D C   
13321 O O   . VAL D 384 ? 0.5376 0.5776 0.5084 -0.0384 -0.0288 0.0336  685 VAL D O   
13322 C CB  . VAL D 384 ? 0.4721 0.5198 0.4344 -0.0406 -0.0260 0.0263  685 VAL D CB  
13323 C CG1 . VAL D 384 ? 0.3106 0.3708 0.2673 -0.0466 -0.0228 0.0246  685 VAL D CG1 
13324 C CG2 . VAL D 384 ? 0.5667 0.6118 0.5275 -0.0386 -0.0253 0.0219  685 VAL D CG2 
13325 N N   . PRO D 385 ? 0.4720 0.5342 0.4463 -0.0367 -0.0213 0.0249  686 PRO D N   
13326 C CA  . PRO D 385 ? 0.4042 0.4702 0.3791 -0.0413 -0.0219 0.0278  686 PRO D CA  
13327 C C   . PRO D 385 ? 0.5381 0.6002 0.5030 -0.0521 -0.0242 0.0332  686 PRO D C   
13328 O O   . PRO D 385 ? 0.7129 0.7776 0.6711 -0.0567 -0.0238 0.0335  686 PRO D O   
13329 C CB  . PRO D 385 ? 0.4607 0.5467 0.4397 -0.0398 -0.0172 0.0223  686 PRO D CB  
13330 C CG  . PRO D 385 ? 0.4439 0.5298 0.4266 -0.0295 -0.0148 0.0168  686 PRO D CG  
13331 C CD  . PRO D 385 ? 0.5237 0.5965 0.5011 -0.0306 -0.0167 0.0180  686 PRO D CD  
13332 N N   . PRO D 386 ? 0.5890 0.6439 0.5510 -0.0570 -0.0264 0.0376  687 PRO D N   
13333 C CA  . PRO D 386 ? 0.5106 0.5558 0.4602 -0.0669 -0.0291 0.0438  687 PRO D CA  
13334 C C   . PRO D 386 ? 0.6102 0.6691 0.5526 -0.0785 -0.0260 0.0434  687 PRO D C   
13335 O O   . PRO D 386 ? 0.7101 0.7597 0.6404 -0.0887 -0.0278 0.0488  687 PRO D O   
13336 C CB  . PRO D 386 ? 0.5107 0.5408 0.4587 -0.0671 -0.0321 0.0475  687 PRO D CB  
13337 C CG  . PRO D 386 ? 0.3872 0.4298 0.3456 -0.0636 -0.0292 0.0425  687 PRO D CG  
13338 C CD  . PRO D 386 ? 0.4339 0.4890 0.4020 -0.0544 -0.0263 0.0369  687 PRO D CD  
13339 N N   . MET D 387 ? 0.5125 0.5931 0.4613 -0.0772 -0.0212 0.0371  688 MET D N   
13340 C CA  . MET D 387 ? 0.4790 0.5780 0.4228 -0.0877 -0.0174 0.0355  688 MET D CA  
13341 C C   . MET D 387 ? 0.5404 0.6595 0.4919 -0.0805 -0.0126 0.0278  688 MET D C   
13342 O O   . MET D 387 ? 0.5033 0.6230 0.4647 -0.0684 -0.0121 0.0237  688 MET D O   
13343 C CB  . MET D 387 ? 0.5947 0.7036 0.5396 -0.0955 -0.0161 0.0355  688 MET D CB  
13344 C CG  . MET D 387 ? 0.6424 0.7680 0.6019 -0.0860 -0.0138 0.0295  688 MET D CG  
13345 S SD  . MET D 387 ? 0.6248 0.7776 0.5867 -0.0968 -0.0105 0.0269  688 MET D SD  
13346 C CE  . MET D 387 ? 0.6592 0.8399 0.6186 -0.1034 -0.0048 0.0227  688 MET D CE  
13347 N N   . SER D 388 ? 0.5626 0.6962 0.5080 -0.0877 -0.0092 0.0260  689 SER D N   
13348 C CA  . SER D 388 ? 0.5139 0.6661 0.4644 -0.0805 -0.0042 0.0180  689 SER D CA  
13349 C C   . SER D 388 ? 0.5346 0.6730 0.4881 -0.0683 -0.0054 0.0152  689 SER D C   
13350 O O   . SER D 388 ? 0.6337 0.7797 0.5940 -0.0575 -0.0022 0.0084  689 SER D O   
13351 C CB  . SER D 388 ? 0.4891 0.6647 0.4507 -0.0754 -0.0002 0.0122  689 SER D CB  
13352 O OG  . SER D 388 ? 0.5620 0.7546 0.5207 -0.0886 0.0015  0.0137  689 SER D OG  
13353 N N   . GLY D 389 ? 0.4785 0.5962 0.4257 -0.0701 -0.0102 0.0206  690 GLY D N   
13354 C CA  . GLY D 389 ? 0.4635 0.5684 0.4127 -0.0614 -0.0118 0.0186  690 GLY D CA  
13355 C C   . GLY D 389 ? 0.6903 0.8029 0.6383 -0.0564 -0.0075 0.0107  690 GLY D C   
13356 O O   . GLY D 389 ? 0.7935 0.9018 0.7472 -0.0460 -0.0060 0.0058  690 GLY D O   
13357 N N   . SER D 390 ? 0.5249 0.6468 0.4640 -0.0637 -0.0053 0.0093  691 SER D N   
13358 C CA  . SER D 390 ? 0.6192 0.7444 0.5548 -0.0593 -0.0016 0.0016  691 SER D CA  
13359 C C   . SER D 390 ? 0.5525 0.6941 0.4935 -0.0509 0.0049  -0.0072 691 SER D C   
13360 O O   . SER D 390 ? 0.5341 0.6744 0.4719 -0.0445 0.0083  -0.0145 691 SER D O   
13361 C CB  . SER D 390 ? 0.6942 0.8238 0.6172 -0.0697 -0.0014 0.0026  691 SER D CB  
13362 O OG  . SER D 390 ? 0.5913 0.7416 0.5110 -0.0763 0.0033  0.0006  691 SER D OG  
13363 N N   . ILE D 391 ? 0.5478 0.7049 0.4962 -0.0503 0.0068  -0.0069 692 ILE D N   
13364 C CA  . ILE D 391 ? 0.5737 0.7475 0.5290 -0.0393 0.0121  -0.0149 692 ILE D CA  
13365 C C   . ILE D 391 ? 0.5302 0.6926 0.4940 -0.0259 0.0107  -0.0160 692 ILE D C   
13366 O O   . ILE D 391 ? 0.5144 0.6893 0.4839 -0.0148 0.0143  -0.0217 692 ILE D O   
13367 C CB  . ILE D 391 ? 0.5734 0.7755 0.5328 -0.0453 0.0152  -0.0151 692 ILE D CB  
13368 C CG1 . ILE D 391 ? 0.4744 0.6757 0.4416 -0.0471 0.0116  -0.0094 692 ILE D CG1 
13369 C CG2 . ILE D 391 ? 0.4891 0.6994 0.4384 -0.0612 0.0160  -0.0120 692 ILE D CG2 
13370 C CD1 . ILE D 391 ? 0.5148 0.7443 0.4848 -0.0559 0.0144  -0.0095 692 ILE D CD1 
13371 N N   . THR D 392 ? 0.5366 0.6762 0.5008 -0.0262 0.0054  -0.0104 693 THR D N   
13372 C CA  . THR D 392 ? 0.5672 0.6924 0.5366 -0.0144 0.0043  -0.0116 693 THR D CA  
13373 C C   . THR D 392 ? 0.5687 0.6734 0.5309 -0.0115 0.0040  -0.0143 693 THR D C   
13374 O O   . THR D 392 ? 0.6681 0.7663 0.6236 -0.0203 0.0020  -0.0121 693 THR D O   
13375 C CB  . THR D 392 ? 0.5796 0.6950 0.5544 -0.0169 -0.0007 -0.0042 693 THR D CB  
13376 O OG1 . THR D 392 ? 0.5732 0.6737 0.5428 -0.0252 -0.0049 0.0012  693 THR D OG1 
13377 C CG2 . THR D 392 ? 0.4731 0.6064 0.4529 -0.0226 -0.0008 -0.0013 693 THR D CG2 
13378 N N   . PRO D 393 ? 0.5379 0.6316 0.5002 0.0003  0.0058  -0.0190 694 PRO D N   
13379 C CA  . PRO D 393 ? 0.5849 0.6591 0.5377 0.0017  0.0065  -0.0231 694 PRO D CA  
13380 C C   . PRO D 393 ? 0.5828 0.6402 0.5337 -0.0062 0.0015  -0.0176 694 PRO D C   
13381 O O   . PRO D 393 ? 0.5890 0.6363 0.5314 -0.0103 0.0016  -0.0204 694 PRO D O   
13382 C CB  . PRO D 393 ? 0.5253 0.5889 0.4778 0.0162  0.0091  -0.0279 694 PRO D CB  
13383 C CG  . PRO D 393 ? 0.6059 0.6777 0.5694 0.0205  0.0070  -0.0230 694 PRO D CG  
13384 C CD  . PRO D 393 ? 0.5875 0.6843 0.5568 0.0124  0.0069  -0.0203 694 PRO D CD  
13385 N N   . VAL D 394 ? 0.5921 0.6472 0.5505 -0.0083 -0.0027 -0.0106 695 VAL D N   
13386 C CA  . VAL D 394 ? 0.5890 0.6306 0.5464 -0.0141 -0.0071 -0.0061 695 VAL D CA  
13387 C C   . VAL D 394 ? 0.5544 0.6008 0.5065 -0.0246 -0.0095 -0.0037 695 VAL D C   
13388 O O   . VAL D 394 ? 0.4900 0.5279 0.4389 -0.0292 -0.0125 -0.0022 695 VAL D O   
13389 C CB  . VAL D 394 ? 0.5645 0.6034 0.5305 -0.0134 -0.0109 0.0007  695 VAL D CB  
13390 C CG1 . VAL D 394 ? 0.5162 0.5459 0.4856 -0.0038 -0.0095 -0.0009 695 VAL D CG1 
13391 C CG2 . VAL D 394 ? 0.4442 0.4972 0.4145 -0.0171 -0.0120 0.0049  695 VAL D CG2 
13392 N N   . PHE D 395 ? 0.4594 0.5205 0.4097 -0.0289 -0.0083 -0.0032 696 PHE D N   
13393 C CA  . PHE D 395 ? 0.5097 0.5748 0.4533 -0.0390 -0.0109 0.0002  696 PHE D CA  
13394 C C   . PHE D 395 ? 0.6106 0.6699 0.5453 -0.0417 -0.0103 -0.0048 696 PHE D C   
13395 O O   . PHE D 395 ? 0.5420 0.5977 0.4730 -0.0480 -0.0147 -0.0012 696 PHE D O   
13396 C CB  . PHE D 395 ? 0.5287 0.6105 0.4700 -0.0438 -0.0084 0.0005  696 PHE D CB  
13397 C CG  . PHE D 395 ? 0.5732 0.6578 0.5061 -0.0544 -0.0114 0.0053  696 PHE D CG  
13398 C CD1 . PHE D 395 ? 0.5654 0.6477 0.4984 -0.0598 -0.0160 0.0140  696 PHE D CD1 
13399 C CD2 . PHE D 395 ? 0.6562 0.7443 0.5794 -0.0588 -0.0098 0.0012  696 PHE D CD2 
13400 C CE1 . PHE D 395 ? 0.6021 0.6846 0.5253 -0.0687 -0.0192 0.0192  696 PHE D CE1 
13401 C CE2 . PHE D 395 ? 0.5526 0.6432 0.4669 -0.0683 -0.0131 0.0062  696 PHE D CE2 
13402 C CZ  . PHE D 395 ? 0.6020 0.6897 0.5161 -0.0730 -0.0179 0.0156  696 PHE D CZ  
13403 N N   . HIS D 396 ? 0.5729 0.6310 0.5034 -0.0364 -0.0050 -0.0133 697 HIS D N   
13404 C CA  . HIS D 396 ? 0.5460 0.5977 0.4659 -0.0393 -0.0034 -0.0196 697 HIS D CA  
13405 C C   . HIS D 396 ? 0.6477 0.6805 0.5659 -0.0368 -0.0042 -0.0221 697 HIS D C   
13406 O O   . HIS D 396 ? 0.6467 0.6707 0.5546 -0.0388 -0.0021 -0.0287 697 HIS D O   
13407 C CB  . HIS D 396 ? 0.5567 0.6156 0.4710 -0.0344 0.0033  -0.0282 697 HIS D CB  
13408 C CG  . HIS D 396 ? 0.5576 0.6371 0.4762 -0.0354 0.0052  -0.0261 697 HIS D CG  
13409 N ND1 . HIS D 396 ? 0.5510 0.6436 0.4633 -0.0451 0.0052  -0.0246 697 HIS D ND1 
13410 C CD2 . HIS D 396 ? 0.5918 0.6817 0.5199 -0.0296 0.0066  -0.0245 697 HIS D CD2 
13411 C CE1 . HIS D 396 ? 0.6184 0.7279 0.5357 -0.0458 0.0071  -0.0225 697 HIS D CE1 
13412 N NE2 . HIS D 396 ? 0.6055 0.7148 0.5329 -0.0366 0.0079  -0.0226 697 HIS D NE2 
13413 N N   . GLN D 397 ? 0.5676 0.5938 0.4946 -0.0333 -0.0069 -0.0171 698 GLN D N   
13414 C CA  . GLN D 397 ? 0.5491 0.5581 0.4749 -0.0317 -0.0074 -0.0186 698 GLN D CA  
13415 C C   . GLN D 397 ? 0.5584 0.5677 0.4865 -0.0401 -0.0132 -0.0131 698 GLN D C   
13416 O O   . GLN D 397 ? 0.6091 0.6255 0.5458 -0.0406 -0.0172 -0.0057 698 GLN D O   
13417 C CB  . GLN D 397 ? 0.4961 0.4991 0.4298 -0.0221 -0.0064 -0.0169 698 GLN D CB  
13418 C CG  . GLN D 397 ? 0.5145 0.5000 0.4465 -0.0221 -0.0072 -0.0170 698 GLN D CG  
13419 C CD  . GLN D 397 ? 0.6126 0.5808 0.5311 -0.0213 -0.0032 -0.0251 698 GLN D CD  
13420 O OE1 . GLN D 397 ? 0.5927 0.5560 0.5062 -0.0124 0.0012  -0.0304 698 GLN D OE1 
13421 N NE2 . GLN D 397 ? 0.6379 0.5969 0.5498 -0.0306 -0.0048 -0.0263 698 GLN D NE2 
13422 N N   . GLU D 398 ? 0.5676 0.5696 0.4874 -0.0466 -0.0136 -0.0169 699 GLU D N   
13423 C CA  . GLU D 398 ? 0.5994 0.6044 0.5222 -0.0539 -0.0190 -0.0125 699 GLU D CA  
13424 C C   . GLU D 398 ? 0.6069 0.6031 0.5369 -0.0504 -0.0195 -0.0099 699 GLU D C   
13425 O O   . GLU D 398 ? 0.5236 0.5048 0.4497 -0.0462 -0.0155 -0.0142 699 GLU D O   
13426 C CB  . GLU D 398 ? 0.5776 0.5793 0.4889 -0.0633 -0.0191 -0.0181 699 GLU D CB  
13427 C CG  . GLU D 398 ? 0.4757 0.4919 0.3824 -0.0703 -0.0221 -0.0168 699 GLU D CG  
13428 C CD  . GLU D 398 ? 0.5950 0.6075 0.4884 -0.0796 -0.0215 -0.0240 699 GLU D CD  
13429 O OE1 . GLU D 398 ? 0.6533 0.6770 0.5405 -0.0857 -0.0235 -0.0240 699 GLU D OE1 
13430 O OE2 . GLU D 398 ? 0.5907 0.5881 0.4783 -0.0816 -0.0188 -0.0296 699 GLU D OE2 
13431 N N   . MET D 399 ? 0.6237 0.6287 0.5632 -0.0515 -0.0244 -0.0029 700 MET D N   
13432 C CA  . MET D 399 ? 0.6299 0.6298 0.5771 -0.0484 -0.0250 0.0000  700 MET D CA  
13433 C C   . MET D 399 ? 0.6545 0.6635 0.6060 -0.0548 -0.0298 0.0033  700 MET D C   
13434 O O   . MET D 399 ? 0.8281 0.8504 0.7828 -0.0563 -0.0345 0.0079  700 MET D O   
13435 C CB  . MET D 399 ? 0.5083 0.5111 0.4650 -0.0402 -0.0256 0.0053  700 MET D CB  
13436 C CG  . MET D 399 ? 0.5720 0.5721 0.5271 -0.0336 -0.0215 0.0028  700 MET D CG  
13437 S SD  . MET D 399 ? 0.6585 0.6688 0.6229 -0.0295 -0.0239 0.0097  700 MET D SD  
13438 C CE  . MET D 399 ? 0.4107 0.4228 0.3733 -0.0231 -0.0187 0.0054  700 MET D CE  
13439 N N   . LEU D 400 ? 0.6033 0.6055 0.5541 -0.0582 -0.0287 0.0013  701 LEU D N   
13440 C CA  . LEU D 400 ? 0.6491 0.6629 0.6060 -0.0635 -0.0327 0.0041  701 LEU D CA  
13441 C C   . LEU D 400 ? 0.6674 0.6844 0.6360 -0.0564 -0.0338 0.0096  701 LEU D C   
13442 O O   . LEU D 400 ? 0.4414 0.4462 0.4107 -0.0508 -0.0303 0.0093  701 LEU D O   
13443 C CB  . LEU D 400 ? 0.5542 0.5600 0.5034 -0.0731 -0.0304 -0.0013 701 LEU D CB  
13444 C CG  . LEU D 400 ? 0.6015 0.6054 0.5382 -0.0825 -0.0299 -0.0073 701 LEU D CG  
13445 C CD1 . LEU D 400 ? 0.6671 0.6579 0.5945 -0.0921 -0.0269 -0.0126 701 LEU D CD1 
13446 C CD2 . LEU D 400 ? 0.6028 0.6295 0.5433 -0.0876 -0.0359 -0.0044 701 LEU D CD2 
13447 N N   . ASN D 401 ? 0.6355 0.6689 0.6124 -0.0559 -0.0388 0.0145  702 ASN D N   
13448 C CA  . ASN D 401 ? 0.6454 0.6828 0.6327 -0.0484 -0.0403 0.0195  702 ASN D CA  
13449 C C   . ASN D 401 ? 0.6563 0.7058 0.6497 -0.0523 -0.0419 0.0198  702 ASN D C   
13450 O O   . ASN D 401 ? 0.6295 0.6940 0.6232 -0.0581 -0.0454 0.0196  702 ASN D O   
13451 C CB  . ASN D 401 ? 0.5601 0.6047 0.5509 -0.0422 -0.0446 0.0251  702 ASN D CB  
13452 C CG  . ASN D 401 ? 0.5503 0.5920 0.5485 -0.0335 -0.0447 0.0292  702 ASN D CG  
13453 O OD1 . ASN D 401 ? 0.6621 0.6951 0.6621 -0.0313 -0.0410 0.0276  702 ASN D OD1 
13454 N ND2 . ASN D 401 ? 0.5446 0.5923 0.5458 -0.0285 -0.0492 0.0344  702 ASN D ND2 
13455 N N   . TYR D 402 ? 0.5479 0.5930 0.5461 -0.0494 -0.0393 0.0203  703 TYR D N   
13456 C CA  . TYR D 402 ? 0.5360 0.5942 0.5407 -0.0532 -0.0399 0.0204  703 TYR D CA  
13457 C C   . TYR D 402 ? 0.6624 0.7136 0.6718 -0.0471 -0.0370 0.0220  703 TYR D C   
13458 O O   . TYR D 402 ? 0.6513 0.6857 0.6571 -0.0423 -0.0341 0.0219  703 TYR D O   
13459 C CB  . TYR D 402 ? 0.5082 0.5658 0.5056 -0.0664 -0.0377 0.0153  703 TYR D CB  
13460 C CG  . TYR D 402 ? 0.5661 0.5983 0.5509 -0.0699 -0.0324 0.0110  703 TYR D CG  
13461 C CD1 . TYR D 402 ? 0.6601 0.6785 0.6421 -0.0706 -0.0281 0.0102  703 TYR D CD1 
13462 C CD2 . TYR D 402 ? 0.6308 0.6529 0.6056 -0.0721 -0.0317 0.0077  703 TYR D CD2 
13463 C CE1 . TYR D 402 ? 0.6660 0.6592 0.6348 -0.0721 -0.0236 0.0067  703 TYR D CE1 
13464 C CE2 . TYR D 402 ? 0.6953 0.6936 0.6578 -0.0733 -0.0268 0.0033  703 TYR D CE2 
13465 C CZ  . TYR D 402 ? 0.7081 0.6912 0.6674 -0.0728 -0.0230 0.0031  703 TYR D CZ  
13466 O OH  . TYR D 402 ? 0.6480 0.6057 0.5937 -0.0723 -0.0185 -0.0009 703 TYR D OH  
13467 N N   . ARG D 403 ? 0.6767 0.7432 0.6945 -0.0472 -0.0378 0.0232  704 ARG D N   
13468 C CA  . ARG D 403 ? 0.6008 0.6656 0.6247 -0.0399 -0.0361 0.0253  704 ARG D CA  
13469 C C   . ARG D 403 ? 0.6276 0.6897 0.6492 -0.0478 -0.0316 0.0228  704 ARG D C   
13470 O O   . ARG D 403 ? 0.6052 0.6854 0.6318 -0.0537 -0.0319 0.0220  704 ARG D O   
13471 C CB  . ARG D 403 ? 0.6170 0.7013 0.6516 -0.0320 -0.0403 0.0287  704 ARG D CB  
13472 C CG  . ARG D 403 ? 0.7649 0.8463 0.8048 -0.0232 -0.0387 0.0305  704 ARG D CG  
13473 C CD  . ARG D 403 ? 0.9114 0.9989 0.9564 -0.0118 -0.0431 0.0342  704 ARG D CD  
13474 N NE  . ARG D 403 ? 1.0333 1.1418 1.0877 -0.0073 -0.0445 0.0346  704 ARG D NE  
13475 C CZ  . ARG D 403 ? 1.1111 1.2270 1.1698 0.0037  -0.0486 0.0375  704 ARG D CZ  
13476 N NH1 . ARG D 403 ? 1.1599 1.2621 1.2131 0.0096  -0.0517 0.0407  704 ARG D NH1 
13477 N NH2 . ARG D 403 ? 1.0007 1.1376 1.0683 0.0089  -0.0495 0.0373  704 ARG D NH2 
13478 N N   . LEU D 404 ? 0.5072 0.5472 0.5204 -0.0482 -0.0275 0.0217  705 LEU D N   
13479 C CA  . LEU D 404 ? 0.5830 0.6148 0.5915 -0.0541 -0.0230 0.0205  705 LEU D CA  
13480 C C   . LEU D 404 ? 0.5833 0.6183 0.5988 -0.0461 -0.0220 0.0233  705 LEU D C   
13481 O O   . LEU D 404 ? 0.5487 0.5808 0.5682 -0.0355 -0.0236 0.0256  705 LEU D O   
13482 C CB  . LEU D 404 ? 0.5588 0.5634 0.5534 -0.0560 -0.0195 0.0186  705 LEU D CB  
13483 C CG  . LEU D 404 ? 0.5444 0.5386 0.5289 -0.0616 -0.0194 0.0151  705 LEU D CG  
13484 C CD1 . LEU D 404 ? 0.4775 0.4461 0.4516 -0.0558 -0.0165 0.0143  705 LEU D CD1 
13485 C CD2 . LEU D 404 ? 0.5364 0.5313 0.5134 -0.0766 -0.0178 0.0118  705 LEU D CD2 
13486 N N   . THR D 405 ? 0.6012 0.6412 0.6168 -0.0522 -0.0190 0.0229  706 THR D N   
13487 C CA  . THR D 405 ? 0.5782 0.6192 0.5982 -0.0457 -0.0172 0.0249  706 THR D CA  
13488 C C   . THR D 405 ? 0.6193 0.6399 0.6276 -0.0507 -0.0125 0.0248  706 THR D C   
13489 O O   . THR D 405 ? 0.6718 0.6839 0.6702 -0.0622 -0.0101 0.0230  706 THR D O   
13490 C CB  . THR D 405 ? 0.5606 0.6291 0.5920 -0.0464 -0.0178 0.0248  706 THR D CB  
13491 O OG1 . THR D 405 ? 0.7213 0.7928 0.7590 -0.0355 -0.0176 0.0266  706 THR D OG1 
13492 C CG2 . THR D 405 ? 0.3602 0.4352 0.3877 -0.0603 -0.0139 0.0230  706 THR D CG2 
13493 N N   . PRO D 406 ? 0.6250 0.6361 0.6325 -0.0428 -0.0111 0.0269  707 PRO D N   
13494 C CA  . PRO D 406 ? 0.5676 0.5851 0.5838 -0.0308 -0.0130 0.0287  707 PRO D CA  
13495 C C   . PRO D 406 ? 0.5692 0.5843 0.5884 -0.0232 -0.0169 0.0292  707 PRO D C   
13496 O O   . PRO D 406 ? 0.5650 0.5686 0.5776 -0.0252 -0.0172 0.0283  707 PRO D O   
13497 C CB  . PRO D 406 ? 0.5332 0.5342 0.5420 -0.0278 -0.0102 0.0302  707 PRO D CB  
13498 C CG  . PRO D 406 ? 0.4729 0.4638 0.4708 -0.0387 -0.0064 0.0298  707 PRO D CG  
13499 C CD  . PRO D 406 ? 0.5394 0.5286 0.5336 -0.0465 -0.0073 0.0276  707 PRO D CD  
13500 N N   . SER D 407 ? 0.5133 0.5381 0.5408 -0.0148 -0.0194 0.0304  708 SER D N   
13501 C CA  . SER D 407 ? 0.6591 0.6816 0.6881 -0.0090 -0.0231 0.0313  708 SER D CA  
13502 C C   . SER D 407 ? 0.5276 0.5510 0.5608 0.0001  -0.0244 0.0328  708 SER D C   
13503 O O   . SER D 407 ? 0.6070 0.6381 0.6444 0.0028  -0.0233 0.0327  708 SER D O   
13504 C CB  . SER D 407 ? 0.8386 0.8746 0.8717 -0.0117 -0.0263 0.0310  708 SER D CB  
13505 O OG  . SER D 407 ? 0.8785 0.9329 0.9201 -0.0091 -0.0276 0.0313  708 SER D OG  
13506 N N   . PHE D 408 ? 0.5240 0.5391 0.5551 0.0043  -0.0266 0.0338  709 PHE D N   
13507 C CA  . PHE D 408 ? 0.4145 0.4283 0.4475 0.0115  -0.0286 0.0351  709 PHE D CA  
13508 C C   . PHE D 408 ? 0.5172 0.5392 0.5536 0.0142  -0.0325 0.0364  709 PHE D C   
13509 O O   . PHE D 408 ? 0.7149 0.7382 0.7498 0.0109  -0.0345 0.0370  709 PHE D O   
13510 C CB  . PHE D 408 ? 0.3926 0.3945 0.4207 0.0130  -0.0290 0.0356  709 PHE D CB  
13511 C CG  . PHE D 408 ? 0.3992 0.3942 0.4240 0.0131  -0.0260 0.0349  709 PHE D CG  
13512 C CD1 . PHE D 408 ? 0.4282 0.4169 0.4484 0.0104  -0.0244 0.0342  709 PHE D CD1 
13513 C CD2 . PHE D 408 ? 0.3718 0.3663 0.3971 0.0165  -0.0249 0.0348  709 PHE D CD2 
13514 C CE1 . PHE D 408 ? 0.5915 0.5735 0.6077 0.0118  -0.0222 0.0342  709 PHE D CE1 
13515 C CE2 . PHE D 408 ? 0.3299 0.3187 0.3514 0.0166  -0.0226 0.0346  709 PHE D CE2 
13516 C CZ  . PHE D 408 ? 0.4717 0.4542 0.4886 0.0146  -0.0215 0.0346  709 PHE D CZ  
13517 N N   . GLU D 409 ? 0.5174 0.5444 0.5573 0.0208  -0.0336 0.0369  710 GLU D N   
13518 C CA  . GLU D 409 ? 0.4611 0.4958 0.5037 0.0259  -0.0376 0.0385  710 GLU D CA  
13519 C C   . GLU D 409 ? 0.5235 0.5458 0.5617 0.0334  -0.0395 0.0400  710 GLU D C   
13520 O O   . GLU D 409 ? 0.5627 0.5752 0.5978 0.0346  -0.0374 0.0389  710 GLU D O   
13521 C CB  . GLU D 409 ? 0.5390 0.5927 0.5895 0.0286  -0.0370 0.0373  710 GLU D CB  
13522 C CG  . GLU D 409 ? 0.6666 0.7338 0.7206 0.0193  -0.0349 0.0355  710 GLU D CG  
13523 C CD  . GLU D 409 ? 0.8411 0.9165 0.8955 0.0149  -0.0383 0.0363  710 GLU D CD  
13524 O OE1 . GLU D 409 ? 0.8202 0.8972 0.8745 0.0210  -0.0428 0.0387  710 GLU D OE1 
13525 O OE2 . GLU D 409 ? 0.9090 0.9879 0.9622 0.0050  -0.0365 0.0346  710 GLU D OE2 
13526 N N   . TYR D 410 ? 0.5402 0.5621 0.5765 0.0382  -0.0438 0.0425  711 TYR D N   
13527 C CA  . TYR D 410 ? 0.5300 0.5380 0.5600 0.0458  -0.0459 0.0441  711 TYR D CA  
13528 C C   . TYR D 410 ? 0.6003 0.6158 0.6347 0.0558  -0.0456 0.0426  711 TYR D C   
13529 O O   . TYR D 410 ? 0.6477 0.6827 0.6911 0.0566  -0.0443 0.0409  711 TYR D O   
13530 C CB  . TYR D 410 ? 0.5684 0.5702 0.5922 0.0472  -0.0508 0.0481  711 TYR D CB  
13531 C CG  . TYR D 410 ? 0.6392 0.6330 0.6572 0.0380  -0.0509 0.0493  711 TYR D CG  
13532 C CD1 . TYR D 410 ? 0.7451 0.7497 0.7660 0.0314  -0.0511 0.0493  711 TYR D CD1 
13533 C CD2 . TYR D 410 ? 0.7298 0.7064 0.7390 0.0354  -0.0505 0.0500  711 TYR D CD2 
13534 C CE1 . TYR D 410 ? 0.8365 0.8351 0.8520 0.0239  -0.0507 0.0498  711 TYR D CE1 
13535 C CE2 . TYR D 410 ? 0.7751 0.7480 0.7798 0.0271  -0.0502 0.0508  711 TYR D CE2 
13536 C CZ  . TYR D 410 ? 0.8179 0.8019 0.8260 0.0221  -0.0502 0.0506  711 TYR D CZ  
13537 O OH  . TYR D 410 ? 0.8918 0.8733 0.8954 0.0148  -0.0495 0.0507  711 TYR D OH  
13538 N N   . GLN D 411 ? 0.5996 0.5996 0.6270 0.0632  -0.0465 0.0428  712 GLN D N   
13539 C CA  . GLN D 411 ? 0.6543 0.6596 0.6844 0.0748  -0.0461 0.0410  712 GLN D CA  
13540 C C   . GLN D 411 ? 0.5461 0.5283 0.5640 0.0831  -0.0490 0.0426  712 GLN D C   
13541 O O   . GLN D 411 ? 0.7792 0.7414 0.7869 0.0771  -0.0497 0.0442  712 GLN D O   
13542 C CB  . GLN D 411 ? 0.7255 0.7363 0.7598 0.0737  -0.0408 0.0366  712 GLN D CB  
13543 C CG  . GLN D 411 ? 0.7242 0.7167 0.7507 0.0674  -0.0385 0.0356  712 GLN D CG  
13544 C CD  . GLN D 411 ? 0.6197 0.6168 0.6487 0.0672  -0.0337 0.0317  712 GLN D CD  
13545 O OE1 . GLN D 411 ? 0.4914 0.5047 0.5275 0.0719  -0.0316 0.0295  712 GLN D OE1 
13546 N NE2 . GLN D 411 ? 0.4078 0.3922 0.4306 0.0616  -0.0321 0.0309  712 GLN D NE2 
13547 N N   . PRO D 412 ? 0.4950 0.4792 0.5127 0.0966  -0.0506 0.0422  713 PRO D N   
13548 C CA  . PRO D 412 ? 0.6929 0.6504 0.6961 0.1052  -0.0533 0.0438  713 PRO D CA  
13549 C C   . PRO D 412 ? 0.7330 0.6677 0.7259 0.1010  -0.0502 0.0409  713 PRO D C   
13550 O O   . PRO D 412 ? 0.7411 0.6834 0.7394 0.0975  -0.0457 0.0367  713 PRO D O   
13551 C CB  . PRO D 412 ? 0.6850 0.6535 0.6923 0.1223  -0.0545 0.0424  713 PRO D CB  
13552 C CG  . PRO D 412 ? 0.5859 0.5889 0.6110 0.1203  -0.0510 0.0391  713 PRO D CG  
13553 C CD  . PRO D 412 ? 0.5154 0.5271 0.5456 0.1048  -0.0508 0.0410  713 PRO D CD  
13554 N N   . ASP D 413 ? 0.7904 0.6967 0.7671 0.1000  -0.0528 0.0434  714 ASP D N   
13555 C CA  . ASP D 413 ? 0.7114 0.5938 0.6755 0.0970  -0.0506 0.0405  714 ASP D CA  
13556 C C   . ASP D 413 ? 0.7598 0.6409 0.7235 0.1098  -0.0482 0.0355  714 ASP D C   
13557 O O   . ASP D 413 ? 0.7991 0.6833 0.7636 0.1245  -0.0502 0.0360  714 ASP D O   
13558 C CB  . ASP D 413 ? 0.7434 0.5942 0.6879 0.0947  -0.0542 0.0443  714 ASP D CB  
13559 C CG  . ASP D 413 ? 0.8199 0.6712 0.7630 0.0804  -0.0558 0.0485  714 ASP D CG  
13560 O OD1 . ASP D 413 ? 0.6584 0.5276 0.6124 0.0703  -0.0532 0.0471  714 ASP D OD1 
13561 O OD2 . ASP D 413 ? 0.9741 0.8068 0.9039 0.0795  -0.0595 0.0533  714 ASP D OD2 
13562 N N   . PRO D 414 ? 0.6547 0.5319 0.6167 0.1055  -0.0439 0.0306  715 PRO D N   
13563 C CA  . PRO D 414 ? 0.6476 0.5288 0.6112 0.1171  -0.0407 0.0251  715 PRO D CA  
13564 C C   . PRO D 414 ? 0.8025 0.6565 0.7499 0.1305  -0.0425 0.0239  715 PRO D C   
13565 O O   . PRO D 414 ? 0.8430 0.7044 0.7935 0.1453  -0.0410 0.0203  715 PRO D O   
13566 C CB  . PRO D 414 ? 0.6157 0.4961 0.5783 0.1067  -0.0364 0.0208  715 PRO D CB  
13567 C CG  . PRO D 414 ? 0.6102 0.4933 0.5751 0.0909  -0.0374 0.0243  715 PRO D CG  
13568 C CD  . PRO D 414 ? 0.7265 0.5966 0.6843 0.0904  -0.0421 0.0296  715 PRO D CD  
13569 N N   . TRP D 415 ? 0.8105 0.6330 0.7398 0.1258  -0.0455 0.0267  716 TRP D N   
13570 C CA  . TRP D 415 ? 0.7826 0.5745 0.6934 0.1389  -0.0472 0.0258  716 TRP D CA  
13571 C C   . TRP D 415 ? 0.8738 0.6699 0.7865 0.1549  -0.0516 0.0301  716 TRP D C   
13572 O O   . TRP D 415 ? 0.9124 0.6820 0.8089 0.1684  -0.0537 0.0301  716 TRP D O   
13573 C CB  . TRP D 415 ? 0.8481 0.6026 0.7365 0.1275  -0.0490 0.0277  716 TRP D CB  
13574 C CG  . TRP D 415 ? 0.9408 0.6973 0.8298 0.1144  -0.0522 0.0343  716 TRP D CG  
13575 C CD1 . TRP D 415 ? 0.9989 0.7452 0.8809 0.1180  -0.0571 0.0409  716 TRP D CD1 
13576 C CD2 . TRP D 415 ? 0.9287 0.6990 0.8253 0.0959  -0.0507 0.0349  716 TRP D CD2 
13577 N NE1 . TRP D 415 ? 0.9001 0.6534 0.7849 0.1020  -0.0583 0.0453  716 TRP D NE1 
13578 C CE2 . TRP D 415 ? 0.9061 0.6745 0.8003 0.0889  -0.0544 0.0415  716 TRP D CE2 
13579 C CE3 . TRP D 415 ? 0.8442 0.6286 0.7489 0.0855  -0.0467 0.0306  716 TRP D CE3 
13580 C CZ2 . TRP D 415 ? 0.8122 0.5930 0.7123 0.0724  -0.0537 0.0432  716 TRP D CZ2 
13581 C CZ3 . TRP D 415 ? 0.8794 0.6756 0.7900 0.0700  -0.0466 0.0328  716 TRP D CZ3 
13582 C CH2 . TRP D 415 ? 0.8640 0.6587 0.7725 0.0638  -0.0499 0.0387  716 TRP D CH2 
13583 N N   . ASN D 416 ? 0.9246 0.7523 0.8553 0.1539  -0.0532 0.0337  717 ASN D N   
13584 C CA  . ASN D 416 ? 0.8911 0.7303 0.8264 0.1697  -0.0575 0.0372  717 ASN D CA  
13585 C C   . ASN D 416 ? 0.8911 0.7638 0.8442 0.1829  -0.0548 0.0325  717 ASN D C   
13586 O O   . ASN D 416 ? 1.0569 0.9370 1.0115 0.2008  -0.0578 0.0335  717 ASN D O   
13587 C CB  . ASN D 416 ? 0.8910 0.7453 0.8339 0.1605  -0.0615 0.0439  717 ASN D CB  
13588 C CG  . ASN D 416 ? 0.8381 0.6606 0.7624 0.1492  -0.0647 0.0494  717 ASN D CG  
13589 O OD1 . ASN D 416 ? 0.9190 0.7054 0.8221 0.1532  -0.0661 0.0501  717 ASN D OD1 
13590 N ND2 . ASN D 416 ? 0.6508 0.4863 0.5820 0.1343  -0.0655 0.0529  717 ASN D ND2 
13591 N N   . THR D 417 ? 0.8645 0.7582 0.8302 0.1748  -0.0491 0.0274  718 THR D N   
13592 C CA  . THR D 417 ? 0.7882 0.7168 0.7711 0.1839  -0.0457 0.0228  718 THR D CA  
13593 C C   . THR D 417 ? 0.8277 0.7502 0.8063 0.1902  -0.0401 0.0152  718 THR D C   
13594 O O   . THR D 417 ? 0.9418 0.8838 0.9281 0.2052  -0.0382 0.0111  718 THR D O   
13595 C CB  . THR D 417 ? 0.8206 0.7824 0.8221 0.1689  -0.0433 0.0233  718 THR D CB  
13596 O OG1 . THR D 417 ? 0.8937 0.8434 0.8910 0.1529  -0.0456 0.0281  718 THR D OG1 
13597 C CG2 . THR D 417 ? 0.8191 0.8177 0.8374 0.1765  -0.0451 0.0245  718 THR D CG2 
13598 N N   . HIS D 418 ? 0.7967 0.6949 0.7635 0.1790  -0.0375 0.0129  719 HIS D N   
13599 C CA  . HIS D 418 ? 0.8643 0.7598 0.8276 0.1821  -0.0318 0.0053  719 HIS D CA  
13600 C C   . HIS D 418 ? 0.8541 0.7276 0.8032 0.2021  -0.0321 0.0014  719 HIS D C   
13601 O O   . HIS D 418 ? 0.9434 0.7843 0.8755 0.2075  -0.0365 0.0045  719 HIS D O   
13602 C CB  . HIS D 418 ? 0.8816 0.7564 0.8344 0.1649  -0.0298 0.0039  719 HIS D CB  
13603 C CG  . HIS D 418 ? 0.9172 0.7872 0.8642 0.1671  -0.0244 -0.0038 719 HIS D CG  
13604 N ND1 . HIS D 418 ? 0.8892 0.7876 0.8493 0.1626  -0.0192 -0.0074 719 HIS D ND1 
13605 C CD2 . HIS D 418 ? 0.9235 0.7626 0.8513 0.1728  -0.0231 -0.0089 719 HIS D CD2 
13606 C CE1 . HIS D 418 ? 0.8974 0.7844 0.8476 0.1656  -0.0151 -0.0142 719 HIS D CE1 
13607 N NE2 . HIS D 418 ? 0.9211 0.7720 0.8516 0.1719  -0.0174 -0.0156 719 HIS D NE2 
13608 N N   . VAL D 419 ? 0.8920 0.7826 0.8471 0.2133  -0.0272 -0.0055 720 VAL D N   
13609 C CA  . VAL D 419 ? 0.9603 0.8301 0.9012 0.2330  -0.0261 -0.0111 720 VAL D CA  
13610 C C   . VAL D 419 ? 0.9533 0.8041 0.8817 0.2263  -0.0208 -0.0184 720 VAL D C   
13611 O O   . VAL D 419 ? 0.8599 0.7351 0.7996 0.2172  -0.0156 -0.0220 720 VAL D O   
13612 C CB  . VAL D 419 ? 0.9951 0.9003 0.9515 0.2530  -0.0244 -0.0145 720 VAL D CB  
13613 C CG1 . VAL D 419 ? 1.0575 0.9474 1.0051 0.2746  -0.0301 -0.0115 720 VAL D CG1 
13614 C CG2 . VAL D 419 ? 0.9312 0.8839 0.9131 0.2430  -0.0237 -0.0115 720 VAL D CG2 
13615 N N   . TRP D 420 ? 1.0089 0.8153 0.9127 0.2303  -0.0220 -0.0204 721 TRP D N   
13616 C CA  . TRP D 420 ? 1.1803 0.9635 1.0687 0.2213  -0.0179 -0.0269 721 TRP D CA  
13617 C C   . TRP D 420 ? 1.2964 1.0860 1.1830 0.2375  -0.0121 -0.0366 721 TRP D C   
13618 O O   . TRP D 420 ? 1.3748 1.1681 1.2620 0.2597  -0.0123 -0.0387 721 TRP D O   
13619 C CB  . TRP D 420 ? 1.1770 0.9087 1.0378 0.2165  -0.0216 -0.0253 721 TRP D CB  
13620 C CG  . TRP D 420 ? 1.0805 0.8071 0.9421 0.1979  -0.0263 -0.0167 721 TRP D CG  
13621 C CD1 . TRP D 420 ? 1.0424 0.7731 0.9095 0.2000  -0.0317 -0.0084 721 TRP D CD1 
13622 C CD2 . TRP D 420 ? 0.9795 0.6987 0.8367 0.1746  -0.0260 -0.0159 721 TRP D CD2 
13623 N NE1 . TRP D 420 ? 0.8916 0.6174 0.7578 0.1795  -0.0342 -0.0028 721 TRP D NE1 
13624 C CE2 . TRP D 420 ? 0.9892 0.7087 0.8498 0.1641  -0.0308 -0.0073 721 TRP D CE2 
13625 C CE3 . TRP D 420 ? 1.0053 0.7195 0.8561 0.1621  -0.0221 -0.0217 721 TRP D CE3 
13626 C CZ2 . TRP D 420 ? 1.0816 0.7975 0.9401 0.1423  -0.0316 -0.0046 721 TRP D CZ2 
13627 C CZ3 . TRP D 420 ? 1.0641 0.7753 0.9129 0.1405  -0.0235 -0.0187 721 TRP D CZ3 
13628 C CH2 . TRP D 420 ? 1.0816 0.7942 0.9347 0.1312  -0.0281 -0.0104 721 TRP D CH2 
13629 N N   . LYS D 421 ? 1.2773 1.0693 1.1613 0.2267  -0.0068 -0.0426 722 LYS D N   
13630 C CA  . LYS D 421 ? 1.2233 1.0235 1.1053 0.2396  -0.0004 -0.0526 722 LYS D CA  
13631 C C   . LYS D 421 ? 1.1111 0.8723 0.9672 0.2357  0.0023  -0.0602 722 LYS D C   
13632 O O   . LYS D 421 ? 1.0296 0.7541 0.8670 0.2239  -0.0011 -0.0582 722 LYS D O   
13633 C CB  . LYS D 421 ? 1.1833 1.0312 1.0882 0.2321  0.0047  -0.0538 722 LYS D CB  
13634 C CG  . LYS D 421 ? 1.1480 1.0043 1.0592 0.2070  0.0040  -0.0488 722 LYS D CG  
13635 C CD  . LYS D 421 ? 1.1069 1.0104 1.0421 0.2013  0.0073  -0.0470 722 LYS D CD  
13636 C CE  . LYS D 421 ? 1.0366 0.9638 0.9895 0.2069  0.0035  -0.0403 722 LYS D CE  
13637 N NZ  . LYS D 421 ? 0.9195 0.8913 0.8938 0.2005  0.0070  -0.0392 722 LYS D NZ  
# 
